ID ALDOA_HUMAN Reviewed; 364 AA. AC P04075; B4DXI7; Q6FH76; Q6FI10; Q96B15; Q9BWD9; Q9UCN2; DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 14-DEC-2022, entry version 250. DE RecName: Full=Fructose-bisphosphate aldolase A {ECO:0000305}; DE EC=4.1.2.13 {ECO:0000269|PubMed:14766013}; DE AltName: Full=Lung cancer antigen NY-LU-1; DE AltName: Full=Muscle-type aldolase; GN Name=ALDOA {ECO:0000312|HGNC:HGNC:414}; Synonyms=ALDA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Liver; RX PubMed=3840020; DOI=10.1016/0006-291x(85)91818-2; RA Sakakibara M., Mukai T., Hori K.; RT "Nucleotide sequence of a cDNA clone for human aldolase: a messenger RNA in RT the liver."; RL Biochem. Biophys. Res. Commun. 131:413-420(1985). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Fibroblast; RX PubMed=3030757; DOI=10.1111/j.1432-1033.1987.tb10984.x; RA Izzo P., Costanzo P., Lupo A., Rippa E., Borghese A.M., Paolella G., RA Salvatore F.; RT "A new human species of aldolase A mRNA from fibroblasts."; RL Eur. J. Biochem. 164:9-13(1987). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=3391172; DOI=10.1111/j.1432-1033.1988.tb14136.x; RA Izzo P., Costanzo P., Lupo A., Rippa E., Paolella G., Salvatore F.; RT "Human aldolase A gene. Structural organization and tissue-specific RT expression by multiple promoters and alternate mRNA processing."; RL Eur. J. Biochem. 174:569-578(1988). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=1999195; DOI=10.1111/j.1432-1033.1991.tb15766.x; RA Mukai T., Arai Y., Yatsuki H., Joh K., Hori K.; RT "An additional promoter functions in the human aldolase A gene, but not in RT rat."; RL Eur. J. Biochem. 195:781-787(1991). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., RA LaBaer J.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Cervix, Eye, Lung, Testis, and Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-108 (ISOFORM 1). RX PubMed=3441006; DOI=10.1016/0022-2836(87)90556-0; RA Maire P., Gautron S., Hakim V., Gregori C., Mennecier F., Kahn A.; RT "Characterization of three optional promoters in the 5' region of the human RT aldolase A gene."; RL J. Mol. Biol. 197:425-438(1987). RN [11] RP PROTEIN SEQUENCE OF 2-364. RX PubMed=3355497; DOI=10.1042/bj2490779; RA Freemont P.S., Dunbar B., Fothergill-Gilmore L.A.; RT "The complete amino acid sequence of human skeletal-muscle fructose- RT bisphosphate aldolase."; RL Biochem. J. 249:779-788(1988). RN [12] RP PROTEIN SEQUENCE OF 2-63 AND 148-358. RX PubMed=6696436; DOI=10.1016/0003-9861(84)90075-4; RA Freemont P.S., Dunbar B., Fothergill L.A.; RT "Human skeletal-muscle aldolase: N-terminal sequence analysis of CNBr- and RT o-iodosobenzoic acid-cleavage fragments."; RL Arch. Biochem. Biophys. 228:342-352(1984). RN [13] RP PROTEIN SEQUENCE OF 2-22. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., RA Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass spectrometric RT identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [14] RP PROTEIN SEQUENCE OF 2-16. RC TISSUE=Colon carcinoma; RX PubMed=1353685; DOI=10.1016/0167-4889(92)90078-p; RA Lee K.N., Maxwell M.D., Patterson M.K. Jr., Birckbichler P.J., Conway E.; RT "Identification of transglutaminase substrates in HT29 colon cancer cells: RT use of 5-(biotinamido)pentylamine as a transglutaminase-specific probe."; RL Biochim. Biophys. Acta 1136:12-16(1992). RN [15] RP PROTEIN SEQUENCE OF 2-13; 29-42; 44-56; 61-69; 88-99; 154-173; 244-258 AND RP 332-342, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex; RA Lubec G., Vishwanath V., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [16] RP NUCLEOTIDE SEQUENCE [MRNA] OF 139-364 (ISOFORM 1/2). RX PubMed=3674018; RA Tolan D.R., Niclas J., Bruce B.D., Lebo R.V.; RT "Evolutionary implications of the human aldolase-A, -B, -C, and RT - pseudogene chromosome locations."; RL Am. J. Hum. Genet. 41:907-924(1987). RN [17] RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Lymphoblast; RX PubMed=14654843; DOI=10.1038/nature02166; RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.; RT "Proteomic characterization of the human centrosome by protein correlation RT profiling."; RL Nature 426:570-574(2003). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [20] RP INTERACTION WITH FBP2. RX PubMed=18214967; DOI=10.1002/prot.21909; RA Gizak A., Maciaszczyk E., Dzugaj A., Eschrich K., Rakus D.; RT "Evolutionary conserved N-terminal region of human muscle fructose 1,6- RT bisphosphatase regulates its activity and the interaction with aldolase."; RL Proteins 72:209-216(2008). RN [21] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36 AND SER-39, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [23] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-42; LYS-108 AND LYS-330, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36 AND SER-39, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [25] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [26] RP MALONYLATION AT LYS-111 AND LYS-312. RX PubMed=21908771; DOI=10.1074/mcp.m111.012658; RA Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y., He W., RA Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C., Dai J., RA Verdin E., Ye Y., Zhao Y.; RT "The first identification of lysine malonylation substrates and its RT regulatory enzyme."; RL Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011). RN [27] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39 AND SER-46, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [28] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22905912; DOI=10.1021/pr300539b; RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P., RA Mariman E.C., Renes J.; RT "Resveratrol-induced changes of the human adipocyte secretion profile."; RL J. Proteome Res. 11:4733-4743(2012). RN [29] RP CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [30] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [31] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-9; SER-36; SER-39 AND SER-46, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [32] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-46 AND SER-272, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [33] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [34] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-42, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [35] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [36] RP HYDROXYBUTYRYLATION AT LYS-147. RX PubMed=29192674; DOI=10.1038/cr.2017.149; RA Huang H., Luo Z., Qi S., Huang J., Xu P., Wang X., Gao L., Li F., Wang J., RA Zhao W., Gu W., Chen Z., Dai L., Dai J., Zhao Y.; RT "Landscape of the regulatory elements for lysine 2-hydroxyisobutyrylation RT pathway."; RL Cell Res. 28:111-125(2018). RN [37] RP HYDROXYBUTYRYLATION AT LYS-99. RX PubMed=29775581; DOI=10.1016/j.molcel.2018.04.011; RA Huang H., Tang S., Ji M., Tang Z., Shimada M., Liu X., Qi S., RA Locasale J.W., Roeder R.G., Zhao Y., Li X.; RT "p300-mediated lysine 2-hydroxyisobutyrylation regulates glycolysis."; RL Mol. Cell 70:663-678(2018). RN [38] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS). RX PubMed=2335208; DOI=10.1016/0014-5793(90)80211-z; RA Gamblin S.J., Cooper B., Millar J.R., Davies G.J., Littlechild J.A., RA Watson H.C.; RT "The crystal structure of human muscle aldolase at 3.0-A resolution."; RL FEBS Lett. 262:282-286(1990). RN [39] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX PubMed=2056525; DOI=10.1016/0022-2836(91)90650-u; RA Gamblin S.J., Davies G.J., Grimes J.M., Jackson R.M., Littlechild J.A., RA Watson H.C.; RT "Activity and specificity of human aldolases."; RL J. Mol. Biol. 219:573-576(1991). RN [40] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). RX PubMed=10048322; DOI=10.1110/ps.8.2.291; RA Dalby A., Dauter Z., Littlechild J.A.; RT "Crystal structure of human muscle aldolase complexed with fructose 1,6- RT bisphosphate: mechanistic implications."; RL Protein Sci. 8:291-297(1999). RN [41] RP VARIANT GSD12 GLY-129, AND CHARACTERIZATION OF VARIANT GSD12 GLY-129. RX PubMed=2825199; DOI=10.1073/pnas.84.23.8623; RA Kishi H., Mukai T., Hirono A., Fujii H., Miwa S., Hori K.; RT "Human aldolase A deficiency associated with a hemolytic anemia: RT thermolabile aldolase due to a single base mutation."; RL Proc. Natl. Acad. Sci. U.S.A. 84:8623-8627(1987). RN [42] RP CHARACTERIZATION OF VARIANT GSD12 GLY-129. RX PubMed=2229018; DOI=10.1093/oxfordjournals.jbchem.a123174; RA Takasaki Y., Takahashi I., Mukai T., Hori K.; RT "Human aldolase A of a hemolytic anemia patient with Asp-128-->Gly RT substitution: characteristics of an enzyme generated in E. coli transfected RT with the expression plasmid pHAAD128G."; RL J. Biochem. 108:153-157(1990). RN [43] RP VARIANT GSD12 LYS-207. RX PubMed=8598869; DOI=10.1056/nejm199604253341705; RA Kreuder J., Borkhardt A., Repp R., Pekrun A., Goettsche B., Gottschalk U., RA Reichmann H., Schachenmayr W., Schlegel K., Lampert F.; RT "Brief report: inherited metabolic myopathy and hemolysis due to a mutation RT in aldolase A."; RL N. Engl. J. Med. 334:1100-1104(1996). RN [44] RP VARIANTS GSD12 303-GLY--TYR-364 DEL AND TYR-339. RX PubMed=14615364; DOI=10.1182/blood-2003-09-3160; RA Yao D.C., Tolan D.R., Murray M.F., Harris D.J., Darras B.T., Geva A., RA Neufeld E.J.; RT "Hemolytic anemia and severe rhabdomyolysis caused by compound heterozygous RT mutations of the gene for erythrocyte/muscle isozyme of aldolase, RT ALDOA(Arg303X/Cys338Tyr)."; RL Blood 103:2401-2403(2004). RN [45] RP VARIANT GSD12 SER-347, BIOPHYSICOCHEMICAL PROPERTIES, CHARACTERIZATION OF RP VARIANTS GSD12 LYS-207 AND SER-347, CATALYTIC ACTIVITY, AND FUNCTION. RX PubMed=14766013; DOI=10.1042/bj20031941; RA Esposito G., Vitagliano L., Costanzo P., Borrelli L., Barone R., Pavone L., RA Izzo P., Zagari A., Salvatore F.; RT "Human aldolase A natural mutants: relationship between flexibility of the RT C-terminal region and enzyme function."; RL Biochem. J. 380:51-56(2004). CC -!- FUNCTION: Catalyzes the reversible conversion of beta-D-fructose 1,6- CC bisphosphate (FBP) into two triose phosphate and plays a key role in CC glycolysis and gluconeogenesis (PubMed:14766013). In addition, may also CC function as scaffolding protein (By similarity). {ECO:0000250, CC ECO:0000269|PubMed:14766013}. CC -!- CATALYTIC ACTIVITY: CC Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3- CC phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729, CC ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13; CC Evidence={ECO:0000269|PubMed:14766013}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14730; CC Evidence={ECO:0000305|PubMed:14766013}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=52 uM for fructose 1,6-bisphosphate (at 30 degrees Celsius) CC {ECO:0000269|PubMed:14766013}; CC Temperature dependence: CC Thermal denaturation midpoint (Tm) is 54.4 degrees Celsius. CC {ECO:0000269|PubMed:14766013}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 4/4. CC -!- SUBUNIT: Homotetramer. Interacts with SNX9 and WAS (By similarity). CC Interacts with FBP2; the interaction blocks FBP2 inhibition by CC physiological concentrations of AMP and reduces inhibition by Ca(2+). CC {ECO:0000250, ECO:0000269|PubMed:18214967}. CC -!- INTERACTION: CC P04075; P04075: ALDOA; NbExp=2; IntAct=EBI-709613, EBI-709613; CC P04075; P09972: ALDOC; NbExp=3; IntAct=EBI-709613, EBI-2952751; CC P04075; P12004: PCNA; NbExp=3; IntAct=EBI-709613, EBI-358311; CC P04075-2; P04075-2: ALDOA; NbExp=4; IntAct=EBI-10194102, EBI-10194102; CC P04075-2; P09972: ALDOC; NbExp=6; IntAct=EBI-10194102, EBI-2952751; CC P04075-2; P42858: HTT; NbExp=6; IntAct=EBI-10194102, EBI-466029; CC P04075-2; P05014: IFNA4; NbExp=3; IntAct=EBI-10194102, EBI-10194381; CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, I band CC {ECO:0000250|UniProtKB:P00883}. Cytoplasm, myofibril, sarcomere, M line CC {ECO:0000250|UniProtKB:P00883}. Note=In skeletal muscle, accumulates CC around the M line and within the I band, colocalizing with FBP2 on both CC sides of the Z line in the absence of Ca(2+). CC {ECO:0000250|UniProtKB:P00883}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P04075-1; Sequence=Displayed; CC Name=2; CC IsoId=P04075-2; Sequence=VSP_047261; CC -!- DISEASE: Glycogen storage disease 12 (GSD12) [MIM:611881]: A metabolic CC disorder associated with increased hepatic glycogen and hemolytic CC anemia. It may lead to myopathy with exercise intolerance and CC rhabdomyolysis. {ECO:0000269|PubMed:14615364, CC ECO:0000269|PubMed:14766013, ECO:0000269|PubMed:2229018, CC ECO:0000269|PubMed:2825199, ECO:0000269|PubMed:8598869}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- MISCELLANEOUS: In vertebrates, three forms of this ubiquitous CC glycolytic enzyme are found, aldolase A in muscle, aldolase B in liver CC and aldolase C in brain. CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M11560; AAA51690.1; -; mRNA. DR EMBL; X05236; CAA28861.1; -; mRNA. DR EMBL; X12447; CAA30979.1; -; Genomic_DNA. DR EMBL; AK301993; BAG63399.1; -; mRNA. DR EMBL; CR536528; CAG38765.1; -; mRNA. DR EMBL; CR541880; CAG46678.1; -; mRNA. DR EMBL; AC093512; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471238; EAW79933.1; -; Genomic_DNA. DR EMBL; BC000367; AAH00367.2; -; mRNA. DR EMBL; BC004333; AAH04333.1; -; mRNA. DR EMBL; BC010660; AAH10660.1; -; mRNA. DR EMBL; BC012880; AAH12880.1; -; mRNA. DR EMBL; BC013614; AAH13614.1; -; mRNA. DR EMBL; BC015888; AAH15888.1; -; mRNA. DR EMBL; BC016170; AAH16170.1; -; mRNA. DR EMBL; BC016800; AAH16800.1; -; mRNA. DR EMBL; M21190; AAA51697.1; -; mRNA. DR CCDS; CCDS10668.1; -. [P04075-1] DR CCDS; CCDS58450.1; -. [P04075-2] DR PIR; S14084; ADHUA. DR RefSeq; NP_000025.1; NM_000034.3. DR RefSeq; NP_001121089.1; NM_001127617.2. [P04075-1] DR RefSeq; NP_001230106.1; NM_001243177.1. [P04075-2] DR RefSeq; NP_908930.1; NM_184041.2. [P04075-1] DR RefSeq; NP_908932.1; NM_184043.2. [P04075-1] DR RefSeq; XP_011544070.1; XM_011545768.2. DR PDB; 1ALD; X-ray; 2.00 A; A=2-364. DR PDB; 2ALD; X-ray; 2.10 A; A=2-364. DR PDB; 4ALD; X-ray; 2.80 A; A=2-364. DR PDB; 5KY6; X-ray; 1.94 A; A/B/C/D=2-364. DR PDB; 6XMH; X-ray; 1.95 A; A/B=1-364. DR PDB; 6XML; X-ray; 1.88 A; A/B=1-364. DR PDB; 6XMM; X-ray; 2.11 A; A/B=1-364. DR PDB; 6XMO; X-ray; 2.60 A; A/B=1-364. DR PDBsum; 1ALD; -. DR PDBsum; 2ALD; -. DR PDBsum; 4ALD; -. DR PDBsum; 5KY6; -. DR PDBsum; 6XMH; -. DR PDBsum; 6XML; -. DR PDBsum; 6XMM; -. DR PDBsum; 6XMO; -. DR AlphaFoldDB; P04075; -. DR SMR; P04075; -. DR BioGRID; 106728; 243. DR IntAct; P04075; 83. DR MINT; P04075; -. DR STRING; 9606.ENSP00000378669; -. DR ChEMBL; CHEMBL2106; -. DR DrugBank; DB04733; 1,6-DI-O-PHOSPHONO-D-MANNITOL. DR DrugBank; DB02512; 1,6-Fructose Diphosphate (Linear Form). DR DrugBank; DB11638; Artenimol. DR DrugBank; DB04326; Dihydroxyacetone phosphate. DR DrugBank; DB08240; N-(4-CHLOROPHENYL)-3-(PHOSPHONOOXY)NAPHTHALENE-2-CARBOXAMIDE. DR DrugBank; DB01593; Zinc. DR DrugBank; DB14487; Zinc acetate. DR DrugBank; DB14533; Zinc chloride. DR DrugBank; DB14548; Zinc sulfate, unspecified form. DR MoonProt; P04075; -. DR CarbonylDB; P04075; -. DR GlyGen; P04075; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P04075; -. DR MetOSite; P04075; -. DR PhosphoSitePlus; P04075; -. DR SwissPalm; P04075; -. DR BioMuta; ALDOA; -. DR DMDM; 113606; -. DR DOSAC-COBS-2DPAGE; P04075; -. DR OGP; P04075; -. DR REPRODUCTION-2DPAGE; IPI00465439; -. DR REPRODUCTION-2DPAGE; P04075; -. DR SWISS-2DPAGE; P04075; -. DR UCD-2DPAGE; P04075; -. DR CPTAC; CPTAC-459; -. DR EPD; P04075; -. DR jPOST; P04075; -. DR MassIVE; P04075; -. DR MaxQB; P04075; -. DR PaxDb; P04075; -. DR PeptideAtlas; P04075; -. DR PRIDE; P04075; -. DR ProteomicsDB; 51647; -. [P04075-1] DR TopDownProteomics; P04075-1; -. [P04075-1] DR Antibodypedia; 1031; 709 antibodies from 37 providers. DR DNASU; 226; -. DR Ensembl; ENST00000412304.6; ENSP00000400452.2; ENSG00000149925.22. [P04075-1] DR Ensembl; ENST00000563060.6; ENSP00000455800.2; ENSG00000149925.22. [P04075-1] DR Ensembl; ENST00000569545.5; ENSP00000455700.1; ENSG00000149925.22. [P04075-1] DR Ensembl; ENST00000642816.3; ENSP00000496166.1; ENSG00000149925.22. [P04075-2] DR Ensembl; ENST00000643777.4; ENSP00000494188.2; ENSG00000149925.22. [P04075-1] DR GeneID; 226; -. DR KEGG; hsa:226; -. DR MANE-Select; ENST00000642816.3; ENSP00000496166.1; NM_001243177.4; NP_001230106.1. [P04075-2] DR UCSC; uc010veg.3; human. [P04075-1] DR CTD; 226; -. DR DisGeNET; 226; -. DR GeneCards; ALDOA; -. DR HGNC; HGNC:414; ALDOA. DR HPA; ENSG00000149925; Group enriched (skeletal muscle, tongue). DR MalaCards; ALDOA; -. DR MIM; 103850; gene. DR MIM; 611881; phenotype. DR neXtProt; NX_P04075; -. DR OpenTargets; ENSG00000149925; -. DR Orphanet; 57; Glycogen storage disease due to aldolase A deficiency. DR PharmGKB; PA24707; -. DR VEuPathDB; HostDB:ENSG00000149925; -. DR eggNOG; KOG1557; Eukaryota. DR GeneTree; ENSGT00950000182987; -. DR HOGENOM; CLU_031243_0_0_1; -. DR InParanoid; P04075; -. DR OMA; DYREMLF; -. DR OrthoDB; 799973at2759; -. DR PhylomeDB; P04075; -. DR TreeFam; TF314203; -. DR BioCyc; MetaCyc:HS07647-MON; -. DR BRENDA; 4.1.2.13; 2681. DR PathwayCommons; P04075; -. DR Reactome; R-HSA-114608; Platelet degranulation. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-70171; Glycolysis. DR Reactome; R-HSA-70263; Gluconeogenesis. DR SABIO-RK; P04075; -. DR SignaLink; P04075; -. DR SIGNOR; P04075; -. DR UniPathway; UPA00109; UER00183. DR BioGRID-ORCS; 226; 760 hits in 1085 CRISPR screens. DR ChiTaRS; ALDOA; human. DR EvolutionaryTrace; P04075; -. DR GeneWiki; Aldolase_A; -. DR GenomeRNAi; 226; -. DR Pharos; P04075; Tbio. DR PRO; PR:P04075; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; P04075; protein. DR Bgee; ENSG00000149925; Expressed in gastrocnemius and 94 other tissues. DR ExpressionAtlas; P04075; baseline and differential. DR Genevisible; P04075; HS. DR GO; GO:0015629; C:actin cytoskeleton; IDA:BHF-UCL. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; IDA:BHF-UCL. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB. DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome. DR GO; GO:0031674; C:I band; TAS:BHF-UCL. DR GO; GO:0031430; C:M band; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005634; C:nucleus; HDA:UniProtKB. DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome. DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome. DR GO; GO:0061827; C:sperm head; IDA:CAFA. DR GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome. DR GO; GO:0003779; F:actin binding; TAS:BHF-UCL. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:0008092; F:cytoskeletal protein binding; IDA:BHF-UCL. DR GO; GO:0070061; F:fructose binding; IDA:BHF-UCL. DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IDA:BHF-UCL. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0015631; F:tubulin binding; TAS:BHF-UCL. DR GO; GO:0007015; P:actin filament organization; TAS:BHF-UCL. DR GO; GO:0006754; P:ATP biosynthetic process; IMP:BHF-UCL. DR GO; GO:0007339; P:binding of sperm to zona pellucida; IMP:CAFA. DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IDA:BHF-UCL. DR GO; GO:0006000; P:fructose metabolic process; IMP:BHF-UCL. DR GO; GO:0006096; P:glycolytic process; IMP:BHF-UCL. DR GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:BHF-UCL. DR GO; GO:0051289; P:protein homotetramerization; ISS:UniProtKB. DR GO; GO:0008360; P:regulation of cell shape; IDA:BHF-UCL. DR GO; GO:0006941; P:striated muscle contraction; IMP:BHF-UCL. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR029768; Aldolase_I_AS. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000741; FBA_I. DR PANTHER; PTHR11627; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1. DR Pfam; PF00274; Glycolytic; 1. DR PROSITE; PS00158; ALDOLASE_CLASS_I; 1. DR AGR; HGNC:414; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; KW Direct protein sequencing; Disease variant; Glycogen storage disease; KW Glycolysis; Hereditary hemolytic anemia; Hydroxylation; Isopeptide bond; KW Lyase; Phosphoprotein; Reference proteome; Schiff base; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:12665801, FT ECO:0000269|PubMed:1353685, ECO:0000269|PubMed:3355497, FT ECO:0000269|PubMed:6696436, ECO:0000269|Ref.15, FT ECO:0007744|PubMed:22223895" FT CHAIN 2..364 FT /note="Fructose-bisphosphate aldolase A" FT /id="PRO_0000216936" FT ACT_SITE 188 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 230 FT /note="Schiff-base intermediate with dihydroxyacetone-P" FT BINDING 56 FT /ligand="substrate" FT BINDING 147 FT /ligand="substrate" FT SITE 364 FT /note="Necessary for preference for fructose 1,6- FT bisphosphate over fructose 1-phosphate" FT MOD_RES 5 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P05065" FT MOD_RES 9 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 36 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163" FT MOD_RES 39 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 42 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 46 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 99 FT /note="N6-(2-hydroxyisobutyryl)lysine" FT /evidence="ECO:0000269|PubMed:29775581" FT MOD_RES 108 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 111 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0000250|UniProtKB:P09972" FT MOD_RES 111 FT /note="N6-malonyllysine; alternate" FT /evidence="ECO:0000269|PubMed:21908771" FT MOD_RES 132 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P05065" FT MOD_RES 147 FT /note="N6-(2-hydroxyisobutyryl)lysine" FT /evidence="ECO:0000269|PubMed:29192674" FT MOD_RES 272 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 312 FT /note="N6-malonyllysine" FT /evidence="ECO:0000269|PubMed:21908771" FT MOD_RES 330 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT CROSSLNK 42 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 42 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT VAR_SEQ 1 FT /note="M -> MARRKPEGSSFNMTHLSMAMAFSFPPVASGQLHPQLGNTQHQTELGK FT ELATTSTM (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_047261" FT VARIANT 82 FT /note="E -> Q (in dbSNP:rs11553107)" FT /id="VAR_048219" FT VARIANT 129 FT /note="D -> G (in GSD12; thermolabile; dbSNP:rs121909533)" FT /evidence="ECO:0000269|PubMed:2229018, FT ECO:0000269|PubMed:2825199" FT /id="VAR_000550" FT VARIANT 142 FT /note="G -> V (in dbSNP:rs11553108)" FT /id="VAR_048220" FT VARIANT 207 FT /note="E -> K (in GSD12; reduces thermal stability; 3-fold FT decrease in catalytic efficiency mostly due to reduced FT substrate affinity; dbSNP:rs121909534)" FT /evidence="ECO:0000269|PubMed:14766013, FT ECO:0000269|PubMed:8598869" FT /id="VAR_044142" FT VARIANT 303..364 FT /note="Missing (in GSD12)" FT /evidence="ECO:0000269|PubMed:14615364" FT /id="VAR_085824" FT VARIANT 339 FT /note="C -> Y (in GSD12)" FT /evidence="ECO:0000269|PubMed:14615364" FT /id="VAR_044143" FT VARIANT 347 FT /note="G -> S (in GSD12; likely benign variant; does not FT affect thermal stability; 4-fold decrease in catalytic FT efficiency due to reduced enzyme activity; FT dbSNP:rs138824667)" FT /evidence="ECO:0000269|PubMed:14766013" FT /id="VAR_044144" FT CONFLICT 73 FT /note="C -> G (in Ref. 3; CAA30979)" FT /evidence="ECO:0000305" FT CONFLICT 180 FT /note="Q -> R (in Ref. 6; CAG46678)" FT /evidence="ECO:0000305" FT CONFLICT 196 FT /note="D -> A (in Ref. 3; CAA30979)" FT /evidence="ECO:0000305" FT CONFLICT 230 FT /note="K -> N (in Ref. 3; CAA30979)" FT /evidence="ECO:0000305" FT CONFLICT 280 FT /note="A -> S (in Ref. 3; CAA30979)" FT /evidence="ECO:0000305" FT HELIX 10..23 FT /evidence="ECO:0007829|PDB:6XML" FT STRAND 29..33 FT /evidence="ECO:0007829|PDB:6XML" FT TURN 37..39 FT /evidence="ECO:0007829|PDB:6XML" FT HELIX 40..45 FT /evidence="ECO:0007829|PDB:6XML" FT TURN 46..48 FT /evidence="ECO:0007829|PDB:6XML" FT HELIX 53..64 FT /evidence="ECO:0007829|PDB:6XML" FT HELIX 68..73 FT /evidence="ECO:0007829|PDB:6XML" FT STRAND 74..79 FT /evidence="ECO:0007829|PDB:6XML" FT HELIX 81..84 FT /evidence="ECO:0007829|PDB:6XML" FT HELIX 94..100 FT /evidence="ECO:0007829|PDB:6XML" FT STRAND 104..108 FT /evidence="ECO:0007829|PDB:6XML" FT STRAND 113..115 FT /evidence="ECO:0007829|PDB:6XML" FT STRAND 119..121 FT /evidence="ECO:0007829|PDB:6XML" FT STRAND 123..125 FT /evidence="ECO:0007829|PDB:6XML" FT HELIX 131..140 FT /evidence="ECO:0007829|PDB:6XML" FT STRAND 145..152 FT /evidence="ECO:0007829|PDB:6XML" FT STRAND 155..157 FT /evidence="ECO:0007829|PDB:5KY6" FT HELIX 161..180 FT /evidence="ECO:0007829|PDB:6XML" FT STRAND 184..191 FT /evidence="ECO:0007829|PDB:6XML" FT HELIX 199..219 FT /evidence="ECO:0007829|PDB:6XML" FT HELIX 224..226 FT /evidence="ECO:0007829|PDB:6XML" FT HELIX 246..258 FT /evidence="ECO:0007829|PDB:6XML" FT STRAND 267..271 FT /evidence="ECO:0007829|PDB:6XML" FT HELIX 277..289 FT /evidence="ECO:0007829|PDB:6XML" FT STRAND 296..303 FT /evidence="ECO:0007829|PDB:6XML" FT HELIX 304..314 FT /evidence="ECO:0007829|PDB:6XML" FT HELIX 318..320 FT /evidence="ECO:0007829|PDB:6XML" FT HELIX 321..338 FT /evidence="ECO:0007829|PDB:6XML" FT TURN 339..341 FT /evidence="ECO:0007829|PDB:6XML" FT STRAND 348..350 FT /evidence="ECO:0007829|PDB:1ALD" FT HELIX 351..354 FT /evidence="ECO:0007829|PDB:6XMH" FT HELIX 357..359 FT /evidence="ECO:0007829|PDB:5KY6" FT HELIX 361..363 FT /evidence="ECO:0007829|PDB:5KY6" SQ SEQUENCE 364 AA; 39420 MW; 0AAED80F755A7BE8 CRC64; MPYQYPALTP EQKKELSDIA HRIVAPGKGI LAADESTGSI AKRLQSIGTE NTEENRRFYR QLLLTADDRV NPCIGGVILF HETLYQKADD GRPFPQVIKS KGGVVGIKVD KGVVPLAGTN GETTTQGLDG LSERCAQYKK DGADFAKWRC VLKIGEHTPS ALAIMENANV LARYASICQQ NGIVPIVEPE ILPDGDHDLK RCQYVTEKVL AAVYKALSDH HIYLEGTLLK PNMVTPGHAC TQKFSHEEIA MATVTALRRT VPPAVTGITF LSGGQSEEEA SINLNAINKC PLLKPWALTF SYGRALQASA LKAWGGKKEN LKAAQEEYVK RALANSLACQ GKYTPSGQAG AAASESLFVS NHAY // ID F16P2_HUMAN Reviewed; 339 AA. AC O00757; Q17R39; Q6FI53; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 27-SEP-2005, sequence version 2. DT 14-DEC-2022, entry version 183. DE RecName: Full=Fructose-1,6-bisphosphatase isozyme 2; DE Short=FBPase 2; DE EC=3.1.3.11; DE AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase 2; DE AltName: Full=Muscle FBPase; GN Name=FBP2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LEU-86. RC TISSUE=Skeletal muscle; RX PubMed=9678974; DOI=10.1016/s0378-1119(98)00181-4; RA Tillman H., Eschrich K.; RT "Isolation and characterization of an allelic cDNA for human muscle RT fructose-1,6-bisphosphatase."; RL Gene 212:295-304(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., RA LaBaer J.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-86. RC TISSUE=Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=12507293; DOI=10.14670/hh-18.135; RA Gizak A., Rakus D., Dzugaj A.; RT "Immunohistochemical localization of human fructose-1,6-bisphosphatase in RT subcellular structures of myocytes."; RL Histol. Histopathol. 18:135-142(2003). RN [6] RP ACTIVITY REGULATION, COFACTOR, MUTAGENESIS OF LYS-21; THR-178 AND GLN-180, RP AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=16213487; DOI=10.1016/j.febslet.2005.09.021; RA Rakus D., Maciaszczyk E., Wawrzycka D., Ulaszewski S., Eschrich K., RA Dzugaj A.; RT "The origin of the high sensitivity of muscle fructose 1,6-bisphosphatase RT towards AMP."; RL FEBS Lett. 579:5577-5581(2005). RN [7] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL RP PROPERTIES, AND MUTAGENESIS OF GLU-70. RX PubMed=17350621; DOI=10.1016/j.febslet.2007.02.051; RA Zarzycki M., Maciaszczyk E., Dzugaj A.; RT "Glu 69 is essential for the high sensitivity of muscle fructose-1,6- RT bisphosphatase inhibition by calcium ions."; RL FEBS Lett. 581:1347-1350(2007). RN [8] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, INTERACTION WITH ALDOA, RP AND MUTAGENESIS OF 1-MET--ASP-10. RX PubMed=18214967; DOI=10.1002/prot.21909; RA Gizak A., Maciaszczyk E., Dzugaj A., Eschrich K., Rakus D.; RT "Evolutionary conserved N-terminal region of human muscle fructose 1,6- RT bisphosphatase regulates its activity and the interaction with aldolase."; RL Proteins 72:209-216(2008). RN [9] RP SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, AND MUTAGENESIS OF RP 204-LYS--LYS-208. RX PubMed=19626708; DOI=10.1002/prot.22506; RA Gizak A., Maciaszczyk-Dziubinska E., Jurowicz M., Rakus D.; RT "Muscle FBPase is targeted to nucleus by its 203KKKGK207 sequence."; RL Proteins 77:262-267(2009). RN [10] RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) OF 2-339 OF MUTANT GLN-70 IN COMPLEX RP WITH FRUCTOSE-6-PHOSPHATE AND AMP, AND SUBUNIT. RX PubMed=22120740; DOI=10.1107/s090744491104385x; RA Zarzycki M., Kolodziejczyk R., Maciaszczyk-Dziubinska E., Wysocki R., RA Jaskolski M., Dzugaj A.; RT "Structure of E69Q mutant of human muscle fructose-1,6-bisphosphatase."; RL Acta Crystallogr. D 67:1028-1034(2011). RN [11] RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 2-339 OF WILD-TYPE AND MUTANT RP ARG-33 IN COMPLEXES WITH FRUCTOSE-6-PHOSPHATE; PHOSPHATE ION; AMP; ZINC ION RP AND MAGNESIUM IONS, COFACTOR, AND SUBUNIT. RX PubMed=24086250; DOI=10.1371/journal.pone.0071242; RA Shi R., Chen Z.Y., Zhu D.W., Li C., Shan Y., Xu G., Lin S.X.; RT "Crystal structures of human muscle fructose-1,6-bisphosphatase: novel RT quaternary states, enhanced AMP affinity, and allosteric signal RT transmission pathway."; RL PLoS ONE 8:E71242-E71242(2013). RN [12] RP VARIANT CORLK MET-115, CHARACTERIZATION OF VARIANT CORLK MET-115, RP INVOLVEMENT IN CORLK, FUNCTION, AND ACTIVITY REGULATION. RX PubMed=33977262; DOI=10.1093/braincomms/fcab036; RA Gizak A., Diegmann S., Dreha-Kulaczewski S., Wisniewski J., Duda P., RA Ohlenbusch A., Huppke B., Henneke M., Hoehne W., Altmueller J., Thiele H., RA Nuernberg P., Rakus D., Gaertner J., Huppke P.; RT "A novel remitting leukodystrophy associated with a variant in FBP2."; RL Brain Commun. 3:fcab036-fcab036(2021). CC -!- FUNCTION: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to CC fructose 6-phosphate in the presence of divalent cations and probably CC participates in glycogen synthesis from carbohydrate precursors, such CC as lactate. {ECO:0000269|PubMed:17350621, ECO:0000269|PubMed:18214967, CC ECO:0000269|PubMed:33977262}. CC -!- CATALYTIC ACTIVITY: CC Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6- CC phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11; CC Evidence={ECO:0000269|PubMed:17350621, ECO:0000269|PubMed:18214967}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:16213487, ECO:0000269|PubMed:24086250}; CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000269|PubMed:16213487, CC ECO:0000269|PubMed:24086250}; CC -!- ACTIVITY REGULATION: Subject to complex allosteric regulation. The CC enzyme can assume an active R-state, or an inactive T-state. CC Intermediate conformations may exist. AMP acts as allosteric inhibitor CC (PubMed:33977262). Fructose 2,6-bisphosphate acts as competitive CC inhibitor. Strongly inhibited by Ca(2+). {ECO:0000269|PubMed:16213487, CC ECO:0000269|PubMed:17350621, ECO:0000269|PubMed:18214967, CC ECO:0000269|PubMed:33977262}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1.3 uM for fructose 1,6-bisphosphate {ECO:0000269|PubMed:16213487, CC ECO:0000269|PubMed:17350621}; CC KM=2.6 uM for fructose 1,6-bisphosphate {ECO:0000269|PubMed:16213487, CC ECO:0000269|PubMed:17350621}; CC Note=The kinetic constants are determined for the recombinant enzyme CC expressed in E.coli.; CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC -!- SUBUNIT: Homotetramer. Interacts with ALDOA; the interaction blocks CC inhibition by physiological concentrations of AMP and reduces CC inhibition by Ca(2+). Interacts with alpha-actinin and F-actin. CC {ECO:0000269|PubMed:18214967, ECO:0000269|PubMed:22120740, CC ECO:0000269|PubMed:24086250}. CC -!- INTERACTION: CC O00757; P09467: FBP1; NbExp=16; IntAct=EBI-719781, EBI-712740; CC O00757; O00757: FBP2; NbExp=5; IntAct=EBI-719781, EBI-719781; CC O00757; P04792: HSPB1; NbExp=3; IntAct=EBI-719781, EBI-352682; CC O00757; O60333-2: KIF1B; NbExp=3; IntAct=EBI-719781, EBI-10975473; CC O00757; O60260-5: PRKN; NbExp=3; IntAct=EBI-719781, EBI-21251460; CC O00757; P60891: PRPS1; NbExp=3; IntAct=EBI-719781, EBI-749195; CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000250}. Cytoplasm. Nucleus. CC Cytoplasm, myofibril, sarcomere, Z line. Note=In neonatal CC cardiomyocytes, distributed throughout the cytosol, accumulating in the CC intercalated disks which occur at the Z line of cardiomyocytes and CC connect adjacent cells, and also located in the nucleus; dissociates CC from the Z line following an increase in cytosolic Ca(2+) concentration CC (By similarity). In muscle precursor cells, localizes predominantly to CC the nucleus and to a lesser extent to the cytoplasm at the CC proliferative phase, while mainly localizing to the cytoplasm at the CC differentiation phase (By similarity). Colocalizes with ALDOA and CC alpha-actinin on both sides of the Z line of skeletal muscle; CC dissociates rapidly from the Z line following an increase in cytosolic CC Ca(2+) concentration. {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscle (at protein level). CC {ECO:0000269|PubMed:12507293}. CC -!- DISEASE: Leukodystrophy, childhood-onset, remitting (CORLK) CC [MIM:619864]: An autosomal dominant disorder characterized by loss of CC developmental abilities, demyelination and leukodystrophy on brain CC imaging, triggered by fever or infection in the first year of life. CC Abnormalities almost completely resolve over a period of 1 to 2 years, CC and affected children regain normal development accompanied by CC remyelination. {ECO:0000269|PubMed:33977262}. Note=The disease may be CC caused by variants affecting the gene represented in this entry. CC -!- MISCELLANEOUS: Specific for the alpha-anomer of the substrate CC (PubMed:22120740). The Arg-33 mutant form has been shown to act on the CC beta-anomer (PubMed:24086250). {ECO:0000305|PubMed:22120740, CC ECO:0000305|PubMed:24086250}. CC -!- SIMILARITY: Belongs to the FBPase class 1 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Y10812; CAA71772.1; -; mRNA. DR EMBL; CR536483; CAG38722.1; -; mRNA. DR EMBL; AL161728; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC113632; AAI13633.1; -; mRNA. DR EMBL; BC117477; AAI17478.1; -; mRNA. DR CCDS; CCDS6711.1; -. DR RefSeq; NP_003828.2; NM_003837.3. DR PDB; 3IFA; X-ray; 1.93 A; A/B/C/D=2-339. DR PDB; 3IFC; X-ray; 1.97 A; A/B/C/D=2-339. DR PDB; 4HE0; X-ray; 2.69 A; A=2-339. DR PDB; 4HE1; X-ray; 2.23 A; A=2-339. DR PDB; 4HE2; X-ray; 1.60 A; A=2-339. DR PDB; 5ET5; X-ray; 1.67 A; A=2-339. DR PDB; 5ET6; X-ray; 1.84 A; A/B/C/D=2-339. DR PDB; 5ET7; X-ray; 2.99 A; A/B/C/D=2-339. DR PDB; 5ET8; X-ray; 1.92 A; A=2-339. DR PDB; 5K54; X-ray; 1.72 A; A=2-339. DR PDB; 5K55; X-ray; 1.98 A; A=2-339. DR PDB; 5K56; X-ray; 2.20 A; A=2-339. DR PDB; 5L0A; X-ray; 2.30 A; A=2-339. DR PDB; 5Q0C; X-ray; 2.40 A; A/B/C/D/E/F/G/H=1-339. DR PDBsum; 3IFA; -. DR PDBsum; 3IFC; -. DR PDBsum; 4HE0; -. DR PDBsum; 4HE1; -. DR PDBsum; 4HE2; -. DR PDBsum; 5ET5; -. DR PDBsum; 5ET6; -. DR PDBsum; 5ET7; -. DR PDBsum; 5ET8; -. DR PDBsum; 5K54; -. DR PDBsum; 5K55; -. DR PDBsum; 5K56; -. DR PDBsum; 5L0A; -. DR PDBsum; 5Q0C; -. DR AlphaFoldDB; O00757; -. DR SMR; O00757; -. DR BioGRID; 114317; 26. DR IntAct; O00757; 24. DR MINT; O00757; -. DR STRING; 9606.ENSP00000364486; -. DR DEPOD; FBP2; -. DR iPTMnet; O00757; -. DR PhosphoSitePlus; O00757; -. DR SwissPalm; O00757; -. DR BioMuta; FBP2; -. DR EPD; O00757; -. DR jPOST; O00757; -. DR MassIVE; O00757; -. DR MaxQB; O00757; -. DR PaxDb; O00757; -. DR PeptideAtlas; O00757; -. DR ProteomicsDB; 48020; -. DR Antibodypedia; 2920; 244 antibodies from 26 providers. DR DNASU; 8789; -. DR Ensembl; ENST00000375337.4; ENSP00000364486.3; ENSG00000130957.5. DR GeneID; 8789; -. DR KEGG; hsa:8789; -. DR MANE-Select; ENST00000375337.4; ENSP00000364486.3; NM_003837.4; NP_003828.2. DR UCSC; uc004auv.5; human. DR CTD; 8789; -. DR DisGeNET; 8789; -. DR GeneCards; FBP2; -. DR HGNC; HGNC:3607; FBP2. DR HPA; ENSG00000130957; Group enriched (skeletal muscle, tongue). DR MIM; 603027; gene. DR MIM; 619864; phenotype. DR neXtProt; NX_O00757; -. DR OpenTargets; ENSG00000130957; -. DR PharmGKB; PA28019; -. DR VEuPathDB; HostDB:ENSG00000130957; -. DR eggNOG; KOG1458; Eukaryota. DR GeneTree; ENSGT00390000015513; -. DR HOGENOM; CLU_039977_1_0_1; -. DR InParanoid; O00757; -. DR OMA; HEKSECY; -. DR OrthoDB; 1381522at2759; -. DR PhylomeDB; O00757; -. DR TreeFam; TF314824; -. DR BioCyc; MetaCyc:HS05462-MON; -. DR BRENDA; 3.1.3.11; 2681. DR PathwayCommons; O00757; -. DR Reactome; R-HSA-70263; Gluconeogenesis. DR SABIO-RK; O00757; -. DR SignaLink; O00757; -. DR SIGNOR; O00757; -. DR UniPathway; UPA00138; -. DR BioGRID-ORCS; 8789; 23 hits in 1069 CRISPR screens. DR EvolutionaryTrace; O00757; -. DR GenomeRNAi; 8789; -. DR Pharos; O00757; Tbio. DR PRO; PR:O00757; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; O00757; protein. DR Bgee; ENSG00000130957; Expressed in hindlimb stylopod muscle and 112 other tissues. DR Genevisible; O00757; HS. DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0030018; C:Z disc; IEA:UniProtKB-SubCell. DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central. DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central. DR GO; GO:0006000; P:fructose metabolic process; IBA:GO_Central. DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central. DR GO; GO:0005986; P:sucrose biosynthetic process; IBA:GO_Central. DR CDD; cd00354; FBPase; 1. DR HAMAP; MF_01855; FBPase_class1; 1. DR InterPro; IPR044015; FBPase_C_dom. DR InterPro; IPR000146; FBPase_class-1. DR InterPro; IPR033391; FBPase_N. DR InterPro; IPR028343; FBPtase. DR InterPro; IPR020548; Fructose_bisphosphatase_AS. DR PANTHER; PTHR11556; FRUCTOSE-1,6-BISPHOSPHATASE-RELATED; 1. DR Pfam; PF00316; FBPase; 1. DR Pfam; PF18913; FBPase_C; 1. DR PIRSF; PIRSF500210; FBPtase; 1. DR PIRSF; PIRSF000904; FBPtase_SBPase; 1. DR PRINTS; PR00115; F16BPHPHTASE. DR PROSITE; PS00124; FBPASE; 1. DR AGR; HGNC:3607; -. PE 1: Evidence at protein level; KW 3D-structure; Allosteric enzyme; Calcium; Carbohydrate metabolism; KW Cell junction; Cytoplasm; Disease variant; Gluconeogenesis; Hydrolase; KW Leukodystrophy; Magnesium; Metal-binding; Nucleus; Phosphoprotein; KW Reference proteome. FT CHAIN 1..339 FT /note="Fructose-1,6-bisphosphatase isozyme 2" FT /id="PRO_0000200504" FT REGION 3..10 FT /note="Important for interaction with ALDOA" FT /evidence="ECO:0000269|PubMed:18214967" FT MOTIF 204..208 FT /note="Nuclear localization signal" FT /evidence="ECO:0000269|PubMed:19626708" FT BINDING 18 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000269|PubMed:22120740" FT BINDING 28..32 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000269|PubMed:22120740" FT BINDING 69 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT BINDING 98 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT BINDING 98 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT BINDING 113..114 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000269|PubMed:22120740" FT BINDING 119 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT BINDING 119 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT BINDING 121 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT BINDING 122 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT BINDING 122 FT /ligand="substrate" FT BINDING 141 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000269|PubMed:22120740" FT BINDING 213..216 FT /ligand="substrate" FT BINDING 245..249 FT /ligand="substrate" FT BINDING 265 FT /ligand="substrate" FT BINDING 275 FT /ligand="substrate" FT BINDING 281 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="3" FT SITE 33 FT /note="Important for the conversion from active R-state to FT inactive T-state in the presence of AMP" FT MOD_RES 216 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q9Z1N1" FT MOD_RES 219 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q9Z1N1" FT VARIANT 86 FT /note="V -> L (in dbSNP:rs573212)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:9678974" FT /id="VAR_024448" FT VARIANT 115 FT /note="V -> M (in CORLK; decreased activity; decreased FT sensitivity to allosteric inhibition by AMP; decreased FT thermal stability)" FT /evidence="ECO:0000269|PubMed:33977262" FT /id="VAR_087242" FT MUTAGEN 1..10 FT /note="Missing: Greatly reduces sensitivity to inhibition FT by AMP and Ca(2+) and activation by Mg(2+). Decreases FT binding to ALDOA." FT /evidence="ECO:0000269|PubMed:18214967" FT MUTAGEN 1..7 FT /note="Missing: Greatly reduces sensitivity to inhibition FT by AMP and Ca(2+) and activation by Mg(2+). Decreases FT binding to ALDOA." FT MUTAGEN 1..6 FT /note="Missing: Reduces sensitivity to inhibition by AMP FT and Ca(2+) and activation by Mg(2+). Decreases binding to FT ALDOA." FT MUTAGEN 1..5 FT /note="Missing: Reduces sensitivity to inhibition by AMP FT and Ca(2+) and activation by Mg(2+). Decreases binding to FT ALDOA." FT MUTAGEN 1..4 FT /note="Missing: Slightly reduces sensitivity to inhibition FT by AMP and Ca(2+) and activation by Mg(2+). Decreases FT binding to ALDOA." FT MUTAGEN 1..3 FT /note="Missing: No effect on kinetic properties but FT decreases binding to ALDOA." FT MUTAGEN 1..2 FT /note="Missing: No effect on kinetic properties and FT interaction with ALDOA." FT MUTAGEN 1 FT /note="Missing: No effect on kinetic properties and FT interaction with ALDOA." FT MUTAGEN 21 FT /note="K->E: Reduces sensitivity to AMP; when associated FT with M-178 and C-180." FT /evidence="ECO:0000269|PubMed:16213487" FT MUTAGEN 33 FT /note="Q->R: Causes conformational change of N-terminal FT residues and decreased sensitivity towards AMP with lack of FT conversion to the inactive T-state in the presence of AMP." FT MUTAGEN 70 FT /note="E->Q: Greatly reduces affinity towards Ca(2+) and FT slightly reduces affinity towards Mg(2+)." FT /evidence="ECO:0000269|PubMed:17350621" FT MUTAGEN 178 FT /note="T->M: Reduces sensitivity to AMP; when associated FT with E-21 and C-180." FT /evidence="ECO:0000269|PubMed:16213487" FT MUTAGEN 180 FT /note="Q->C: Reduces sensitivity to AMP; when associated FT with E-21 and M-178." FT /evidence="ECO:0000269|PubMed:16213487" FT MUTAGEN 204..208 FT /note="KKKGK->AAAGA,EEEGE: Almost completely abolishes FT nuclear localization." FT /evidence="ECO:0000269|PubMed:19626708" FT MUTAGEN 204 FT /note="K->E: Minor reduction in nuclear localization." FT MUTAGEN 205 FT /note="K->E: Minor reduction in nuclear localization." FT MUTAGEN 206 FT /note="K->E: Greatly reduces nuclear lozalization." FT MUTAGEN 208 FT /note="K->E: Significantly reduces nuclear localization." FT HELIX 14..24 FT /evidence="ECO:0007829|PDB:4HE2" FT HELIX 30..50 FT /evidence="ECO:0007829|PDB:4HE2" FT TURN 51..54 FT /evidence="ECO:0007829|PDB:4HE2" FT TURN 58..61 FT /evidence="ECO:0007829|PDB:5ET6" FT STRAND 70..72 FT /evidence="ECO:0007829|PDB:4HE0" FT HELIX 74..87 FT /evidence="ECO:0007829|PDB:4HE2" FT TURN 88..90 FT /evidence="ECO:0007829|PDB:4HE2" FT STRAND 92..97 FT /evidence="ECO:0007829|PDB:4HE2" FT HELIX 108..110 FT /evidence="ECO:0007829|PDB:4HE2" FT STRAND 111..122 FT /evidence="ECO:0007829|PDB:4HE2" FT HELIX 124..126 FT /evidence="ECO:0007829|PDB:4HE2" FT TURN 127..130 FT /evidence="ECO:0007829|PDB:4HE2" FT STRAND 133..141 FT /evidence="ECO:0007829|PDB:4HE2" FT STRAND 145..147 FT /evidence="ECO:0007829|PDB:5Q0C" FT HELIX 150..153 FT /evidence="ECO:0007829|PDB:4HE2" FT HELIX 157..159 FT /evidence="ECO:0007829|PDB:4HE2" FT STRAND 161..180 FT /evidence="ECO:0007829|PDB:4HE2" FT STRAND 182..188 FT /evidence="ECO:0007829|PDB:4HE2" FT TURN 189..192 FT /evidence="ECO:0007829|PDB:4HE2" FT STRAND 193..201 FT /evidence="ECO:0007829|PDB:4HE2" FT STRAND 208..211 FT /evidence="ECO:0007829|PDB:4HE2" FT HELIX 214..219 FT /evidence="ECO:0007829|PDB:4HE2" FT HELIX 222..232 FT /evidence="ECO:0007829|PDB:4HE2" FT STRAND 235..237 FT /evidence="ECO:0007829|PDB:4HE2" FT HELIX 249..259 FT /evidence="ECO:0007829|PDB:4HE2" FT STRAND 262..265 FT /evidence="ECO:0007829|PDB:4HE2" FT STRAND 268..270 FT /evidence="ECO:0007829|PDB:5ET5" FT STRAND 275..277 FT /evidence="ECO:0007829|PDB:4HE2" FT TURN 278..281 FT /evidence="ECO:0007829|PDB:4HE2" FT HELIX 282..291 FT /evidence="ECO:0007829|PDB:4HE2" FT STRAND 295..297 FT /evidence="ECO:0007829|PDB:4HE2" FT STRAND 299..302 FT /evidence="ECO:0007829|PDB:4HE2" FT HELIX 303..305 FT /evidence="ECO:0007829|PDB:4HE2" FT STRAND 317..321 FT /evidence="ECO:0007829|PDB:4HE2" FT HELIX 322..335 FT /evidence="ECO:0007829|PDB:4HE2" SQ SEQUENCE 339 AA; 36743 MW; 196B06D744710BC4 CRC64; MTDRSPFETD MLTLTRYVME KGRQAKGTGE LTQLLNSMLT AIKAISSAVR KAGLAHLYGI AGSVNVTGDE VKKLDVLSNS LVINMVQSSY STCVLVSEEN KDAIITAKEK RGKYVVCFDP LDGSSNIDCL ASIGTIFAIY RKTSEDEPSE KDALQCGRNI VAAGYALYGS ATLVALSTGQ GVDLFMLDPA LGEFVLVEKD VKIKKKGKIY SLNEGYAKYF DAATTEYVQK KKFPEDGSAP YGARYVGSMV ADVHRTLVYG GIFLYPANQK SPKGKLRLLY ECNPVAYIIE QAGGLATTGT QPVLDVKPEA IHQRVPLILG SPEDVQEYLT CVQKNQAGS // ID ALDOC_HUMAN Reviewed; 364 AA. AC P09972; B2R5R3; Q3SYL3; Q6FH94; Q6P0L5; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 14-DEC-2022, entry version 214. DE RecName: Full=Fructose-bisphosphate aldolase C; DE EC=4.1.2.13; DE AltName: Full=Brain-type aldolase; GN Name=ALDOC; Synonyms=ALDC; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3105602; DOI=10.1016/0300-9084(87)90246-x; RA Rottmann W.H., Deselms K.R., Niclas J., Camerato T., Holman P.S., RA Green C.J., Tolan D.R.; RT "The complete amino acid sequence of the human aldolase C isozyme derived RT from genomic clones."; RL Biochimie 69:137-145(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3267224; DOI=10.1093/nar/16.10.4733; RA Buono P., Paolella G., Mancini F.P., Izzo P., Salvatore F.; RT "The complete nucleotide sequence of the gene coding for the human aldolase RT C."; RL Nucleic Acids Res. 16:4733-4733(1988). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2209624; DOI=10.1111/j.1432-1033.1990.tb19294.x; RA Buono P., Mancini F.P., Izzo P., Salvatore F.; RT "Characterization of the transcription-initiation site and of the promoter RT region within the 5' flanking region of the human aldolase C gene."; RL Eur. J. Biochem. 192:805-811(1990). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RA Yu W., Gibbs R.A.; RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Cerebellum; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Colon, Eye, and Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [10] RP INTERACTION WITH ATP6V1E1. RX PubMed=11399750; DOI=10.1074/jbc.m008768200; RA Lu M., Holliday L.S., Zhang L., Dunn W.A. Jr., Gluck S.L.; RT "Interaction between aldolase and vacuolar H+-ATPase: evidence for direct RT coupling of glycolysis to the ATP-hydrolyzing proton pump."; RL J. Biol. Chem. 276:30407-30413(2001). RN [11] RP INTERACTION WITH PLD2. RX PubMed=11876650; DOI=10.1021/bi015700a; RA Kim J.H., Lee S., Kim J.H., Lee T.G., Hirata M., Suh P.-G., Ryu S.H.; RT "Phospholipase D2 directly interacts with aldolase via its PH domain."; RL Biochemistry 41:3414-3421(2002). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-111, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-39 AND SER-45, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [17] RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 1-364, CATALYTIC ACTIVITY, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=15537755; DOI=10.1110/ps.04915904; RA Arakaki T.L., Pezza J.A., Cronin M.A., Hopkins C.E., Zimmer D.B., RA Tolan D.R., Allen K.N.; RT "Structure of human brain fructose 1,6-(bis)phosphate aldolase: linking RT isozyme structure with function."; RL Protein Sci. 13:3077-3084(2004). CC -!- CATALYTIC ACTIVITY: CC Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3- CC phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729, CC ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13; CC Evidence={ECO:0000269|PubMed:15537755}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=10.7 uM for fructose 1,6-bisphosphate CC {ECO:0000269|PubMed:15537755}; CC KM=16 mM for fructose 1-phosphate {ECO:0000269|PubMed:15537755}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 4/4. CC -!- SUBUNIT: Homotetramer. Interacts with ATP6V1E1. May interact with PLD2. CC {ECO:0000269|PubMed:11399750, ECO:0000269|PubMed:11876650}. CC -!- INTERACTION: CC P09972; P04075: ALDOA; NbExp=3; IntAct=EBI-2952751, EBI-709613; CC P09972; P04075-2: ALDOA; NbExp=6; IntAct=EBI-2952751, EBI-10194102; CC P09972; Q49AR9: ANKS1A; NbExp=3; IntAct=EBI-2952751, EBI-11954519; CC P09972; Q8TBB1: LNX1; NbExp=6; IntAct=EBI-2952751, EBI-739832; CC -!- MISCELLANEOUS: In vertebrates, three forms of this ubiquitous CC glycolytic enzyme are found, aldolase A in muscle, aldolase B in liver CC and aldolase C in brain. CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase CC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAI03761.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X05196; CAA28825.1; -; Genomic_DNA. DR EMBL; X07292; CAA30270.1; -; Genomic_DNA. DR EMBL; AF054987; AAC09348.1; -; mRNA. DR EMBL; BT007006; AAP35652.1; -; mRNA. DR EMBL; CR541862; CAG46660.1; -; mRNA. DR EMBL; CR541881; CAG46679.1; -; mRNA. DR EMBL; AK312281; BAG35210.1; -; mRNA. DR EMBL; CH471159; EAW51104.1; -; Genomic_DNA. DR EMBL; BC003613; AAH03613.3; -; mRNA. DR EMBL; BC103760; AAI03761.1; ALT_INIT; mRNA. DR EMBL; BC065565; AAH65565.2; -; mRNA. DR EMBL; BC106925; AAI06926.1; -; mRNA. DR EMBL; BC106926; AAI06927.1; -; mRNA. DR CCDS; CCDS11236.1; -. DR PIR; A25861; ADHUC. DR RefSeq; NP_005156.1; NM_005165.2. DR RefSeq; XP_005258006.1; XM_005257949.2. DR RefSeq; XP_011522858.1; XM_011524556.1. DR PDB; 1XFB; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L=1-364. DR PDBsum; 1XFB; -. DR AlphaFoldDB; P09972; -. DR SMR; P09972; -. DR BioGRID; 106731; 95. DR IntAct; P09972; 19. DR MINT; P09972; -. DR STRING; 9606.ENSP00000226253; -. DR ChEMBL; CHEMBL4295709; -. DR GlyGen; P09972; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P09972; -. DR PhosphoSitePlus; P09972; -. DR SwissPalm; P09972; -. DR BioMuta; ALDOC; -. DR DMDM; 113613; -. DR UCD-2DPAGE; P09972; -. DR CPTAC; CPTAC-1372; -. DR CPTAC; CPTAC-1373; -. DR CPTAC; CPTAC-1374; -. DR CPTAC; CPTAC-1375; -. DR CPTAC; CPTAC-1376; -. DR EPD; P09972; -. DR jPOST; P09972; -. DR MassIVE; P09972; -. DR MaxQB; P09972; -. DR PaxDb; P09972; -. DR PeptideAtlas; P09972; -. DR PRIDE; P09972; -. DR ProteomicsDB; 52287; -. DR Antibodypedia; 1111; 459 antibodies from 33 providers. DR DNASU; 230; -. DR Ensembl; ENST00000226253.9; ENSP00000226253.4; ENSG00000109107.14. DR Ensembl; ENST00000395321.6; ENSP00000378731.2; ENSG00000109107.14. DR GeneID; 230; -. DR KEGG; hsa:230; -. DR MANE-Select; ENST00000226253.9; ENSP00000226253.4; NM_005165.3; NP_005156.1. DR UCSC; uc002hbp.4; human. DR CTD; 230; -. DR DisGeNET; 230; -. DR GeneCards; ALDOC; -. DR HGNC; HGNC:418; ALDOC. DR HPA; ENSG00000109107; Tissue enhanced (brain, choroid plexus, retina). DR MIM; 103870; gene. DR neXtProt; NX_P09972; -. DR OpenTargets; ENSG00000109107; -. DR PharmGKB; PA24711; -. DR VEuPathDB; HostDB:ENSG00000109107; -. DR eggNOG; KOG1557; Eukaryota. DR GeneTree; ENSGT00950000182987; -. DR HOGENOM; CLU_031243_0_0_1; -. DR InParanoid; P09972; -. DR OMA; WRELLYS; -. DR OrthoDB; 799973at2759; -. DR PhylomeDB; P09972; -. DR TreeFam; TF314203; -. DR BioCyc; MetaCyc:HS03200-MON; -. DR PathwayCommons; P09972; -. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-70171; Glycolysis. DR Reactome; R-HSA-70263; Gluconeogenesis. DR SABIO-RK; P09972; -. DR SignaLink; P09972; -. DR SIGNOR; P09972; -. DR UniPathway; UPA00109; UER00183. DR BioGRID-ORCS; 230; 34 hits in 1078 CRISPR screens. DR ChiTaRS; ALDOC; human. DR EvolutionaryTrace; P09972; -. DR GeneWiki; Aldolase_C; -. DR GenomeRNAi; 230; -. DR Pharos; P09972; Tbio. DR PRO; PR:P09972; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; P09972; protein. DR Bgee; ENSG00000109107; Expressed in right hemisphere of cerebellum and 187 other tissues. DR ExpressionAtlas; P09972; baseline and differential. DR Genevisible; P09972; HS. DR GO; GO:0005856; C:cytoskeleton; IC:BHF-UCL. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome. DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome. DR GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome. DR GO; GO:0008092; F:cytoskeletal protein binding; IDA:BHF-UCL. DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IDA:UniProtKB. DR GO; GO:0030855; P:epithelial cell differentiation; IEP:UniProtKB. DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IDA:UniProtKB. DR GO; GO:0006000; P:fructose metabolic process; TAS:ProtInc. DR GO; GO:0006094; P:gluconeogenesis; IEA:Ensembl. DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR029768; Aldolase_I_AS. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000741; FBA_I. DR PANTHER; PTHR11627; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1. DR Pfam; PF00274; Glycolytic; 1. DR PROSITE; PS00158; ALDOLASE_CLASS_I; 1. DR AGR; HGNC:418; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Glycolysis; Lyase; Phosphoprotein; KW Reference proteome; Schiff base. FT CHAIN 1..364 FT /note="Fructose-bisphosphate aldolase C" FT /id="PRO_0000216947" FT ACT_SITE 188 FT /note="Proton acceptor" FT /evidence="ECO:0000250" FT ACT_SITE 230 FT /note="Schiff-base intermediate with dihydroxyacetone-P" FT BINDING 56 FT /ligand="substrate" FT BINDING 147 FT /ligand="substrate" FT SITE 364 FT /note="Necessary for preference for fructose 1,6- FT bisphosphate over fructose 1-phosphate" FT MOD_RES 5 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:P05065" FT MOD_RES 36 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 39 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 45 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 111 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19413330" FT MOD_RES 132 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P05065" FT CONFLICT 311 FT /note="L -> V (in Ref. 2; CAA30270)" FT /evidence="ECO:0000305" FT HELIX 10..23 FT /evidence="ECO:0007829|PDB:1XFB" FT STRAND 29..33 FT /evidence="ECO:0007829|PDB:1XFB" FT HELIX 37..45 FT /evidence="ECO:0007829|PDB:1XFB" FT HELIX 53..64 FT /evidence="ECO:0007829|PDB:1XFB" FT HELIX 68..70 FT /evidence="ECO:0007829|PDB:1XFB" FT TURN 71..73 FT /evidence="ECO:0007829|PDB:1XFB" FT STRAND 74..79 FT /evidence="ECO:0007829|PDB:1XFB" FT HELIX 82..85 FT /evidence="ECO:0007829|PDB:1XFB" FT HELIX 94..100 FT /evidence="ECO:0007829|PDB:1XFB" FT STRAND 104..108 FT /evidence="ECO:0007829|PDB:1XFB" FT STRAND 113..115 FT /evidence="ECO:0007829|PDB:1XFB" FT STRAND 119..121 FT /evidence="ECO:0007829|PDB:1XFB" FT STRAND 123..125 FT /evidence="ECO:0007829|PDB:1XFB" FT HELIX 131..140 FT /evidence="ECO:0007829|PDB:1XFB" FT STRAND 145..152 FT /evidence="ECO:0007829|PDB:1XFB" FT HELIX 161..179 FT /evidence="ECO:0007829|PDB:1XFB" FT TURN 180..182 FT /evidence="ECO:0007829|PDB:1XFB" FT STRAND 184..191 FT /evidence="ECO:0007829|PDB:1XFB" FT HELIX 199..219 FT /evidence="ECO:0007829|PDB:1XFB" FT HELIX 224..226 FT /evidence="ECO:0007829|PDB:1XFB" FT HELIX 246..257 FT /evidence="ECO:0007829|PDB:1XFB" FT TURN 258..260 FT /evidence="ECO:0007829|PDB:1XFB" FT STRAND 267..271 FT /evidence="ECO:0007829|PDB:1XFB" FT HELIX 277..288 FT /evidence="ECO:0007829|PDB:1XFB" FT STRAND 295..303 FT /evidence="ECO:0007829|PDB:1XFB" FT HELIX 304..314 FT /evidence="ECO:0007829|PDB:1XFB" FT HELIX 321..338 FT /evidence="ECO:0007829|PDB:1XFB" FT TURN 339..341 FT /evidence="ECO:0007829|PDB:1XFB" SQ SEQUENCE 364 AA; 39456 MW; 506A570B3E507971 CRC64; MPHSYPALSA EQKKELSDIA LRIVAPGKGI LAADESVGSM AKRLSQIGVE NTEENRRLYR QVLFSADDRV KKCIGGVIFF HETLYQKDDN GVPFVRTIQD KGIVVGIKVD KGVVPLAGTD GETTTQGLDG LSERCAQYKK DGADFAKWRC VLKISERTPS ALAILENANV LARYASICQQ NGIVPIVEPE ILPDGDHDLK RCQYVTEKVL AAVYKALSDH HVYLEGTLLK PNMVTPGHAC PIKYTPEEIA MATVTALRRT VPPAVPGVTF LSGGQSEEEA SFNLNAINRC PLPRPWALTF SYGRALQASA LNAWRGQRDN AGAATEEFIK RAEVNGLAAQ GKYEGSGEDG GAAAQSLYIA NHAY // ID IFNA4_HUMAN Reviewed; 189 AA. AC P05014; P13358; Q14CS4; Q5VV15; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2005, sequence version 2. DT 14-DEC-2022, entry version 195. DE RecName: Full=Interferon alpha-4; DE Short=IFN-alpha-4; DE AltName: Full=Interferon alpha-4B; DE AltName: Full=Interferon alpha-76; DE AltName: Full=Interferon alpha-M1; DE Flags: Precursor; GN Name=IFNA4; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=6089830; RA Linnane A.W., Beilharz M.W., McMullen G.L., Macreadie I.G., Murphy M., RA Nisbet I.T., Novitski C.E., Woodrow G.C.; RT "Nucleotide sequence and expression in E. coli of a human interferon-alpha RT gene selected from a genomic library using synthetic oligonucleotides."; RL Biochem. Int. 8:725-732(1984). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALPHA-4B THR-74 AND RP VAL-137. RX PubMed=4057246; DOI=10.1016/0022-2836(85)90401-2; RA Henco K., Brosius J., Fujisawa A., Fujisawa J., Haynes J.R., Hochstadt J., RA Kovacic T., Pasek M., Schamboeck A., Schmid J., Todokoro K., Waelchli M., RA Nagata S., Weissmann C.; RT "Structural relationship of human interferon alpha genes and pseudogenes."; RL J. Mol. Biol. 185:227-260(1985). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT THR-74. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-74. RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP PROTEIN SEQUENCE OF 24-56. RX PubMed=9425112; DOI=10.1042/bj3290295; RA Nyman T.A., Toeloe H., Parkkinen J., Kalkkinen N.; RT "Identification of nine interferon-alpha subtypes produced by Sendai virus- RT induced human peripheral blood leucocytes."; RL Biochem. J. 329:295-302(1998). RN [7] RP POLYMORPHISM. RX PubMed=9335434; DOI=10.1089/jir.1997.17.559; RA Hussain M., Gill D.S., Liao M.-J.; RT "Both variant forms of interferon-alpha4 gene (IFNA4a and IFNA4b) are RT present in the human population."; RL J. Interferon Cytokine Res. 17:559-566(1997). CC -!- FUNCTION: Produced by macrophages, IFN-alpha have antiviral activities. CC Interferon stimulates the production of two enzymes: a protein kinase CC and an oligoadenylate synthetase. CC -!- INTERACTION: CC P05014; P04075-2: ALDOA; NbExp=3; IntAct=EBI-10194381, EBI-10194102; CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- POLYMORPHISM: Two forms exist; alpha-4a (shown here) and alpha-4b CC (PubMed:9335434). They seem to be equally abundant (PubMed:9335434). CC {ECO:0000269|PubMed:9335434}. CC -!- SIMILARITY: Belongs to the alpha/beta interferon family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M27318; AAA52726.1; -; mRNA. DR EMBL; X02955; CAA26701.1; -; Genomic_DNA. DR EMBL; AL512606; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471071; EAW58621.1; -; Genomic_DNA. DR EMBL; BC074965; AAH74965.1; -; mRNA. DR EMBL; BC074966; AAH74966.1; -; mRNA. DR EMBL; BC113640; AAI13641.1; -; mRNA. DR EMBL; BC113642; AAI13643.1; -; mRNA. DR CCDS; CCDS6498.1; -. DR PIR; E23753; IVHU4B. DR PIR; I52347; I52347. DR RefSeq; NP_066546.1; NM_021068.2. DR AlphaFoldDB; P05014; -. DR SMR; P05014; -. DR BioGRID; 109664; 43. DR ComplexPortal; CPX-5998; Interferon alpha receptor-ligand complex, IFNA4 variant. DR IntAct; P05014; 11. DR STRING; 9606.ENSP00000412897; -. DR ChEMBL; CHEMBL3856161; -. DR iPTMnet; P05014; -. DR PhosphoSitePlus; P05014; -. DR BioMuta; IFNA4; -. DR DMDM; 84029375; -. DR jPOST; P05014; -. DR MassIVE; P05014; -. DR PaxDb; P05014; -. DR PeptideAtlas; P05014; -. DR ABCD; P05014; 2 sequenced antibodies. DR Antibodypedia; 24852; 186 antibodies from 21 providers. DR DNASU; 3441; -. DR Ensembl; ENST00000421715.3; ENSP00000412897.1; ENSG00000236637.5. DR GeneID; 3441; -. DR KEGG; hsa:3441; -. DR MANE-Select; ENST00000421715.3; ENSP00000412897.1; NM_021068.4; NP_066546.1. DR UCSC; uc003zon.3; human. DR CTD; 3441; -. DR DisGeNET; 3441; -. DR GeneCards; IFNA4; -. DR HGNC; HGNC:5425; IFNA4. DR HPA; ENSG00000236637; Not detected. DR MIM; 147564; gene. DR neXtProt; NX_P05014; -. DR OpenTargets; ENSG00000236637; -. DR PharmGKB; PA29664; -. DR VEuPathDB; HostDB:ENSG00000236637; -. DR eggNOG; ENOG502SQAC; Eukaryota. DR GeneTree; ENSGT01000000214430; -. DR HOGENOM; CLU_109427_0_0_1; -. DR InParanoid; P05014; -. DR OMA; MARSCAF; -. DR OrthoDB; 1358010at2759; -. DR PhylomeDB; P05014; -. DR TreeFam; TF336177; -. DR PathwayCommons; P05014; -. DR Reactome; R-HSA-909733; Interferon alpha/beta signaling. DR Reactome; R-HSA-912694; Regulation of IFNA/IFNB signaling. DR Reactome; R-HSA-933541; TRAF6 mediated IRF7 activation. DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses. DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production. DR SignaLink; P05014; -. DR BioGRID-ORCS; 3441; 56 hits in 980 CRISPR screens. DR GeneWiki; IFNA4; -. DR GenomeRNAi; 3441; -. DR Pharos; P05014; Tbio. DR PRO; PR:P05014; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; P05014; protein. DR Bgee; ENSG00000236637; Expressed in aorta and 2 other tissues. DR Genevisible; P05014; HS. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central. DR GO; GO:0005132; F:type I interferon receptor binding; IBA:GO_Central. DR GO; GO:0002250; P:adaptive immune response; IBA:GO_Central. DR GO; GO:0030183; P:B cell differentiation; IBA:GO_Central. DR GO; GO:0042100; P:B cell proliferation; IBA:GO_Central. DR GO; GO:0098586; P:cellular response to virus; NAS:ComplexPortal. DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central. DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW. DR GO; GO:0006959; P:humoral immune response; IBA:GO_Central. DR GO; GO:0002323; P:natural killer cell activation involved in immune response; IBA:GO_Central. DR GO; GO:0033141; P:positive regulation of peptidyl-serine phosphorylation of STAT protein; IBA:GO_Central. DR GO; GO:0043330; P:response to exogenous dsRNA; IBA:GO_Central. DR GO; GO:0009615; P:response to virus; TAS:ProtInc. DR GO; GO:0002286; P:T cell activation involved in immune response; IBA:GO_Central. DR GO; GO:0060337; P:type I interferon-mediated signaling pathway; NAS:ComplexPortal. DR CDD; cd00095; IFab; 1. DR Gene3D; 1.20.1250.10; -; 1. DR InterPro; IPR009079; 4_helix_cytokine-like_core. DR InterPro; IPR000471; Interferon_alpha/beta/delta. DR PANTHER; PTHR11691; TYPE I INTERFERON; 1. DR Pfam; PF00143; Interferon; 1. DR PRINTS; PR00266; INTERFERONAB. DR SMART; SM00076; IFabd; 1. DR SUPFAM; SSF47266; 4-helical cytokines; 1. DR PROSITE; PS00252; INTERFERON_A_B_D; 1. DR AGR; HGNC:5425; -. PE 1: Evidence at protein level; KW Antiviral defense; Cytokine; Direct protein sequencing; Disulfide bond; KW Reference proteome; Secreted; Signal. FT SIGNAL 1..23 FT /evidence="ECO:0000269|PubMed:9425112" FT CHAIN 24..189 FT /note="Interferon alpha-4" FT /id="PRO_0000016361" FT DISULFID 24..122 FT /evidence="ECO:0000250" FT DISULFID 52..162 FT /evidence="ECO:0000250" FT VARIANT 49 FT /note="H -> P (in dbSNP:rs201964250)" FT /id="VAR_034010" FT VARIANT 74 FT /note="A -> T (in alpha-4B; dbSNP:rs1062571)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:4057246, ECO:0000269|Ref.4" FT /id="VAR_013002" FT VARIANT 137 FT /note="E -> V (in alpha-4B; dbSNP:rs3750480)" FT /evidence="ECO:0000269|PubMed:4057246" FT /id="VAR_013003" SQ SEQUENCE 189 AA; 21808 MW; 828DF9C33ABC337F CRC64; MALSFSLLMA VLVLSYKSIC SLGCDLPQTH SLGNRRALIL LAQMGRISHF SCLKDRHDFG FPEEEFDGHQ FQKAQAISVL HEMIQQTFNL FSTEDSSAAW EQSLLEKFST ELYQQLNDLE ACVIQEVGVE ETPLMNEDSI LAVRKYFQRI TLYLTEKKYS PCAWEVVRAE IMRSLSFSTN LQKRLRRKD // ID WASP_HUMAN Reviewed; 502 AA. AC P42768; Q9BU11; Q9UNJ9; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 14-DEC-2022, entry version 244. DE RecName: Full=Actin nucleation-promoting factor WAS {ECO:0000305}; DE AltName: Full=Wiskott-Aldrich syndrome protein; DE Short=WASp; GN Name=WAS; Synonyms=IMD2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY. RC TISSUE=T-cell; RX PubMed=8069912; DOI=10.1016/0092-8674(94)90528-2; RA Derry J.M.J., Ochs H.D., Francke U.; RT "Isolation of a novel gene mutated in Wiskott-Aldrich syndrome."; RL Cell 78:635-644(1994). RN [2] RP ERRATUM OF PUBMED:8069912. RX PubMed=8001129; RA Derry J.M.J., Ochs H.D., Francke U.; RL Cell 79:923-923(1994). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS WAS TRP-43; MET-45; LEU-58; RP LYS-133 AND THR-134. RX PubMed=7753869; DOI=10.1073/pnas.92.10.4706; RA Kwan S.-P., Hagemann T.L., Radtke B.E., Blaese R.M., Rosen F.S.; RT "Identification of mutations in the Wiskott-Aldrich syndrome gene and RT characterization of a polymorphic dinucleotide repeat at DXS6940, adjacent RT to the disease gene."; RL Proc. Natl. Acad. Sci. U.S.A. 92:4706-4710(1995). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=10066431; DOI=10.1006/bbrc.1999.0292; RA Hagemann T.L., Kwan S.-P.; RT "The identification and characterization of two promoters and the complete RT genomic sequence for the Wiskott-Aldrich syndrome gene."; RL Biochem. Biophys. Res. Commun. 256:104-109(1999). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lymph; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP PROTEIN SEQUENCE OF 2-13. RC TISSUE=Platelet; RX PubMed=12665801; DOI=10.1038/nbt810; RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., RA Vandekerckhove J.; RT "Exploring proteomes and analyzing protein processing by mass spectrometric RT identification of sorted N-terminal peptides."; RL Nat. Biotechnol. 21:566-569(2003). RN [8] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=8625410; DOI=10.1016/s0092-8674(00)81050-8; RA Symons M., Derry J.M., Karlak B., Jiang S., Lemahieu V., Mccormick F., RA Francke U., Abo A.; RT "Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, RT is implicated in actin polymerization."; RL Cell 84:723-734(1996). RN [9] RP INTERACTION WITH CDC42. RX PubMed=8643625; DOI=10.1073/pnas.93.11.5615; RA Kolluri R., Tolias K.F., Carpenter C.L., Rosen F.S., Kirchhausen T.; RT "Direct interaction of the Wiskott-Aldrich syndrome protein with the GTPase RT Cdc42."; RL Proc. Natl. Acad. Sci. U.S.A. 93:5615-5618(1996). RN [10] RP FUNCTION, AND INTERACTION WITH WIP. RX PubMed=9405671; DOI=10.1073/pnas.94.26.14671; RA Ramesh N., Anton I.M., Hartwig J.H., Geha R.S.; RT "WIP, a protein associated with Wiskott-Aldrich syndrome protein, induces RT actin polymerization and redistribution in lymphoid cells."; RL Proc. Natl. Acad. Sci. U.S.A. 94:14671-14676(1997). RN [11] RP FUNCTION, PHOSPHORYLATION AT TYR-291 BY HCK, IDENTIFICATION BY MASS RP SPECTROMETRY, AND INTERACTION WITH HCK. RX PubMed=12235133; DOI=10.1074/jbc.m203346200; RA Cory G.O., Garg R., Cramer R., Ridley A.J.; RT "Phosphorylation of tyrosine 291 enhances the ability of WASp to stimulate RT actin polymerization and filopodium formation. Wiskott-Aldrich Syndrome RT protein."; RL J. Biol. Chem. 277:45115-45121(2002). RN [12] RP FUNCTION, PHOSPHORYLATION AT SER-483 AND SER-484, AND INTERACTION WITH THE RP ARP2/3 COMPLEX. RX PubMed=12769847; DOI=10.1016/s1097-2765(03)00172-2; RA Cory G.O.C., Cramer R., Blanchoin L., Ridley A.J.; RT "Phosphorylation of the WASP-VCA domain increases its affinity for the RT Arp2/3 complex and enhances actin polymerization by WASP."; RL Mol. Cell 11:1229-1239(2003). RN [13] RP PHOSPHORYLATION AT TYR-291 BY FYN. RX PubMed=14707117; DOI=10.1084/jem.20030976; RA Badour K., Zhang J., Shi F., Leng Y., Collins M., Siminovitch K.A.; RT "Fyn and PTP-PEST-mediated regulation of Wiskott-Aldrich syndrome protein RT (WASp) tyrosine phosphorylation is required for coupling T cell antigen RT receptor engagement to WASp effector function and T cell activation."; RL J. Exp. Med. 199:99-112(2004). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-291, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-291; SER-483 AND SER-484, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-291 AND SER-483, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [17] RP FUNCTION, SUBCELLULAR LOCATION, AND INVOLVEMENT IN WAS. RX PubMed=20574068; DOI=10.1126/scitranslmed.3000813; RA Taylor M.D., Sadhukhan S., Kottangada P., Ramgopal A., Sarkar K., RA D'Silva S., Selvakumar A., Candotti F., Vyas Y.M.; RT "Nuclear role of WASp in the pathogenesis of dysregulated TH1 immunity in RT human Wiskott-Aldrich syndrome."; RL Sci. Transl. Med. 2:37RA44-37RA44(2010). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-221, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [20] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [21] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [22] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=29925947; DOI=10.1038/s41586-018-0237-5; RA Schrank B.R., Aparicio T., Li Y., Chang W., Chait B.T., Gundersen G.G., RA Gottesman M.E., Gautier J.; RT "Nuclear ARP2/3 drives DNA break clustering for homology-directed repair."; RL Nature 559:61-66(2018). RN [23] RP STRUCTURE BY NMR OF 230-288 IN COMPLEX WITH CDC42. RX PubMed=10360578; DOI=10.1038/20726; RA Abdul-Manan N., Aghazadeh B., Liu G.A., Majumdar A., Ouerfelli O., RA Siminovitch K.A., Rosen M.K.; RT "Structure of Cdc42 in complex with the GTPase-binding domain of the RT 'Wiskott-Aldrich syndrome' protein."; RL Nature 399:379-383(1999). RN [24] RP STRUCTURE BY NMR OF 242-492, AND CONFORMATION CHANGE. RX PubMed=10724160; DOI=10.1038/35004513; RA Kim A.S., Kakalis L.T., Abdul-Manan N., Liu G.A., Rosen M.K.; RT "Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome RT protein."; RL Nature 404:151-158(2000). RN [25] RP STRUCTURE BY NMR OF 242-310 IN COMPLEX WITH WISKOSTATIN. RX PubMed=15235593; DOI=10.1038/nsmb796; RA Peterson J.R., Bickford L.C., Morgan D., Kim A.S., Ouerfelli O., RA Kirschner M.W., Rosen M.K.; RT "Chemical inhibition of N-WASP by stabilization of a native autoinhibited RT conformation."; RL Nat. Struct. Mol. Biol. 11:747-755(2004). RN [26] RP X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF 430-458 IN COMPLEX WITH ACTIN, RP FUNCTION, AND SUBUNIT. RX PubMed=16275905; DOI=10.1073/pnas.0507021102; RA Chereau D., Kerff F., Graceffa P., Grabarek Z., Langsetmo K., Dominguez R.; RT "Actin-bound structures of Wiskott-Aldrich syndrome protein (WASP)-homology RT domain 2 and the implications for filament assembly."; RL Proc. Natl. Acad. Sci. U.S.A. 102:16644-16649(2005). RN [27] RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 488-502 IN COMPLEX WITH ALDOA. RX PubMed=17329259; DOI=10.1074/jbc.m611505200; RA St-Jean M., Izard T., Sygusch J.; RT "A hydrophobic pocket in the active site of glycolytic aldolase mediates RT interactions with Wiskott-Aldrich syndrome protein."; RL J. Biol. Chem. 282:14309-14315(2007). RN [28] RP STRUCTURE BY NMR OF 242-310, FUNCTION, AND INTERACTION WITH E.COLI ESPF(U). RX PubMed=18650809; DOI=10.1038/nature07160; RA Cheng H.C., Skehan B.M., Campellone K.G., Leong J.M., Rosen M.K.; RT "Structural mechanism of WASP activation by the enterohaemorrhagic E. coli RT effector EspF(U)."; RL Nature 454:1009-1013(2008). RN [29] RP VARIANTS WAS HIS-30 DEL; LYS-31; MET-75; PRO-82; CYS-86; HIS-86; CYS-97; RP LYS-133 AND GLU-476. RX PubMed=8528198; DOI=10.1093/hmg/4.7.1119; RA Kolluri R., Shehabeldin A., Peacocke M., Lamhonwah A.-M., RA Teichert-Kuliszewska K., Weissman S.M., Siminovitch K.A.; RT "Identification of WASP mutations in patients with Wiskott-Aldrich syndrome RT and isolated thrombocytopenia reveals allelic heterogeneity at the WAS RT locus."; RL Hum. Mol. Genet. 4:1119-1126(1995). RN [30] RP VARIANTS THC1 PHE-27; ILE-48 AND LYS-477, AND VARIANTS WAS MET-75; LEU-86; RP HIS-86; LYS-131 AND CYS-187. RX PubMed=8528199; DOI=10.1093/hmg/4.7.1127; RA Derry J.M.J., Kerns J.A., Weinberg K.I., Ochs H.D., Volpini V., RA Estivill X., Walker A.P., Francke U.; RT "WASP gene mutations in Wiskott-Aldrich syndrome and X-linked RT thrombocytopenia."; RL Hum. Mol. Genet. 4:1127-1135(1995). RN [31] RP VARIANTS THC1 VAL-56 AND GLU-236. RX PubMed=7795648; DOI=10.1038/ng0495-414; RA Villa A., Notarangelo L., Macchi P., Mantuano E., Cavagni G., Brugnoni D., RA Strina D., Patrosso M.C., Ramenghi U., Sacco M.G., Ugazio A., Vezzoni P.; RT "X-linked thrombocytopenia and Wiskott-Aldrich syndrome are allelic RT diseases with mutations in the WASP gene."; RL Nat. Genet. 9:414-417(1995). RN [32] RP VARIANT WAS HIS-86. RX PubMed=8682510; DOI=10.1007/s004390050162; RA Schindelhauer D., Weiss M., Hellebrand H., Golla A., Hergersberg M., RA Seger R., Belohradsky B.H., Meindl A.; RT "Wiskott-Aldrich syndrome: no strict genotype-phenotype correlations but RT clustering of missense mutations in the amino-terminal part of the WASP RT gene product."; RL Hum. Genet. 98:68-76(1996). RN [33] RP VARIANTS WAS TRP-43; MET-45; MET-75 AND CYS-86. RX PubMed=9126958; RA Remold-O'Donnell E., Cooley J., Shcherbina A., Hagemann T.L., Kwan S.-P., RA Kenney D.M., Rosen F.S.; RT "Variable expression of WASP in B cell lines of Wiskott-Aldrich syndrome RT patients."; RL J. Immunol. 158:4021-4025(1997). RN [34] RP VARIANTS WAS LYS-31 AND MET-45. RX PubMed=9098856; DOI=10.1203/00006450-199704000-00013; RA Ariga T., Yamada M., Sakiyama Y.; RT "Mutation analysis of five Japanese families with Wiskott-Aldrich syndrome RT and determination of the family members' carrier status using three RT different methods."; RL Pediatr. Res. 41:535-540(1997). RN [35] RP VARIANTS WAS MET-75; LEU-84; ASP-89 AND LYS-133. RX PubMed=9683546; DOI=10.1006/clin.1998.4557; RA MacCarthy-Morrogh L., Gaspar H.B., Wang Y.-C., Katz F., Thompson L., RA Layton M., Jones A.M., Kinnon C.; RT "Absence of expression of the Wiskott-Aldrich syndrome protein in RT peripheral blood cells of Wiskott-Aldrich syndrome patients."; RL Clin. Immunol. Immunopathol. 88:22-27(1998). RN [36] RP VARIANT WAS VAL-56. RX PubMed=9713366; RX DOI=10.1002/(sici)1096-9896(199805)185:1<99::aid-path48>3.0.co;2-l; RA Facchetti F., Blanzuoli L., Vermi W., Notarangelo L.D., Giliani S., RA Fiorini M., Fasth A., Stewart D.M., Nelson D.L.; RT "Defective actin polymerization in EBV-transformed B-cell lines from RT patients with the Wiskott-Aldrich syndrome."; RL J. Pathol. 185:99-107(1998). RN [37] RP VARIANT WAS LYS-133. RX PubMed=9445409; DOI=10.1056/nejm199801293380504; RA Parolini O., Ressmann G., Haas O.A., Pawlowsky J., Gadner H., Knapp W., RA Holter W.; RT "X-linked Wiskott-Aldrich syndrome in a girl."; RL N. Engl. J. Med. 338:291-295(1998). RN [38] RP VARIANT THC1 MET-45. RX PubMed=11167787; DOI=10.1046/j.1365-2141.2001.02465.x; RA Ho L.L., Ayling J., Prosser I., Kronenberg H., Iland H., Joshua D.; RT "Missense C168T in the Wiskott-Aldrich Syndrome protein gene is a common RT mutation in X-linked thrombocytopenia."; RL Br. J. Haematol. 112:76-80(2001). RN [39] RP VARIANT XLN PRO-270, AND CHARACTERIZATION OF VARIANT XLN PRO-270. RX PubMed=11242115; DOI=10.1038/85886; RA Devriendt K., Kim A.S., Mathijs G., Frints S.G.M., Schwartz M., RA Van Den Oord J.J., Verhoef G.E.G., Boogaerts M.A., Fryns J.-P., You D., RA Rosen M.K., Vandenberghe P.; RT "Constitutively activating mutation in WASP causes X-linked severe RT congenital neutropenia."; RL Nat. Genet. 27:313-317(2001). RN [40] RP VARIANTS WAS ARG-73; CYS-86 AND LYS-133, AND VARIANTS THC1 MET-75 AND RP CYS-83. RX PubMed=10447259; RX DOI=10.1002/(sici)1098-1004(1999)14:1<54::aid-humu7>3.0.co;2-e; RA Lemahieu V., Gastier J.M., Francke U.; RT "Novel mutations in the Wiskott-Aldrich syndrome protein gene and their RT effects on transcriptional, translational, and clinical phenotypes."; RL Hum. Mutat. 14:54-66(1999). RN [41] RP VARIANTS THC1 ARG-58 AND ASN-481. RX PubMed=11877312; DOI=10.1182/blood.v99.6.2268; RA Notarangelo L.D., Mazza C., Giliani S., D'Aria C., Gandellini F., RA Ravelli C., Locatelli M.G., Nelson D.L., Ochs H.D., Notarangelo L.D.; RT "Missense mutations of the WASP gene cause intermittent X-linked RT thrombocytopenia."; RL Blood 99:2268-2269(2002). RN [42] RP VARIANTS WAS HIS-52 AND TRP-70. RX PubMed=11793485; DOI=10.1002/humu.9013; RA El-Hakeh J., Rosenzweig S., Oleastro M., Basack N., Berozdnik L., RA Molina F., Rivas E.M., Zelazko M., Danielian S.; RT "Wiskott-Aldrich syndrome in Argentina: 17 unique, including nine novel, RT mutations."; RL Hum. Mutat. 19:186-187(2002). RN [43] RP VARIANT THR-56. RX PubMed=24115682; DOI=10.1002/pbc.24787; RA Wada T., Itoh M., Maeba H., Toma T., Niida Y., Saikawa Y., Yachie A.; RT "Intermittent X-linked thrombocytopenia with a novel WAS gene mutation."; RL Pediatr. Blood Cancer 61:746-748(2014). RN [44] RP VARIANT LYS-131. RX PubMed=26566883; DOI=10.1136/jmedgenet-2015-103179; RA Rafiullah R., Aslamkhan M., Paramasivam N., Thiel C., Mustafa G., RA Wiemann S., Schlesner M., Wade R.C., Rappold G.A., Berkel S.; RT "Homozygous missense mutation in the LMAN2L gene segregates with RT intellectual disability in a large consanguineous Pakistani family."; RL J. Med. Genet. 53:138-144(2016). CC -!- FUNCTION: Effector protein for Rho-type GTPases that regulates actin CC filament reorganization via its interaction with the Arp2/3 complex CC (PubMed:12235133, PubMed:12769847, PubMed:16275905). Important for CC efficient actin polymerization (PubMed:8625410, PubMed:12235133, CC PubMed:16275905). Possible regulator of lymphocyte and platelet CC function (PubMed:9405671). Mediates actin filament reorganization and CC the formation of actin pedestals upon infection by pathogenic bacteria CC (PubMed:18650809). In addition to its role in the cytoplasmic CC cytoskeleton, also promotes actin polymerization in the nucleus, CC thereby regulating gene transcription and repair of damaged DNA CC (PubMed:20574068). Promotes homologous recombination (HR) repair in CC response to DNA damage by promoting nuclear actin polymerization, CC leading to drive motility of double-strand breaks (DSBs) CC (PubMed:29925947). {ECO:0000269|PubMed:12235133, CC ECO:0000269|PubMed:12769847, ECO:0000269|PubMed:16275905, CC ECO:0000269|PubMed:18650809, ECO:0000269|PubMed:20574068, CC ECO:0000269|PubMed:29925947, ECO:0000269|PubMed:8625410, CC ECO:0000269|PubMed:9405671}. CC -!- SUBUNIT: Binds the Arp2/3 complex (PubMed:12769847). Interacts with CC CDC42, RAC, NCK, HCK, FYN, SRC kinase FGR, BTK, ABL1, PSTPIP1, WIP, and CC to the p85 subunit of PLC-gamma (PubMed:8643625, PubMed:9405671, CC PubMed:12235133, PubMed:10360578, PubMed:15235593). Interacts (via C- CC terminus) with ALDOA (PubMed:17329259). Interacts with NCK1 (via SH3 CC domains) (By similarity). Interacts with FCHSD2 (By similarity). CC {ECO:0000250|UniProtKB:P70315, ECO:0000269|PubMed:10360578, CC ECO:0000269|PubMed:12235133, ECO:0000269|PubMed:12769847, CC ECO:0000269|PubMed:15235593, ECO:0000269|PubMed:17329259, CC ECO:0000269|PubMed:8643625, ECO:0000269|PubMed:9405671}. CC -!- SUBUNIT: (Microbial infection) Interacts with E.coli effector protein CC EspF(U). {ECO:0000269|PubMed:18650809}. CC -!- INTERACTION: CC P42768; Q9P2A4: ABI3; NbExp=4; IntAct=EBI-346375, EBI-742038; CC P42768; Q92624: APPBP2; NbExp=3; IntAct=EBI-346375, EBI-743771; CC P42768; Q06187: BTK; NbExp=4; IntAct=EBI-346375, EBI-624835; CC P42768; P60953: CDC42; NbExp=12; IntAct=EBI-346375, EBI-81752; CC P42768; Q14247: CTTN; NbExp=3; IntAct=EBI-346375, EBI-351886; CC P42768; P08631: HCK; NbExp=9; IntAct=EBI-346375, EBI-346340; CC P42768; O43639: NCK2; NbExp=3; IntAct=EBI-346375, EBI-713635; CC P42768; Q8WV41: SNX33; NbExp=3; IntAct=EBI-346375, EBI-2481535; CC P42768; Q9Y5X1: SNX9; NbExp=2; IntAct=EBI-346375, EBI-77848; CC P42768; O94875: SORBS2; NbExp=3; IntAct=EBI-346375, EBI-311323; CC P42768; P11387: TOP1; NbExp=3; IntAct=EBI-346375, EBI-876302; CC P42768; P57075-2: UBASH3A; NbExp=3; IntAct=EBI-346375, EBI-7353612; CC P42768; P42768: WAS; NbExp=4; IntAct=EBI-346375, EBI-346375; CC P42768; O43516: WIPF1; NbExp=25; IntAct=EBI-346375, EBI-346356; CC P42768; O43516-4: WIPF1; NbExp=3; IntAct=EBI-346375, EBI-12052927; CC P42768; P0DJ88: espF(U); Xeno; NbExp=3; IntAct=EBI-346375, EBI-10039462; CC P42768; P08103: Hck; Xeno; NbExp=3; IntAct=EBI-346375, EBI-6248894; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:8625410}. Nucleus {ECO:0000269|PubMed:20574068, CC ECO:0000269|PubMed:29925947}. CC -!- TISSUE SPECIFICITY: Expressed predominantly in the thymus. Also found, CC to a much lesser extent, in the spleen. {ECO:0000269|PubMed:8069912}. CC -!- DOMAIN: The WH1 (Wasp homology 1) domain may bind a Pro-rich ligand. CC -!- DOMAIN: The CRIB (Cdc42/Rac-interactive-binding) region binds to the C- CC terminal WH2 domain in the autoinhibited state of the protein. Binding CC of Rho-type GTPases to the CRIB induces a conformation change and leads CC to activation. CC -!- PTM: Phosphorylated at Tyr-291 by FYN and HCK, inducing WAS effector CC activity after TCR engagement. Phosphorylation at Tyr-291 enhances WAS CC activity in promoting actin polymerization and filopodia formation. CC {ECO:0000269|PubMed:12235133, ECO:0000269|PubMed:12769847, CC ECO:0000269|PubMed:14707117}. CC -!- DISEASE: Wiskott-Aldrich syndrome (WAS) [MIM:301000]: An X-linked CC recessive immunodeficiency characterized by eczema, thrombocytopenia, CC recurrent infections, and bloody diarrhea. Death usually occurs before CC age 10. {ECO:0000269|PubMed:10447259, ECO:0000269|PubMed:11793485, CC ECO:0000269|PubMed:20574068, ECO:0000269|PubMed:7753869, CC ECO:0000269|PubMed:8528198, ECO:0000269|PubMed:8528199, CC ECO:0000269|PubMed:8682510, ECO:0000269|PubMed:9098856, CC ECO:0000269|PubMed:9126958, ECO:0000269|PubMed:9445409, CC ECO:0000269|PubMed:9683546, ECO:0000269|PubMed:9713366}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Thrombocytopenia 1 (THC1) [MIM:313900]: A form of CC thrombocytopenia, a hematologic disorder defined by a decrease in the CC number of platelets in circulating blood, resulting in the potential CC for increased bleeding and decreased ability for clotting. CC {ECO:0000269|PubMed:10447259, ECO:0000269|PubMed:11167787, CC ECO:0000269|PubMed:11877312, ECO:0000269|PubMed:7795648, CC ECO:0000269|PubMed:8528199}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Neutropenia, severe congenital, X-linked (XLN) [MIM:300299]: A CC disorder of hematopoiesis characterized by maturation arrest of CC granulopoiesis at the level of promyelocytes with peripheral blood CC absolute neutrophil counts below 0.5 x 10(9)/l and early onset of CC severe bacterial infections. {ECO:0000269|PubMed:11242115}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SEQUENCE CAUTION: CC Sequence=AAH02961.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAH02961.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=WASbase; Note=WAS mutation db; CC URL="http://structure.bmc.lu.se/idbase/WASbase/"; CC -!- WEB RESOURCE: Name=WASPbase; Note=WAS mutation db; CC URL="http://pidj.rcai.riken.jp/waspbase/"; CC -!- WEB RESOURCE: Name=Wikipedia; Note=Wiskott-Aldrich syndrome protein CC entry; CC URL="https://en.wikipedia.org/wiki/Wiskott-Aldrich_syndrome_protein"; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/WASID42801chXp11.html"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U12707; AAA62663.1; -; mRNA. DR EMBL; U18935; AAA60381.1; -; Genomic_DNA. DR EMBL; U19927; AAC50140.1; -; mRNA. DR EMBL; AF115549; AAD26691.1; -; Genomic_DNA. DR EMBL; AF196970; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC002961; AAH02961.1; ALT_INIT; mRNA. DR EMBL; BC012738; AAH12738.1; -; mRNA. DR CCDS; CCDS14303.1; -. DR PIR; A54747; A55197. DR RefSeq; NP_000368.1; NM_000377.2. DR PDB; 1CEE; NMR; -; B=230-288. DR PDB; 1EJ5; NMR; -; A=242-310, A=461-492. DR PDB; 1T84; NMR; -; A=242-310, A=461-492. DR PDB; 2A3Z; X-ray; 2.08 A; C=430-458. DR PDB; 2K42; NMR; -; A=242-310. DR PDB; 2OT0; X-ray; 2.05 A; E/F/G/H=488-502. DR PDBsum; 1CEE; -. DR PDBsum; 1EJ5; -. DR PDBsum; 1T84; -. DR PDBsum; 2A3Z; -. DR PDBsum; 2K42; -. DR PDBsum; 2OT0; -. DR AlphaFoldDB; P42768; -. DR BMRB; P42768; -. DR SMR; P42768; -. DR BioGRID; 113293; 78. DR CORUM; P42768; -. DR DIP; DIP-431N; -. DR ELM; P42768; -. DR IntAct; P42768; 52. DR MINT; P42768; -. DR STRING; 9606.ENSP00000365891; -. DR DrugBank; DB01731; (S)-wiskostatin. DR iPTMnet; P42768; -. DR PhosphoSitePlus; P42768; -. DR BioMuta; WAS; -. DR EPD; P42768; -. DR jPOST; P42768; -. DR MassIVE; P42768; -. DR MaxQB; P42768; -. DR PaxDb; P42768; -. DR PeptideAtlas; P42768; -. DR ProteomicsDB; 55550; -. DR Antibodypedia; 701; 520 antibodies from 42 providers. DR DNASU; 7454; -. DR Ensembl; ENST00000376701.5; ENSP00000365891.4; ENSG00000015285.12. DR Ensembl; ENST00000698625.1; ENSP00000513844.1; ENSG00000015285.12. DR GeneID; 7454; -. DR KEGG; hsa:7454; -. DR MANE-Select; ENST00000376701.5; ENSP00000365891.4; NM_000377.3; NP_000368.1. DR UCSC; uc004dkm.5; human. DR CTD; 7454; -. DR DisGeNET; 7454; -. DR GeneCards; WAS; -. DR GeneReviews; WAS; -. DR HGNC; HGNC:12731; WAS. DR HPA; ENSG00000015285; Tissue enhanced (bone marrow, lymphoid tissue). DR MalaCards; WAS; -. DR MIM; 300299; phenotype. DR MIM; 300392; gene. DR MIM; 301000; phenotype. DR MIM; 313900; phenotype. DR neXtProt; NX_P42768; -. DR OpenTargets; ENSG00000015285; -. DR Orphanet; 906; Wiskott-Aldrich syndrome. DR Orphanet; 86788; X-linked severe congenital neutropenia. DR Orphanet; 852; X-linked thrombocytopenia with normal platelets. DR PharmGKB; PA37342; -. DR VEuPathDB; HostDB:ENSG00000015285; -. DR eggNOG; KOG3671; Eukaryota. DR GeneTree; ENSGT00730000110895; -. DR HOGENOM; CLU_015385_3_2_1; -. DR InParanoid; P42768; -. DR OMA; VGNTYWI; -. DR OrthoDB; 1407277at2759; -. DR PhylomeDB; P42768; -. DR TreeFam; TF316736; -. DR PathwayCommons; P42768; -. DR Reactome; R-HSA-202433; Generation of second messenger molecules. DR Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation. DR Reactome; R-HSA-5663213; RHO GTPases Activate WASPs and WAVEs. DR Reactome; R-HSA-9013148; CDC42 GTPase cycle. DR Reactome; R-HSA-9013149; RAC1 GTPase cycle. DR Reactome; R-HSA-9013409; RHOJ GTPase cycle. DR Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis. DR SignaLink; P42768; -. DR SIGNOR; P42768; -. DR BioGRID-ORCS; 7454; 16 hits in 701 CRISPR screens. DR ChiTaRS; WAS; human. DR EvolutionaryTrace; P42768; -. DR GeneWiki; Wiskott%E2%80%93Aldrich_syndrome_protein; -. DR GenomeRNAi; 7454; -. DR Pharos; P42768; Tbio. DR PRO; PR:P42768; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; P42768; protein. DR Bgee; ENSG00000015285; Expressed in granulocyte and 177 other tissues. DR ExpressionAtlas; P42768; baseline and differential. DR Genevisible; P42768; HS. DR GO; GO:0015629; C:actin cytoskeleton; TAS:ProtInc. DR GO; GO:0005884; C:actin filament; IDA:CAFA. DR GO; GO:0005911; C:cell-cell junction; IEA:Ensembl. DR GO; GO:0005829; C:cytosol; IDA:CAFA. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0045335; C:phagocytic vesicle; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0035861; C:site of double-strand break; IDA:UniProtKB. DR GO; GO:0012506; C:vesicle membrane; IEA:Ensembl. DR GO; GO:0003779; F:actin binding; IEA:InterPro. DR GO; GO:0030695; F:GTPase regulator activity; TAS:ProtInc. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0043274; F:phospholipase binding; IPI:BHF-UCL. DR GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL. DR GO; GO:0017124; F:SH3 domain binding; IPI:UniProtKB. DR GO; GO:0031267; F:small GTPase binding; IPI:CAFA. DR GO; GO:0030041; P:actin filament polymerization; IDA:UniProtKB. DR GO; GO:0030048; P:actin filament-based movement; IBA:GO_Central. DR GO; GO:0008154; P:actin polymerization or depolymerization; TAS:ProtInc. DR GO; GO:0007596; P:blood coagulation; TAS:ProtInc. DR GO; GO:0032488; P:Cdc42 protein signal transduction; IMP:CAFA. DR GO; GO:0071346; P:cellular response to type II interferon; IEA:Ensembl. DR GO; GO:0006952; P:defense response; TAS:ProtInc. DR GO; GO:0016197; P:endosomal transport; IEA:Ensembl. DR GO; GO:0008544; P:epidermis development; TAS:ProtInc. DR GO; GO:0006955; P:immune response; IMP:HGNC-UCL. DR GO; GO:2000146; P:negative regulation of cell motility; IMP:CACAO. DR GO; GO:0051497; P:negative regulation of stress fiber assembly; IMP:CAFA. DR GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IEA:InterPro. DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IDA:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0065003; P:protein-containing complex assembly; TAS:ProtInc. DR GO; GO:0008064; P:regulation of actin polymerization or depolymerization; IMP:CAFA. DR GO; GO:0010591; P:regulation of lamellipodium assembly; IGI:CAFA. DR GO; GO:0051492; P:regulation of stress fiber assembly; IGI:CAFA. DR GO; GO:0002625; P:regulation of T cell antigen processing and presentation; IMP:CACAO. DR GO; GO:0042110; P:T cell activation; IEA:Ensembl. DR CDD; cd01205; EVH1_WASP-like; 1. DR DisProt; DP01171; -. DR Gene3D; 2.30.29.30; -; 1. DR Gene3D; 3.90.810.10; -; 2. DR IDEAL; IID00269; -. DR InterPro; IPR000095; CRIB_dom. DR InterPro; IPR036936; CRIB_dom_sf. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR011026; WAS_C. DR InterPro; IPR027641; WASP. DR InterPro; IPR033927; WASPfam_EVH1. DR InterPro; IPR000697; WH1/EVH1_dom. DR InterPro; IPR003124; WH2_dom. DR PANTHER; PTHR23202:SF79; WASP ACTIN NUCLEATION-PROMOTING FACTOR A-RELATED; 2. DR Pfam; PF00786; PBD; 1. DR Pfam; PF00568; WH1; 1. DR Pfam; PF02205; WH2; 1. DR SMART; SM00285; PBD; 1. DR SMART; SM00461; WH1; 1. DR SMART; SM00246; WH2; 1. DR SUPFAM; SSF47912; Wiscott-Aldrich syndrome protein, WASP, C-terminal domain; 2. DR PROSITE; PS50108; CRIB; 1. DR PROSITE; PS50229; WH1; 1. DR PROSITE; PS51082; WH2; 1. DR AGR; HGNC:12731; -. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Cytoskeleton; Direct protein sequencing; KW Disease variant; Nucleus; Phosphoprotein; Reference proteome; Repeat. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:12665801" FT CHAIN 2..502 FT /note="Actin nucleation-promoting factor WAS" FT /id="PRO_0000188990" FT DOMAIN 39..148 FT /note="WH1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00410" FT DOMAIN 238..251 FT /note="CRIB" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00057" FT REPEAT 337..346 FT /note="GRSGPLPPXP motif 1" FT REPEAT 376..385 FT /note="GRSGPLPPXP motif 2" FT DOMAIN 430..447 FT /note="WH2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00406" FT REGION 146..240 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 307..502 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 310..325 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 344..421 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 440..461 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 488..502 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 221 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 291 FT /note="Phosphotyrosine; by FYN and HCK" FT /evidence="ECO:0000269|PubMed:12235133, FT ECO:0000269|PubMed:14707117, ECO:0007744|PubMed:15592455, FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:19690332" FT MOD_RES 483 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000269|PubMed:12769847, FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:19690332" FT MOD_RES 484 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000269|PubMed:12769847, FT ECO:0007744|PubMed:18088087" FT VARIANT 27 FT /note="L -> F (in THC1)" FT /evidence="ECO:0000269|PubMed:8528199" FT /id="VAR_005823" FT VARIANT 30 FT /note="Missing (in THC1)" FT /evidence="ECO:0000269|PubMed:8528198" FT /id="VAR_005824" FT VARIANT 31 FT /note="E -> K (in WAS; dbSNP:rs1557006239)" FT /evidence="ECO:0000269|PubMed:8528198, FT ECO:0000269|PubMed:9098856" FT /id="VAR_005825" FT VARIANT 43 FT /note="C -> W (in WAS; moderate form)" FT /evidence="ECO:0000269|PubMed:7753869, FT ECO:0000269|PubMed:9126958" FT /id="VAR_008105" FT VARIANT 45 FT /note="T -> M (in WAS and THC1; dbSNP:rs132630273)" FT /evidence="ECO:0000269|PubMed:11167787, FT ECO:0000269|PubMed:7753869, ECO:0000269|PubMed:9098856, FT ECO:0000269|PubMed:9126958" FT /id="VAR_008106" FT VARIANT 48 FT /note="T -> I (in THC1)" FT /evidence="ECO:0000269|PubMed:8528199" FT /id="VAR_005826" FT VARIANT 52 FT /note="Q -> H (in WAS)" FT /evidence="ECO:0000269|PubMed:11793485" FT /id="VAR_012710" FT VARIANT 56 FT /note="A -> T (found in a patient with THC1; unknown FT pathological significance)" FT /evidence="ECO:0000269|PubMed:24115682" FT /id="VAR_074020" FT VARIANT 56 FT /note="A -> V (in THC1; dbSNP:rs132630269)" FT /evidence="ECO:0000269|PubMed:7795648, FT ECO:0000269|PubMed:9713366" FT /id="VAR_005827" FT VARIANT 58 FT /note="P -> L (in WAS)" FT /evidence="ECO:0000269|PubMed:7753869" FT /id="VAR_022806" FT VARIANT 58 FT /note="P -> R (in THC1; dbSNP:rs132630275)" FT /evidence="ECO:0000269|PubMed:11877312" FT /id="VAR_033255" FT VARIANT 70 FT /note="G -> W (in WAS)" FT /evidence="ECO:0000269|PubMed:11793485" FT /id="VAR_012711" FT VARIANT 73 FT /note="C -> R (in WAS; severe form)" FT /evidence="ECO:0000269|PubMed:10447259" FT /id="VAR_008107" FT VARIANT 75 FT /note="V -> M (in THC1; dbSNP:rs782290433)" FT /evidence="ECO:0000269|PubMed:10447259, FT ECO:0000269|PubMed:8528198, ECO:0000269|PubMed:8528199, FT ECO:0000269|PubMed:9126958, ECO:0000269|PubMed:9683546" FT /id="VAR_005828" FT VARIANT 82 FT /note="S -> P (in WAS; attenuated form; dbSNP:rs132630272)" FT /evidence="ECO:0000269|PubMed:8528198" FT /id="VAR_005829" FT VARIANT 83 FT /note="Y -> C (in THC1)" FT /evidence="ECO:0000269|PubMed:10447259" FT /id="VAR_008108" FT VARIANT 84 FT /note="F -> L (in WAS; severe form)" FT /evidence="ECO:0000269|PubMed:9683546" FT /id="VAR_008109" FT VARIANT 86 FT /note="R -> C (in WAS)" FT /evidence="ECO:0000269|PubMed:10447259, FT ECO:0000269|PubMed:8528198, ECO:0000269|PubMed:9126958" FT /id="VAR_005832" FT VARIANT 86 FT /note="R -> H (in WAS; dbSNP:rs132630268)" FT /evidence="ECO:0000269|PubMed:8528198, FT ECO:0000269|PubMed:8528199, ECO:0000269|PubMed:8682510" FT /id="VAR_005830" FT VARIANT 86 FT /note="R -> L (in WAS; dbSNP:rs132630268)" FT /evidence="ECO:0000269|PubMed:8528199" FT /id="VAR_005831" FT VARIANT 89 FT /note="G -> D (in WAS; mild form; dbSNP:rs139857045)" FT /evidence="ECO:0000269|PubMed:9683546" FT /id="VAR_008110" FT VARIANT 97 FT /note="W -> C (in WAS; attenuated form)" FT /evidence="ECO:0000269|PubMed:8528198" FT /id="VAR_005833" FT VARIANT 131 FT /note="E -> K (in WAS; found in a patient with MRT52; FT dbSNP:rs146220228)" FT /evidence="ECO:0000269|PubMed:26566883, FT ECO:0000269|PubMed:8528199" FT /id="VAR_005834" FT VARIANT 133 FT /note="E -> K (in WAS; severe form)" FT /evidence="ECO:0000269|PubMed:10447259, FT ECO:0000269|PubMed:7753869, ECO:0000269|PubMed:8528198, FT ECO:0000269|PubMed:9445409, ECO:0000269|PubMed:9683546" FT /id="VAR_005835" FT VARIANT 134 FT /note="A -> T (in WAS)" FT /evidence="ECO:0000269|PubMed:7753869" FT /id="VAR_022807" FT VARIANT 187 FT /note="G -> C (in WAS)" FT /evidence="ECO:0000269|PubMed:8528199" FT /id="VAR_005836" FT VARIANT 236 FT /note="A -> E (in THC1)" FT /evidence="ECO:0000269|PubMed:7795648" FT /id="VAR_005837" FT VARIANT 270 FT /note="L -> P (in XLN; a constitutively activating FT mutation; dbSNP:rs132630274)" FT /evidence="ECO:0000269|PubMed:11242115" FT /id="VAR_033256" FT VARIANT 476 FT /note="K -> E (in WAS)" FT /evidence="ECO:0000269|PubMed:8528198" FT /id="VAR_005838" FT VARIANT 477 FT /note="R -> K (in THC1)" FT /evidence="ECO:0000269|PubMed:8528199" FT /id="VAR_005839" FT VARIANT 481 FT /note="I -> N (in THC1; dbSNP:rs132630276)" FT /evidence="ECO:0000269|PubMed:11877312" FT /id="VAR_033257" FT CONFLICT 332 FT /note="V -> A (in Ref. 4; AAD26691)" FT /evidence="ECO:0000305" FT TURN 235..237 FT /evidence="ECO:0007829|PDB:1CEE" FT STRAND 245..250 FT /evidence="ECO:0007829|PDB:1CEE" FT TURN 254..256 FT /evidence="ECO:0007829|PDB:1CEE" FT TURN 260..262 FT /evidence="ECO:0007829|PDB:1EJ5" FT HELIX 265..271 FT /evidence="ECO:0007829|PDB:1CEE" FT TURN 272..275 FT /evidence="ECO:0007829|PDB:1CEE" FT HELIX 278..281 FT /evidence="ECO:0007829|PDB:1EJ5" FT HELIX 284..296 FT /evidence="ECO:0007829|PDB:1EJ5" FT HELIX 299..309 FT /evidence="ECO:0007829|PDB:1EJ5" FT HELIX 432..440 FT /evidence="ECO:0007829|PDB:2A3Z" SQ SEQUENCE 502 AA; 52913 MW; 7228428672B7CB78 CRC64; MSGGPMGGRP GGRGAPAVQQ NIPSTLLQDH ENQRLFEMLG RKCLTLATAV VQLYLALPPG AEHWTKEHCG AVCFVKDNPQ KSYFIRLYGL QAGRLLWEQE LYSQLVYSTP TPFFHTFAGD DCQAGLNFAD EDEAQAFRAL VQEKIQKRNQ RQSGDRRQLP PPPTPANEER RGGLPPLPLH PGGDQGGPPV GPLSLGLATV DIQNPDITSS RYRGLPAPGP SPADKKRSGK KKISKADIGA PSGFKHVSHV GWDPQNGFDV NNLDPDLRSL FSRAGISEAQ LTDAETSKLI YDFIEDQGGL EAVRQEMRRQ EPLPPPPPPS RGGNQLPRPP IVGGNKGRSG PLPPVPLGIA PPPPTPRGPP PPGRGGPPPP PPPATGRSGP LPPPPPGAGG PPMPPPPPPP PPPPSSGNGP APPPLPPALV PAGGLAPGGG RGALLDQIRQ GIQLNKTPGA PESSALQPPP QSSEGLVGAL MHVMQKRSRA IHSSDEGEDQ AGDEDEDDEW DD // ID PCNA_HUMAN Reviewed; 261 AA. AC P12004; B2R897; D3DW02; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 1. DT 14-DEC-2022, entry version 244. DE RecName: Full=Proliferating cell nuclear antigen; DE Short=PCNA; DE AltName: Full=Cyclin; GN Name=PCNA; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX PubMed=2882507; DOI=10.1073/pnas.84.6.1575; RA Almendral J.M., Huebsch D., Blundell P.A., Macdonald-Bravo H., Bravo R.; RT "Cloning and sequence of the human nuclear protein cyclin: homology with RT DNA-binding proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 84:1575-1579(1987). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2565339; DOI=10.1016/s0021-9258(18)83257-4; RA Travali S., Ku D.H., Rizzo M.G., Ottavio L., Baserga R., Calabretta B.; RT "Structure of the human gene for the proliferating cell nuclear antigen."; RL J. Biol. Chem. 264:7466-7472(1989). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NIEHS SNPs program; RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skeletal muscle; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Bone marrow, and Lung; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP PROTEIN SEQUENCE OF 1-26. RX PubMed=2882422; DOI=10.1038/326471a0; RA Prelich G., Kostura M., Marshak D.R., Mathews M.B., Stillman B.; RT "The cell-cycle regulated proliferating cell nuclear antigen is required RT for SV40 DNA replication in vitro."; RL Nature 326:471-475(1987). RN [9] RP PROTEIN SEQUENCE OF 169-181, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Fetal brain cortex; RA Lubec G., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [10] RP INTERACTION WITH ERCC5/XPG. RX PubMed=9305916; DOI=10.1074/jbc.272.39.24522; RA Gary R., Ludwig D.L., Cornelius H.L., MacInnes M.A., Park M.S.; RT "The DNA repair endonuclease XPG binds to proliferating cell nuclear RT antigen (PCNA) and shares sequence elements with the PCNA-binding regions RT of FEN-1 and cyclin-dependent kinase inhibitor p21."; RL J. Biol. Chem. 272:24522-24529(1997). RN [11] RP INTERACTION WITH DNMT1. RX PubMed=9302295; DOI=10.1126/science.277.5334.1996; RA Chuang L.S.-H., Ian H.-I., Koh T.-W., Ng H.-H., Xu G., Li B.F.L.; RT "Human DNA-(cytosine-5) methyltransferase-PCNA complex as a target for RT p21WAF1."; RL Science 277:1996-2000(1997). RN [12] RP INTERACTION WITH CDC6. RX PubMed=9566895; DOI=10.1128/mcb.18.5.2758; RA Saha P., Chen J., Thome K.C., Lawlis S.J., Hou Z.H., Hendricks M., RA Parvin J.D., Dutta A.; RT "Human CDC6/Cdc18 associates with Orc1 and cyclin-cdk and is selectively RT eliminated from the nucleus at the onset of S phase."; RL Mol. Cell. Biol. 18:2758-2767(1998). RN [13] RP INTERACTION WITH POLD3 AND CDKN1A, AND MUTAGENESIS OF 43-SER--VAL-45; RP 125-GLN--ILE-128; 188-VAL--LYS-190 AND 251-LEU--LYS-254. RX PubMed=11595739; DOI=10.1074/jbc.m106990200; RA Ducoux M., Urbach S., Baldacci G., Huebscher U., Koundrioukoff S., RA Christensen J., Hughes P.; RT "Mediation of proliferating cell nuclear antigen (PCNA)-dependent DNA RT replication through a conserved p21(Cip1)-like PCNA-binding motif present RT in the third subunit of human DNA polymerase delta."; RL J. Biol. Chem. 276:49258-49266(2001). RN [14] RP INTERACTION WITH APEX2. RX PubMed=11376153; DOI=10.1093/nar/29.11.2349; RA Tsuchimoto D., Sakai Y., Sakumi K., Nishioka K., Sasaki M., Fujiwara T., RA Nakabeppu Y.; RT "Human APE2 protein is mostly localized in the nuclei and to some extent in RT the mitochondria, while nuclear APE2 is partly associated with RT proliferating cell nuclear antigen."; RL Nucleic Acids Res. 29:2349-2360(2001). RN [15] RP INTERACTION WITH POLK. RX PubMed=11784855; DOI=10.1128/mcb.22.3.784-791.2002; RA Haracska L., Unk I., Johnson R.E., Phillips B.B., Hurwitz J., Prakash L., RA Prakash S.; RT "Stimulation of DNA synthesis activity of human DNA polymerase kappa by RT PCNA."; RL Mol. Cell. Biol. 22:784-791(2002). RN [16] RP INTERACTION WITH DNTTIP2. RX PubMed=12786946; DOI=10.1046/j.1365-2443.2003.00656.x; RA Fujita K., Shimazaki N., Ohta Y., Kubota T., Ibe S., Toji S., Tamai K., RA Fujisaki S., Hayano T., Koiwai O.; RT "Terminal deoxynucleotidyltransferase forms a ternary complex with a novel RT chromatin remodeling protein with 82 kDa and core histone."; RL Genes Cells 8:559-571(2003). RN [17] RP INTERACTION WITH POLDIP2. RC TISSUE=Placenta; RX PubMed=12522211; DOI=10.1074/jbc.m208694200; RA Liu L., Rodriguez-Belmonte E.M., Mazloum N., Xie B., Lee M.Y.W.T.; RT "Identification of a novel protein, PDIP38, that interacts with the p50 RT subunit of DNA polymerase delta and proliferating cell nuclear antigen."; RL J. Biol. Chem. 278:10041-10047(2003). RN [18] RP INTERACTION WITH EXO1. RX PubMed=15225546; DOI=10.1016/j.molcel.2004.06.016; RA Dzantiev L., Constantin N., Genschel J., Iyer R.R., Burgers P.M., RA Modrich P.; RT "A defined human system that supports bidirectional mismatch-provoked RT excision."; RL Mol. Cell 15:31-41(2004). RN [19] RP UBIQUITINATION, AND INTERACTION WITH POLH. RX PubMed=15149598; DOI=10.1016/s1097-2765(04)00259-x; RA Kannouche P.L., Wing J., Lehmann A.R.; RT "Interaction of human DNA polymerase eta with monoubiquitinated PCNA: a RT possible mechanism for the polymerase switch in response to DNA damage."; RL Mol. Cell 14:491-500(2004). RN [20] RP INTERACTION WITH BAZ1B AND SMARCA5. RX PubMed=15543136; DOI=10.1038/ncb1196; RA Poot R.A., Bozhenok L., van den Berg D.L.C., Steffensen S., Ferreira F., RA Grimaldi M., Gilbert N., Ferreira J., Varga-Weisz P.D.; RT "The Williams syndrome transcription factor interacts with PCNA to target RT chromatin remodelling by ISWI to replication foci."; RL Nat. Cell Biol. 6:1236-1244(2004). RN [21] RP INTERACTION WITH POLD1; POLD3 AND POLD4. RX PubMed=16510448; DOI=10.1074/jbc.m600322200; RA Li H., Xie B., Zhou Y., Rahmeh A., Trusa S., Zhang S., Gao Y., Lee E.Y., RA Lee M.Y.; RT "Functional roles of p12, the fourth subunit of human DNA polymerase RT delta."; RL J. Biol. Chem. 281:14748-14755(2006). RN [22] RP INTERACTION WITH SHPRH, UBIQUITINATION AT LYS-164, AND MUTAGENESIS OF RP LYS-164. RX PubMed=17130289; DOI=10.1083/jcb.200606145; RA Motegi A., Sood R., Moinova H., Markowitz S.D., Liu P.P., Myung K.; RT "Human SHPRH suppresses genomic instability through proliferating cell RT nuclear antigen polyubiquitination."; RL J. Cell Biol. 175:703-708(2006). RN [23] RP INTERACTION WITH CDT1. RX PubMed=16949367; DOI=10.1016/j.molcel.2006.08.010; RA Jin J., Arias E.E., Chen J., Harper J.W., Walter J.C.; RT "A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2, which is RT required for S phase destruction of the replication factor Cdt1."; RL Mol. Cell 23:709-721(2006). RN [24] RP PHOSPHORYLATION AT TYR-211 BY EGFR, MUTAGENESIS OF TYR-211, AND INTERACTION RP WITH EGFR. RX PubMed=17115032; DOI=10.1038/ncb1501; RA Wang S.C., Nakajima Y., Yu Y.L., Xia W., Chen C.T., Yang C.C., RA McIntush E.W., Li L.Y., Hawke D.H., Kobayashi R., Hung M.C.; RT "Tyrosine phosphorylation controls PCNA function through protein RT stability."; RL Nat. Cell Biol. 8:1359-1368(2006). RN [25] RP UBIQUITINATION AT LYS-164, AND MUTAGENESIS OF LYS-164. RX PubMed=17108083; DOI=10.1073/pnas.0608595103; RA Unk I., Hajdu I., Fatyol K., Szakal B., Blastyak A., Bermudez V., RA Hurwitz J., Prakash L., Prakash S., Haracska L.; RT "Human SHPRH is a ubiquitin ligase for Mms2-Ubc13-dependent RT polyubiquitylation of proliferating cell nuclear antigen."; RL Proc. Natl. Acad. Sci. U.S.A. 103:18107-18112(2006). RN [26] RP UBIQUITINATION. RX PubMed=18948756; DOI=10.4161/cc.7.21.6949; RA Zhang S., Chea J., Meng X., Zhou Y., Lee E.Y.C., Lee M.Y.W.T.; RT "PCNA is ubiquitinated by RNF8."; RL Cell Cycle 7:3399-3404(2008). RN [27] RP INTERACTION WITH CDKN1A. RX PubMed=18794347; DOI=10.1101/gad.1676108; RA Abbas T., Sivaprasad U., Terai K., Amador V., Pagano M., Dutta A.; RT "PCNA-dependent regulation of p21 ubiquitylation and degradation via the RT CRL4Cdt2 ubiquitin ligase complex."; RL Genes Dev. 22:2496-2506(2008). RN [28] RP INTERACTION WITH DDX11. RX PubMed=18499658; DOI=10.1074/jbc.m802696200; RA Farina A., Shin J.H., Kim D.H., Bermudez V.P., Kelman Z., Seo Y.S., RA Hurwitz J.; RT "Studies with the human cohesin establishment factor, ChlR1. Association of RT ChlR1 with Ctf18-RFC and Fen1."; RL J. Biol. Chem. 283:20925-20936(2008). RN [29] RP INTERACTION WITH CDKN1A. RX PubMed=18703516; DOI=10.1074/jbc.m806045200; RA Nishitani H., Shiomi Y., Iida H., Michishita M., Takami T., Tsurimoto T.; RT "CDK inhibitor p21 is degraded by a proliferating cell nuclear antigen- RT coupled Cul4-DDB1Cdt2 pathway during S phase and after UV irradiation."; RL J. Biol. Chem. 283:29045-29052(2008). RN [30] RP FUNCTION, AND INTERACTION WITH APEX2. RX PubMed=19443450; DOI=10.1093/nar/gkp357; RA Burkovics P., Hajdu I., Szukacsov V., Unk I., Haracska L.; RT "Role of PCNA-dependent stimulation of 3'-phosphodiesterase and 3'-5' RT exonuclease activities of human Ape2 in repair of oxidative DNA damage."; RL Nucleic Acids Res. 37:4247-4255(2009). RN [31] RP UBIQUITINATION, AND INTERACTION WITH HLTF. RX PubMed=18316726; DOI=10.1073/pnas.0800563105; RA Unk I., Hajdu I., Fatyol K., Hurwitz J., Yoon J.-H., Prakash L., RA Prakash S., Haracska L.; RT "Human HLTF functions as a ubiquitin ligase for proliferating cell nuclear RT antigen polyubiquitination."; RL Proc. Natl. Acad. Sci. U.S.A. 105:3768-3773(2008). RN [32] RP UBIQUITINATION, FUNCTION, INTERACTION WITH HLTF AND SHPRH, AND MUTAGENESIS RP OF LYS-164. RX PubMed=18719106; DOI=10.1073/pnas.0805685105; RA Motegi A., Liaw H.-J., Lee K.-Y., Roest H.P., Maas A., Wu X., Moinova H., RA Markowitz S.D., Ding H., Hoeijmakers J.H.J., Myung K.; RT "Polyubiquitination of proliferating cell nuclear antigen by HLTF and SHPRH RT prevents genomic instability from stalled replication forks."; RL Proc. Natl. Acad. Sci. U.S.A. 105:12411-12416(2008). RN [33] RP INTERACTION WITH NUDT15, AND ACETYLATION AT LYS-14. RX PubMed=19419956; DOI=10.1074/jbc.m109.015289; RA Yu Y., Cai J.-P., Tu B., Wu L., Zhao Y., Liu X., Li L., McNutt M.A., RA Feng J., He Q., Yang Y., Wang H., Sekiguchi M., Zhu W.-G.; RT "Proliferating cell nuclear antigen is protected from degradation by RT forming a complex with MutT Homolog2."; RL J. Biol. Chem. 284:19310-19320(2009). RN [34] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-77; LYS-80 AND LYS-248, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [35] RP INTERACTION WITH ATAD5. RX PubMed=20147293; DOI=10.1074/jbc.m109.092544; RA Lee K.Y., Yang K., Cohn M.A., Sikdar N., D'Andrea A.D., Myung K.; RT "Human ELG1 regulates the level of ubiquitinated proliferating cell nuclear RT antigen (PCNA) through Its interactions with PCNA and USP1."; RL J. Biol. Chem. 285:10362-10369(2010). RN [36] RP INTERACTION WITH MAPK15. RX PubMed=20733054; DOI=10.1083/jcb.201002124; RA Groehler A.L., Lannigan D.A.; RT "A chromatin-bound kinase, ERK8, protects genomic integrity by inhibiting RT HDM2-mediated degradation of the DNA clamp PCNA."; RL J. Cell Biol. 190:575-586(2010). RN [37] RP UBIQUITINATION, AND MUTAGENESIS OF LYS-164. RX PubMed=20129063; DOI=10.1016/j.molcel.2009.12.018; RA Terai K., Abbas T., Jazaeri A.A., Dutta A.; RT "CRL4(Cdt2) E3 ubiquitin ligase monoubiquitinates PCNA to promote RT translesion DNA synthesis."; RL Mol. Cell 37:143-149(2010). RN [38] RP UBIQUITINATION IN RESPONSE TO UV IRRADIATION. RX PubMed=20227374; DOI=10.1016/j.molcel.2010.02.009; RA Ogi T., Limsirichaikul S., Overmeer R.M., Volker M., Takenaka K., RA Cloney R., Nakazawa Y., Niimi A., Miki Y., Jaspers N.G., Mullenders L.H., RA Yamashita S., Fousteri M.I., Lehmann A.R.; RT "Three DNA polymerases, recruited by different mechanisms, carry out NER RT repair synthesis in human cells."; RL Mol. Cell 37:714-727(2010). RN [39] RP INTERACTION WITH POLN. RX PubMed=19995904; DOI=10.1128/mcb.01124-09; RA Moldovan G.L., Madhavan M.V., Mirchandani K.D., McCaffrey R.M., RA Vinciguerra P., D'Andrea A.D.; RT "DNA polymerase POLN participates in cross-link repair and homologous RT recombination."; RL Mol. Cell. Biol. 30:1088-1096(2010). RN [40] RP INTERACTION WITH SETMAR. RX PubMed=20457750; DOI=10.1093/nar/gkq339; RA De Haro L.P., Wray J., Williamson E.A., Durant S.T., Corwin L., RA Gentry A.C., Osheroff N., Lee S.H., Hromas R., Nickoloff J.A.; RT "Metnase promotes restart and repair of stalled and collapsed replication RT forks."; RL Nucleic Acids Res. 38:5681-5691(2010). RN [41] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [42] RP INTERACTION WITH SMARCAD1. RX PubMed=21549307; DOI=10.1016/j.molcel.2011.02.036; RA Rowbotham S.P., Barki L., Neves-Costa A., Santos F., Dean W., Hawkes N., RA Choudhary P., Will W.R., Webster J., Oxley D., Green C.M., Varga-Weisz P., RA Mermoud J.E.; RT "Maintenance of silent chromatin through replication requires SWI/SNF-like RT chromatin remodeler SMARCAD1."; RL Mol. Cell 42:285-296(2011). RN [43] RP INTERACTION WITH PCLAF. RX PubMed=21628590; DOI=10.1073/pnas.1106136108; RA Emanuele M.J., Ciccia A., Elia A.E., Elledge S.J.; RT "Proliferating cell nuclear antigen (PCNA)-associated KIAA0101/PAF15 RT protein is a cell cycle-regulated anaphase-promoting complex/cyclosome RT substrate."; RL Proc. Natl. Acad. Sci. U.S.A. 108:9845-9850(2011). RN [44] RP INTERACTION WITH POLD3. RX PubMed=22148433; DOI=10.1021/bi201638e; RA Rahmeh A.A., Zhou Y., Xie B., Li H., Lee E.Y., Lee M.Y.; RT "Phosphorylation of the p68 subunit of Pol delta acts as a molecular switch RT to regulate its interaction with PCNA."; RL Biochemistry 51:416-424(2012). RN [45] RP INTERACTION WITH PARPBP, AND SUMOYLATION. RX PubMed=22153967; DOI=10.1016/j.molcel.2011.11.010; RA Moldovan G.L., Dejsuphong D., Petalcorin M.I., Hofmann K., Takeda S., RA Boulton S.J., D'Andrea A.D.; RT "Inhibition of homologous recombination by the PCNA-interacting protein RT PARI."; RL Mol. Cell 45:75-86(2012). RN [46] RP INTERACTION WITH SPRTN. RX PubMed=22681887; DOI=10.1016/j.molcel.2012.05.020; RA Centore R.C., Yazinski S.A., Tse A., Zou L.; RT "Spartan/C1orf124, a reader of PCNA ubiquitylation and a regulator of UV- RT induced DNA damage response."; RL Mol. Cell 46:625-635(2012). RN [47] RP INTERACTION WITH ZRANB3. RX PubMed=22759634; DOI=10.1101/gad.193516.112; RA Weston R., Peeters H., Ahel D.; RT "ZRANB3 is a structure-specific ATP-dependent endonuclease involved in RT replication stress response."; RL Genes Dev. 26:1558-1572(2012). RN [48] RP INTERACTION WITH ZRANB3. RX PubMed=22705370; DOI=10.1016/j.molcel.2012.05.025; RA Yuan J., Ghosal G., Chen J.; RT "The HARP-like domain-containing protein AH2/ZRANB3 binds to PCNA and RT participates in cellular response to replication stress."; RL Mol. Cell 47:410-421(2012). RN [49] RP INTERACTION WITH PCLAF. RX PubMed=23000965; DOI=10.1038/ncb2579; RA Povlsen L.K., Beli P., Wagner S.A., Poulsen S.L., Sylvestersen K.B., RA Poulsen J.W., Nielsen M.L., Bekker-Jensen S., Mailand N., Choudhary C.; RT "Systems-wide analysis of ubiquitylation dynamics reveals a key role for RT PAF15 ubiquitylation in DNA-damage bypass."; RL Nat. Cell Biol. 14:1089-1098(2012). RN [50] RP INTERACTION WITH ZRANB3. RX PubMed=22704558; DOI=10.1016/j.molcel.2012.05.024; RA Ciccia A., Nimonkar A.V., Hu Y., Hajdu I., Achar Y.J., Izhar L., RA Petit S.A., Adamson B., Yoon J.C., Kowalczykowski S.C., Livingston D.M., RA Haracska L., Elledge S.J.; RT "Polyubiquitinated PCNA recruits the ZRANB3 translocase to maintain genomic RT integrity after replication stress."; RL Mol. Cell 47:396-409(2012). RN [51] RP INTERACTION WITH CDKN1C. RX PubMed=22634751; DOI=10.1038/ng.2275; RA Arboleda V.A., Lee H., Parnaik R., Fleming A., Banerjee A., RA Ferraz-de-Souza B., Delot E.C., Rodriguez-Fernandez I.A., Braslavsky D., RA Bergada I., Dell'Angelica E.C., Nelson S.F., Martinez-Agosto J.A., RA Achermann J.C., Vilain E.; RT "Mutations in the PCNA-binding domain of CDKN1C cause IMAGe syndrome."; RL Nat. Genet. 44:788-792(2012). RN [52] RP INTERACTION WITH ANKRD17. RX PubMed=23711367; DOI=10.1016/j.febslet.2013.05.037; RA Menning M., Kufer T.A.; RT "A role for the Ankyrin repeat containing protein Ankrd17 in Nod1- and RT Nod2-mediated inflammatory responses."; RL FEBS Lett. 587:2137-2142(2013). RN [53] RP INTERACTION WITH FBH1. RX PubMed=23677613; DOI=10.1093/nar/gkt397; RA Bacquin A., Pouvelle C., Siaud N., Perderiset M., Salome-Desnoulez S., RA Tellier-Lebegue C., Lopez B., Charbonnier J.B., Kannouche P.L.; RT "The helicase FBH1 is tightly regulated by PCNA via CRL4(Cdt2)-mediated RT proteolysis in human cells."; RL Nucleic Acids Res. 41:6501-6513(2013). RN [54] RP INTERACTION WITH RTEL1, AND SUBCELLULAR LOCATION. RX PubMed=24115439; DOI=10.1126/science.1241779; RA Vannier J.B., Sandhu S., Petalcorin M.I., Wu X., Nabi Z., Ding H., RA Boulton S.J.; RT "RTEL1 is a replisome-associated helicase that promotes telomere and RT genome-wide replication."; RL Science 342:239-242(2013). RN [55] RP FUNCTION, AND INTERACTION WITH PARP10. RX PubMed=24695737; DOI=10.1074/jbc.m114.556340; RA Nicolae C.M., Aho E.R., Vlahos A.H., Choe K.N., De S., Karras G.I., RA Moldovan G.L.; RT "The ADP-ribosyltransferase PARP10/ARTD10 interacts with proliferating cell RT nuclear antigen (PCNA) and is required for DNA damage tolerance."; RL J. Biol. Chem. 289:13627-13637(2014). RN [56] RP INVOLVEMENT IN ATLD2, INTERACTION WITH FEN1; LIG1 AND ERCC5, VARIANT ATLD2 RP ILE-228, AND CHARACTERIZATION OF VARIANT ATDL2 ILE-228. RX PubMed=24911150; DOI=10.1172/jci74593; RA Baple E.L., Chambers H., Cross H.E., Fawcett H., Nakazawa Y., Chioza B.A., RA Harlalka G.V., Mansour S., Sreekantan-Nair A., Patton M.A., RA Muggenthaler M., Rich P., Wagner K., Coblentz R., Stein C.K., Last J.I., RA Taylor A.M., Jackson A.P., Ogi T., Lehmann A.R., Green C.M., Crosby A.H.; RT "Hypomorphic PCNA mutation underlies a human DNA repair disorder."; RL J. Clin. Invest. 124:3137-3146(2014). RN [57] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [58] RP INTERACTION WITH FAM111A. RX PubMed=24561620; DOI=10.1038/ncb2918; RA Alabert C., Bukowski-Wills J.C., Lee S.B., Kustatscher G., Nakamura K., RA de Lima Alves F., Menard P., Mejlvang J., Rappsilber J., Groth A.; RT "Nascent chromatin capture proteomics determines chromatin dynamics during RT DNA replication and identifies unknown fork components."; RL Nat. Cell Biol. 16:281-293(2014). RN [59] RP FUNCTION, TRIMERIZATION, INTERACTION WITH CREBBP; EP300 AND POLD1, RP ACETYLATION, UBIQUITINATION, ASSOCIATION WITH CHROMATIN, AND MUTAGENESIS OF RP LYS-13; LYS-14; LYS-20; LYS-77 AND LYS-80. RX PubMed=24939902; DOI=10.1093/nar/gku533; RA Cazzalini O., Sommatis S., Tillhon M., Dutto I., Bachi A., Rapp A., RA Nardo T., Scovassi A.I., Necchi D., Cardoso M.C., Stivala L.A., RA Prosperi E.; RT "CBP and p300 acetylate PCNA to link its degradation with nucleotide RT excision repair synthesis."; RL Nucleic Acids Res. 42:8433-8448(2014). RN [60] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-164, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [61] RP METHYLATION. RX PubMed=25732820; DOI=10.1016/j.celrep.2015.01.054; RA Perry J.J., Ballard G.D., Albert A.E., Dobrolecki L.E., Malkas L.H., RA Hoelz D.J.; RT "Human C6orf211 encodes Armt1, a protein carboxyl methyltransferase that RT targets PCNA and is linked to the DNA damage response."; RL Cell Rep. 10:1288-1296(2015). RN [62] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-164, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033; RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., RA Vertegaal A.C.; RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."; RL Cell Rep. 10:1778-1791(2015). RN [63] RP INTERACTION WITH ALKBH2, AND MUTAGENESIS OF 43-SER--VAL-45; RP 125-GLN--ILE-128 AND 188-VAL--LYS-190. RX PubMed=26408825; DOI=10.1016/j.dnarep.2015.09.008; RA Fu D., Samson L.D., Huebscher U., van Loon B.; RT "The interaction between ALKBH2 DNA repair enzyme and PCNA is direct, RT mediated by the hydrophobic pocket of PCNA and perturbed in naturally- RT occurring ALKBH2 variants."; RL DNA Repair 35:13-18(2015). RN [64] RP INTERACTION WITH HERPES VIRUS 8 PROTEIN LANA1 (MICROBIAL INFECTION). RX PubMed=26223641; DOI=10.1128/jvi.01524-15; RA Sun Z., Jha H.C., Robertson E.S.; RT "Bub1 in Complex with LANA Recruits PCNA To Regulate Kaposi's Sarcoma- RT Associated Herpesvirus Latent Replication and DNA Translesion Synthesis."; RL J. Virol. 89:10206-10218(2015). RN [65] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-164, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.o114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., RA Vertegaal A.C.; RT "System-wide analysis of SUMOylation dynamics in response to replication RT stress reveals novel small ubiquitin-like modified target proteins and RT acceptor lysines relevant for genome stability."; RL Mol. Cell. Proteomics 14:1419-1434(2015). RN [66] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [67] RP INTERACTION WITH TRAIP. RX PubMed=27462463; DOI=10.1038/celldisc.2016.16; RA Feng W., Guo Y., Huang J., Deng Y., Zang J., Huen M.S.; RT "TRAIP regulates replication fork recovery and progression via PCNA."; RL Cell Discov. 2:16016-16016(2016). RN [68] RP INTERACTION WITH SDE2. RX PubMed=27906959; DOI=10.1371/journal.pgen.1006465; RA Jo U., Cai W., Wang J., Kwon Y., D'Andrea A.D., Kim H.; RT "PCNA-dependent cleavage and degradation of SDE2 regulates response to RT replication stress."; RL PLoS Genet. 12:E1006465-E1006465(2016). RN [69] RP INTERACTION WITH DONSON. RX PubMed=28191891; DOI=10.1038/ng.3790; RA Reynolds J.J., Bicknell L.S., Carroll P., Higgs M.R., Shaheen R., RA Murray J.E., Papadopoulos D.K., Leitch A., Murina O., Tarnauskaite Z., RA Wessel S.R., Zlatanou A., Vernet A., von Kriegsheim A., Mottram R.M., RA Logan C.V., Bye H., Li Y., Brean A., Maddirevula S., Challis R.C., RA Skouloudaki K., Almoisheer A., Alsaif H.S., Amar A., Prescott N.J., RA Bober M.B., Duker A., Faqeih E., Seidahmed M.Z., Al Tala S., Alswaid A., RA Ahmed S., Al-Aama J.Y., Altmueller J., Al Balwi M., Brady A.F., Chessa L., RA Cox H., Fischetto R., Heller R., Henderson B.D., Hobson E., Nuernberg P., RA Percin E.F., Peron A., Spaccini L., Quigley A.J., Thakur S., Wise C.A., RA Yoon G., Alnemer M., Tomancak P., Yigit G., Taylor A.M., Reijns M.A., RA Simpson M.A., Cortez D., Alkuraya F.S., Mathew C.G., Jackson A.P., RA Stewart G.S.; RT "Mutations in DONSON disrupt replication fork stability and cause RT microcephalic dwarfism."; RL Nat. Genet. 49:537-549(2017). RN [70] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-164 AND LYS-254, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [71] RP INTERACTION WITH DDI2. RX PubMed=29290612; DOI=10.1016/j.molcel.2017.11.035; RA Kottemann M.C., Conti B.A., Lach F.P., Smogorzewska A.; RT "Removal of RTF2 from Stalled Replisomes Promotes Maintenance of Genome RT Integrity."; RL Mol. Cell 69:24-35.E5(2018). RN [72] RP INTERACTION WITH HMCES. RX PubMed=30554877; DOI=10.1016/j.cell.2018.10.055; RA Mohni K.N., Wessel S.R., Zhao R., Wojciechowski A.C., Luzwick J.W., RA Layden H., Eichman B.F., Thompson P.S., Mehta K.P.M., Cortez D.; RT "HMCES maintains genome integrity by shielding abasic sites in single- RT strand DNA."; RL Cell 176:144-153(2019). RN [73] RP FUNCTION. RX PubMed=35585232; DOI=10.1038/s41586-022-04759-1; RA Baris Y., Taylor M.R.G., Aria V., Yeeles J.T.P.; RT "Fast and efficient DNA replication with purified human proteins."; RL Nature 606:204-210(2022). RN [74] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). RX PubMed=8861913; DOI=10.1016/s0092-8674(00)81347-1; RA Gulbis J.M., Kelman Z., Hurwitz J., O'Donnell M., Kuriyan J.; RT "Structure of the C-terminal region of p21(WAF1/CIP1) complexed with human RT PCNA."; RL Cell 87:297-306(1996). RN [75] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH FEN1. RX PubMed=15616578; DOI=10.1038/sj.emboj.7600519; RA Sakurai S., Kitano K., Yamaguchi H., Hamada K., Okada K., Fukuda K., RA Uchida M., Ohtsuka E., Morioka H., Hakoshima T.; RT "Structural basis for recruitment of human flap endonuclease 1 to PCNA."; RL EMBO J. 24:683-693(2005). RN [76] {ECO:0007744|PDB:5IY4} RP X-RAY CRYSTALLOGRAPHY (2.94 ANGSTROMS) IN COMPLEX WITH SPRTN. RX PubMed=27084448; DOI=10.1016/j.bbrc.2016.04.053; RA Wang Y., Xu M., Jiang T.; RT "Crystal structure of human PCNA in complex with the PIP box of DVC1."; RL Biochem. Biophys. Res. Commun. 474:264-270(2016). RN [77] {ECO:0007744|PDB:4ZTD} RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 2-254 IN COMPLEX WITH TRAIP. RX PubMed=26711499; DOI=10.1083/jcb.201506071; RA Hoffmann S., Smedegaard S., Nakamura K., Mortuza G.B., Raschle M., RA Ibanez de Opakua A., Oka Y., Feng Y., Blanco F.J., Mann M., Montoya G., RA Groth A., Bekker-Jensen S., Mailand N.; RT "TRAIP is a PCNA-binding ubiquitin ligase that protects genome stability RT after replication stress."; RL J. Cell Biol. 212:63-75(2016). RN [78] {ECO:0007744|PDB:5YCO} RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS), INTERACTION WITH UHRF2, AND RP MUTAGENESIS OF MET-40; ILE-128; TYR-250 AND ALA-252. RX PubMed=28951215; DOI=10.1016/j.bbrc.2017.09.102; RA Chen W., Wu M., Hang T., Wang C., Zhang X., Zang J.; RT "Structure insights into the molecular mechanism of the interaction between RT UHRF2 and PCNA."; RL Biochem. Biophys. Res. Commun. 494:575-580(2017). CC -!- FUNCTION: Auxiliary protein of DNA polymerase delta and epsilon, is CC involved in the control of eukaryotic DNA replication by increasing the CC polymerase's processibility during elongation of the leading strand CC (PubMed:35585232). Induces a robust stimulatory effect on the 3'-5' CC exonuclease and 3'-phosphodiesterase, but not apurinic-apyrimidinic CC (AP) endonuclease, APEX2 activities. Has to be loaded onto DNA in order CC to be able to stimulate APEX2. Plays a key role in DNA damage response CC (DDR) by being conveniently positioned at the replication fork to CC coordinate DNA replication with DNA repair and DNA damage tolerance CC pathways (PubMed:24939902). Acts as a loading platform to recruit DDR CC proteins that allow completion of DNA replication after DNA damage and CC promote postreplication repair: Monoubiquitinated PCNA leads to CC recruitment of translesion (TLS) polymerases, while 'Lys-63'-linked CC polyubiquitination of PCNA is involved in error-free pathway and CC employs recombination mechanisms to synthesize across the lesion CC (PubMed:24695737). {ECO:0000269|PubMed:18719106, CC ECO:0000269|PubMed:19443450, ECO:0000269|PubMed:24695737, CC ECO:0000269|PubMed:24939902, ECO:0000269|PubMed:35585232}. CC -!- SUBUNIT: Homotrimer (PubMed:24939902). Interacts with p300/EP300; the CC interaction occurs on chromatin in UV-irradiated damaged cells CC (PubMed:24939902). Interacts with CREBBP (via transactivation domain CC and C-terminus); the interaction occurs on chromatin in UV-irradiated CC damaged cells (PubMed:24939902). Directly interacts with POLD1, POLD3 CC and POLD4 subunits of the DNA polymerase delta complex, POLD3 being the CC major interacting partner; the interaction with POLD3 is inhibited by CC CDKN1A/p21(CIP1) (PubMed:11595739, PubMed:16510448, PubMed:22148433, CC PubMed:24939902). Forms a complex with activator 1 heteropentamer in CC the presence of ATP. Interacts with EXO1, POLH, POLK, DNMT1, ERCC5, CC FEN1, CDC6 and POLDIP2 (PubMed:9305916, PubMed:9302295, PubMed:9566895, CC PubMed:11784855, PubMed:12522211, PubMed:15225546, PubMed:15149598, CC PubMed:24911150, PubMed:15616578). Interacts with APEX2; this CC interaction is triggered by reactive oxygen species and increased by CC misincorporation of uracil in nuclear DNA (PubMed:11376153, CC PubMed:19443450). Forms a ternary complex with DNTTIP2 and core histone CC (PubMed:12786946). Interacts with KCTD10 and PPP1R15A (By similarity). CC Interacts with SMARCA5/SNF2H (PubMed:15543136). Interacts with CC BAZ1B/WSTF; the interaction is direct and is required for BAZ1B/WSTF CC binding to replication foci during S phase (PubMed:15543136). Interacts CC with HLTF and SHPRH (PubMed:17130289, PubMed:18316726, CC PubMed:18719106). Interacts with NUDT15; this interaction is disrupted CC in response to UV irradiation and acetylation (PubMed:19419956). CC Interacts with CDKN1A/p21(CIP1) and CDT1; interacts via their PIP-box CC which also recruits the DCX(DTL) complex. The interaction with CDKN1A CC inhibits POLD3 binding (PubMed:11595739, PubMed:16949367, CC PubMed:18794347, PubMed:18703516). Interacts with DDX11 CC (PubMed:18499658). Interacts with EGFR; positively regulates PCNA CC (PubMed:17115032). Interacts with PARPBP (PubMed:22153967). Interacts CC (when ubiquitinated) with SPRTN; leading to enhance RAD18-mediated PCNA CC ubiquitination (PubMed:22681887, PubMed:27084448). Interacts (when CC polyubiquitinated) with ZRANB3 (PubMed:22704558, PubMed:22705370, CC PubMed:22759634). Interacts with SMARCAD1 (PubMed:21549307). Interacts CC with CDKN1C (PubMed:22634751). Interacts with PCLAF (via PIP-box) CC (PubMed:21628590, PubMed:23000965). Interacts with RTEL1 (via PIP-box); CC the interaction is direct and essential for the suppression of telomere CC fragility (PubMed:24115439). Interacts with FAM111A (via PIP-box); the CC interaction is direct and required for PCNA loading on chromatin CC binding (PubMed:24561620). Interacts with LIG1 (PubMed:24911150). CC Interacts with SETMAR (PubMed:20457750). Interacts with ANKRD17 CC (PubMed:23711367). Interacts with FBXO18/FBH1 (via PIP-box); the CC interaction recruits the DCX(DTL) complex and promotes ubiquitination CC and degradation of FBXO18/FBH1 (PubMed:23677613). Interacts with POLN CC (PubMed:19995904). Interacts with SDE2 (via PIP-box); the interaction CC is direct and prevents ultraviolet light induced monoubiquitination CC (PubMed:27906959). Component of the replisome complex composed of at CC least DONSON, MCM2, MCM7, PCNA and TICRR; interaction at least with CC PCNA occurs during DNA replication (PubMed:28191891). Interacts with CC MAPK15; the interaction is chromatin binding dependent and prevents CC MDM2-mediated PCNA destruction by inhibiting the association of PCNA CC with MDM2 (PubMed:20733054). Interacts with PARP10 (via PIP-box) CC (PubMed:24695737). Interacts with DDI2 (PubMed:29290612). Interacts CC with HMCES (via PIP-box) (PubMed:30554877). Interacts with TRAIP (via CC PIP-box) (PubMed:27462463, PubMed:26711499). Interacts with UHRF2 CC (PubMed:28951215). Interacts with ALKBH2; this interaction is enhanced CC during the S-phase of the cell cycle. Interacts with ATAD5; the CC interaction promotes USP1-mediated PCNA deubiquitination CC (PubMed:20147293). {ECO:0000250|UniProtKB:P04961, CC ECO:0000250|UniProtKB:P17918, ECO:0000269|PubMed:11376153, CC ECO:0000269|PubMed:11595739, ECO:0000269|PubMed:11784855, CC ECO:0000269|PubMed:12522211, ECO:0000269|PubMed:12786946, CC ECO:0000269|PubMed:15149598, ECO:0000269|PubMed:15225546, CC ECO:0000269|PubMed:15543136, ECO:0000269|PubMed:15616578, CC ECO:0000269|PubMed:16510448, ECO:0000269|PubMed:16949367, CC ECO:0000269|PubMed:17115032, ECO:0000269|PubMed:17130289, CC ECO:0000269|PubMed:18316726, ECO:0000269|PubMed:18499658, CC ECO:0000269|PubMed:18703516, ECO:0000269|PubMed:18719106, CC ECO:0000269|PubMed:18794347, ECO:0000269|PubMed:19419956, CC ECO:0000269|PubMed:19443450, ECO:0000269|PubMed:19995904, CC ECO:0000269|PubMed:20147293, ECO:0000269|PubMed:20457750, CC ECO:0000269|PubMed:20733054, ECO:0000269|PubMed:21549307, CC ECO:0000269|PubMed:21628590, ECO:0000269|PubMed:22148433, CC ECO:0000269|PubMed:22153967, ECO:0000269|PubMed:22634751, CC ECO:0000269|PubMed:22681887, ECO:0000269|PubMed:22704558, CC ECO:0000269|PubMed:22705370, ECO:0000269|PubMed:22759634, CC ECO:0000269|PubMed:23000965, ECO:0000269|PubMed:23677613, CC ECO:0000269|PubMed:23711367, ECO:0000269|PubMed:24115439, CC ECO:0000269|PubMed:24561620, ECO:0000269|PubMed:24695737, CC ECO:0000269|PubMed:24911150, ECO:0000269|PubMed:24939902, CC ECO:0000269|PubMed:26408825, ECO:0000269|PubMed:27084448, CC ECO:0000269|PubMed:27462463, ECO:0000269|PubMed:27906959, CC ECO:0000269|PubMed:28191891, ECO:0000269|PubMed:29290612, CC ECO:0000269|PubMed:30554877, ECO:0000269|PubMed:9302295, CC ECO:0000269|PubMed:9305916, ECO:0000269|PubMed:9566895}. CC -!- SUBUNIT: (Microbial infection) Interacts with herpes virus 8 protein CC LANA1. {ECO:0000269|PubMed:26223641}. CC -!- INTERACTION: CC P12004; P04075: ALDOA; NbExp=3; IntAct=EBI-358311, EBI-709613; CC P12004; P03950: ANG; NbExp=4; IntAct=EBI-358311, EBI-525291; CC P12004; P07355: ANXA2; NbExp=2; IntAct=EBI-358311, EBI-352622; CC P12004; P61769: B2M; NbExp=3; IntAct=EBI-358311, EBI-714718; CC P12004; P38936: CDKN1A; NbExp=37; IntAct=EBI-358311, EBI-375077; CC P12004; P42771: CDKN2A; NbExp=8; IntAct=EBI-358311, EBI-375053; CC P12004; Q9H211: CDT1; NbExp=2; IntAct=EBI-358311, EBI-456953; CC P12004; Q13111: CHAF1A; NbExp=4; IntAct=EBI-358311, EBI-1020839; CC P12004; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-358311, EBI-11522780; CC P12004; P68104: EEF1A1; NbExp=2; IntAct=EBI-358311, EBI-352162; CC P12004; P06733: ENO1; NbExp=3; IntAct=EBI-358311, EBI-353877; CC P12004; P39748: FEN1; NbExp=19; IntAct=EBI-358311, EBI-707816; CC P12004; P04406: GAPDH; NbExp=3; IntAct=EBI-358311, EBI-354056; CC P12004; Q14527: HLTF; NbExp=2; IntAct=EBI-358311, EBI-1045161; CC P12004; Q9H160: ING2; NbExp=3; IntAct=EBI-358311, EBI-389787; CC P12004; Q9H063: MAF1; NbExp=4; IntAct=EBI-358311, EBI-720354; CC P12004; P20585: MSH3; NbExp=6; IntAct=EBI-358311, EBI-1164205; CC P12004; O95944: NCR2; NbExp=7; IntAct=EBI-358311, EBI-14058375; CC P12004; P61970: NUTF2; NbExp=3; IntAct=EBI-358311, EBI-591778; CC P12004; Q15004: PCLAF; NbExp=5; IntAct=EBI-358311, EBI-10971436; CC P12004; P12004: PCNA; NbExp=11; IntAct=EBI-358311, EBI-358311; CC P12004; P18669: PGAM1; NbExp=2; IntAct=EBI-358311, EBI-717905; CC P12004; P00558: PGK1; NbExp=2; IntAct=EBI-358311, EBI-709599; CC P12004; P28340: POLD1; NbExp=3; IntAct=EBI-358311, EBI-716569; CC P12004; P49005: POLD2; NbExp=3; IntAct=EBI-358311, EBI-372354; CC P12004; Q15054: POLD3; NbExp=7; IntAct=EBI-358311, EBI-864956; CC P12004; Q9HCU8: POLD4; NbExp=4; IntAct=EBI-358311, EBI-864968; CC P12004; P30041: PRDX6; NbExp=2; IntAct=EBI-358311, EBI-2255129; CC P12004; Q9UBF6: RNF7; NbExp=3; IntAct=EBI-358311, EBI-398632; CC P12004; Q86TU7: SETD3; NbExp=3; IntAct=EBI-358311, EBI-2908049; CC P12004; Q8IWU4: SLC30A8; NbExp=3; IntAct=EBI-358311, EBI-10262251; CC P12004; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-358311, EBI-742688; CC P12004; A2RU14: TMEM218; NbExp=4; IntAct=EBI-358311, EBI-10173151; CC P12004; P60174: TPI1; NbExp=2; IntAct=EBI-358311, EBI-717475; CC P12004; Q5FWF4: ZRANB3; NbExp=8; IntAct=EBI-358311, EBI-13954615; CC P12004; Q8TE30; NbExp=6; IntAct=EBI-358311, EBI-8874509; CC P12004; Q9Z111: Gadd45g; Xeno; NbExp=9; IntAct=EBI-358311, EBI-1173616; CC P12004; Q1K9H5: PB1; Xeno; NbExp=2; IntAct=EBI-358311, EBI-6050669; CC P12004; B4URF7: PB2; Xeno; NbExp=2; IntAct=EBI-358311, EBI-6050648; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15543136, CC ECO:0000269|PubMed:24115439, ECO:0000269|PubMed:24939902}. CC Note=Colocalizes with CREBBP, EP300 and POLD1 to sites of DNA damage CC (PubMed:24939902). Forms nuclear foci representing sites of ongoing DNA CC replication and vary in morphology and number during S phase CC (PubMed:15543136). Co-localizes with SMARCA5/SNF2H and BAZ1B/WSTF at CC replication foci during S phase (PubMed:15543136). Together with APEX2, CC is redistributed in discrete nuclear foci in presence of oxidative DNA CC damaging agents. {ECO:0000269|PubMed:15543136, CC ECO:0000269|PubMed:24939902}. CC -!- PTM: Phosphorylated. Phosphorylation at Tyr-211 by EGFR stabilizes CC chromatin-associated PCNA. {ECO:0000269|PubMed:17115032}. CC -!- PTM: Acetylated by CREBBP and p300/EP300; preferentially acetylated by CC CREBBP on Lys-80, Lys-13 and Lys-14 and on Lys-77 by p300/EP300 upon CC loading on chromatin in response to UV irradiation (PubMed:24939902, CC PubMed:19419956). Lysine acetylation disrupts association with CC chromatin, hence promoting PCNA ubiquitination and proteasomal CC degradation in response to UV damage in a CREBBP- and EP300-dependent CC manner (PubMed:24939902). Acetylation disrupts interaction with NUDT15 CC and promotes degradation (PubMed:19419956). CC {ECO:0000269|PubMed:24939902}. CC -!- PTM: Ubiquitinated (PubMed:24939902, PubMed:20227374). Following DNA CC damage, can be either monoubiquitinated to stimulate direct bypass of CC DNA lesions by specialized DNA polymerases or polyubiquitinated to CC promote recombination-dependent DNA synthesis across DNA lesions by CC template switching mechanisms. Following induction of replication CC stress, monoubiquitinated by the UBE2B-RAD18 complex on Lys-164, CC leading to recruit translesion (TLS) polymerases, which are able to CC synthesize across DNA lesions in a potentially error-prone manner. An CC error-free pathway also exists and requires non-canonical CC polyubiquitination on Lys-164 through 'Lys-63' linkage of ubiquitin CC moieties by the E2 complex UBE2N-UBE2V2 and the E3 ligases, HLTF, RNF8 CC and SHPRH. This error-free pathway, also known as template switching, CC employs recombination mechanisms to synthesize across the lesion, using CC as a template the undamaged, newly synthesized strand of the sister CC chromatid. Monoubiquitination at Lys-164 also takes place in undamaged CC proliferating cells, and is mediated by the DCX(DTL) complex, leading CC to enhance PCNA-dependent translesion DNA synthesis. Sumoylated during CC S phase. {ECO:0000269|PubMed:15149598, ECO:0000269|PubMed:17108083, CC ECO:0000269|PubMed:17130289, ECO:0000269|PubMed:18316726, CC ECO:0000269|PubMed:18719106, ECO:0000269|PubMed:18948756, CC ECO:0000269|PubMed:20129063, ECO:0000269|PubMed:20227374, CC ECO:0000269|PubMed:22153967, ECO:0000269|PubMed:24939902}. CC -!- PTM: Methylated on glutamate residues by ARMT1/C6orf211. CC {ECO:0000269|PubMed:25732820}. CC -!- DISEASE: Ataxia-telangiectasia-like disorder 2 (ATLD2) [MIM:615919]: A CC neurodegenerative disorder due to defects in DNA excision repair. ATLD2 CC is characterized by developmental delay, ataxia, sensorineural hearing CC loss, short stature, cutaneous and ocular telangiectasia, and CC photosensitivity. {ECO:0000269|PubMed:24911150}. Note=The disease is CC caused by variants affecting the gene represented in this entry. CC -!- MISCELLANEOUS: Antibodies against PCNA are present in sera from CC patients with systemic lupus erythematosus. CC -!- SIMILARITY: Belongs to the PCNA family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/pcna/"; CC -!- WEB RESOURCE: Name=Wikipedia; Note=PCNA entry; CC URL="https://en.wikipedia.org/wiki/PCNA"; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/PCNAID41670ch20p12.html"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M15796; AAA35736.1; -; mRNA. DR EMBL; J04718; AAA60040.1; -; Genomic_DNA. DR EMBL; AF527838; AAM78556.1; -; Genomic_DNA. DR EMBL; AK313286; BAG36094.1; -; mRNA. DR EMBL; AL121924; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471133; EAX10428.1; -; Genomic_DNA. DR EMBL; CH471133; EAX10429.1; -; Genomic_DNA. DR EMBL; CH471133; EAX10430.1; -; Genomic_DNA. DR EMBL; BC000491; AAH00491.1; -; mRNA. DR EMBL; BC062439; AAH62439.1; -; mRNA. DR CCDS; CCDS13087.1; -. DR PIR; A27445; WMHUET. DR RefSeq; NP_002583.1; NM_002592.2. DR RefSeq; NP_872590.1; NM_182649.1. DR PDB; 1AXC; X-ray; 2.60 A; A/C/E=1-261. DR PDB; 1U76; X-ray; 2.60 A; A/C/E=1-261. DR PDB; 1U7B; X-ray; 1.88 A; A=1-261. DR PDB; 1UL1; X-ray; 2.90 A; A/B/C=1-261. DR PDB; 1VYJ; X-ray; 2.80 A; A/C/E/G/I/K=1-261. DR PDB; 1VYM; X-ray; 2.30 A; A/B/C=1-261. DR PDB; 1W60; X-ray; 3.15 A; A/B=1-261. DR PDB; 2ZVK; X-ray; 2.70 A; A/B/C=1-261. DR PDB; 2ZVL; X-ray; 2.50 A; A/B/C/D/E/F=1-261. DR PDB; 2ZVM; X-ray; 2.30 A; A/B/C=1-261. DR PDB; 3JA9; EM; 22.00 A; A/B/C=1-261. DR PDB; 3P87; X-ray; 2.99 A; A/B/C/D/E/F=1-261. DR PDB; 3TBL; X-ray; 2.90 A; A/B/C=1-261. DR PDB; 3VKX; X-ray; 2.10 A; A=1-261. DR PDB; 3WGW; X-ray; 2.80 A; A/B=1-261. DR PDB; 4D2G; X-ray; 2.65 A; A/B/C=1-261. DR PDB; 4RJF; X-ray; 2.01 A; A/C/E=1-261. DR PDB; 4ZTD; X-ray; 2.20 A; A/B/C=2-254. DR PDB; 5E0T; X-ray; 2.67 A; A/B/C=1-261. DR PDB; 5E0U; X-ray; 1.93 A; A/B/C=1-261. DR PDB; 5E0V; X-ray; 2.07 A; A/B=1-261. DR PDB; 5IY4; X-ray; 2.94 A; A/C/E=1-261. DR PDB; 5MAV; X-ray; 2.58 A; A/B/C/D/E/F=1-261. DR PDB; 5MLO; X-ray; 1.96 A; A/C/E=1-261. DR PDB; 5MLW; X-ray; 2.45 A; A/C/E=1-261. DR PDB; 5MOM; X-ray; 2.27 A; A/B/C=1-258. DR PDB; 5YCO; X-ray; 2.20 A; A/B/C/D=1-261. DR PDB; 5YD8; X-ray; 2.30 A; X/Y/Z=1-261. DR PDB; 6CBI; X-ray; 2.75 A; A/B/C/D/E/F=1-261. DR PDB; 6EHT; X-ray; 3.20 A; A/B=1-254, C=1-255. DR PDB; 6FCM; X-ray; 2.80 A; A/C/E=1-261. DR PDB; 6FCN; X-ray; 3.22 A; A/C/E=1-261. DR PDB; 6GIS; X-ray; 2.82 A; A/B/C=1-261. DR PDB; 6GWS; X-ray; 2.90 A; A/B/C=1-261. DR PDB; 6HVO; X-ray; 2.10 A; A/B/C=1-261. DR PDB; 6K3A; X-ray; 2.30 A; A/C/E=1-261. DR PDB; 6QC0; X-ray; 3.50 A; A/C/E=1-261. DR PDB; 6QCG; X-ray; 3.40 A; A/B/C/D/E/F=1-261. DR PDB; 6S1M; EM; 4.27 A; E/F/G=1-261. DR PDB; 6S1N; EM; 4.86 A; E/F/G=1-261. DR PDB; 6S1O; EM; 8.10 A; E/F/G=1-261. DR PDB; 6TNY; EM; 3.08 A; E/F/G=1-261. DR PDB; 6TNZ; EM; 4.05 A; E/F/G=1-261. DR PDB; 6VVO; EM; 3.40 A; F/G/H=1-261. DR PDB; 7EFA; X-ray; 2.70 A; A=1-261. DR PDB; 7KQ0; X-ray; 2.40 A; A/C/E=1-259. DR PDB; 7KQ1; X-ray; 3.30 A; A/C/E=1-259. DR PDB; 7M5L; X-ray; 3.00 A; A/B/C=1-258. DR PDB; 7M5M; X-ray; 3.00 A; A/B/C=1-259. DR PDB; 7M5N; X-ray; 3.11 A; A/B/C=1-259. DR PDB; 7NV0; EM; 3.40 A; B/C/D=1-261. DR PDB; 7NV1; EM; 6.40 A; B/C/D=1-261. DR PDBsum; 1AXC; -. DR PDBsum; 1U76; -. DR PDBsum; 1U7B; -. DR PDBsum; 1UL1; -. DR PDBsum; 1VYJ; -. DR PDBsum; 1VYM; -. DR PDBsum; 1W60; -. DR PDBsum; 2ZVK; -. DR PDBsum; 2ZVL; -. DR PDBsum; 2ZVM; -. DR PDBsum; 3JA9; -. DR PDBsum; 3P87; -. DR PDBsum; 3TBL; -. DR PDBsum; 3VKX; -. DR PDBsum; 3WGW; -. DR PDBsum; 4D2G; -. DR PDBsum; 4RJF; -. DR PDBsum; 4ZTD; -. DR PDBsum; 5E0T; -. DR PDBsum; 5E0U; -. DR PDBsum; 5E0V; -. DR PDBsum; 5IY4; -. DR PDBsum; 5MAV; -. DR PDBsum; 5MLO; -. DR PDBsum; 5MLW; -. DR PDBsum; 5MOM; -. DR PDBsum; 5YCO; -. DR PDBsum; 5YD8; -. DR PDBsum; 6CBI; -. DR PDBsum; 6EHT; -. DR PDBsum; 6FCM; -. DR PDBsum; 6FCN; -. DR PDBsum; 6GIS; -. DR PDBsum; 6GWS; -. DR PDBsum; 6HVO; -. DR PDBsum; 6K3A; -. DR PDBsum; 6QC0; -. DR PDBsum; 6QCG; -. DR PDBsum; 6S1M; -. DR PDBsum; 6S1N; -. DR PDBsum; 6S1O; -. DR PDBsum; 6TNY; -. DR PDBsum; 6TNZ; -. DR PDBsum; 6VVO; -. DR PDBsum; 7EFA; -. DR PDBsum; 7KQ0; -. DR PDBsum; 7KQ1; -. DR PDBsum; 7M5L; -. DR PDBsum; 7M5M; -. DR PDBsum; 7M5N; -. DR PDBsum; 7NV0; -. DR PDBsum; 7NV1; -. DR AlphaFoldDB; P12004; -. DR BMRB; P12004; -. DR SASBDB; P12004; -. DR SMR; P12004; -. DR BioGRID; 111142; 469. DR ComplexPortal; CPX-538; PCNA homotrimer. DR CORUM; P12004; -. DR DIP; DIP-1098N; -. DR ELM; P12004; -. DR IntAct; P12004; 433. DR MINT; P12004; -. DR STRING; 9606.ENSP00000368458; -. DR BindingDB; P12004; -. DR ChEMBL; CHEMBL2346488; -. DR DrugBank; DB00945; Acetylsalicylic acid. DR DrugBank; DB00279; Liothyronine. DR DrugCentral; P12004; -. DR MoonDB; P12004; Predicted. DR GlyGen; P12004; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P12004; -. DR MetOSite; P12004; -. DR PhosphoSitePlus; P12004; -. DR SwissPalm; P12004; -. DR BioMuta; PCNA; -. DR DMDM; 129694; -. DR SWISS-2DPAGE; P12004; -. DR CPTAC; CPTAC-1224; -. DR CPTAC; CPTAC-1225; -. DR CPTAC; CPTAC-3242; -. DR CPTAC; CPTAC-3243; -. DR CPTAC; CPTAC-3244; -. DR CPTAC; CPTAC-3245; -. DR CPTAC; CPTAC-558; -. DR CPTAC; CPTAC-559; -. DR CPTAC; CPTAC-722; -. DR EPD; P12004; -. DR jPOST; P12004; -. DR MassIVE; P12004; -. DR MaxQB; P12004; -. DR PaxDb; P12004; -. DR PeptideAtlas; P12004; -. DR ProteomicsDB; 52816; -. DR TopDownProteomics; P12004; -. DR ABCD; P12004; 1 sequenced antibody. DR Antibodypedia; 3769; 2661 antibodies from 53 providers. DR CPTC; P12004; 4 antibodies. DR DNASU; 5111; -. DR Ensembl; ENST00000379143.10; ENSP00000368438.5; ENSG00000132646.11. DR Ensembl; ENST00000379160.3; ENSP00000368458.3; ENSG00000132646.11. DR GeneID; 5111; -. DR KEGG; hsa:5111; -. DR MANE-Select; ENST00000379143.10; ENSP00000368438.5; NM_182649.2; NP_872590.1. DR UCSC; uc002wlp.4; human. DR CTD; 5111; -. DR DisGeNET; 5111; -. DR GeneCards; PCNA; -. DR HGNC; HGNC:8729; PCNA. DR HPA; ENSG00000132646; Tissue enhanced (bone). DR MalaCards; PCNA; -. DR MIM; 176740; gene. DR MIM; 615919; phenotype. DR neXtProt; NX_P12004; -. DR OpenTargets; ENSG00000132646; -. DR Orphanet; 438134; PCNA-related progressive neurodegenerative photosensitivity syndrome. DR PharmGKB; PA263; -. DR VEuPathDB; HostDB:ENSG00000132646; -. DR eggNOG; KOG1636; Eukaryota. DR GeneTree; ENSGT00390000004965; -. DR HOGENOM; CLU_043978_3_0_1; -. DR InParanoid; P12004; -. DR OMA; EMKLINM; -. DR OrthoDB; 1012066at2759; -. DR PhylomeDB; P12004; -. DR TreeFam; TF313441; -. DR PathwayCommons; P12004; -. DR Reactome; R-HSA-110312; Translesion synthesis by REV1. DR Reactome; R-HSA-110314; Recognition of DNA damage by PCNA-containing replication complex. DR Reactome; R-HSA-110320; Translesion Synthesis by POLH. DR Reactome; R-HSA-1362277; Transcription of E2F targets under negative control by DREAM complex. DR Reactome; R-HSA-174411; Polymerase switching on the C-strand of the telomere. DR Reactome; R-HSA-174414; Processive synthesis on the C-strand of the telomere. DR Reactome; R-HSA-174417; Telomere C-strand (Lagging Strand) Synthesis. DR Reactome; R-HSA-174437; Removal of the Flap Intermediate from the C-strand. DR Reactome; R-HSA-4615885; SUMOylation of DNA replication proteins. DR Reactome; R-HSA-5358565; Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha). DR Reactome; R-HSA-5358606; Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta). DR Reactome; R-HSA-5651801; PCNA-Dependent Long Patch Base Excision Repair. DR Reactome; R-HSA-5655862; Translesion synthesis by POLK. DR Reactome; R-HSA-5656121; Translesion synthesis by POLI. DR Reactome; R-HSA-5656169; Termination of translesion DNA synthesis. DR Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR). DR Reactome; R-HSA-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER. DR Reactome; R-HSA-5696400; Dual Incision in GG-NER. DR Reactome; R-HSA-6782135; Dual incision in TC-NER. DR Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER. DR Reactome; R-HSA-6804114; TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest. DR Reactome; R-HSA-69091; Polymerase switching. DR Reactome; R-HSA-69166; Removal of the Flap Intermediate. DR Reactome; R-HSA-69183; Processive synthesis on the lagging strand. DR Reactome; R-HSA-69205; G1/S-Specific Transcription. DR Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins. DR SignaLink; P12004; -. DR SIGNOR; P12004; -. DR BioGRID-ORCS; 5111; 828 hits in 1071 CRISPR screens. DR ChiTaRS; PCNA; human. DR EvolutionaryTrace; P12004; -. DR GeneWiki; Proliferating_cell_nuclear_antigen; -. DR GenomeRNAi; 5111; -. DR Pharos; P12004; Tchem. DR PRO; PR:P12004; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; P12004; protein. DR Bgee; ENSG00000132646; Expressed in oocyte and 196 other tissues. DR Genevisible; P12004; HS. DR GO; GO:0005813; C:centrosome; IDA:MGI. DR GO; GO:0000785; C:chromatin; IDA:UniProtKB. DR GO; GO:0000781; C:chromosome, telomeric region; HDA:BHF-UCL. DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IEA:Ensembl. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0005652; C:nuclear lamina; IEA:Ensembl. DR GO; GO:0043596; C:nuclear replication fork; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0043626; C:PCNA complex; IDA:UniProtKB. DR GO; GO:0070557; C:PCNA-p21 complex; IDA:UniProtKB. DR GO; GO:0005657; C:replication fork; IDA:MGI. DR GO; GO:0030894; C:replisome; TAS:BHF-UCL. DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB. DR GO; GO:0003684; F:damaged DNA binding; IDA:UniProtKB. DR GO; GO:0032139; F:dinucleotide insertion or deletion binding; IDA:BHF-UCL. DR GO; GO:0070182; F:DNA polymerase binding; IPI:UniProtKB. DR GO; GO:0030337; F:DNA polymerase processivity factor activity; IBA:GO_Central. DR GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL. DR GO; GO:0035035; F:histone acetyltransferase binding; IPI:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0032405; F:MutLalpha complex binding; IDA:HGNC-UCL. DR GO; GO:0030331; F:nuclear estrogen receptor binding; IEA:Ensembl. DR GO; GO:0008022; F:protein C-terminus binding; IMP:UniProtKB. DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB. DR GO; GO:0000701; F:purine-specific mismatch base pair DNA N-glycosylase activity; IDA:BHF-UCL. DR GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:UniProtKB. DR GO; GO:0006287; P:base-excision repair, gap-filling; IEA:Ensembl. DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl. DR GO; GO:0034644; P:cellular response to UV; IDA:UniProtKB. DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl. DR GO; GO:0030855; P:epithelial cell differentiation; IEP:UniProtKB. DR GO; GO:0044849; P:estrous cycle; IEA:Ensembl. DR GO; GO:0007507; P:heart development; IEA:Ensembl. DR GO; GO:0006272; P:leading strand elongation; IBA:GO_Central. DR GO; GO:0097421; P:liver regeneration; IEA:Ensembl. DR GO; GO:0006298; P:mismatch repair; IDA:BHF-UCL. DR GO; GO:1902990; P:mitotic telomere maintenance via semi-conservative replication; ISS:BHF-UCL. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl. DR GO; GO:0032077; P:positive regulation of deoxyribonuclease activity; IDA:UniProtKB. DR GO; GO:0045739; P:positive regulation of DNA repair; IMP:UniProtKB. DR GO; GO:0045740; P:positive regulation of DNA replication; IMP:UniProtKB. DR GO; GO:1900264; P:positive regulation of DNA-directed DNA polymerase activity; IMP:UniProtKB. DR GO; GO:0031297; P:replication fork processing; ISS:BHF-UCL. DR GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl. DR GO; GO:0071548; P:response to dexamethasone; IEA:Ensembl. DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl. DR GO; GO:1902065; P:response to L-glutamate; IEA:Ensembl. DR GO; GO:0019985; P:translesion synthesis; IDA:UniProtKB. DR HAMAP; MF_00317; DNApol_clamp_arch; 1. DR IDEAL; IID00022; -. DR InterPro; IPR000730; Pr_cel_nuc_antig. DR InterPro; IPR022649; Pr_cel_nuc_antig_C. DR InterPro; IPR022659; Pr_cel_nuc_antig_CS. DR InterPro; IPR022648; Pr_cel_nuc_antig_N. DR Pfam; PF02747; PCNA_C; 1. DR Pfam; PF00705; PCNA_N; 1. DR PRINTS; PR00339; PCNACYCLIN. DR TIGRFAMs; TIGR00590; pcna; 1. DR PROSITE; PS01251; PCNA_1; 1. DR PROSITE; PS00293; PCNA_2; 1. DR AGR; HGNC:8729; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Deafness; Direct protein sequencing; KW Disease variant; DNA damage; DNA repair; DNA replication; DNA-binding; KW Dwarfism; Host-virus interaction; Isopeptide bond; Methylation; KW Neurodegeneration; Nucleus; Phosphoprotein; Reference proteome; KW Ubl conjugation. FT CHAIN 1..261 FT /note="Proliferating cell nuclear antigen" FT /id="PRO_0000149158" FT DNA_BIND 61..80 FT /evidence="ECO:0000255" FT REGION 7..100 FT /note="Interaction with NUDT15" FT /evidence="ECO:0000269|PubMed:19419956" FT MOD_RES 14 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:19419956" FT MOD_RES 77 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 80 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 211 FT /note="Phosphotyrosine; by EGFR" FT /evidence="ECO:0000269|PubMed:17115032" FT MOD_RES 248 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT CROSSLNK 164 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25114211, FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 164 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin); alternate" FT /evidence="ECO:0000269|PubMed:17108083, FT ECO:0000269|PubMed:17130289" FT CROSSLNK 254 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VARIANT 228 FT /note="S -> I (in ATLD2; a hypomorphic mutation affecting FT DNA repair in response to UV; results in significantly FT decreased interaction with FEN1, LIG1 and ERCC5; FT dbSNP:rs369958038)" FT /evidence="ECO:0000269|PubMed:24911150" FT /id="VAR_071871" FT MUTAGEN 13 FT /note="K->R: Inhibits acetylation, recruitment to DNA FT damage sites, inducible ubiquitination and protein FT degradation, DNA replication and repair synthesis FT efficiencies, but homotrimer formation, nuclear recruitment FT to DNA damage sites, interactions with CREBBP, EP300 and FT POLD1 are similar as the wild-type; in association with FT R-14; R-20; R-77 and R-80." FT /evidence="ECO:0000269|PubMed:24939902" FT MUTAGEN 14 FT /note="K->R: Inhibits acetylation, recruitment to DNA FT damage sites, inducible ubiquitination and protein FT degradation, DNA replication and repair synthesis FT efficiencies, but homotrimer formation, nuclear recruitment FT to DNA damage sites, interactions with CREBBP, EP300 and FT POLD1 are similar as the wild-type; in association with FT R-13; R-20; R-77 and R-80." FT /evidence="ECO:0000269|PubMed:24939902" FT MUTAGEN 20 FT /note="K->R: Inhibits acetylation, recruitment to DNA FT damage sites, inducible ubiquitination and protein FT degradation, DNA replication and repair synthesis FT efficiencies, but homotrimer formation, nuclear recruitment FT to DNA damage sites, interactions with CREBBP, EP300 and FT POLD1 are similar as the wild-type; in association with FT R-13; R-14; R-77 and R-80." FT /evidence="ECO:0000269|PubMed:24939902" FT MUTAGEN 40 FT /note="M->A: Complete loss of interaction with UHRF2." FT /evidence="ECO:0000269|PubMed:11595739" FT MUTAGEN 43..45 FT /note="SHV->AAA: No effect on POLD3-binding. Impairs FT binding to ALKBH2." FT /evidence="ECO:0000269|PubMed:11595739, FT ECO:0000269|PubMed:26408825" FT MUTAGEN 77 FT /note="K->A: Inhibits recruitment to DNA damage sites, but FT nuclear localization is similar as the wild-type; in FT association with A-80." FT /evidence="ECO:0000269|PubMed:24939902" FT MUTAGEN 77 FT /note="K->R: Inhibits acetylation, recruitment to DNA FT damage sites, inducible ubiquitination and protein FT degradation, DNA replication and repair synthesis FT efficiencies, but homotrimer formation, nuclear recruitment FT to DNA damage sites, interactions with CREBBP, EP300 and FT POLD1 are similar as the wild-type; in association with FT R-13; R-14; R-20 and R-80." FT /evidence="ECO:0000269|PubMed:24939902" FT MUTAGEN 80 FT /note="K->A: Inhibits recruitment to DNA damage sites, but FT nuclear localization is similar as the wild-type; in FT association with A-77." FT /evidence="ECO:0000269|PubMed:24939902" FT MUTAGEN 80 FT /note="K->R: Inhibits acetylation, recruitment to DNA FT damage sites, inducible ubiquitination and protein FT degradation, DNA replication and repair synthesis FT efficiencies, but homotrimer formation, nuclear recruitment FT to DNA damage sites, interactions with CREBBP, EP300 and FT POLD1 are similar as the wild-type; in association with FT R-13; R-14; R-20 and R-77." FT /evidence="ECO:0000269|PubMed:24939902" FT MUTAGEN 125..128 FT /note="QLGI->AAAA: Strong decrease in POLD3-binding. FT Impairs binding to ALKBH2." FT /evidence="ECO:0000269|PubMed:11595739, FT ECO:0000269|PubMed:26408825" FT MUTAGEN 128 FT /note="I->A: Complete loss of interaction with UHRF2." FT /evidence="ECO:0000269|PubMed:11595739" FT MUTAGEN 164 FT /note="K->R: Abolishes ubiquitination. No effect on FT interaction with SHPRH." FT /evidence="ECO:0000269|PubMed:17108083, FT ECO:0000269|PubMed:17130289, ECO:0000269|PubMed:18719106, FT ECO:0000269|PubMed:20129063" FT MUTAGEN 188..190 FT /note="VDK->AAA: No effect on POLD3-binding. No effect on FT ALKBH2-binding." FT /evidence="ECO:0000269|PubMed:11595739, FT ECO:0000269|PubMed:26408825" FT MUTAGEN 211 FT /note="Y->F: Alters chromatin-associated PCNA stability and FT its function in DNA replication and repair." FT /evidence="ECO:0000269|PubMed:17115032" FT MUTAGEN 250 FT /note="Y->A: Complete loss of interaction with UHRF2." FT /evidence="ECO:0000269|PubMed:11595739" FT MUTAGEN 251..254 FT /note="LAPK->AAAA: Decrease in POLD3-binding." FT /evidence="ECO:0000269|PubMed:11595739" FT MUTAGEN 252 FT /note="A->G: Complete loss of interaction with UHRF2." FT /evidence="ECO:0000269|PubMed:11595739" FT STRAND 2..7 FT /evidence="ECO:0007829|PDB:1U7B" FT HELIX 10..20 FT /evidence="ECO:0007829|PDB:1U7B" FT STRAND 24..31 FT /evidence="ECO:0007829|PDB:1U7B" FT STRAND 34..40 FT /evidence="ECO:0007829|PDB:1U7B" FT STRAND 44..53 FT /evidence="ECO:0007829|PDB:1U7B" FT HELIX 54..56 FT /evidence="ECO:0007829|PDB:1U7B" FT STRAND 57..64 FT /evidence="ECO:0007829|PDB:1U7B" FT STRAND 66..71 FT /evidence="ECO:0007829|PDB:1U7B" FT HELIX 72..79 FT /evidence="ECO:0007829|PDB:1U7B" FT STRAND 87..92 FT /evidence="ECO:0007829|PDB:1U7B" FT STRAND 94..96 FT /evidence="ECO:0007829|PDB:1VYM" FT STRAND 97..104 FT /evidence="ECO:0007829|PDB:1U7B" FT STRAND 106..109 FT /evidence="ECO:0007829|PDB:4RJF" FT STRAND 111..117 FT /evidence="ECO:0007829|PDB:1U7B" FT STRAND 121..126 FT /evidence="ECO:0007829|PDB:5E0U" FT STRAND 134..140 FT /evidence="ECO:0007829|PDB:1U7B" FT HELIX 141..152 FT /evidence="ECO:0007829|PDB:1U7B" FT STRAND 156..163 FT /evidence="ECO:0007829|PDB:1U7B" FT STRAND 166..173 FT /evidence="ECO:0007829|PDB:1U7B" FT STRAND 176..182 FT /evidence="ECO:0007829|PDB:1U7B" FT HELIX 191..193 FT /evidence="ECO:0007829|PDB:5E0U" FT STRAND 196..201 FT /evidence="ECO:0007829|PDB:1U7B" FT STRAND 203..208 FT /evidence="ECO:0007829|PDB:1U7B" FT HELIX 209..215 FT /evidence="ECO:0007829|PDB:1U7B" FT HELIX 216..221 FT /evidence="ECO:0007829|PDB:1U7B" FT STRAND 223..229 FT /evidence="ECO:0007829|PDB:1U7B" FT STRAND 231..233 FT /evidence="ECO:0007829|PDB:1VYM" FT STRAND 235..241 FT /evidence="ECO:0007829|PDB:1U7B" FT TURN 242..244 FT /evidence="ECO:0007829|PDB:1U7B" FT STRAND 245..251 FT /evidence="ECO:0007829|PDB:1U7B" FT STRAND 254..256 FT /evidence="ECO:0007829|PDB:7KQ1" SQ SEQUENCE 261 AA; 28769 MW; E6F08E7EDBC48B00 CRC64; MFEARLVQGS ILKKVLEALK DLINEACWDI SSSGVNLQSM DSSHVSLVQL TLRSEGFDTY RCDRNLAMGV NLTSMSKILK CAGNEDIITL RAEDNADTLA LVFEAPNQEK VSDYEMKLMD LDVEQLGIPE QEYSCVVKMP SGEFARICRD LSHIGDAVVI SCAKDGVKFS ASGELGNGNI KLSQTSNVDK EEEAVTIEMN EPVQLTFALR YLNFFTKATP LSSTVTLSMS ADVPLVVEYK IADMGHLKYY LAPKIEDEEG S // ID HD_HUMAN Reviewed; 3142 AA. AC P42858; Q9UQB7; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 2. DT 14-DEC-2022, entry version 220. DE RecName: Full=Huntingtin; DE AltName: Full=Huntington disease protein; DE Short=HD protein; DE Contains: DE RecName: Full=Huntingtin, myristoylated N-terminal fragment; GN Name=HTT; Synonyms=HD, IT15; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND INVOLVEMENT IN HD. RC TISSUE=Retina; RX PubMed=8458085; DOI=10.1016/0092-8674(93)90585-e; RA Macdonald M., Ambrose C.M., Duyao M.P., Myers R.H., Lin C.S., Srinidhi J., RA Barnes G., Taylor S.A., James M., Groot N., McFarlane H., Jenkins B., RA Anderson M.A., Wexler N.S., Gusella J.F., Bates G.P., Baxendale S., RA Hummerich H., Kirby S., North M., Youngman S., Mott R., Zehetner G., RA Sedlacek Z., Poustka A., Frischauf A.-M., Lehrach H., Buckler A.J., RA Church D., Doucette-Stamm L., O'Donovan M.C., Riba-Ramirez L., Shah M., RA Stanton V.P., Strobel S.A., Draths K.M., Wales J.L., Dervan P., RA Housman D.E., Altherr M., Shiang R., Thompson L., Fielder T., Wasmuth J.J., RA Tagle D., Valdes J., Elmer L., Allard M., Castilla L., Swaroop M., RA Blanchard K., Collins F.S., Snell R., Holloway T., Gillespie K., Datson N., RA Shaw S., Harper P.S.; RT "A novel gene containing a trinucleotide repeat that is expanded and RT unstable on Huntington's disease chromosomes."; RL Cell 72:971-983(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX PubMed=11013077; DOI=10.1006/geno.2000.6317; RA Matsuyama N., Hadano S., Onoe K., Osuga H., Shouguchi-Miyata J., Gondo Y., RA Ikeda J.-E.; RT "Identification and characterization of the miniature pig Huntington's RT disease gene homolog: evidence for conservation and polymorphism in the CAG RT triplet repeat."; RL Genomics 69:72-85(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-203. RX PubMed=8197474; DOI=10.1007/bf02257483; RA Ambrose C.M., Duyao M.P., Barnes G., Bates G.P., Lin C.S., Srinidhi J., RA Baxendale S., Hummerich H., Lehrach H., Altherr M., Wasmuth J., Buckler A., RA Church D., Housman D., Berks M., Micklem G., Durbin R., Dodge A., Read A., RA Gusella J.F., Macdonald M.E.; RT "Structure and expression of the Huntington's disease gene: evidence RT against simple inactivation due to an expanded CAG repeat."; RL Somat. Cell Mol. Genet. 20:27-38(1994). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-88. RX PubMed=7759106; DOI=10.1016/0888-7543(95)80014-d; RA Lin B., Nasir J., Kalchman M.A., McDonald H., Zeisler J., Goldberg Y.P., RA Hayden M.R.; RT "Structural analysis of the 5' region of mouse and human Huntington disease RT genes reveals conservation of putative promoter region and di- and RT trinucleotide polymorphisms."; RL Genomics 25:707-715(1995). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 2561-3142, AND VARIANT ILE-2786. RC TISSUE=Brain, Caudate nucleus, Frontal cortex, Muscle, and Retina; RX PubMed=7903579; DOI=10.1093/hmg/2.10.1541; RA Lin B., Rommens J.M., Graham R.K., Kalchman M., Macdonald H., Nasir J., RA Delaney A., Goldberg Y.P., Hayden M.R.; RT "Differential 3' polyadenylation of the Huntington disease gene results in RT two mRNA species with variable tissue expression."; RL Hum. Mol. Genet. 2:1541-1545(1993). RN [7] RP SUBCELLULAR LOCATION. RX PubMed=7647777; DOI=10.1038/ng0595-104; RA Trottier Y., Devys D., Imbert G., Saudou F., An I., Lutz Y., Weber C., RA Agid Y., Hirsch E.C., Mandel J.-L.; RT "Cellular localization of the Huntington's disease protein and RT discrimination of the normal and mutated form."; RL Nat. Genet. 10:104-110(1995). RN [8] RP PROTEOLYTIC CLEAVAGE BY CASPASE-3. RX PubMed=8696339; DOI=10.1038/ng0896-442; RA Goldberg Y.P., Nicholson D.W., Rasper D.M., Kalchman M.A., Koide H.B., RA Graham R.K., Bromm M., Kazemi-Esfarjani P., Thornberry N.A., RA Vaillancourt J.P., Hayden M.R.; RT "Cleavage of huntingtin by apopain, a proapoptotic cysteine protease, is RT modulated by the polyglutamine tract."; RL Nat. Genet. 13:442-449(1996). RN [9] RP PROTEOLYTIC CLEAVAGE BY CASPASE-3 AT ASP-511, AND MUTAGENESIS OF ASP-511 RP AND ASP-528. RX PubMed=9535906; DOI=10.1074/jbc.273.15.9158; RA Wellington C.L., Ellerby L.M., Hackam A.S., Margolis R.L., Trifiro M.A., RA Singaraja R., McCutcheon K., Salvesen G.S., Propp S.S., Bromm M., RA Rowland K.J., Zhang T., Rasper D., Roy S., Thornberry N., Pinsky L., RA Kakizuka A., Ross C.A., Nicholson D.W., Bredesen D.E., Hayden M.R.; RT "Caspase cleavage of gene products associated with triplet expansion RT disorders generates truncated fragments containing the polyglutamine RT tract."; RL J. Biol. Chem. 273:9158-9167(1998). RN [10] RP INTERACTION WITH PRPF40A AND SETD2. RX PubMed=9700202; DOI=10.1093/hmg/7.9.1463; RA Faber P.W., Barnes G.T., Srinidhi J., Chen J., Gusella J.F., RA MacDonald M.E.; RT "Huntingtin interacts with a family of WW domain proteins."; RL Hum. Mol. Genet. 7:1463-1474(1998). RN [11] RP INTERACTION WITH PQBP1. RC TISSUE=Brain; RX PubMed=10332029; DOI=10.1093/hmg/8.6.977; RA Waragai M., Lammers C.-H., Takeuchi S., Imafuku I., Udagawa Y., RA Kanazawa I., Kawabata M., Mouradian M.M., Okazawa H.; RT "PQBP-1, a novel polyglutamine tract binding protein, inhibits RT transcription activation by Brn-2 and affects cell survival."; RL Hum. Mol. Genet. 8:977-987(1999). RN [12] RP PROTEOLYTIC CLEAVAGE BY CASPASE-6 AT ASP-584, AND MUTAGENESIS OF ASP-584. RX PubMed=10770929; DOI=10.1074/jbc.m001475200; RA Wellington C.L., Singaraja R., Ellerby L., Savill J., Roy S., Leavitt B., RA Cattaneo E., Hackam A., Sharp A., Thornberry N., Nicholson D.W., RA Bredesen D.E., Hayden M.R.; RT "Inhibiting caspase cleavage of huntingtin reduces toxicity and aggregate RT formation in neuronal and nonneuronal cells."; RL J. Biol. Chem. 275:19831-19838(2000). RN [13] RP INTERACTION WITH SETD2. RX PubMed=10958656; DOI=10.1093/hmg/9.14.2175; RA Passani L.A., Bedford M.T., Faber P.W., McGinnis K.M., Sharp A.H., RA Gusella J.F., Vonsattel J.-P., MacDonald M.E.; RT "Huntingtin's WW domain partners in Huntington's disease post-mortem brain RT fulfill genetic criteria for direct involvement in Huntington's disease RT pathogenesis."; RL Hum. Mol. Genet. 9:2175-2182(2000). RN [14] RP INTERACTION WITH SETD2. RX PubMed=11461154; DOI=10.1006/mcne.2001.1004; RA Rega S., Stiewe T., Chang D.-I., Pollmeier B., Esche H., Bardenheuer W., RA Marquitan G., Puetzer B.M.; RT "Identification of the full-length huntingtin-interacting protein RT p231HBP/HYPB as a DNA-binding factor."; RL Mol. Cell. Neurosci. 18:68-79(2001). RN [15] RP NUCLEAR EXPORT SIGNAL. RX PubMed=12783847; DOI=10.1093/hmg/ddg156; RA Xia J., Lee D.H., Taylor J., Vandelft M., Truant R.; RT "Huntingtin contains a highly conserved nuclear export signal."; RL Hum. Mol. Genet. 12:1393-1403(2003). RN [16] RP INTERACTION WITH TPR, AND SUBCELLULAR LOCATION. RX PubMed=15654337; DOI=10.1038/ng1503; RA Cornett J., Cao F., Wang C.E., Ross C.A., Bates G.P., Li S.H., Li X.J.; RT "Polyglutamine expansion of huntingtin impairs its nuclear export."; RL Nat. Genet. 37:198-204(2005). RN [17] RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=16391387; DOI=10.1385/nmm:7:4:297; RA Sayer J.A., Manczak M., Akileswaran L., Reddy P.H., Coghlan V.M.; RT "Interaction of the nuclear matrix protein NAKAP with HypA and huntingtin: RT implications for nuclear toxicity in Huntington's disease pathogenesis."; RL NeuroMolecular Med. 7:297-310(2005). RN [18] RP SUBCELLULAR LOCATION, SUBUNIT, IDENTIFICATION IN A COMPLEX WITH RP F8A1/F8A2/F8A3 AND RAB5A, AND INTERACTION WITH F8A1/F8A2/F8A3. RX PubMed=16476778; DOI=10.1083/jcb.200509091; RA Pal A., Severin F., Lommer B., Shevchenko A., Zerial M.; RT "Huntingtin-HAP40 complex is a novel Rab5 effector that regulates early RT endosome motility and is up-regulated in Huntington's disease."; RL J. Cell Biol. 172:605-618(2006). RN [19] RP INTERACTION WITH SYVN, AND UBIQUITINATION. RX PubMed=17141218; DOI=10.1016/j.yexcr.2006.10.031; RA Yang H., Zhong X., Ballar P., Luo S., Shen Y., Rubinsztein D.C., RA Monteiro M.J., Fang S.; RT "Ubiquitin ligase Hrd1 enhances the degradation and suppresses the toxicity RT of polyglutamine-expanded huntingtin."; RL Exp. Cell Res. 313:538-550(2007). RN [20] RP PHOSPHORYLATION AT SER-1179 AND SER-1199. RX PubMed=17611284; DOI=10.1523/jneurosci.1831-07.2007; RA Anne S.L., Saudou F., Humbert S.; RT "Phosphorylation of huntingtin by cyclin-dependent kinase 5 is induced by RT DNA damage and regulates wild-type and mutant huntingtin toxicity in RT neurons."; RL J. Neurosci. 27:7318-7328(2007). RN [21] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1870, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [23] RP INTERACTION WITH PFN1. RX PubMed=18573880; DOI=10.1128/mcb.00079-08; RA Shao J., Welch W.J., Diprospero N.A., Diamond M.I.; RT "Phosphorylation of profilin by ROCK1 regulates polyglutamine RT aggregation."; RL Mol. Cell. Biol. 28:5196-5208(2008). RN [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-411; SER-1870 AND SER-1874, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [25] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432 AND SER-1874, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [27] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1870 AND SER-1874, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [28] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [29] RP ACETYLATION AT LYS-9; LYS-176; LYS-234; LYS-343 AND LYS-442. RX PubMed=21685499; DOI=10.1074/mcp.m111.009829; RA Cong X., Held J.M., Degiacomo F., Bonner A., Chen J.M., Schilling B., RA Czerwieniec G.A., Gibson B.W., Ellerby L.M.; RT "Mass spectrometric identification of novel lysine acetylation sites in RT huntingtin."; RL Mol. Cell. Proteomics 0:0-0(2011). RN [30] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [31] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-640; SER-643; SER-1199 AND RP SER-1874, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [32] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [33] RP INTERACTION WITH ZDHHC17 AND ZDHHC13, AND MUTAGENESIS OF ILE-495; GLN-498 RP AND PRO-499. RX PubMed=26198635; DOI=10.1074/jbc.m115.657668; RA Lemonidis K., Sanchez-Perez M.C., Chamberlain L.H.; RT "Identification of a novel sequence motif recognized by the ankyrin repeat RT domain of zDHHC17/13 S-acyltransferases."; RL J. Biol. Chem. 290:21939-21950(2015). RN [34] RP INTERACTION WITH ZDHHC17. RX PubMed=28882895; DOI=10.1074/jbc.m117.799650; RA Lemonidis K., MacLeod R., Baillie G.S., Chamberlain L.H.; RT "Peptide array based screening reveals a large number of proteins RT interacting with the ankyrin repeat domain of the zDHHC17 S- RT acyltransferase."; RL J. Biol. Chem. 292:17190-17202(2017). RN [35] RP INTERACTION WITH ZDHHC17, AND MUTAGENESIS OF 498-GLN-PRO-499. RX PubMed=28757145; DOI=10.1016/j.str.2017.06.018; RA Verardi R., Kim J.S., Ghirlando R., Banerjee A.; RT "Structural basis for substrate recognition by the ankyrin repeat domain of RT human DHHC17 palmitoyltransferase."; RL Structure 0:0-0(2017). RN [36] RP FUNCTION, SUBCELLULAR LOCATION, MYRISTOYLATION AT GLY-551, AND MUTAGENESIS RP OF GLY-551. RX PubMed=24459296; DOI=10.1093/hmg/ddu027; RA Martin D.D., Heit R.J., Yap M.C., Davidson M.W., Hayden M.R., RA Berthiaume L.G.; RT "Identification of a post-translationally myristoylated autophagy-inducing RT domain released by caspase cleavage of huntingtin."; RL Hum. Mol. Genet. 23:3166-3179(2014). RN [37] RP PROTEOLYTIC CLEAVAGE AT ASP-550, MYRISTOYLATION AT GLY-551, MUTAGENESIS OF RP ASP-550 AND GLY-551, AND CHARACTERIZATION OF VARIANT GLU-551. RX PubMed=29802276; DOI=10.1038/s41598-018-25903-w; RA Martin D.D.O., Kay C., Collins J.A., Nguyen Y.T., Slama R.A., Hayden M.R.; RT "A human huntingtin SNP alters post-translational modification and RT pathogenic proteolysis of the protein causing Huntington disease."; RL Sci. Rep. 8:8096-8096(2018). RN [38] {ECO:0007744|PDB:3IO4, ECO:0007744|PDB:3IO6, ECO:0007744|PDB:3IOR, ECO:0007744|PDB:3IOT, ECO:0007744|PDB:3IOU, ECO:0007744|PDB:3IOV, ECO:0007744|PDB:3IOW} RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 1-64, AND DOMAIN. RX PubMed=19748341; DOI=10.1016/j.str.2009.08.002; RA Kim M.W., Chelliah Y., Kim S.W., Otwinowski Z., Bezprozvanny I.; RT "Secondary structure of Huntingtin amino-terminal region."; RL Structure 17:1205-1212(2009). RN [39] {ECO:0007744|PDB:3LRH} RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 5-18. RX PubMed=21968397; DOI=10.1016/j.jmb.2011.09.034; RA Schiefner A., Chatwell L., Korner J., Neumaier I., Colby D.W., Volkmer R., RA Wittrup K.D., Skerra A.; RT "A disulfide-free single-domain V(L) intrabody with blocking activity RT towards huntingtin reveals a novel mode of epitope recognition."; RL J. Mol. Biol. 414:337-355(2011). RN [40] {ECO:0007744|PDB:2LD0, ECO:0007744|PDB:2LD2} RP STRUCTURE BY NMR OF 1-17. RX PubMed=23931318; DOI=10.1016/j.bpj.2013.06.030; RA Michalek M., Salnikov E.S., Bechinger B.; RT "Structure and topology of the huntingtin 1-17 membrane anchor by a RT combined solution and solid-state NMR approach."; RL Biophys. J. 105:699-710(2013). RN [41] {ECO:0007744|PDB:4FE8, ECO:0007744|PDB:4FEB, ECO:0007744|PDB:4FEC, ECO:0007744|PDB:4FED} RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 1-64. RX PubMed=23370273; DOI=10.4161/pri.23807; RA Kim M.; RT "Beta conformation of polyglutamine track revealed by a crystal structure RT of Huntingtin N-terminal region with insertion of three histidine RT residues."; RL Prion 7:221-228(2013). RN [42] {ECO:0007744|PDB:4RAV} RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-17. RX PubMed=25861763; DOI=10.1016/j.jmb.2015.03.021; RA De Genst E., Chirgadze D.Y., Klein F.A., Butler D.C., Matak-Vinkovic D., RA Trottier Y., Huston J.S., Messer A., Dobson C.M.; RT "Structure of a single-chain Fv bound to the 17 N-terminal residues of RT huntingtin provides insights into pathogenic amyloid formation and RT suppression."; RL J. Mol. Biol. 427:2166-2178(2015). RN [43] {ECO:0007744|PDB:6EZ8} RP STRUCTURE BY ELECTRON MICROSCOPY (4.00 ANGSTROMS) IN COMPLEX WITH RP F8A1/F8A2/F8A3, AND INTERACTION WITH F8A1/F8A2/F8A3. RX PubMed=29466333; DOI=10.1038/nature25502; RA Guo Q., Huang B., Cheng J., Seefelder M., Engler T., Pfeifer G., Oeckl P., RA Otto M., Moser F., Maurer M., Pautsch A., Baumeister W., RA Fernandez-Busnadiego R., Kochanek S.; RT "The cryo-electron microscopy structure of huntingtin."; RL Nature 555:117-120(2018). RN [44] RP INVOLVEMENT IN LOMARS, AND VARIANT LOMARS LEU-2717. RX PubMed=27329733; DOI=10.1038/ejhg.2016.74; RA Rodan L.H., Cohen J., Fatemi A., Gillis T., Lucente D., Gusella J., RA Picker J.D.; RT "A novel neurodevelopmental disorder associated with compound heterozygous RT variants in the huntingtin gene."; RL Eur. J. Hum. Genet. 24:1826-1827(2016). RN [45] RP VARIANT LOMARS LEU-703, AND VARIANT MET-1260. RX PubMed=26740508; DOI=10.1136/jmedgenet-2015-103568; RA Lopes F., Barbosa M., Ameur A., Soares G., de Sa J., Dias A.I., RA Oliveira G., Cabral P., Temudo T., Calado E., Cruz I.F., Vieira J.P., RA Oliveira R., Esteves S., Sauer S., Jonasson I., Syvaenen A.C., RA Gyllensten U., Pinto D., Maciel P.; RT "Identification of novel genetic causes of Rett syndrome-like phenotypes."; RL J. Med. Genet. 53:190-199(2016). CC -!- FUNCTION: [Huntingtin]: May play a role in microtubule-mediated CC transport or vesicle function. CC -!- FUNCTION: [Huntingtin, myristoylated N-terminal fragment]: Promotes the CC formation of autophagic vesicles. {ECO:0000269|PubMed:24459296}. CC -!- SUBUNIT: Interacts with PFN1 (PubMed:18573880). Interacts through its CC N-terminus with PRPF40A (PubMed:9700202). Interacts with PQBP1 CC (PubMed:10332029). Interacts with SETD2 (PubMed:9700202, CC PubMed:10958656, PubMed:11461154). Interacts with SH3GLB1 (By CC similarity). Interacts with SYVN (PubMed:17141218). Interacts with TPR; CC the interaction is inhibited by forms of Huntingtin with expanded CC polyglutamine stretch (PubMed:15654337). Interacts with ZDHHC13 (via CC ANK repeats) (PubMed:26198635). Interacts with ZDHHC17 (via ANK CC repeats) (PubMed:26198635, PubMed:28882895, PubMed:28757145). Interacts CC with F8A1/F8A2/F8A3 (PubMed:29466333, PubMed:16476778). Found in a CC complex with F8A1/F8A2/F8A3, HTT and RAB5A; mediates the recruitment of CC HTT by RAB5A (PubMed:16476778). {ECO:0000250|UniProtKB:P42859, CC ECO:0000269|PubMed:10332029, ECO:0000269|PubMed:10958656, CC ECO:0000269|PubMed:11461154, ECO:0000269|PubMed:15654337, CC ECO:0000269|PubMed:16476778, ECO:0000269|PubMed:17141218, CC ECO:0000269|PubMed:18573880, ECO:0000269|PubMed:26198635, CC ECO:0000269|PubMed:28757145, ECO:0000269|PubMed:28882895, CC ECO:0000269|PubMed:29466333, ECO:0000269|PubMed:9700202}. CC -!- INTERACTION: CC P42858; Q9H7C9: AAMDC; NbExp=3; IntAct=EBI-466029, EBI-10308705; CC P42858; Q6PCB6: ABHD17C; NbExp=21; IntAct=EBI-466029, EBI-22011868; CC P42858; Q9ULW3: ABT1; NbExp=9; IntAct=EBI-466029, EBI-2602396; CC P42858; P60709: ACTB; NbExp=3; IntAct=EBI-466029, EBI-353944; CC P42858; P63261: ACTG1; NbExp=16; IntAct=EBI-466029, EBI-351292; CC P42858; P42025: ACTR1B; NbExp=3; IntAct=EBI-466029, EBI-367493; CC P42858; Q15848: ADIPOQ; NbExp=9; IntAct=EBI-466029, EBI-10827839; CC P42858; Q9Y4W6: AFG3L2; NbExp=3; IntAct=EBI-466029, EBI-358755; CC P42858; Q53H12: AGK; NbExp=3; IntAct=EBI-466029, EBI-2269837; CC P42858; Q53H12-2: AGK; NbExp=12; IntAct=EBI-466029, EBI-25944242; CC P42858; Q5TGY3: AHDC1; NbExp=12; IntAct=EBI-466029, EBI-948813; CC P42858; Q9UIJ7: AK3; NbExp=9; IntAct=EBI-466029, EBI-3916527; CC P42858; P14550: AKR1A1; NbExp=6; IntAct=EBI-466029, EBI-372388; CC P42858; P31749: AKT1; NbExp=3; IntAct=EBI-466029, EBI-296087; CC P42858; Q3SY69: ALDH1L2; NbExp=3; IntAct=EBI-466029, EBI-6916128; CC P42858; P04075-2: ALDOA; NbExp=6; IntAct=EBI-466029, EBI-10194102; CC P42858; Q9H553: ALG2; NbExp=3; IntAct=EBI-466029, EBI-25806804; CC P42858; Q8IWZ3-3: ANKHD1; NbExp=3; IntAct=EBI-466029, EBI-25833200; CC P42858; Q6ZTN6-2: ANKRD13D; NbExp=9; IntAct=EBI-466029, EBI-25840993; CC P42858; Q5TZF3-1: ANKRD45; NbExp=3; IntAct=EBI-466029, EBI-22011535; CC P42858; Q16853: AOC3; NbExp=3; IntAct=EBI-466029, EBI-3921628; CC P42858; P63010-2: AP2B1; NbExp=18; IntAct=EBI-466029, EBI-11529439; CC P42858; O00203: AP3B1; NbExp=6; IntAct=EBI-466029, EBI-1044383; CC P42858; Q9Y2T2: AP3M1; NbExp=3; IntAct=EBI-466029, EBI-2371151; CC P42858; P05067: APP; NbExp=6; IntAct=EBI-466029, EBI-77613; CC P42858; P48444: ARCN1; NbExp=3; IntAct=EBI-466029, EBI-1044491; CC P42858; Q9NP61: ARFGAP3; NbExp=22; IntAct=EBI-466029, EBI-2875816; CC P42858; P53365: ARFIP2; NbExp=3; IntAct=EBI-466029, EBI-638194; CC P42858; Q8N264: ARHGAP24; NbExp=3; IntAct=EBI-466029, EBI-988764; CC P42858; Q52LW3-2: ARHGAP29; NbExp=3; IntAct=EBI-466029, EBI-22012297; CC P42858; Q0P5N6: ARL16; NbExp=18; IntAct=EBI-466029, EBI-10186132; CC P42858; Q6P1M9: ARMCX5; NbExp=6; IntAct=EBI-466029, EBI-10252512; CC P42858; Q86TN1: ARNT2; NbExp=9; IntAct=EBI-466029, EBI-25844820; CC P42858; Q9Y575-3: ASB3; NbExp=6; IntAct=EBI-466029, EBI-14199987; CC P42858; Q6XD76: ASCL4; NbExp=6; IntAct=EBI-466029, EBI-10254793; CC P42858; Q96FT7-4: ASIC4; NbExp=3; IntAct=EBI-466029, EBI-9089489; CC P42858; Q12797-6: ASPH; NbExp=6; IntAct=EBI-466029, EBI-12092171; CC P42858; Q12797-7: ASPH; NbExp=3; IntAct=EBI-466029, EBI-25953099; CC P42858; Q96DT6: ATG4C; NbExp=15; IntAct=EBI-466029, EBI-3225845; CC P42858; Q8WXF7: ATL1; NbExp=18; IntAct=EBI-466029, EBI-2410266; CC P42858; P25705: ATP5F1A; NbExp=3; IntAct=EBI-466029, EBI-351437; CC P42858; P24539: ATP5PB; NbExp=3; IntAct=EBI-466029, EBI-1044810; CC P42858; P48047: ATP5PO; NbExp=6; IntAct=EBI-466029, EBI-355815; CC P42858; Q15904: ATP6AP1; NbExp=3; IntAct=EBI-466029, EBI-714667; CC P42858; P61421: ATP6V0D1; NbExp=6; IntAct=EBI-466029, EBI-954063; CC P42858; P21281: ATP6V1B2; NbExp=3; IntAct=EBI-466029, EBI-4290814; CC P42858; Q9UI12: ATP6V1H; NbExp=3; IntAct=EBI-466029, EBI-724719; CC P42858; Q9UQB8-3: BAIAP2; NbExp=18; IntAct=EBI-466029, EBI-9091996; CC P42858; Q9UQB8-6: BAIAP2; NbExp=18; IntAct=EBI-466029, EBI-9092016; CC P42858; Q16520: BATF; NbExp=12; IntAct=EBI-466029, EBI-749503; CC P42858; Q9NRL2: BAZ1A; NbExp=4; IntAct=EBI-466029, EBI-927511; CC P42858; Q9BUW7: BBLN; NbExp=6; IntAct=EBI-466029, EBI-752084; CC P42858; Q8WY36-3: BBX; NbExp=6; IntAct=EBI-466029, EBI-22013474; CC P42858; P51572: BCAP31; NbExp=4; IntAct=EBI-466029, EBI-77683; CC P42858; Q14457: BECN1; NbExp=14; IntAct=EBI-466029, EBI-949378; CC P42858; Q00994: BEX3; NbExp=6; IntAct=EBI-466029, EBI-741753; CC P42858; O15392: BIRC5; NbExp=15; IntAct=EBI-466029, EBI-518823; CC P42858; Q9GZL8: BPESC1; NbExp=15; IntAct=EBI-466029, EBI-25861458; CC P42858; P38398-6: BRCA1; NbExp=3; IntAct=EBI-466029, EBI-25833510; CC P42858; Q8WUW1: BRK1; NbExp=6; IntAct=EBI-466029, EBI-2837444; CC P42858; Q13901: C1D; NbExp=6; IntAct=EBI-466029, EBI-3844053; CC P42858; Q6P1W5: C1orf94; NbExp=3; IntAct=EBI-466029, EBI-946029; CC P42858; Q9BXJ4: C1QTNF3; NbExp=3; IntAct=EBI-466029, EBI-10697546; CC P42858; Q9NUB4: C20orf141; NbExp=6; IntAct=EBI-466029, EBI-9088162; CC P42858; Q6P5X5-2: C22orf39; NbExp=3; IntAct=EBI-466029, EBI-10692329; CC P42858; Q8N865: C7orf31; NbExp=3; IntAct=EBI-466029, EBI-10174456; CC P42858; Q9BRJ6: C7orf50; NbExp=6; IntAct=EBI-466029, EBI-751612; CC P42858; Q8IVU9: CABCOCO1; NbExp=3; IntAct=EBI-466029, EBI-21771960; CC P42858; P62158: CALM3; NbExp=10; IntAct=EBI-466029, EBI-397435; CC P42858; Q14012: CAMK1; NbExp=3; IntAct=EBI-466029, EBI-6380130; CC P42858; Q8N5S9-2: CAMKK1; NbExp=9; IntAct=EBI-466029, EBI-25850646; CC P42858; Q9HC96: CAPN10; NbExp=12; IntAct=EBI-466029, EBI-3915761; CC P42858; P29466-3: CASP1; NbExp=3; IntAct=EBI-466029, EBI-12248206; CC P42858; P42574: CASP3; NbExp=9; IntAct=EBI-466029, EBI-524064; CC P42858; P55212: CASP6; NbExp=15; IntAct=EBI-466029, EBI-718729; CC P42858; P55210: CASP7; NbExp=12; IntAct=EBI-466029, EBI-523958; CC P42858; P22681: CBL; NbExp=18; IntAct=EBI-466029, EBI-518228; CC P42858; P35520: CBS; NbExp=12; IntAct=EBI-466029, EBI-740135; CC P42858; Q5JTY5: CBWD3; NbExp=6; IntAct=EBI-466029, EBI-723434; CC P42858; P83916: CBX1; NbExp=15; IntAct=EBI-466029, EBI-78129; CC P42858; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-466029, EBI-744556; CC P42858; Q96M83-3: CCDC7; NbExp=18; IntAct=EBI-466029, EBI-18211613; CC P42858; Q9Y3X0: CCDC9; NbExp=3; IntAct=EBI-466029, EBI-2557532; CC P42858; Q13939: CCIN; NbExp=3; IntAct=EBI-466029, EBI-25879469; CC P42858; Q9NPC3: CCNB1IP1; NbExp=6; IntAct=EBI-466029, EBI-745269; CC P42858; P24863: CCNC; NbExp=9; IntAct=EBI-466029, EBI-395261; CC P42858; O96020: CCNE2; NbExp=6; IntAct=EBI-466029, EBI-375033; CC P42858; P51959: CCNG1; NbExp=3; IntAct=EBI-466029, EBI-3905829; CC P42858; P78371: CCT2; NbExp=6; IntAct=EBI-466029, EBI-357407; CC P42858; P48643: CCT5; NbExp=3; IntAct=EBI-466029, EBI-355710; CC P42858; P40227: CCT6A; NbExp=10; IntAct=EBI-466029, EBI-356687; CC P42858; P50990: CCT8; NbExp=4; IntAct=EBI-466029, EBI-356507; CC P42858; P13987: CD59; NbExp=10; IntAct=EBI-466029, EBI-297972; CC P42858; Q9H3Q1: CDC42EP4; NbExp=3; IntAct=EBI-466029, EBI-744665; CC P42858; Q99459: CDC5L; NbExp=3; IntAct=EBI-466029, EBI-374880; CC P42858; O00311: CDC7; NbExp=3; IntAct=EBI-466029, EBI-374980; CC P42858; Q9BWT1: CDCA7; NbExp=3; IntAct=EBI-466029, EBI-7054803; CC P42858; P55290: CDH13; NbExp=6; IntAct=EBI-466029, EBI-7205595; CC P42858; O95674: CDS2; NbExp=9; IntAct=EBI-466029, EBI-3913685; CC P42858; Q8N2Z9: CENPS; NbExp=3; IntAct=EBI-466029, EBI-5529649; CC P42858; Q7Z7K6: CENPV; NbExp=15; IntAct=EBI-466029, EBI-1210604; CC P42858; Q9P2H0: CEP126; NbExp=2; IntAct=EBI-466029, EBI-473176; CC P42858; Q53EZ4: CEP55; NbExp=9; IntAct=EBI-466029, EBI-747776; CC P42858; Q96MT8-3: CEP63; NbExp=12; IntAct=EBI-466029, EBI-11522539; CC P42858; Q8NHQ1-3: CEP70; NbExp=6; IntAct=EBI-466029, EBI-11526150; CC P42858; P41208: CETN2; NbExp=13; IntAct=EBI-466029, EBI-1789926; CC P42858; Q9Y6H1: CHCHD2; NbExp=10; IntAct=EBI-466029, EBI-2321769; CC P42858; Q9NX63: CHCHD3; NbExp=6; IntAct=EBI-466029, EBI-743375; CC P42858; Q12873: CHD3; NbExp=3; IntAct=EBI-466029, EBI-523590; CC P42858; Q9HD42: CHMP1A; NbExp=12; IntAct=EBI-466029, EBI-1057156; CC P42858; O43633: CHMP2A; NbExp=3; IntAct=EBI-466029, EBI-2692789; CC P42858; Q9H444: CHMP4B; NbExp=7; IntAct=EBI-466029, EBI-749627; CC P42858; Q9UHD4: CIDEB; NbExp=3; IntAct=EBI-466029, EBI-7062247; CC P42858; P06732: CKM; NbExp=3; IntAct=EBI-466029, EBI-4287089; CC P42858; Q9Y240: CLEC11A; NbExp=12; IntAct=EBI-466029, EBI-3957044; CC P42858; Q92478: CLEC2B; NbExp=9; IntAct=EBI-466029, EBI-13350535; CC P42858; Q16740: CLPP; NbExp=6; IntAct=EBI-466029, EBI-1056029; CC P42858; Q8NCR9: CLRN3; NbExp=9; IntAct=EBI-466029, EBI-9091272; CC P42858; Q9H9A5: CNOT10; NbExp=4; IntAct=EBI-466029, EBI-1054261; CC P42858; Q9H9A5-3: CNOT10; NbExp=3; IntAct=EBI-466029, EBI-25957177; CC P42858; Q9UIV1: CNOT7; NbExp=13; IntAct=EBI-466029, EBI-2105113; CC P42858; P09543: CNP; NbExp=10; IntAct=EBI-466029, EBI-1059219; CC P42858; Q96MW5: COG8; NbExp=12; IntAct=EBI-466029, EBI-720875; CC P42858; P53618: COPB1; NbExp=6; IntAct=EBI-466029, EBI-359063; CC P42858; Q9UNS2: COPS3; NbExp=22; IntAct=EBI-466029, EBI-350590; CC P42858; Q86WV2: COX4I1; NbExp=3; IntAct=EBI-466029, EBI-10260134; CC P42858; P10606: COX5B; NbExp=7; IntAct=EBI-466029, EBI-1053725; CC P42858; P12074: COX6A1; NbExp=4; IntAct=EBI-466029, EBI-2115950; CC P42858; P09669: COX6C; NbExp=4; IntAct=EBI-466029, EBI-715040; CC P42858; Q9UKF6: CPSF3; NbExp=3; IntAct=EBI-466029, EBI-1044699; CC P42858; A2RRE8: CPT1B; NbExp=6; IntAct=EBI-466029, EBI-25865477; CC P42858; Q9BSW2: CRACR2A; NbExp=9; IntAct=EBI-466029, EBI-739773; CC P42858; P16220: CREB1; NbExp=3; IntAct=EBI-466029, EBI-711855; CC P42858; Q92793: CREBBP; NbExp=2; IntAct=EBI-466029, EBI-81215; CC P42858; Q6UXH1-2: CRELD2; NbExp=6; IntAct=EBI-466029, EBI-21670927; CC P42858; P46108: CRK; NbExp=3; IntAct=EBI-466029, EBI-886; CC P42858; Q14194: CRMP1; NbExp=14; IntAct=EBI-466029, EBI-473101; CC P42858; P02489: CRYAA; NbExp=3; IntAct=EBI-466029, EBI-6875961; CC P42858; P53672: CRYBA2; NbExp=3; IntAct=EBI-466029, EBI-750444; CC P42858; P04141: CSF2; NbExp=15; IntAct=EBI-466029, EBI-1809826; CC P42858; P48730-2: CSNK1D; NbExp=15; IntAct=EBI-466029, EBI-9087876; CC P42858; P50461: CSRP3; NbExp=3; IntAct=EBI-466029, EBI-5658719; CC P42858; Q9H6J7-2: CSTPP1; NbExp=6; IntAct=EBI-466029, EBI-13328871; CC P42858; P56545-3: CTBP2; NbExp=3; IntAct=EBI-466029, EBI-10171902; CC P42858; P35222: CTNNB1; NbExp=14; IntAct=EBI-466029, EBI-491549; CC P42858; Q13618: CUL3; NbExp=3; IntAct=EBI-466029, EBI-456129; CC P42858; Q93034: CUL5; NbExp=10; IntAct=EBI-466029, EBI-1057139; CC P42858; Q8TB03: CXorf38; NbExp=15; IntAct=EBI-466029, EBI-12024320; CC P42858; P08574: CYC1; NbExp=7; IntAct=EBI-466029, EBI-1224514; CC P42858; P20815: CYP3A5; NbExp=3; IntAct=EBI-466029, EBI-3908011; CC P42858; Q5D0E6-2: DALRD3; NbExp=9; IntAct=EBI-466029, EBI-9090939; CC P42858; Q9UN19: DAPP1; NbExp=9; IntAct=EBI-466029, EBI-3918199; CC P42858; Q9UER7: DAXX; NbExp=15; IntAct=EBI-466029, EBI-77321; CC P42858; Q15038: DAZAP2; NbExp=3; IntAct=EBI-466029, EBI-724310; CC P42858; Q9UJU6: DBNL; NbExp=3; IntAct=EBI-466029, EBI-751783; CC P42858; P61962: DCAF7; NbExp=10; IntAct=EBI-466029, EBI-359808; CC P42858; Q9H816: DCLRE1B; NbExp=9; IntAct=EBI-466029, EBI-3508943; CC P42858; Q13561: DCTN2; NbExp=12; IntAct=EBI-466029, EBI-715074; CC P42858; Q9UJW0: DCTN4; NbExp=3; IntAct=EBI-466029, EBI-2134033; CC P42858; Q9UHI6: DDX20; NbExp=6; IntAct=EBI-466029, EBI-347658; CC P42858; Q9NR30: DDX21; NbExp=3; IntAct=EBI-466029, EBI-357942; CC P42858; O00148: DDX39A; NbExp=3; IntAct=EBI-466029, EBI-348253; CC P42858; Q9UJV9: DDX41; NbExp=6; IntAct=EBI-466029, EBI-1046350; CC P42858; Q14154: DELE1; NbExp=18; IntAct=EBI-466029, EBI-2805660; CC P42858; P78524: DENND2B; NbExp=3; IntAct=EBI-466029, EBI-962633; CC P42858; P17661: DES; NbExp=9; IntAct=EBI-466029, EBI-1055572; CC P42858; Q05D60: DEUP1; NbExp=15; IntAct=EBI-466029, EBI-748597; CC P42858; Q5T7M9-2: DIPK1A; NbExp=3; IntAct=EBI-466029, EBI-25960650; CC P42858; P09622: DLD; NbExp=3; IntAct=EBI-466029, EBI-353366; CC P42858; P36957: DLST; NbExp=3; IntAct=EBI-466029, EBI-351007; CC P42858; O60479: DLX3; NbExp=3; IntAct=EBI-466029, EBI-3908248; CC P42858; P31689: DNAJA1; NbExp=17; IntAct=EBI-466029, EBI-347834; CC P42858; Q96EY1: DNAJA3; NbExp=5; IntAct=EBI-466029, EBI-356767; CC P42858; Q9UDY4: DNAJB4; NbExp=3; IntAct=EBI-466029, EBI-356960; CC P42858; O75190-2: DNAJB6; NbExp=3; IntAct=EBI-466029, EBI-12593112; CC P42858; Q9NVH1: DNAJC11; NbExp=3; IntAct=EBI-466029, EBI-1055336; CC P42858; Q5F1R6: DNAJC21; NbExp=6; IntAct=EBI-466029, EBI-2654581; CC P42858; Q9NNZ3: DNAJC4; NbExp=12; IntAct=EBI-466029, EBI-4397791; CC P42858; O14645: DNALI1; NbExp=15; IntAct=EBI-466029, EBI-395638; CC P42858; Q05193: DNM1; NbExp=3; IntAct=EBI-466029, EBI-713135; CC P42858; P50570-2: DNM2; NbExp=6; IntAct=EBI-466029, EBI-10968534; CC P42858; Q9H147: DNTTIP1; NbExp=15; IntAct=EBI-466029, EBI-2795449; CC P42858; Q9H3H5: DPAGT1; NbExp=3; IntAct=EBI-466029, EBI-3922860; CC P42858; Q16555: DPYSL2; NbExp=3; IntAct=EBI-466029, EBI-1104711; CC P42858; Q9BPU6: DPYSL5; NbExp=9; IntAct=EBI-466029, EBI-724653; CC P42858; Q14204: DYNC1H1; NbExp=8; IntAct=EBI-466029, EBI-356015; CC P42858; P63167: DYNLL1; NbExp=10; IntAct=EBI-466029, EBI-349105; CC P42858; A0AVK6: E2F8; NbExp=12; IntAct=EBI-466029, EBI-7779316; CC P42858; Q13011: ECH1; NbExp=2; IntAct=EBI-466029, EBI-711968; CC P42858; O60869: EDF1; NbExp=6; IntAct=EBI-466029, EBI-781301; CC P42858; Q3B7T1: EDRF1; NbExp=18; IntAct=EBI-466029, EBI-2870947; CC P42858; Q05639: EEF1A2; NbExp=3; IntAct=EBI-466029, EBI-354943; CC P42858; P24534: EEF1B2; NbExp=7; IntAct=EBI-466029, EBI-354334; CC P42858; P29692: EEF1D; NbExp=6; IntAct=EBI-466029, EBI-358607; CC P42858; P13639: EEF2; NbExp=3; IntAct=EBI-466029, EBI-352560; CC P42858; Q12805: EFEMP1; NbExp=3; IntAct=EBI-466029, EBI-536772; CC P42858; O14602: EIF1AY; NbExp=6; IntAct=EBI-466029, EBI-286439; CC P42858; P20042: EIF2S2; NbExp=12; IntAct=EBI-466029, EBI-711977; CC P42858; P41091: EIF2S3; NbExp=3; IntAct=EBI-466029, EBI-1054228; CC P42858; O75821: EIF3G; NbExp=4; IntAct=EBI-466029, EBI-366632; CC P42858; Q13347: EIF3I; NbExp=13; IntAct=EBI-466029, EBI-354047; CC P42858; Q14240-2: EIF4A2; NbExp=3; IntAct=EBI-466029, EBI-10232522; CC P42858; O60573: EIF4E2; NbExp=4; IntAct=EBI-466029, EBI-398610; CC P42858; P55010: EIF5; NbExp=3; IntAct=EBI-466029, EBI-286450; CC P42858; O95163: ELP1; NbExp=4; IntAct=EBI-466029, EBI-347559; CC P42858; Q9Y6C2-2: EMILIN1; NbExp=3; IntAct=EBI-466029, EBI-11748557; CC P42858; Q8TC29: ENKUR; NbExp=6; IntAct=EBI-466029, EBI-9246952; CC P42858; P06733: ENO1; NbExp=13; IntAct=EBI-466029, EBI-353877; CC P42858; Q9Y5L3: ENTPD2; NbExp=3; IntAct=EBI-466029, EBI-3913907; CC P42858; O75356: ENTPD5; NbExp=3; IntAct=EBI-466029, EBI-7416931; CC P42858; A0A0C4DH22: EPB41L1; NbExp=6; IntAct=EBI-466029, EBI-25865535; CC P42858; Q8TE68-3: EPS8L1; NbExp=3; IntAct=EBI-466029, EBI-21574901; CC P42858; Q2NKX8: ERCC6L; NbExp=20; IntAct=EBI-466029, EBI-1042535; CC P42858; A1L162: ERICH2; NbExp=3; IntAct=EBI-466029, EBI-2682520; CC P42858; Q96DN0: ERP27; NbExp=3; IntAct=EBI-466029, EBI-953772; CC P42858; Q6NXG1-3: ESRP1; NbExp=6; IntAct=EBI-466029, EBI-21567429; CC P42858; Q9UI08-2: EVL; NbExp=20; IntAct=EBI-466029, EBI-6448852; CC P42858; Q01844-4: EWSR1; NbExp=3; IntAct=EBI-466029, EBI-25896785; CC P42858; O00471: EXOC5; NbExp=3; IntAct=EBI-466029, EBI-949824; CC P42858; Q99504: EYA3; NbExp=6; IntAct=EBI-466029, EBI-9089567; CC P42858; P15311: EZR; NbExp=4; IntAct=EBI-466029, EBI-1056902; CC P42858; P23610: F8A3; NbExp=3; IntAct=EBI-466029, EBI-5663973; CC P42858; Q6SJ93: FAM111B; NbExp=12; IntAct=EBI-466029, EBI-6309082; CC P42858; Q96GL9: FAM163A; NbExp=12; IntAct=EBI-466029, EBI-11793142; CC P42858; Q96KS9: FAM167A; NbExp=6; IntAct=EBI-466029, EBI-10290462; CC P42858; Q5HYJ3-3: FAM76B; NbExp=6; IntAct=EBI-466029, EBI-11956087; CC P42858; Q5JUQ0: FAM78A; NbExp=3; IntAct=EBI-466029, EBI-21900888; CC P42858; Q8IZU1: FAM9A; NbExp=18; IntAct=EBI-466029, EBI-8468186; CC P42858; Q9NPI8: FANCF; NbExp=3; IntAct=EBI-466029, EBI-81589; CC P42858; Q8TC84: FANK1; NbExp=3; IntAct=EBI-466029, EBI-21975404; CC P42858; Q9NSD9: FARSB; NbExp=3; IntAct=EBI-466029, EBI-353803; CC P42858; P49327: FASN; NbExp=13; IntAct=EBI-466029, EBI-356658; CC P42858; Q53R41: FASTKD1; NbExp=9; IntAct=EBI-466029, EBI-3957005; CC P42858; Q8NFZ0: FBH1; NbExp=6; IntAct=EBI-466029, EBI-724767; CC P42858; P09467: FBP1; NbExp=3; IntAct=EBI-466029, EBI-712740; CC P42858; Q99689: FEZ1; NbExp=6; IntAct=EBI-466029, EBI-396435; CC P42858; Q9UHY8: FEZ2; NbExp=18; IntAct=EBI-466029, EBI-396453; CC P42858; Q13643: FHL3; NbExp=9; IntAct=EBI-466029, EBI-741101; CC P42858; Q9BVA6: FICD; NbExp=3; IntAct=EBI-466029, EBI-3907198; CC P42858; P26885: FKBP2; NbExp=6; IntAct=EBI-466029, EBI-719873; CC P42858; O75955: FLOT1; NbExp=4; IntAct=EBI-466029, EBI-603643; CC P42858; Q8N3X1: FNBP4; NbExp=6; IntAct=EBI-466029, EBI-310600; CC P42858; Q3SYB3: FOXD4L6; NbExp=6; IntAct=EBI-466029, EBI-6425864; CC P42858; Q6PIV2: FOXR1; NbExp=12; IntAct=EBI-466029, EBI-10253815; CC P42858; O95073-2: FSBP; NbExp=3; IntAct=EBI-466029, EBI-10696047; CC P42858; P02792: FTL; NbExp=20; IntAct=EBI-466029, EBI-713279; CC P42858; P06241-3: FYN; NbExp=12; IntAct=EBI-466029, EBI-10691738; CC P42858; Q9ULV1: FZD4; NbExp=9; IntAct=EBI-466029, EBI-2466380; CC P42858; Q7L622: G2E3; NbExp=6; IntAct=EBI-466029, EBI-751757; CC P42858; Q13283: G3BP1; NbExp=16; IntAct=EBI-466029, EBI-1047359; CC P42858; Q9UQC2: GAB2; NbExp=3; IntAct=EBI-466029, EBI-975200; CC P42858; Q8N4A0: GALNT4; NbExp=12; IntAct=EBI-466029, EBI-21555925; CC P42858; P04406: GAPDH; NbExp=7; IntAct=EBI-466029, EBI-354056; CC P42858; P28676: GCA; NbExp=3; IntAct=EBI-466029, EBI-947242; CC P42858; P14136: GFAP; NbExp=10; IntAct=EBI-466029, EBI-744302; CC P42858; Q9NXC2: GFOD1; NbExp=9; IntAct=EBI-466029, EBI-8799578; CC P42858; Q9UG22: GIMAP2; NbExp=6; IntAct=EBI-466029, EBI-15891037; CC P42858; Q9Y2X7: GIT1; NbExp=10; IntAct=EBI-466029, EBI-466061; CC P42858; P48060: GLIPR1; NbExp=3; IntAct=EBI-466029, EBI-2833130; CC P42858; P09471: GNAO1; NbExp=7; IntAct=EBI-466029, EBI-715087; CC P42858; P62873: GNB1; NbExp=10; IntAct=EBI-466029, EBI-357130; CC P42858; P62879: GNB2; NbExp=10; IntAct=EBI-466029, EBI-356942; CC P42858; Q08379: GOLGA2; NbExp=3; IntAct=EBI-466029, EBI-618309; CC P42858; Q9H4A5: GOLPH3L; NbExp=20; IntAct=EBI-466029, EBI-4403434; CC P42858; Q8IYG2: GPC3; NbExp=3; IntAct=EBI-466029, EBI-25896879; CC P42858; Q8IV16: GPIHBP1; NbExp=3; IntAct=EBI-466029, EBI-9080234; CC P42858; P51674: GPM6A; NbExp=4; IntAct=EBI-466029, EBI-7187133; CC P42858; Q86YB0: GPM6A; NbExp=3; IntAct=EBI-466029, EBI-25966592; CC P42858; Q7Z602: GPR141; NbExp=3; IntAct=EBI-466029, EBI-21649723; CC P42858; Q96D09: GPRASP2; NbExp=5; IntAct=EBI-466029, EBI-473189; CC P42858; Q96SL4: GPX7; NbExp=3; IntAct=EBI-466029, EBI-749411; CC P42858; Q13588: GRAP; NbExp=12; IntAct=EBI-466029, EBI-2847510; CC P42858; Q8IY40: GRIK2; NbExp=9; IntAct=EBI-466029, EBI-25832107; CC P42858; P49840: GSK3A; NbExp=6; IntAct=EBI-466029, EBI-1044067; CC P42858; Q9Y5Q9: GTF3C3; NbExp=12; IntAct=EBI-466029, EBI-1054873; CC P42858; Q9BZE4: GTPBP4; NbExp=3; IntAct=EBI-466029, EBI-1056249; CC P42858; O75409: H2AP; NbExp=16; IntAct=EBI-466029, EBI-6447217; CC P42858; Q93079: H2BC9; NbExp=18; IntAct=EBI-466029, EBI-352469; CC P42858; Q6NXT2: H3-5; NbExp=15; IntAct=EBI-466029, EBI-2868501; CC P42858; P68431: H3C12; NbExp=20; IntAct=EBI-466029, EBI-79722; CC P42858; Q71DI3: H3C15; NbExp=18; IntAct=EBI-466029, EBI-750650; CC P42858; P62805: H4C9; NbExp=3; IntAct=EBI-466029, EBI-302023; CC P42858; P40939: HADHA; NbExp=3; IntAct=EBI-466029, EBI-356720; CC P42858; P54257-2: HAP1; NbExp=8; IntAct=EBI-466029, EBI-9392340; CC P42858; Q99871: HAUS7; NbExp=18; IntAct=EBI-466029, EBI-395719; CC P42858; O00165: HAX1; NbExp=14; IntAct=EBI-466029, EBI-357001; CC P42858; Q8N779: hCG_1998195; NbExp=15; IntAct=EBI-466029, EBI-10267476; CC P42858; Q969S8: HDAC10; NbExp=21; IntAct=EBI-466029, EBI-301762; CC P42858; Q9UBN7: HDAC6; NbExp=9; IntAct=EBI-466029, EBI-301697; CC P42858; Q9HCC6: HES4; NbExp=12; IntAct=EBI-466029, EBI-2680288; CC P42858; Q9UBP5: HEY2; NbExp=2; IntAct=EBI-466029, EBI-750630; CC P42858; O00291: HIP1; NbExp=7; IntAct=EBI-466029, EBI-473886; CC P42858; Q9BW71: HIRIP3; NbExp=6; IntAct=EBI-466029, EBI-723624; CC P42858; P52790: HK3; NbExp=3; IntAct=EBI-466029, EBI-2965780; CC P42858; P08397: HMBS; NbExp=3; IntAct=EBI-466029, EBI-9090148; CC P42858; Q9NP66: HMG20A; NbExp=2; IntAct=EBI-466029, EBI-740641; CC P42858; Q9P0W2: HMG20B; NbExp=3; IntAct=EBI-466029, EBI-713401; CC P42858; P09429: HMGB1; NbExp=13; IntAct=EBI-466029, EBI-389432; CC P42858; P07910: HNRNPC; NbExp=7; IntAct=EBI-466029, EBI-357966; CC P42858; P07910-2: HNRNPC; NbExp=9; IntAct=EBI-466029, EBI-5280084; CC P42858; P61978: HNRNPK; NbExp=12; IntAct=EBI-466029, EBI-304185; CC P42858; P20719: HOXA5; NbExp=9; IntAct=EBI-466029, EBI-8470697; CC P42858; O43248: HOXC11; NbExp=7; IntAct=EBI-466029, EBI-2652631; CC P42858; P09017: HOXC4; NbExp=16; IntAct=EBI-466029, EBI-3923226; CC P42858; P00492: HPRT1; NbExp=15; IntAct=EBI-466029, EBI-748210; CC P42858; P0DMV8: HSPA1A; NbExp=9; IntAct=EBI-466029, EBI-11052499; CC P42858; P54652: HSPA2; NbExp=3; IntAct=EBI-466029, EBI-356991; CC P42858; P11142: HSPA8; NbExp=14; IntAct=EBI-466029, EBI-351896; CC P42858; P42858: HTT; NbExp=11; IntAct=EBI-466029, EBI-466029; CC P42858; Q12891: HYAL2; NbExp=9; IntAct=EBI-466029, EBI-2806068; CC P42858; Q9NX55: HYPK; NbExp=4; IntAct=EBI-466029, EBI-1048743; CC P42858; Q02363: ID2; NbExp=6; IntAct=EBI-466029, EBI-713450; CC P42858; Q8IY31-2: IFT20; NbExp=6; IntAct=EBI-466029, EBI-11742277; CC P42858; Q8IY31-3: IFT20; NbExp=18; IntAct=EBI-466029, EBI-9091197; CC P42858; Q9NWB7: IFT57; NbExp=3; IntAct=EBI-466029, EBI-725672; CC P42858; P22692: IGFBP4; NbExp=6; IntAct=EBI-466029, EBI-2831948; CC P42858; Q14005-2: IL16; NbExp=15; IntAct=EBI-466029, EBI-17178971; CC P42858; Q16891: IMMT; NbExp=7; IntAct=EBI-466029, EBI-473801; CC P42858; P29218-3: IMPA1; NbExp=6; IntAct=EBI-466029, EBI-12330251; CC P42858; Q9UNL4: ING4; NbExp=3; IntAct=EBI-466029, EBI-2866661; CC P42858; Q8WYH8-2: ING5; NbExp=18; IntAct=EBI-466029, EBI-21602071; CC P42858; Q8NBZ0: INO80E; NbExp=3; IntAct=EBI-466029, EBI-769401; CC P42858; Q8TEX9: IPO4; NbExp=7; IntAct=EBI-466029, EBI-395967; CC P42858; O00410-3: IPO5; NbExp=3; IntAct=EBI-466029, EBI-9641587; CC P42858; Q6DN90-2: IQSEC1; NbExp=18; IntAct=EBI-466029, EBI-21911304; CC P42858; Q96N16: JAKMIP1; NbExp=10; IntAct=EBI-466029, EBI-2680803; CC P42858; Q92993: KAT5; NbExp=15; IntAct=EBI-466029, EBI-399080; CC P42858; Q13303: KCNAB2; NbExp=3; IntAct=EBI-466029, EBI-948729; CC P42858; Q9Y691: KCNMB2; NbExp=3; IntAct=EBI-466029, EBI-7932244; CC P42858; Q96SI1-2: KCTD15; NbExp=6; IntAct=EBI-466029, EBI-12382297; CC P42858; Q8N5Z5: KCTD17; NbExp=3; IntAct=EBI-466029, EBI-743960; CC P42858; A0A384DVV8: KIAA0040; NbExp=3; IntAct=EBI-466029, EBI-20764875; CC P42858; Q6ZU52: KIAA0408; NbExp=6; IntAct=EBI-466029, EBI-739493; CC P42858; Q5T5P2-6: KIAA1217; NbExp=3; IntAct=EBI-466029, EBI-10188326; CC P42858; O14901: KLF11; NbExp=7; IntAct=EBI-466029, EBI-948266; CC P42858; Q9Y4X4: KLF12; NbExp=3; IntAct=EBI-466029, EBI-750750; CC P42858; P57682: KLF3; NbExp=6; IntAct=EBI-466029, EBI-8472267; CC P42858; Q53G59: KLHL12; NbExp=3; IntAct=EBI-466029, EBI-740929; CC P42858; Q9Y2M5: KLHL20; NbExp=9; IntAct=EBI-466029, EBI-714379; CC P42858; O60259: KLK8; NbExp=3; IntAct=EBI-466029, EBI-3915857; CC P42858; O15229-2: KMO; NbExp=3; IntAct=EBI-466029, EBI-21870540; CC P42858; Q9Y448: KNSTRN; NbExp=3; IntAct=EBI-466029, EBI-373334; CC P42858; O00505: KPNA3; NbExp=11; IntAct=EBI-466029, EBI-358297; CC P42858; P05783: KRT18; NbExp=6; IntAct=EBI-466029, EBI-297888; CC P42858; P08727: KRT19; NbExp=6; IntAct=EBI-466029, EBI-742756; CC P42858; P35900: KRT20; NbExp=9; IntAct=EBI-466029, EBI-742094; CC P42858; Q14525: KRT33B; NbExp=12; IntAct=EBI-466029, EBI-1049638; CC P42858; P60409: KRTAP10-7; NbExp=9; IntAct=EBI-466029, EBI-10172290; CC P42858; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-466029, EBI-1052037; CC P42858; Q8IUC2: KRTAP8-1; NbExp=6; IntAct=EBI-466029, EBI-10261141; CC P42858; Q9BYQ4: KRTAP9-2; NbExp=9; IntAct=EBI-466029, EBI-1044640; CC P42858; Q96JM7-2: L3MBTL3; NbExp=3; IntAct=EBI-466029, EBI-11985629; CC P42858; O43813: LANCL1; NbExp=10; IntAct=EBI-466029, EBI-3046631; CC P42858; Q92615: LARP4B; NbExp=3; IntAct=EBI-466029, EBI-1052558; CC P42858; O95447: LCA5L; NbExp=18; IntAct=EBI-466029, EBI-8473670; CC P42858; Q5T7P3: LCE1B; NbExp=15; IntAct=EBI-466029, EBI-10245913; CC P42858; Q86U70-2: LDB1; NbExp=3; IntAct=EBI-466029, EBI-11979761; CC P42858; Q9BYZ2: LDHAL6B; NbExp=18; IntAct=EBI-466029, EBI-1108377; CC P42858; P07195: LDHB; NbExp=9; IntAct=EBI-466029, EBI-358748; CC P42858; O95751: LDOC1; NbExp=5; IntAct=EBI-466029, EBI-740738; CC P42858; Q8TCE9: LGALS14; NbExp=3; IntAct=EBI-466029, EBI-10274069; CC P42858; Q9H2C1: LHX5; NbExp=15; IntAct=EBI-466029, EBI-25835523; CC P42858; Q9UPM6: LHX6; NbExp=12; IntAct=EBI-466029, EBI-10258746; CC P42858; Q68G74: LHX8; NbExp=12; IntAct=EBI-466029, EBI-8474075; CC P42858; Q9H9Z2: LIN28A; NbExp=18; IntAct=EBI-466029, EBI-2462365; CC P42858; Q8N0U6: LINC00518; NbExp=6; IntAct=EBI-466029, EBI-10264791; CC P42858; Q9H0V9: LMAN2L; NbExp=3; IntAct=EBI-466029, EBI-9091707; CC P42858; Q8TBB1: LNX1; NbExp=6; IntAct=EBI-466029, EBI-739832; CC P42858; Q8N448: LNX2; NbExp=3; IntAct=EBI-466029, EBI-2340947; CC P42858; A2RU56: LOC401296; NbExp=9; IntAct=EBI-466029, EBI-9088215; CC P42858; Q1L5Z9: LONRF2; NbExp=3; IntAct=EBI-466029, EBI-2510853; CC P42858; Q14693: LPIN1; NbExp=12; IntAct=EBI-466029, EBI-5278370; CC P42858; Q96CN5: LRRC45; NbExp=3; IntAct=EBI-466029, EBI-2805176; CC P42858; Q32MZ4: LRRFIP1; NbExp=3; IntAct=EBI-466029, EBI-1369100; CC P42858; O95777: LSM8; NbExp=15; IntAct=EBI-466029, EBI-347779; CC P42858; Q9Y383: LUC7L2; NbExp=9; IntAct=EBI-466029, EBI-352851; CC P42858; Q8N1E2: LYG1; NbExp=3; IntAct=EBI-466029, EBI-13309213; CC P42858; Q9H063: MAF1; NbExp=3; IntAct=EBI-466029, EBI-720354; CC P42858; P43357: MAGEA3; NbExp=6; IntAct=EBI-466029, EBI-5651459; CC P42858; Q96M61: MAGEB18; NbExp=16; IntAct=EBI-466029, EBI-741835; CC P42858; Q8N7X4: MAGEB6; NbExp=2; IntAct=EBI-466029, EBI-6447163; CC P42858; Q96EH3: MALSU1; NbExp=6; IntAct=EBI-466029, EBI-2339737; CC P42858; Q99683: MAP3K5; NbExp=6; IntAct=EBI-466029, EBI-476263; CC P42858; Q00266: MAT1A; NbExp=3; IntAct=EBI-466029, EBI-967087; CC P42858; P43243: MATR3; NbExp=4; IntAct=EBI-466029, EBI-352602; CC P42858; P56270-2: MAZ; NbExp=3; IntAct=EBI-466029, EBI-12068586; CC P42858; Q9UIS9: MBD1; NbExp=2; IntAct=EBI-466029, EBI-867196; CC P42858; O95243-2: MBD4; NbExp=19; IntAct=EBI-466029, EBI-6448717; CC P42858; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-466029, EBI-348259; CC P42858; Q9HAF1: MEAF6; NbExp=6; IntAct=EBI-466029, EBI-399266; CC P42858; P51608: MECP2; NbExp=18; IntAct=EBI-466029, EBI-1189067; CC P42858; Q96RN5: MED15; NbExp=3; IntAct=EBI-466029, EBI-394506; CC P42858; Q96RN5-2: MED15; NbExp=6; IntAct=EBI-466029, EBI-11030807; CC P42858; Q15528-2: MED22; NbExp=12; IntAct=EBI-466029, EBI-12954271; CC P42858; Q9H204: MED28; NbExp=9; IntAct=EBI-466029, EBI-514199; CC P42858; Q96HR3: MED30; NbExp=3; IntAct=EBI-466029, EBI-394659; CC P42858; Q9Y3C7: MED31; NbExp=9; IntAct=EBI-466029, EBI-394707; CC P42858; P50221: MEOX1; NbExp=19; IntAct=EBI-466029, EBI-2864512; CC P42858; Q8N6F8: METTL27; NbExp=9; IntAct=EBI-466029, EBI-8487781; CC P42858; Q8TDB4: MGARP; NbExp=21; IntAct=EBI-466029, EBI-4397720; CC P42858; O94851: MICAL2; NbExp=3; IntAct=EBI-466029, EBI-2804835; CC P42858; A4FUJ8: MKL1; NbExp=15; IntAct=EBI-466029, EBI-21250407; CC P42858; Q9BUB5: MKNK1; NbExp=18; IntAct=EBI-466029, EBI-73837; CC P42858; Q9H000: MKRN2; NbExp=12; IntAct=EBI-466029, EBI-2341005; CC P42858; P22033: MMUT; NbExp=12; IntAct=EBI-466029, EBI-2690467; CC P42858; P51948: MNAT1; NbExp=9; IntAct=EBI-466029, EBI-716139; CC P42858; P41218: MNDA; NbExp=18; IntAct=EBI-466029, EBI-2829677; CC P42858; Q16653-13: MOG; NbExp=12; IntAct=EBI-466029, EBI-24226707; CC P42858; Q15014: MORF4L2; NbExp=12; IntAct=EBI-466029, EBI-399257; CC P42858; Q8N594: MPND; NbExp=3; IntAct=EBI-466029, EBI-2512452; CC P42858; P49959: MRE11; NbExp=5; IntAct=EBI-466029, EBI-396513; CC P42858; Q9Y605: MRFAP1; NbExp=19; IntAct=EBI-466029, EBI-995714; CC P42858; Q96HT8: MRFAP1L1; NbExp=21; IntAct=EBI-466029, EBI-748896; CC P42858; Q9BYD1: MRPL13; NbExp=3; IntAct=EBI-466029, EBI-1054936; CC P42858; O43196-4: MSH5; NbExp=3; IntAct=EBI-466029, EBI-25860238; CC P42858; Q9Y3D2: MSRB2; NbExp=12; IntAct=EBI-466029, EBI-9092052; CC P42858; P35548: MSX2; NbExp=12; IntAct=EBI-466029, EBI-6447480; CC P42858; P02795: MT2A; NbExp=6; IntAct=EBI-466029, EBI-996616; CC P42858; O43312: MTSS1; NbExp=3; IntAct=EBI-466029, EBI-473954; CC P42858; Q9ULD2-3: MTUS1; NbExp=3; IntAct=EBI-466029, EBI-18051665; CC P42858; Q9ULD2-4: MTUS1; NbExp=9; IntAct=EBI-466029, EBI-25866497; CC P42858; O15069: NACAD; NbExp=15; IntAct=EBI-466029, EBI-7108375; CC P42858; Q9ULW6: NAP1L2; NbExp=3; IntAct=EBI-466029, EBI-3911716; CC P42858; P54920: NAPA; NbExp=3; IntAct=EBI-466029, EBI-749652; CC P42858; Q14596: NBR1; NbExp=3; IntAct=EBI-466029, EBI-742698; CC P42858; P14598: NCF1; NbExp=6; IntAct=EBI-466029, EBI-395044; CC P42858; Q969V3: NCLN; NbExp=9; IntAct=EBI-466029, EBI-1056979; CC P42858; O75376: NCOR1; NbExp=3; IntAct=EBI-466029, EBI-347233; CC P42858; Q99608: NDN; NbExp=6; IntAct=EBI-466029, EBI-718177; CC P42858; Q9P0J0: NDUFA13; NbExp=4; IntAct=EBI-466029, EBI-372742; CC P42858; Q16795: NDUFA9; NbExp=7; IntAct=EBI-466029, EBI-1045087; CC P42858; O96000: NDUFB10; NbExp=13; IntAct=EBI-466029, EBI-1246371; CC P42858; O96000-2: NDUFB10; NbExp=3; IntAct=EBI-466029, EBI-25930682; CC P42858; Q9Y6M9: NDUFB9; NbExp=10; IntAct=EBI-466029, EBI-713654; CC P42858; P28331-5: NDUFS1; NbExp=6; IntAct=EBI-466029, EBI-25876328; CC P42858; O43920: NDUFS5; NbExp=7; IntAct=EBI-466029, EBI-1246091; CC P42858; O76041: NEBL; NbExp=18; IntAct=EBI-466029, EBI-2880203; CC P42858; I6L9F6: NEFL; NbExp=9; IntAct=EBI-466029, EBI-10178578; CC P42858; Q86SG6: NEK8; NbExp=3; IntAct=EBI-466029, EBI-1752987; CC P42858; Q13562: NEUROD1; NbExp=6; IntAct=EBI-466029, EBI-3908303; CC P42858; P19838-2: NFKB1; NbExp=3; IntAct=EBI-466029, EBI-1452242; CC P42858; Q8N5V2: NGEF; NbExp=3; IntAct=EBI-466029, EBI-718372; CC P42858; Q9NX24: NHP2; NbExp=3; IntAct=EBI-466029, EBI-1050064; CC P42858; Q9UBE8: NLK; NbExp=3; IntAct=EBI-466029, EBI-366978; CC P42858; Q96AM0: NLRP1; NbExp=3; IntAct=EBI-466029, EBI-25860999; CC P42858; O00746: NME4; NbExp=20; IntAct=EBI-466029, EBI-744871; CC P42858; P56597: NME5; NbExp=6; IntAct=EBI-466029, EBI-740667; CC P42858; Q9C002: NMES1; NbExp=3; IntAct=EBI-466029, EBI-3905285; CC P42858; Q9Y239: NOD1; NbExp=9; IntAct=EBI-466029, EBI-1051262; CC P42858; O15130-2: NPFF; NbExp=18; IntAct=EBI-466029, EBI-25840002; CC P42858; Q9Y639-1: NPTN; NbExp=6; IntAct=EBI-466029, EBI-12839590; CC P42858; Q13133-2: NR1H3; NbExp=3; IntAct=EBI-466029, EBI-12699353; CC P42858; Q86WQ0: NR2C2AP; NbExp=3; IntAct=EBI-466029, EBI-10260040; CC P42858; Q6X4W1-6: NSMF; NbExp=6; IntAct=EBI-466029, EBI-25842707; CC P42858; P36639-4: NUDT1; NbExp=6; IntAct=EBI-466029, EBI-25834643; CC P42858; Q9NZJ9: NUDT4; NbExp=6; IntAct=EBI-466029, EBI-4280066; CC P42858; Q7Z417: NUFIP2; NbExp=6; IntAct=EBI-466029, EBI-1210753; CC P42858; Q9BVL2: NUP58; NbExp=7; IntAct=EBI-466029, EBI-2811583; CC P42858; Q9NPJ8-3: NXT2; NbExp=15; IntAct=EBI-466029, EBI-10698339; CC P42858; Q96GC1: ODF2L; NbExp=3; IntAct=EBI-466029, EBI-12176953; CC P42858; Q02218: OGDH; NbExp=3; IntAct=EBI-466029, EBI-747213; CC P42858; Q86WS3: OOSP2; NbExp=9; IntAct=EBI-466029, EBI-25888682; CC P42858; Q6B0I4: OPCML; NbExp=3; IntAct=EBI-466029, EBI-25954356; CC P42858; Q96CV9: OPTN; NbExp=13; IntAct=EBI-466029, EBI-748974; CC P42858; Q96CV9-2: OPTN; NbExp=18; IntAct=EBI-466029, EBI-9091423; CC P42858; Q92882: OSTF1; NbExp=5; IntAct=EBI-466029, EBI-1051152; CC P42858; Q3ZCN5: OTOGL; NbExp=3; IntAct=EBI-466029, EBI-25954043; CC P42858; Q8IVL6-2: P3H3; NbExp=6; IntAct=EBI-466029, EBI-12149899; CC P42858; P13674: P4HA1; NbExp=5; IntAct=EBI-466029, EBI-1237386; CC P42858; Q6VY07: PACS1; NbExp=18; IntAct=EBI-466029, EBI-2555014; CC P42858; Q9BY11: PACSIN1; NbExp=3; IntAct=EBI-466029, EBI-721769; CC P42858; Q13177: PAK2; NbExp=2; IntAct=EBI-466029, EBI-1045887; CC P42858; Q9P286: PAK5; NbExp=3; IntAct=EBI-466029, EBI-741896; CC P42858; Q9NP74: PALMD; NbExp=6; IntAct=EBI-466029, EBI-2811699; CC P42858; Q8N3R9: PALS1; NbExp=3; IntAct=EBI-466029, EBI-2513978; CC P42858; Q86WK9: PAQR7; NbExp=3; IntAct=EBI-466029, EBI-10694587; CC P42858; Q99497: PARK7; NbExp=6; IntAct=EBI-466029, EBI-1164361; CC P42858; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-466029, EBI-11022007; CC P42858; Q9BYU1: PBX4; NbExp=3; IntAct=EBI-466029, EBI-10302990; CC P42858; Q9Y5G3-2: PCDHGB1; NbExp=3; IntAct=EBI-466029, EBI-21584477; CC P42858; Q6UW60-2: PCSK4; NbExp=3; IntAct=EBI-466029, EBI-25960845; CC P42858; P54750-4: PDE1A; NbExp=3; IntAct=EBI-466029, EBI-25952361; CC P42858; Q15119: PDK2; NbExp=10; IntAct=EBI-466029, EBI-726271; CC P42858; Q96HC4: PDLIM5; NbExp=9; IntAct=EBI-466029, EBI-751267; CC P42858; O15530-4: PDPK1; NbExp=6; IntAct=EBI-466029, EBI-9087775; CC P42858; Q13113: PDZK1IP1; NbExp=21; IntAct=EBI-466029, EBI-716063; CC P42858; Q96FA3: PELI1; NbExp=3; IntAct=EBI-466029, EBI-448369; CC P42858; Q9BRX2: PELO; NbExp=12; IntAct=EBI-466029, EBI-1043580; CC P42858; O00541: PES1; NbExp=3; IntAct=EBI-466029, EBI-1053271; CC P42858; Q99471: PFDN5; NbExp=3; IntAct=EBI-466029, EBI-357275; CC P42858; P35080: PFN2; NbExp=7; IntAct=EBI-466029, EBI-473138; CC P42858; O75925: PIAS1; NbExp=19; IntAct=EBI-466029, EBI-629434; CC P42858; Q8N2W9: PIAS4; NbExp=6; IntAct=EBI-466029, EBI-473160; CC P42858; Q8WXW3: PIBF1; NbExp=3; IntAct=EBI-466029, EBI-2558770; CC P42858; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-466029, EBI-79165; CC P42858; Q8WWB5: PIH1D2; NbExp=3; IntAct=EBI-466029, EBI-10232538; CC P42858; P42336: PIK3CA; NbExp=3; IntAct=EBI-466029, EBI-2116585; CC P42858; P27986: PIK3R1; NbExp=7; IntAct=EBI-466029, EBI-79464; CC P42858; P27986-2: PIK3R1; NbExp=18; IntAct=EBI-466029, EBI-9090282; CC P42858; O00459: PIK3R2; NbExp=6; IntAct=EBI-466029, EBI-346930; CC P42858; Q92569: PIK3R3; NbExp=18; IntAct=EBI-466029, EBI-79893; CC P42858; Q9BXM7: PINK1; NbExp=9; IntAct=EBI-466029, EBI-2846068; CC P42858; Q96J94: PIWIL1; NbExp=3; IntAct=EBI-466029, EBI-527417; CC P42858; P14618: PKM; NbExp=9; IntAct=EBI-466029, EBI-353408; CC P42858; Q9BS22: PLA2G1B; NbExp=3; IntAct=EBI-466029, EBI-25961917; CC P42858; Q9UP65: PLA2G4C; NbExp=12; IntAct=EBI-466029, EBI-25848809; CC P42858; Q15149: PLEC; NbExp=4; IntAct=EBI-466029, EBI-297903; CC P42858; Q6ZR37: PLEKHG7; NbExp=12; IntAct=EBI-466029, EBI-12891828; CC P42858; Q9HCM2-3: PLXNA4; NbExp=3; IntAct=EBI-466029, EBI-25962330; CC P42858; Q6P1K2-3: PMF1; NbExp=3; IntAct=EBI-466029, EBI-12906008; CC P42858; Q8NBT0: POC1A; NbExp=15; IntAct=EBI-466029, EBI-2557132; CC P42858; Q9H2U2-3: PPA2; NbExp=3; IntAct=EBI-466029, EBI-25972548; CC P42858; Q9H2U2-6: PPA2; NbExp=3; IntAct=EBI-466029, EBI-25972564; CC P42858; Q07869: PPARA; NbExp=3; IntAct=EBI-466029, EBI-78615; CC P42858; Q03181-2: PPARD; NbExp=3; IntAct=EBI-466029, EBI-10223258; CC P42858; P37231: PPARG; NbExp=16; IntAct=EBI-466029, EBI-781384; CC P42858; Q59EV6: PPGB; NbExp=10; IntAct=EBI-466029, EBI-14210385; CC P42858; O43447: PPIH; NbExp=10; IntAct=EBI-466029, EBI-1055615; CC P42858; O60437: PPL; NbExp=8; IntAct=EBI-466029, EBI-368321; CC P42858; P62136: PPP1CA; NbExp=10; IntAct=EBI-466029, EBI-357253; CC P42858; Q96T49: PPP1R16B; NbExp=3; IntAct=EBI-466029, EBI-10293968; CC P42858; Q6ZMI0-5: PPP1R21; NbExp=9; IntAct=EBI-466029, EBI-25835994; CC P42858; Q16537: PPP2R5E; NbExp=15; IntAct=EBI-466029, EBI-968374; CC P42858; O75170-4: PPP6R2; NbExp=3; IntAct=EBI-466029, EBI-11079164; CC P42858; O60828: PQBP1; NbExp=3; IntAct=EBI-466029, EBI-713867; CC P42858; P49642: PRIM1; NbExp=3; IntAct=EBI-466029, EBI-726050; CC P42858; P17612: PRKACA; NbExp=3; IntAct=EBI-466029, EBI-476586; CC P42858; P55345: PRMT2; NbExp=3; IntAct=EBI-466029, EBI-78458; CC P42858; P04156: PRNP; NbExp=13; IntAct=EBI-466029, EBI-977302; CC P42858; Q53TL4: PRO0132; NbExp=3; IntAct=EBI-466029, EBI-25960611; CC P42858; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-466029, EBI-1567797; CC P42858; O75400: PRPF40A; NbExp=15; IntAct=EBI-466029, EBI-473291; CC P42858; O75400-2: PRPF40A; NbExp=9; IntAct=EBI-466029, EBI-5280197; CC P42858; Q96M27: PRRC1; NbExp=7; IntAct=EBI-466029, EBI-2560879; CC P42858; Q8WUY3: PRUNE2; NbExp=3; IntAct=EBI-466029, EBI-743880; CC P42858; P25786: PSMA1; NbExp=3; IntAct=EBI-466029, EBI-359352; CC P42858; P25789: PSMA4; NbExp=4; IntAct=EBI-466029, EBI-359310; CC P42858; P60900: PSMA6; NbExp=4; IntAct=EBI-466029, EBI-357793; CC P42858; O14818: PSMA7; NbExp=13; IntAct=EBI-466029, EBI-603272; CC P42858; P20618: PSMB1; NbExp=7; IntAct=EBI-466029, EBI-372273; CC P42858; P49721: PSMB2; NbExp=7; IntAct=EBI-466029, EBI-359335; CC P42858; P49720: PSMB3; NbExp=3; IntAct=EBI-466029, EBI-603340; CC P42858; P28072: PSMB6; NbExp=3; IntAct=EBI-466029, EBI-359288; CC P42858; P28062-2: PSMB8; NbExp=3; IntAct=EBI-466029, EBI-372312; CC P42858; P17980: PSMC3; NbExp=6; IntAct=EBI-466029, EBI-359720; CC P42858; O00487: PSMD14; NbExp=7; IntAct=EBI-466029, EBI-722193; CC P42858; O43242: PSMD3; NbExp=3; IntAct=EBI-466029, EBI-357622; CC P42858; P55036: PSMD4; NbExp=5; IntAct=EBI-466029, EBI-359318; CC P42858; P51665: PSMD7; NbExp=10; IntAct=EBI-466029, EBI-357659; CC P42858; Q13635-3: PTCH1; NbExp=3; IntAct=EBI-466029, EBI-14199621; CC P42858; P41222: PTGDS; NbExp=3; IntAct=EBI-466029, EBI-948821; CC P42858; Q13882: PTK6; NbExp=4; IntAct=EBI-466029, EBI-1383632; CC P42858; Q9UHX1-2: PUF60; NbExp=6; IntAct=EBI-466029, EBI-11529177; CC P42858; Q9UHX1-6: PUF60; NbExp=9; IntAct=EBI-466029, EBI-11085298; CC P42858; P47897: QARS1; NbExp=6; IntAct=EBI-466029, EBI-347462; CC P42858; Q15286: RAB35; NbExp=3; IntAct=EBI-466029, EBI-722275; CC P42858; P61020: RAB5B; NbExp=3; IntAct=EBI-466029, EBI-399401; CC P42858; P54725: RAD23A; NbExp=3; IntAct=EBI-466029, EBI-746453; CC P42858; P78406: RAE1; NbExp=4; IntAct=EBI-466029, EBI-724495; CC P42858; P62826: RAN; NbExp=6; IntAct=EBI-466029, EBI-286642; CC P42858; P46060: RANGAP1; NbExp=10; IntAct=EBI-466029, EBI-396091; CC P42858; Q8WZA2: RAPGEF4; NbExp=3; IntAct=EBI-466029, EBI-948476; CC P42858; Q13702-2: RAPSN; NbExp=18; IntAct=EBI-466029, EBI-22012855; CC P42858; P20936: RASA1; NbExp=3; IntAct=EBI-466029, EBI-1026476; CC P42858; Q6T310: RASL11A; NbExp=3; IntAct=EBI-466029, EBI-4401868; CC P42858; Q9NS23-4: RASSF1; NbExp=3; IntAct=EBI-466029, EBI-438710; CC P42858; P50749: RASSF2; NbExp=3; IntAct=EBI-466029, EBI-960081; CC P42858; Q8WWW0-2: RASSF5; NbExp=3; IntAct=EBI-466029, EBI-960502; CC P42858; O43251-3: RBFOX2; NbExp=3; IntAct=EBI-466029, EBI-11531589; CC P42858; P57052: RBM11; NbExp=9; IntAct=EBI-466029, EBI-741332; CC P42858; P52756: RBM5; NbExp=6; IntAct=EBI-466029, EBI-714003; CC P42858; Q93062-3: RBPMS; NbExp=3; IntAct=EBI-466029, EBI-740343; CC P42858; Q9UKA8: RCAN3; NbExp=18; IntAct=EBI-466029, EBI-9091952; CC P42858; Q15293: RCN1; NbExp=3; IntAct=EBI-466029, EBI-948278; CC P42858; Q9GZR2: REXO4; NbExp=3; IntAct=EBI-466029, EBI-2856313; CC P42858; Q8IXN7: RIMKLA; NbExp=3; IntAct=EBI-466029, EBI-21890191; CC P42858; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-466029, EBI-726876; CC P42858; Q5TAB7: RIPPLY2; NbExp=6; IntAct=EBI-466029, EBI-10246897; CC P42858; Q6ZNA4-2: RNF111; NbExp=18; IntAct=EBI-466029, EBI-21535400; CC P42858; Q9ULX5: RNF112; NbExp=21; IntAct=EBI-466029, EBI-25829984; CC P42858; Q96D59: RNF183; NbExp=3; IntAct=EBI-466029, EBI-743938; CC P42858; Q5VTR2: RNF20; NbExp=24; IntAct=EBI-466029, EBI-2372238; CC P42858; Q9H0F5-2: RNF38; NbExp=21; IntAct=EBI-466029, EBI-25866807; CC P42858; O75150: RNF40; NbExp=12; IntAct=EBI-466029, EBI-744408; CC P42858; P26373: RPL13; NbExp=10; IntAct=EBI-466029, EBI-356849; CC P42858; Q6NZ55: RPL13; NbExp=3; IntAct=EBI-466029, EBI-10252046; CC P42858; P61313: RPL15; NbExp=3; IntAct=EBI-466029, EBI-443462; CC P42858; Q07020: RPL18; NbExp=12; IntAct=EBI-466029, EBI-352694; CC P42858; P84098: RPL19; NbExp=6; IntAct=EBI-466029, EBI-916524; CC P42858; P35268: RPL22; NbExp=3; IntAct=EBI-466029, EBI-354533; CC P42858; Q9UNX3: RPL26L1; NbExp=3; IntAct=EBI-466029, EBI-2949703; CC P42858; P61353: RPL27; NbExp=6; IntAct=EBI-466029, EBI-352760; CC P42858; P62899: RPL31; NbExp=3; IntAct=EBI-466029, EBI-1053664; CC P42858; P36578: RPL4; NbExp=14; IntAct=EBI-466029, EBI-348313; CC P42858; P25398: RPS12; NbExp=3; IntAct=EBI-466029, EBI-354542; CC P42858; P62244: RPS15A; NbExp=3; IntAct=EBI-466029, EBI-347895; CC P42858; P39019: RPS19; NbExp=3; IntAct=EBI-466029, EBI-354451; CC P42858; P62979: RPS27A; NbExp=6; IntAct=EBI-466029, EBI-357375; CC P42858; P23396: RPS3; NbExp=3; IntAct=EBI-466029, EBI-351193; CC P42858; P46782: RPS5; NbExp=3; IntAct=EBI-466029, EBI-350569; CC P42858; Q16799-3: RTN1; NbExp=9; IntAct=EBI-466029, EBI-10180131; CC P42858; Q6ZNE9: RUFY4; NbExp=3; IntAct=EBI-466029, EBI-10181525; CC P42858; Q66K80: RUSC1-AS1; NbExp=6; IntAct=EBI-466029, EBI-10248967; CC P42858; Q96GQ5: RUSF1; NbExp=3; IntAct=EBI-466029, EBI-8636004; CC P42858; P48443: RXRG; NbExp=18; IntAct=EBI-466029, EBI-712405; CC P42858; Q8N488: RYBP; NbExp=9; IntAct=EBI-466029, EBI-752324; CC P42858; P25815: S100P; NbExp=9; IntAct=EBI-466029, EBI-743700; CC P42858; Q8N6K7-2: SAMD3; NbExp=3; IntAct=EBI-466029, EBI-11528848; CC P42858; G3V2R1: SAMD4A; NbExp=3; IntAct=EBI-466029, EBI-21264240; CC P42858; O75446: SAP30; NbExp=3; IntAct=EBI-466029, EBI-632609; CC P42858; Q6UVJ0: SASS6; NbExp=15; IntAct=EBI-466029, EBI-1570153; CC P42858; Q9BY12-3: SCAPER; NbExp=6; IntAct=EBI-466029, EBI-25837959; CC P42858; Q8WVM8: SCFD1; NbExp=3; IntAct=EBI-466029, EBI-722569; CC P42858; Q96NL6-3: SCLT1; NbExp=3; IntAct=EBI-466029, EBI-25961722; CC P42858; Q12765-2: SCRN1; NbExp=3; IntAct=EBI-466029, EBI-12027936; CC P42858; O00560: SDCBP; NbExp=12; IntAct=EBI-466029, EBI-727004; CC P42858; P55735-3: SEC13; NbExp=15; IntAct=EBI-466029, EBI-12235008; CC P42858; Q15437: SEC23B; NbExp=3; IntAct=EBI-466029, EBI-742673; CC P42858; Q96T21: SECISBP2; NbExp=3; IntAct=EBI-466029, EBI-954116; CC P42858; O43236: SEPTIN4; NbExp=3; IntAct=EBI-466029, EBI-1047513; CC P42858; Q14141: SEPTIN6; NbExp=18; IntAct=EBI-466029, EBI-745901; CC P42858; Q16181-2: SEPTIN7; NbExp=9; IntAct=EBI-466029, EBI-10176094; CC P42858; Q9UHV2: SERTAD1; NbExp=3; IntAct=EBI-466029, EBI-748601; CC P42858; Q9BYW2: SETD2; NbExp=4; IntAct=EBI-466029, EBI-945869; CC P42858; Q15047-2: SETDB1; NbExp=15; IntAct=EBI-466029, EBI-9090795; CC P42858; Q12874: SF3A3; NbExp=3; IntAct=EBI-466029, EBI-1051880; CC P42858; Q15393: SF3B3; NbExp=3; IntAct=EBI-466029, EBI-346977; CC P42858; Q9BWM7: SFXN3; NbExp=9; IntAct=EBI-466029, EBI-1171999; CC P42858; Q2NKQ1-4: SGSM1; NbExp=12; IntAct=EBI-466029, EBI-10182463; CC P42858; Q99961: SH3GL1; NbExp=3; IntAct=EBI-466029, EBI-697911; CC P42858; Q99963: SH3GL3; NbExp=9; IntAct=EBI-466029, EBI-473910; CC P42858; Q9NR46: SH3GLB2; NbExp=3; IntAct=EBI-466029, EBI-749607; CC P42858; Q8IYI0: SHLD1; NbExp=3; IntAct=EBI-466029, EBI-2560428; CC P42858; Q9Y2K2-7: SIK3; NbExp=3; IntAct=EBI-466029, EBI-17172855; CC P42858; Q96ST3: SIN3A; NbExp=4; IntAct=EBI-466029, EBI-347218; CC P42858; P43004: SLC1A2; NbExp=12; IntAct=EBI-466029, EBI-3440986; CC P42858; Q02978: SLC25A11; NbExp=6; IntAct=EBI-466029, EBI-359174; CC P42858; Q00325-2: SLC25A3; NbExp=3; IntAct=EBI-466029, EBI-5456178; CC P42858; Q8NCS7: SLC44A5; NbExp=3; IntAct=EBI-466029, EBI-21504521; CC P42858; Q12824: SMARCB1; NbExp=9; IntAct=EBI-466029, EBI-358419; CC P42858; Q8TAQ2-2: SMARCC2; NbExp=3; IntAct=EBI-466029, EBI-11990400; CC P42858; Q96GM5: SMARCD1; NbExp=12; IntAct=EBI-466029, EBI-358489; CC P42858; Q16637-3: SMN2; NbExp=9; IntAct=EBI-466029, EBI-395447; CC P42858; Q9HCE7-2: SMURF1; NbExp=6; IntAct=EBI-466029, EBI-9845742; CC P42858; P60880-2: SNAP25; NbExp=9; IntAct=EBI-466029, EBI-12177361; CC P42858; O95721: SNAP29; NbExp=3; IntAct=EBI-466029, EBI-490676; CC P42858; P37840: SNCA; NbExp=4; IntAct=EBI-466029, EBI-985879; CC P42858; P62316: SNRPD2; NbExp=3; IntAct=EBI-466029, EBI-297993; CC P42858; P62306: SNRPF; NbExp=3; IntAct=EBI-466029, EBI-356900; CC P42858; Q13573: SNW1; NbExp=12; IntAct=EBI-466029, EBI-632715; CC P42858; Q9UMY4: SNX12; NbExp=3; IntAct=EBI-466029, EBI-1752602; CC P42858; O60749: SNX2; NbExp=6; IntAct=EBI-466029, EBI-1046690; CC P42858; Q8WV41: SNX33; NbExp=6; IntAct=EBI-466029, EBI-2481535; CC P42858; Q8WXH5: SOCS4; NbExp=3; IntAct=EBI-466029, EBI-3942425; CC P42858; Q9BX66: SORBS1; NbExp=4; IntAct=EBI-466029, EBI-433642; CC P42858; O95416: SOX14; NbExp=12; IntAct=EBI-466029, EBI-9087806; CC P42858; Q9BT81: SOX7; NbExp=15; IntAct=EBI-466029, EBI-7239117; CC P42858; Q02447: SP3; NbExp=4; IntAct=EBI-466029, EBI-348158; CC P42858; Q3SY56: SP6; NbExp=3; IntAct=EBI-466029, EBI-11175533; CC P42858; Q99932-2: SPAG8; NbExp=18; IntAct=EBI-466029, EBI-11959123; CC P42858; Q9NY87: SPANXC; NbExp=3; IntAct=EBI-466029, EBI-10316585; CC P42858; Q7Z6I5: SPATA12; NbExp=3; IntAct=EBI-466029, EBI-10696971; CC P42858; Q8NHS9: SPATA22; NbExp=9; IntAct=EBI-466029, EBI-7067260; CC P42858; Q8IUW3: SPATA2L; NbExp=6; IntAct=EBI-466029, EBI-2510414; CC P42858; P61009: SPCS3; NbExp=6; IntAct=EBI-466029, EBI-6166040; CC P42858; Q01892: SPIB; NbExp=18; IntAct=EBI-466029, EBI-2800992; CC P42858; Q1W4C9: SPINK13; NbExp=3; IntAct=EBI-466029, EBI-25953827; CC P42858; Q7Z698: SPRED2; NbExp=6; IntAct=EBI-466029, EBI-7082156; CC P42858; Q13501: SQSTM1; NbExp=8; IntAct=EBI-466029, EBI-307104; CC P42858; P36956: SREBF1; NbExp=3; IntAct=EBI-466029, EBI-948313; CC P42858; Q7Z6B7: SRGAP1; NbExp=4; IntAct=EBI-466029, EBI-2481729; CC P42858; O75044: SRGAP2; NbExp=3; IntAct=EBI-466029, EBI-1051034; CC P42858; O43295: SRGAP3; NbExp=4; IntAct=EBI-466029, EBI-368166; CC P42858; Q8IXS7: SRGAP3; NbExp=3; IntAct=EBI-466029, EBI-18616594; CC P42858; Q9BXP5: SRRT; NbExp=3; IntAct=EBI-466029, EBI-712721; CC P42858; Q9BXP5-3: SRRT; NbExp=6; IntAct=EBI-466029, EBI-25866384; CC P42858; Q9BXP5-4: SRRT; NbExp=3; IntAct=EBI-466029, EBI-16701991; CC P42858; P05455: SSB; NbExp=3; IntAct=EBI-466029, EBI-358037; CC P42858; Q9NP77: SSU72; NbExp=3; IntAct=EBI-466029, EBI-2515416; CC P42858; P50502: ST13; NbExp=13; IntAct=EBI-466029, EBI-357285; CC P42858; O75886: STAM2; NbExp=6; IntAct=EBI-466029, EBI-373258; CC P42858; P49675: STAR; NbExp=3; IntAct=EBI-466029, EBI-722932; CC P42858; Q9H668: STN1; NbExp=3; IntAct=EBI-466029, EBI-746930; CC P42858; Q9Y3F4: STRAP; NbExp=4; IntAct=EBI-466029, EBI-727414; CC P42858; A1L378: STRC; NbExp=6; IntAct=EBI-466029, EBI-22013242; CC P42858; Q9UNE7: STUB1; NbExp=12; IntAct=EBI-466029, EBI-357085; CC P42858; O14662-5: STX16; NbExp=15; IntAct=EBI-466029, EBI-9089968; CC P42858; P61764: STXBP1; NbExp=7; IntAct=EBI-466029, EBI-960169; CC P42858; Q9BR01-2: SULT4A1; NbExp=15; IntAct=EBI-466029, EBI-25831443; CC P42858; Q8NBJ7: SUMF2; NbExp=6; IntAct=EBI-466029, EBI-723091; CC P42858; P63165: SUMO1; NbExp=3; IntAct=EBI-466029, EBI-80140; CC P42858; P55854: SUMO3; NbExp=9; IntAct=EBI-466029, EBI-474067; CC P42858; A1L190: SYCE3; NbExp=15; IntAct=EBI-466029, EBI-10283466; CC P42858; Q92797: SYMPK; NbExp=3; IntAct=EBI-466029, EBI-1051992; CC P42858; Q92797-2: SYMPK; NbExp=9; IntAct=EBI-466029, EBI-21560407; CC P42858; P08247: SYP; NbExp=13; IntAct=EBI-466029, EBI-9071725; CC P42858; Q9BQS2-2: SYT15; NbExp=3; IntAct=EBI-466029, EBI-13373352; CC P42858; Q8N9I0: SYT2; NbExp=10; IntAct=EBI-466029, EBI-8032987; CC P42858; Q9BQG1: SYT3; NbExp=12; IntAct=EBI-466029, EBI-17284568; CC P42858; Q5T7P8-2: SYT6; NbExp=3; IntAct=EBI-466029, EBI-10246152; CC P42858; O75410: TACC1; NbExp=4; IntAct=EBI-466029, EBI-624237; CC P42858; O75410-7: TACC1; NbExp=12; IntAct=EBI-466029, EBI-12007872; CC P42858; Q86TJ2-3: TADA2B; NbExp=3; IntAct=EBI-466029, EBI-18173581; CC P42858; P37802: TAGLN2; NbExp=3; IntAct=EBI-466029, EBI-1056740; CC P42858; P37837: TALDO1; NbExp=3; IntAct=EBI-466029, EBI-1056712; CC P42858; Q6NW12: TANK; NbExp=9; IntAct=EBI-466029, EBI-25948253; CC P42858; Q92844: TANK; NbExp=3; IntAct=EBI-466029, EBI-356349; CC P42858; Q92844-3: TANK; NbExp=3; IntAct=EBI-466029, EBI-25967460; CC P42858; Q9H2K8: TAOK3; NbExp=3; IntAct=EBI-466029, EBI-1384100; CC P42858; Q5VWN6: TASOR2; NbExp=12; IntAct=EBI-466029, EBI-745958; CC P42858; Q92609: TBC1D5; NbExp=3; IntAct=EBI-466029, EBI-742381; CC P42858; Q32MN6: TBP; NbExp=9; IntAct=EBI-466029, EBI-10239991; CC P42858; Q16650: TBR1; NbExp=12; IntAct=EBI-466029, EBI-1047158; CC P42858; Q9Y458: TBX22; NbExp=12; IntAct=EBI-466029, EBI-6427217; CC P42858; O14776: TCERG1; NbExp=9; IntAct=EBI-466029, EBI-473271; CC P42858; P17987: TCP1; NbExp=3; IntAct=EBI-466029, EBI-356553; CC P42858; Q8TDR4: TCP10L; NbExp=3; IntAct=EBI-466029, EBI-3923210; CC P42858; P28347-2: TEAD1; NbExp=18; IntAct=EBI-466029, EBI-12151837; CC P42858; Q86WV5: TEN1; NbExp=9; IntAct=EBI-466029, EBI-2562799; CC P42858; Q96A09: TENT5B; NbExp=6; IntAct=EBI-466029, EBI-752030; CC P42858; Q15554-4: TERF2; NbExp=15; IntAct=EBI-466029, EBI-25840535; CC P42858; Q96M34: TEX55; NbExp=3; IntAct=EBI-466029, EBI-25961624; CC P42858; Q03403: TFF2; NbExp=18; IntAct=EBI-466029, EBI-4314702; CC P42858; Q92734: TFG; NbExp=3; IntAct=EBI-466029, EBI-357061; CC P42858; O95455: TGDS; NbExp=3; IntAct=EBI-466029, EBI-1761487; CC P42858; P37173: TGFBR2; NbExp=3; IntAct=EBI-466029, EBI-296151; CC P42858; P21980-2: TGM2; NbExp=6; IntAct=EBI-466029, EBI-25842075; CC P42858; Q96MW7: TIGD1; NbExp=9; IntAct=EBI-466029, EBI-9091586; CC P42858; O60220: TIMM8A; NbExp=15; IntAct=EBI-466029, EBI-1049822; CC P42858; Q08117: TLE5; NbExp=3; IntAct=EBI-466029, EBI-717810; CC P42858; Q9BZW5-2: TM6SF1; NbExp=3; IntAct=EBI-466029, EBI-25852210; CC P42858; Q96EY4: TMA16; NbExp=3; IntAct=EBI-466029, EBI-1045338; CC P42858; Q9NUM4: TMEM106B; NbExp=3; IntAct=EBI-466029, EBI-10490807; CC P42858; Q12893: TMEM115; NbExp=3; IntAct=EBI-466029, EBI-8633987; CC P42858; Q6UW68: TMEM205; NbExp=3; IntAct=EBI-466029, EBI-6269551; CC P42858; Q8WW34-2: TMEM239; NbExp=3; IntAct=EBI-466029, EBI-11528917; CC P42858; Q9NV96-2: TMEM30A; NbExp=3; IntAct=EBI-466029, EBI-12921610; CC P42858; Q9BTV4: TMEM43; NbExp=3; IntAct=EBI-466029, EBI-721293; CC P42858; Q9BQJ4: TMEM47; NbExp=3; IntAct=EBI-466029, EBI-13370320; CC P42858; Q8IUR5-4: TMTC1; NbExp=6; IntAct=EBI-466029, EBI-9089156; CC P42858; Q71RG4-4: TMUB2; NbExp=6; IntAct=EBI-466029, EBI-25831574; CC P42858; Q13829: TNFAIP1; NbExp=3; IntAct=EBI-466029, EBI-2505861; CC P42858; O00300: TNFRSF11B; NbExp=3; IntAct=EBI-466029, EBI-15481185; CC P42858; O95150: TNFSF15; NbExp=3; IntAct=EBI-466029, EBI-16355546; CC P42858; Q96KP6: TNIP3; NbExp=9; IntAct=EBI-466029, EBI-2509913; CC P42858; P22105-1: TNXB; NbExp=3; IntAct=EBI-466029, EBI-20753895; CC P42858; Q9NS69: TOMM22; NbExp=6; IntAct=EBI-466029, EBI-1047508; CC P42858; P04637: TP53; NbExp=19; IntAct=EBI-466029, EBI-366083; CC P42858; P60174: TPI1; NbExp=6; IntAct=EBI-466029, EBI-717475; CC P42858; Q12933: TRAF2; NbExp=3; IntAct=EBI-466029, EBI-355744; CC P42858; O14545: TRAFD1; NbExp=5; IntAct=EBI-466029, EBI-1396921; CC P42858; P19474: TRIM21; NbExp=21; IntAct=EBI-466029, EBI-81290; CC P42858; Q9UPQ4-2: TRIM35; NbExp=9; IntAct=EBI-466029, EBI-17716262; CC P42858; P0CI25: TRIM49; NbExp=9; IntAct=EBI-466029, EBI-6427421; CC P42858; Q15642-2: TRIP10; NbExp=18; IntAct=EBI-466029, EBI-6550597; CC P42858; Q15654: TRIP6; NbExp=3; IntAct=EBI-466029, EBI-742327; CC P42858; Q99614: TTC1; NbExp=9; IntAct=EBI-466029, EBI-742074; CC P42858; Q6DKK2: TTC19; NbExp=3; IntAct=EBI-466029, EBI-948354; CC P42858; Q5W5X9-3: TTC23; NbExp=18; IntAct=EBI-466029, EBI-9090990; CC P42858; Q71U36: TUBA1A; NbExp=3; IntAct=EBI-466029, EBI-302552; CC P42858; P07437: TUBB; NbExp=9; IntAct=EBI-466029, EBI-350864; CC P42858; Q9BUF5: TUBB6; NbExp=3; IntAct=EBI-466029, EBI-356735; CC P42858; Q9UGJ1-2: TUBGCP4; NbExp=6; IntAct=EBI-466029, EBI-10964469; CC P42858; Q15672: TWIST1; NbExp=3; IntAct=EBI-466029, EBI-1797287; CC P42858; Q8WVJ9: TWIST2; NbExp=15; IntAct=EBI-466029, EBI-1797313; CC P42858; Q99757: TXN2; NbExp=3; IntAct=EBI-466029, EBI-2932492; CC P42858; Q6PKC3: TXNDC11; NbExp=7; IntAct=EBI-466029, EBI-749812; CC P42858; Q01081: U2AF1; NbExp=3; IntAct=EBI-466029, EBI-632461; CC P42858; P22314: UBA1; NbExp=3; IntAct=EBI-466029, EBI-709688; CC P42858; Q9BSL1: UBAC1; NbExp=26; IntAct=EBI-466029, EBI-749370; CC P42858; P0CG48: UBC; NbExp=3; IntAct=EBI-466029, EBI-3390054; CC P42858; Q9Y2X8: UBE2D4; NbExp=3; IntAct=EBI-466029, EBI-745527; CC P42858; P62256: UBE2H; NbExp=3; IntAct=EBI-466029, EBI-2129909; CC P42858; P63279: UBE2I; NbExp=3; IntAct=EBI-466029, EBI-80168; CC P42858; P61086: UBE2K; NbExp=24; IntAct=EBI-466029, EBI-473850; CC P42858; Q9UHD9: UBQLN2; NbExp=12; IntAct=EBI-466029, EBI-947187; CC P42858; Q92890: UFD1; NbExp=7; IntAct=EBI-466029, EBI-1994090; CC P42858; O75385: ULK1; NbExp=8; IntAct=EBI-466029, EBI-908831; CC P42858; Q495M9: USH1G; NbExp=3; IntAct=EBI-466029, EBI-8601749; CC P42858; Q9UMW8: USP18; NbExp=3; IntAct=EBI-466029, EBI-356206; CC P42858; O75604-3: USP2; NbExp=6; IntAct=EBI-466029, EBI-10696113; CC P42858; Q9UPU5: USP24; NbExp=21; IntAct=EBI-466029, EBI-1642365; CC P42858; Q8NFA0-2: USP32; NbExp=18; IntAct=EBI-466029, EBI-12220239; CC P42858; Q93008: USP9X; NbExp=8; IntAct=EBI-466029, EBI-302524; CC P42858; Q9BVJ6: UTP14A; NbExp=4; IntAct=EBI-466029, EBI-473284; CC P42858; Q9NYH9: UTP6; NbExp=3; IntAct=EBI-466029, EBI-749211; CC P42858; Q08AM6: VAC14; NbExp=3; IntAct=EBI-466029, EBI-2107455; CC P42858; Q9HCJ6: VAT1L; NbExp=3; IntAct=EBI-466029, EBI-10234766; CC P42858; P55072: VCP; NbExp=10; IntAct=EBI-466029, EBI-355164; CC P42858; P45880: VDAC2; NbExp=22; IntAct=EBI-466029, EBI-354022; CC P42858; P40337-2: VHL; NbExp=12; IntAct=EBI-466029, EBI-12157263; CC P42858; P09327-2: VIL1; NbExp=3; IntAct=EBI-466029, EBI-25958818; CC P42858; P08670: VIM; NbExp=4; IntAct=EBI-466029, EBI-353844; CC P42858; Q9UK41: VPS28; NbExp=16; IntAct=EBI-466029, EBI-727424; CC P42858; Q8NEZ2: VPS37A; NbExp=6; IntAct=EBI-466029, EBI-2850578; CC P42858; O75351: VPS4B; NbExp=3; IntAct=EBI-466029, EBI-2514459; CC P42858; Q9BTA9: WAC; NbExp=5; IntAct=EBI-466029, EBI-749118; CC P42858; Q9BTA9-5: WAC; NbExp=3; IntAct=EBI-466029, EBI-25956668; CC P42858; O75554: WBP4; NbExp=3; IntAct=EBI-466029, EBI-7251981; CC P42858; Q8IZQ1: WDFY3; NbExp=10; IntAct=EBI-466029, EBI-1569256; CC P42858; Q9GZS3: WDR61; NbExp=22; IntAct=EBI-466029, EBI-358545; CC P42858; A4D1P6: WDR91; NbExp=16; IntAct=EBI-466029, EBI-718046; CC P42858; Q15007-2: WTAP; NbExp=3; IntAct=EBI-466029, EBI-25840023; CC P42858; O00308: WWP2; NbExp=9; IntAct=EBI-466029, EBI-743923; CC P42858; Q9HCS7: XAB2; NbExp=3; IntAct=EBI-466029, EBI-295232; CC P42858; Q8WTP9: XAGE3; NbExp=3; IntAct=EBI-466029, EBI-6448284; CC P42858; P12956: XRCC6; NbExp=21; IntAct=EBI-466029, EBI-353208; CC P42858; O95070: YIF1A; NbExp=12; IntAct=EBI-466029, EBI-2799703; CC P42858; P31946: YWHAB; NbExp=11; IntAct=EBI-466029, EBI-359815; CC P42858; Q9H869-2: YY1AP1; NbExp=3; IntAct=EBI-466029, EBI-12150045; CC P42858; Q9H171: ZBP1; NbExp=6; IntAct=EBI-466029, EBI-6264672; CC P42858; Q05516: ZBTB16; NbExp=4; IntAct=EBI-466029, EBI-711925; CC P42858; O43167-2: ZBTB24; NbExp=9; IntAct=EBI-466029, EBI-25842419; CC P42858; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-466029, EBI-14104088; CC P42858; Q6PEW1: ZCCHC12; NbExp=3; IntAct=EBI-466029, EBI-748373; CC P42858; Q8IUH5: ZDHHC17; NbExp=30; IntAct=EBI-466029, EBI-524753; CC P42858; Q8WVZ1-3: ZDHHC19; NbExp=3; IntAct=EBI-466029, EBI-25961277; CC P42858; G3V1X1: ZFC3H1; NbExp=5; IntAct=EBI-466029, EBI-6448783; CC P42858; Q6ZN57: ZFP2; NbExp=12; IntAct=EBI-466029, EBI-7236323; CC P42858; Q96K21: ZFYVE19; NbExp=21; IntAct=EBI-466029, EBI-6448240; CC P42858; Q9UKY1: ZHX1; NbExp=6; IntAct=EBI-466029, EBI-347767; CC P42858; Q96EF9: ZHX1-C8orf76; NbExp=18; IntAct=EBI-466029, EBI-25830993; CC P42858; Q9BRR0: ZKSCAN3; NbExp=3; IntAct=EBI-466029, EBI-1965777; CC P42858; Q15776: ZKSCAN8; NbExp=9; IntAct=EBI-466029, EBI-2602314; CC P42858; Q96NC0: ZMAT2; NbExp=20; IntAct=EBI-466029, EBI-2682299; CC P42858; O95789-4: ZMYM6; NbExp=3; IntAct=EBI-466029, EBI-12949277; CC P42858; P52744: ZNF138; NbExp=9; IntAct=EBI-466029, EBI-10746567; CC P42858; Q9UJW8-4: ZNF180; NbExp=9; IntAct=EBI-466029, EBI-12055755; CC P42858; P17023: ZNF19; NbExp=3; IntAct=EBI-466029, EBI-12884200; CC P42858; Q9BSG1: ZNF2; NbExp=3; IntAct=EBI-466029, EBI-8489229; CC P42858; Q9Y2X9: ZNF281; NbExp=3; IntAct=EBI-466029, EBI-396200; CC P42858; Q9HBT8: ZNF286A; NbExp=9; IntAct=EBI-466029, EBI-10754950; CC P42858; Q9NR11-2: ZNF302; NbExp=3; IntAct=EBI-466029, EBI-12988373; CC P42858; Q8N895: ZNF366; NbExp=15; IntAct=EBI-466029, EBI-2813661; CC P42858; Q9C0F3: ZNF436; NbExp=15; IntAct=EBI-466029, EBI-8489702; CC P42858; Q8N0Y2-2: ZNF444; NbExp=9; IntAct=EBI-466029, EBI-12010736; CC P42858; Q6ZNH5: ZNF497; NbExp=9; IntAct=EBI-466029, EBI-10486136; CC P42858; O60304: ZNF500; NbExp=6; IntAct=EBI-466029, EBI-18234077; CC P42858; Q8N988-2: ZNF557; NbExp=12; IntAct=EBI-466029, EBI-10699005; CC P42858; Q68EA5: ZNF57; NbExp=15; IntAct=EBI-466029, EBI-8490788; CC P42858; Q7Z3I7: ZNF572; NbExp=9; IntAct=EBI-466029, EBI-10172590; CC P42858; Q96N77-2: ZNF641; NbExp=18; IntAct=EBI-466029, EBI-12939666; CC P42858; Q8N720: ZNF655; NbExp=14; IntAct=EBI-466029, EBI-625509; CC P42858; Q5TEC3: ZNF697; NbExp=3; IntAct=EBI-466029, EBI-25845217; CC P42858; Q3KNS6-3: ZNF829; NbExp=6; IntAct=EBI-466029, EBI-18036029; CC P42858; O15535: ZSCAN9; NbExp=9; IntAct=EBI-466029, EBI-751531; CC P42858; Q2QGD7: ZXDC; NbExp=3; IntAct=EBI-466029, EBI-1538838; CC P42858; A8K3Q9; NbExp=3; IntAct=EBI-466029, EBI-10174314; CC P42858; A8K878; NbExp=21; IntAct=EBI-466029, EBI-25831303; CC P42858; B7Z3E8; NbExp=6; IntAct=EBI-466029, EBI-25831617; CC P42858; Q0VG73; NbExp=6; IntAct=EBI-466029, EBI-25953074; CC P42858; Q7L8T7; NbExp=6; IntAct=EBI-466029, EBI-25831943; CC P42858; Q86V28; NbExp=6; IntAct=EBI-466029, EBI-10259496; CC P42858; Q96IQ6; NbExp=6; IntAct=EBI-466029, EBI-10295632; CC P42858; O88485: Dync1i1; Xeno; NbExp=2; IntAct=EBI-466029, EBI-492834; CC P42858; P54256: Hap1; Xeno; NbExp=3; IntAct=EBI-466029, EBI-994539; CC P42858; P51660: Hsd17b4; Xeno; NbExp=15; IntAct=EBI-466029, EBI-8328056; CC P42858; P29994: Itpr1; Xeno; NbExp=2; IntAct=EBI-466029, EBI-8614640; CC P42858; Q99KR7: Ppif; Xeno; NbExp=3; IntAct=EBI-466029, EBI-6455001; CC -!- SUBCELLULAR LOCATION: [Huntingtin]: Cytoplasm CC {ECO:0000269|PubMed:15654337, ECO:0000269|PubMed:16476778, CC ECO:0000269|PubMed:7647777}. Nucleus {ECO:0000269|PubMed:15654337, CC ECO:0000269|PubMed:16391387}. Early endosome CC {ECO:0000269|PubMed:16476778}. Note=The mutant Huntingtin protein CC colocalizes with AKAP8L in the nuclear matrix of Huntington disease CC neurons. Shuttles between cytoplasm and nucleus in a Ran GTPase- CC independent manner (PubMed:15654337). Recruits onto early endosomes in CC a Rab5- and HAP40-dependent fashion (PubMed:16476778). CC {ECO:0000269|PubMed:15654337, ECO:0000269|PubMed:16476778}. CC -!- SUBCELLULAR LOCATION: [Huntingtin, myristoylated N-terminal fragment]: CC Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:24459296}. CC -!- TISSUE SPECIFICITY: Expressed in the brain cortex (at protein level). CC Widely expressed with the highest level of expression in the brain CC (nerve fibers, varicosities, and nerve endings). In the brain, the CC regions where it can be mainly found are the cerebellar cortex, the CC neocortex, the striatum, and the hippocampal formation. CC {ECO:0000269|PubMed:16391387}. CC -!- DOMAIN: The N-terminal Gln-rich and Pro-rich domain has great CC conformational flexibility and is likely to exist in a fluctuating CC equilibrium of alpha-helical, random coil, and extended conformations. CC {ECO:0000269|PubMed:19748341}. CC -!- PTM: [Huntingtin]: Cleaved by caspases downstream of the polyglutamine CC stretch (PubMed:8696339, PubMed:9535906, PubMed:10770929, CC PubMed:29802276). The resulting N-terminal fragments are cytotoxic and CC provokes apoptosis (PubMed:10770929). {ECO:0000269|PubMed:10770929, CC ECO:0000269|PubMed:29802276, ECO:0000269|PubMed:8696339, CC ECO:0000269|PubMed:9535906}. CC -!- PTM: [Huntingtin]: Forms with expanded polyglutamine expansion are CC specifically ubiquitinated by SYVN1, which promotes their proteasomal CC degradation. {ECO:0000269|PubMed:17141218}. CC -!- PTM: [Huntingtin]: Phosphorylation at Ser-1179 and Ser-1199 by CDK5 in CC response to DNA damage in nuclei of neurons protects neurons against CC polyglutamine expansion as well as DNA damage mediated toxicity. CC {ECO:0000269|PubMed:17611284}. CC -!- PTM: [Huntingtin, myristoylated N-terminal fragment]: Myristoylated at CC Gly-551, following proteolytic cleavage at Asp-550. CC {ECO:0000269|PubMed:24459296, ECO:0000269|PubMed:29802276}. CC -!- POLYMORPHISM: The poly-Gln region of HTT is highly polymorphic (10 to CC 35 repeats) in the normal population and is expanded to about 36-120 CC repeats in Huntington disease patients. The repeat length usually CC increases in successive generations, but contracts also on occasion. CC The adjacent poly-Pro region is also polymorphic and varies between 7- CC 12 residues. Polyglutamine expansion leads to elevated susceptibility CC to apopain cleavage and likely result in accelerated neuronal apoptosis CC (PubMed:8696339). {ECO:0000269|PubMed:8696339}. CC -!- DISEASE: Huntington disease (HD) [MIM:143100]: A neurodegenerative CC disorder characterized by involuntary movements (chorea), general motor CC impairment, psychiatric disorders and dementia. Onset of the disease CC occurs usually in the third or fourth decade of life. Onset and CC clinical course depend on the degree of poly-Gln repeat expansion, CC longer expansions resulting in earlier onset and more severe clinical CC manifestations. Neuropathology of Huntington disease displays a CC distinctive pattern with loss of neurons, especially in the caudate and CC putamen. {ECO:0000269|PubMed:8458085}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- DISEASE: Lopes-Maciel-Rodan syndrome (LOMARS) [MIM:617435]: An CC autosomal recessive neurodevelopmental disorder characterized by CC developmental regression in infancy, delayed psychomotor development, CC severe intellectual disability, and cerebral and cerebellar atrophy. CC Additional features include swallowing problems, dystonia, CC bradykinesia, and continuous manual stereotypies without chorea. Some CC patients manifest seizures. {ECO:0000269|PubMed:26740508, CC ECO:0000269|PubMed:27329733}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the huntingtin family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Huntingtin entry; CC URL="https://en.wikipedia.org/wiki/Huntingtin"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L12392; AAB38240.1; -; mRNA. DR EMBL; AB016794; BAA36753.1; -; mRNA. DR EMBL; Z49154; CAA89024.1; -; Genomic_DNA. DR EMBL; Z49155; CAA89025.1; -; Genomic_DNA. DR EMBL; Z49208; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z49769; CAA89839.1; -; Genomic_DNA. DR EMBL; Z68756; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z69649; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; L27350; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; L27351; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; L27352; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; L27353; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; L27354; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; L34020; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; L20431; AAA52702.1; -; mRNA. DR PIR; A46068; A46068. DR RefSeq; NP_002102.4; NM_002111.8. DR PDB; 2LD0; NMR; -; A=1-17. DR PDB; 2LD2; NMR; -; A=1-17. DR PDB; 3IO4; X-ray; 3.63 A; A/B/C=1-64. DR PDB; 3IO6; X-ray; 3.70 A; A/B/C=1-64. DR PDB; 3IOR; X-ray; 3.60 A; A/B/C=1-64. DR PDB; 3IOT; X-ray; 3.50 A; A/B/C=1-64. DR PDB; 3IOU; X-ray; 3.70 A; A/B/C=1-64. DR PDB; 3IOV; X-ray; 3.70 A; A/B/C=1-64. DR PDB; 3IOW; X-ray; 3.50 A; A/B/C=1-64. DR PDB; 3LRH; X-ray; 2.60 A; B/D/F/H/J/L/N/P=5-18. DR PDB; 4FE8; X-ray; 3.00 A; A/B/C=1-64. DR PDB; 4FEB; X-ray; 2.80 A; A/B/C=1-64. DR PDB; 4FEC; X-ray; 3.00 A; A/B/C=1-64. DR PDB; 4FED; X-ray; 2.81 A; A/B/C=1-64. DR PDB; 4RAV; X-ray; 2.50 A; E/F=1-17. DR PDB; 6EZ8; EM; 4.00 A; A=1-3142. DR PDB; 6N8C; NMR; -; A/B/C/D=2-24. DR PDB; 6RMH; EM; 9.60 A; A=1-3142. DR PDB; 6X9O; EM; 2.60 A; A=1-3142. DR PDB; 6YEJ; EM; 18.20 A; A=18-3142. DR PDB; 7DXJ; EM; 3.60 A; A=1-3142. DR PDB; 7DXK; EM; 4.10 A; A=18-3142. DR PDBsum; 2LD0; -. DR PDBsum; 2LD2; -. DR PDBsum; 3IO4; -. DR PDBsum; 3IO6; -. DR PDBsum; 3IOR; -. DR PDBsum; 3IOT; -. DR PDBsum; 3IOU; -. DR PDBsum; 3IOV; -. DR PDBsum; 3IOW; -. DR PDBsum; 3LRH; -. DR PDBsum; 4FE8; -. DR PDBsum; 4FEB; -. DR PDBsum; 4FEC; -. DR PDBsum; 4FED; -. DR PDBsum; 4RAV; -. DR PDBsum; 6EZ8; -. DR PDBsum; 6N8C; -. DR PDBsum; 6RMH; -. DR PDBsum; 6X9O; -. DR PDBsum; 6YEJ; -. DR PDBsum; 7DXJ; -. DR PDBsum; 7DXK; -. DR BMRB; P42858; -. DR SMR; P42858; -. DR BioGRID; 109314; 447. DR CORUM; P42858; -. DR DIP; DIP-32492N; -. DR ELM; P42858; -. DR IntAct; P42858; 1110. DR MINT; P42858; -. DR STRING; 9606.ENSP00000347184; -. DR BindingDB; P42858; -. DR ChEMBL; CHEMBL5514; -. DR DrugBank; DB09130; Copper. DR MoonDB; P42858; Predicted. DR GlyGen; P42858; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; P42858; -. DR MetOSite; P42858; -. DR PhosphoSitePlus; P42858; -. DR SwissPalm; P42858; -. DR BioMuta; HTT; -. DR DMDM; 296434520; -. DR EPD; P42858; -. DR jPOST; P42858; -. DR MassIVE; P42858; -. DR MaxQB; P42858; -. DR PaxDb; P42858; -. DR PeptideAtlas; P42858; -. DR ProteomicsDB; 55561; -. DR ABCD; P42858; 2 sequenced antibodies. DR Antibodypedia; 3449; 834 antibodies from 40 providers. DR DNASU; 3064; -. DR Ensembl; ENST00000355072.11; ENSP00000347184.5; ENSG00000197386.14. DR GeneID; 3064; -. DR KEGG; hsa:3064; -. DR MANE-Select; ENST00000355072.11; ENSP00000347184.5; NM_001388492.1; NP_001375421.1. DR UCSC; uc062uto.1; human. DR CTD; 3064; -. DR DisGeNET; 3064; -. DR GeneCards; HTT; -. DR GeneReviews; HTT; -. DR HGNC; HGNC:4851; HTT. DR HPA; ENSG00000197386; Low tissue specificity. DR MalaCards; HTT; -. DR MIM; 143100; phenotype. DR MIM; 613004; gene. DR MIM; 617435; phenotype. DR neXtProt; NX_P42858; -. DR OpenTargets; ENSG00000197386; -. DR Orphanet; 399; Huntington disease. DR Orphanet; 248111; Juvenile Huntington disease. DR Orphanet; 528084; Non-specific syndromic intellectual disability. DR PharmGKB; PA164741646; -. DR VEuPathDB; HostDB:ENSG00000197386; -. DR eggNOG; ENOG502QR1D; Eukaryota. DR GeneTree; ENSGT00390000015863; -. DR HOGENOM; CLU_000428_0_0_1; -. DR InParanoid; P42858; -. DR OMA; HTCSLIY; -. DR OrthoDB; 33894at2759; -. DR PhylomeDB; P42858; -. DR TreeFam; TF323608; -. DR PathwayCommons; P42858; -. DR Reactome; R-HSA-9022692; Regulation of MECP2 expression and activity. DR SignaLink; P42858; -. DR SIGNOR; P42858; -. DR BioGRID-ORCS; 3064; 34 hits in 1086 CRISPR screens. DR ChiTaRS; HTT; human. DR EvolutionaryTrace; P42858; -. DR GeneWiki; Huntingtin; -. DR GenomeRNAi; 3064; -. DR Pharos; P42858; Tchem. DR PRO; PR:P42858; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; P42858; protein. DR Bgee; ENSG00000197386; Expressed in sural nerve and 132 other tissues. DR ExpressionAtlas; P42858; baseline and differential. DR Genevisible; P42858; HS. DR GO; GO:0005776; C:autophagosome; IDA:UniProtKB. DR GO; GO:0030424; C:axon; IDA:UniProtKB. DR GO; GO:0005814; C:centriole; IDA:SYSCILIA_CCNET. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0030425; C:dendrite; IDA:UniProtKB. DR GO; GO:0005769; C:early endosome; IDA:UniProtKB. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0016234; C:inclusion body; IMP:CAFA. DR GO; GO:0005770; C:late endosome; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IMP:CAFA. DR GO; GO:0099524; C:postsynaptic cytosol; IDA:SynGO. DR GO; GO:0099523; C:presynaptic cytosol; IDA:SynGO. DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB. DR GO; GO:0048487; F:beta-tubulin binding; IDA:UniProtKB. DR GO; GO:0034452; F:dynactin binding; IPI:UniProtKB. DR GO; GO:0045505; F:dynein intermediate chain binding; IDA:UniProtKB. DR GO; GO:0031072; F:heat shock protein binding; IPI:CAFA. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0019900; F:kinase binding; IPI:ParkinsonsUK-UCL. DR GO; GO:0002039; F:p53 binding; IPI:UniProtKB. DR GO; GO:0005522; F:profilin binding; IPI:UniProtKB. DR GO; GO:0044325; F:transmembrane transporter binding; IDA:UniProtKB. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:UniProtKB. DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB. DR GO; GO:0099111; P:microtubule-based transport; IBA:GO_Central. DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:UniProtKB. DR GO; GO:1905337; P:positive regulation of aggrephagy; IMP:ParkinsonsUK-UCL. DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:CAFA. DR GO; GO:1903599; P:positive regulation of autophagy of mitochondrion; IMP:ParkinsonsUK-UCL. DR GO; GO:0045724; P:positive regulation of cilium assembly; IMP:SYSCILIA_CCNET. DR GO; GO:0031587; P:positive regulation of inositol 1,4,5-trisphosphate-sensitive calcium-release channel activity; IDA:UniProtKB. DR GO; GO:1904504; P:positive regulation of lipophagy; IMP:ParkinsonsUK-UCL. DR GO; GO:0031648; P:protein destabilization; IMP:CAFA. DR GO; GO:1905289; P:regulation of CAMKK-AMPK signaling cascade; IMP:ARUK-UCL. DR GO; GO:2000479; P:regulation of cAMP-dependent protein kinase activity; IMP:ARUK-UCL. DR GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; IMP:dictyBase. DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IMP:UniProtKB. DR GO; GO:0047496; P:vesicle transport along microtubule; IMP:UniProtKB. DR GO; GO:0042297; P:vocal learning; IMP:AgBase. DR Gene3D; 1.25.10.10; -; 2. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR000091; Huntingtin. DR InterPro; IPR028426; Huntingtin_fam. DR InterPro; IPR024613; Huntingtin_middle-repeat. DR PANTHER; PTHR10170; HUNTINGTON DISEASE PROTEIN; 1. DR Pfam; PF12372; DUF3652; 1. DR PRINTS; PR00375; HUNTINGTIN. DR SUPFAM; SSF48371; ARM repeat; 2. DR AGR; HGNC:4851; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Apoptosis; Cytoplasm; Cytoplasmic vesicle; KW Disease variant; Endosome; Intellectual disability; Lipoprotein; Myristate; KW Neurodegeneration; Nucleus; Phosphoprotein; Reference proteome; Repeat; KW Triplet repeat expansion; Ubl conjugation. FT CHAIN 1..3142 FT /note="Huntingtin" FT /id="PRO_0000083942" FT CHAIN 551..584 FT /note="Huntingtin, myristoylated N-terminal fragment" FT /id="PRO_0000447477" FT REPEAT 204..241 FT /note="HEAT 1" FT REPEAT 246..283 FT /note="HEAT 2" FT REPEAT 316..360 FT /note="HEAT 3" FT REPEAT 802..839 FT /note="HEAT 4" FT REPEAT 902..940 FT /note="HEAT 5" FT REGION 3..13 FT /note="Sufficient for interaction with TPR" FT /evidence="ECO:0000269|PubMed:15654337" FT REGION 14..85 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 447..469 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 491..502 FT /note="Interaction with ZDHHC17" FT /evidence="ECO:0000269|PubMed:28757145" FT REGION 517..583 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1176..1225 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2330..2351 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2633..2662 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 2395..2404 FT /note="Nuclear export signal" FT /evidence="ECO:0000250" FT COMPBIAS 14..35 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 36..82 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 531..583 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1205..1225 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2335..2349 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 511..512 FT /note="Cleavage; by caspase-3" FT /evidence="ECO:0000269|PubMed:9535906" FT SITE 528..529 FT /note="Cleavage; by caspase-3" FT /evidence="ECO:0000255" FT SITE 550..551 FT /note="Cleavage; by caspase-3" FT /evidence="ECO:0000269|PubMed:29802276" FT SITE 584..585 FT /note="Cleavage; by caspase-6" FT /evidence="ECO:0000269|PubMed:10770929" FT SITE 587..588 FT /note="Cleavage; by caspase-3" FT /evidence="ECO:0000255" FT MOD_RES 9 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:21685499" FT MOD_RES 176 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:21685499" FT MOD_RES 234 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:21685499" FT MOD_RES 343 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:21685499" FT MOD_RES 411 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 417 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P42859" FT MOD_RES 419 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P42859" FT MOD_RES 432 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:24275569" FT MOD_RES 442 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:21685499" FT MOD_RES 640 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 643 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1179 FT /note="Phosphoserine; by CDK5" FT /evidence="ECO:0000269|PubMed:17611284" FT MOD_RES 1199 FT /note="Phosphoserine; by CDK5" FT /evidence="ECO:0000269|PubMed:17611284, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1870 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231" FT MOD_RES 1874 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT LIPID 551 FT /note="N-myristoyl glycine" FT /evidence="ECO:0000269|PubMed:24459296, FT ECO:0000269|PubMed:29802276" FT VARIANT 18 FT /note="Q -> QQQ" FT /id="VAR_005268" FT VARIANT 551 FT /note="G -> E (inhibits proteolytic cleavage at D-550; FT abolishes post-translational myristoylation; results in FT increased cleavage at D-511; dbSNP:rs118005095)" FT /evidence="ECO:0000269|PubMed:29802276" FT /id="VAR_081737" FT VARIANT 703 FT /note="P -> L (in LOMARS; dbSNP:rs768047421)" FT /evidence="ECO:0000269|PubMed:26740508" FT /id="VAR_079026" FT VARIANT 893 FT /note="G -> R (in dbSNP:rs363075)" FT /id="VAR_060170" FT VARIANT 1064 FT /note="V -> I (in dbSNP:rs35892913)" FT /id="VAR_060171" FT VARIANT 1091 FT /note="I -> M (in dbSNP:rs1143646)" FT /id="VAR_060172" FT VARIANT 1173 FT /note="T -> A (in dbSNP:rs3025843)" FT /id="VAR_060173" FT VARIANT 1260 FT /note="T -> M (found in a patient with Rett syndrome-like FT phenotype; unknown pathological significance; FT dbSNP:rs34315806)" FT /evidence="ECO:0000269|PubMed:26740508" FT /id="VAR_060174" FT VARIANT 1382 FT /note="E -> A (in dbSNP:rs3025837)" FT /id="VAR_054017" FT VARIANT 1385 FT /note="N -> H (in dbSNP:rs3025837)" FT /id="VAR_060175" FT VARIANT 1720 FT /note="T -> N (in dbSNP:rs363125)" FT /id="VAR_060176" FT VARIANT 2113 FT /note="D -> Y (in dbSNP:rs1143648)" FT /id="VAR_060177" FT VARIANT 2309 FT /note="Y -> H (in dbSNP:rs362331)" FT /id="VAR_060178" FT VARIANT 2717 FT /note="F -> L (in LOMARS; dbSNP:rs1085307052)" FT /evidence="ECO:0000269|PubMed:27329733" FT /id="VAR_079027" FT VARIANT 2786 FT /note="V -> I (in dbSNP:rs362272)" FT /evidence="ECO:0000269|PubMed:7903579" FT /id="VAR_060179" FT MUTAGEN 495 FT /note="I->A: Inhibits interaction with ZDHHC13 and FT ZDHHC17." FT /evidence="ECO:0000269|PubMed:26198635" FT MUTAGEN 498..499 FT /note="QP->AA: Abolishes interaction with ZDHHC17." FT /evidence="ECO:0000269|PubMed:28757145" FT MUTAGEN 498 FT /note="Q->A: Inhibits interaction with ZDHHC13 and FT ZDHHC17." FT /evidence="ECO:0000269|PubMed:26198635" FT MUTAGEN 499 FT /note="P->A: Inhibits interaction with ZDHHC13 and FT ZDHHC17." FT /evidence="ECO:0000269|PubMed:26198635" FT MUTAGEN 511 FT /note="D->A: Loss of proteolytic cleavage." FT /evidence="ECO:0000269|PubMed:9535906" FT MUTAGEN 528 FT /note="D->A: No effect on proteolytic cleavage." FT /evidence="ECO:0000269|PubMed:9535906" FT MUTAGEN 550 FT /note="D->E: Loss of proteolytic cleavage. Loss of FT myristoylation." FT /evidence="ECO:0000269|PubMed:29802276" FT MUTAGEN 551 FT /note="G->A: Loss of myristoylation." FT /evidence="ECO:0000269|PubMed:24459296, FT ECO:0000269|PubMed:29802276" FT MUTAGEN 551 FT /note="G->S: Loss of myristoylation." FT /evidence="ECO:0000269|PubMed:29802276" FT MUTAGEN 584 FT /note="D->A: Loss of proteolytic cleavage." FT /evidence="ECO:0000269|PubMed:10770929" FT CONFLICT 823 FT /note="C -> S (in Ref. 2; BAA36753)" FT /evidence="ECO:0000305" FT HELIX 4..10 FT /evidence="ECO:0007829|PDB:4RAV" FT STRAND 13..15 FT /evidence="ECO:0007829|PDB:4RAV" FT HELIX 23..26 FT /evidence="ECO:0007829|PDB:3IOT" FT TURN 30..32 FT /evidence="ECO:0007829|PDB:3IOT" FT HELIX 97..109 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 119..132 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 135..137 FT /evidence="ECO:0007829|PDB:6X9O" FT STRAND 139..141 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 142..157 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 159..175 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 180..191 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 192..196 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 202..217 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 222..239 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 240..242 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 245..256 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 257..260 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 264..279 FT /evidence="ECO:0007829|PDB:6X9O" FT STRAND 281..283 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 284..297 FT /evidence="ECO:0007829|PDB:6X9O" FT STRAND 302..304 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 309..321 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 322..324 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 351..364 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 370..385 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 389..396 FT /evidence="ECO:0007829|PDB:6X9O" FT STRAND 397..399 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 400..403 FT /evidence="ECO:0007829|PDB:6X9O" FT STRAND 676..678 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 680..692 FT /evidence="ECO:0007829|PDB:6X9O" FT STRAND 696..699 FT /evidence="ECO:0007829|PDB:6X9O" FT TURN 704..706 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 709..725 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 727..731 FT /evidence="ECO:0007829|PDB:6X9O" FT STRAND 732..734 FT /evidence="ECO:0007829|PDB:6X9O" FT TURN 741..743 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 750..758 FT /evidence="ECO:0007829|PDB:6X9O" FT TURN 762..764 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 765..782 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 787..797 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 804..806 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 808..815 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 820..838 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 843..853 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 854..858 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 862..873 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 877..886 FT /evidence="ECO:0007829|PDB:6X9O" FT TURN 890..893 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 894..896 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 903..910 FT /evidence="ECO:0007829|PDB:6X9O" FT TURN 911..913 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 914..917 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 921..934 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 935..937 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 949..961 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 996..1014 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1019..1035 FT /evidence="ECO:0007829|PDB:6X9O" FT TURN 1038..1040 FT /evidence="ECO:0007829|PDB:6X9O" FT TURN 1042..1045 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1065..1074 FT /evidence="ECO:0007829|PDB:6X9O" FT STRAND 1076..1078 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1079..1081 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1083..1098 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1101..1103 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1135..1156 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1234..1250 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1262..1277 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1278..1280 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1283..1286 FT /evidence="ECO:0007829|PDB:6X9O" FT TURN 1287..1289 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1290..1300 FT /evidence="ECO:0007829|PDB:6X9O" FT TURN 1301..1303 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1305..1319 FT /evidence="ECO:0007829|PDB:6X9O" FT TURN 1324..1326 FT /evidence="ECO:0007829|PDB:6X9O" FT TURN 1356..1359 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1360..1372 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1422..1425 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1426..1438 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1442..1457 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1462..1465 FT /evidence="ECO:0007829|PDB:6X9O" FT STRAND 1467..1469 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1470..1484 FT /evidence="ECO:0007829|PDB:6X9O" FT TURN 1491..1493 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1494..1506 FT /evidence="ECO:0007829|PDB:6X9O" FT STRAND 1508..1515 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1517..1529 FT /evidence="ECO:0007829|PDB:6X9O" FT STRAND 1530..1532 FT /evidence="ECO:0007829|PDB:6X9O" FT TURN 1534..1537 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1538..1550 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1563..1577 FT /evidence="ECO:0007829|PDB:6X9O" FT TURN 1578..1580 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1582..1598 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1602..1620 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1628..1640 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1643..1646 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1650..1656 FT /evidence="ECO:0007829|PDB:6X9O" FT STRAND 1663..1665 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1666..1686 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1689..1698 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1703..1706 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1708..1715 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1736..1756 FT /evidence="ECO:0007829|PDB:6X9O" FT TURN 1760..1763 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1766..1788 FT /evidence="ECO:0007829|PDB:6X9O" FT STRAND 1789..1791 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1793..1803 FT /evidence="ECO:0007829|PDB:6X9O" FT STRAND 1808..1812 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1815..1823 FT /evidence="ECO:0007829|PDB:6X9O" FT TURN 1824..1828 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1830..1842 FT /evidence="ECO:0007829|PDB:6X9O" FT TURN 1848..1850 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1851..1854 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1889..1908 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1914..1929 FT /evidence="ECO:0007829|PDB:6X9O" FT TURN 1930..1932 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1934..1944 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1947..1958 FT /evidence="ECO:0007829|PDB:6X9O" FT TURN 1959..1965 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1967..1978 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1982..1984 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 1987..1994 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2002..2021 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2024..2030 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2033..2045 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2048..2051 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2053..2066 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2097..2108 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2116..2123 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2128..2130 FT /evidence="ECO:0007829|PDB:6X9O" FT TURN 2131..2136 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2142..2144 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2145..2156 FT /evidence="ECO:0007829|PDB:6X9O" FT TURN 2157..2159 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2163..2181 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2201..2208 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2215..2217 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2218..2229 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2232..2234 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2237..2239 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2245..2266 FT /evidence="ECO:0007829|PDB:6X9O" FT STRAND 2267..2269 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2272..2285 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2289..2295 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2301..2319 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2354..2368 FT /evidence="ECO:0007829|PDB:6X9O" FT TURN 2369..2374 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2379..2381 FT /evidence="ECO:0007829|PDB:6X9O" FT STRAND 2386..2388 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2389..2400 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2403..2409 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2413..2417 FT /evidence="ECO:0007829|PDB:6X9O" FT STRAND 2426..2429 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2437..2439 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2443..2456 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2461..2475 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2498..2512 FT /evidence="ECO:0007829|PDB:6X9O" FT STRAND 2516..2518 FT /evidence="ECO:0007829|PDB:6X9O" FT TURN 2522..2524 FT /evidence="ECO:0007829|PDB:6X9O" FT STRAND 2537..2542 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2543..2562 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2594..2596 FT /evidence="ECO:0007829|PDB:6X9O" FT TURN 2598..2600 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2619..2625 FT /evidence="ECO:0007829|PDB:6X9O" FT STRAND 2663..2666 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2668..2680 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2694..2707 FT /evidence="ECO:0007829|PDB:6X9O" FT TURN 2708..2710 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2714..2730 FT /evidence="ECO:0007829|PDB:6X9O" FT STRAND 2736..2738 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2739..2752 FT /evidence="ECO:0007829|PDB:6X9O" FT STRAND 2757..2760 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2763..2771 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2776..2790 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2802..2816 FT /evidence="ECO:0007829|PDB:6X9O" FT STRAND 2821..2824 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2826..2842 FT /evidence="ECO:0007829|PDB:6X9O" FT TURN 2844..2846 FT /evidence="ECO:0007829|PDB:6X9O" FT TURN 2851..2853 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2854..2863 FT /evidence="ECO:0007829|PDB:6X9O" FT TURN 2867..2869 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2872..2887 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2897..2900 FT /evidence="ECO:0007829|PDB:6X9O" FT TURN 2904..2906 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2912..2928 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2952..2967 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2970..2987 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2990..2992 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 2994..3001 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 3009..3023 FT /evidence="ECO:0007829|PDB:6X9O" FT TURN 3024..3027 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 3031..3037 FT /evidence="ECO:0007829|PDB:6X9O" FT STRAND 3040..3042 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 3049..3062 FT /evidence="ECO:0007829|PDB:6X9O" FT TURN 3067..3069 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 3070..3072 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 3073..3077 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 3085..3100 FT /evidence="ECO:0007829|PDB:6X9O" FT TURN 3101..3103 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 3106..3116 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 3117..3119 FT /evidence="ECO:0007829|PDB:6X9O" FT TURN 3122..3126 FT /evidence="ECO:0007829|PDB:6X9O" FT HELIX 3127..3135 FT /evidence="ECO:0007829|PDB:6X9O" SQ SEQUENCE 3142 AA; 347603 MW; A267509E84D52F0D CRC64; MATLEKLMKA FESLKSFQQQ QQQQQQQQQQ QQQQQQQQPP PPPPPPPPPQ LPQPPPQAQP LLPQPQPPPP PPPPPPGPAV AEEPLHRPKK ELSATKKDRV NHCLTICENI VAQSVRNSPE FQKLLGIAME LFLLCSDDAE SDVRMVADEC LNKVIKALMD SNLPRLQLEL YKEIKKNGAP RSLRAALWRF AELAHLVRPQ KCRPYLVNLL PCLTRTSKRP EESVQETLAA AVPKIMASFG NFANDNEIKV LLKAFIANLK SSSPTIRRTA AGSAVSICQH SRRTQYFYSW LLNVLLGLLV PVEDEHSTLL ILGVLLTLRY LVPLLQQQVK DTSLKGSFGV TRKEMEVSPS AEQLVQVYEL TLHHTQHQDH NVVTGALELL QQLFRTPPPE LLQTLTAVGG IGQLTAAKEE SGGRSRSGSI VELIAGGGSS CSPVLSRKQK GKVLLGEEEA LEDDSESRSD VSSSALTASV KDEISGELAA SSGVSTPGSA GHDIITEQPR SQHTLQADSV DLASCDLTSS ATDGDEEDIL SHSSSQVSAV PSDPAMDLND GTQASSPISD SSQTTTEGPD SAVTPSDSSE IVLDGTDNQY LGLQIGQPQD EDEEATGILP DEASEAFRNS SMALQQAHLL KNMSHCRQPS DSSVDKFVLR DEATEPGDQE NKPCRIKGDI GQSTDDDSAP LVHCVRLLSA SFLLTGGKNV LVPDRDVRVS VKALALSCVG AAVALHPESF FSKLYKVPLD TTEYPEEQYV SDILNYIDHG DPQVRGATAI LCGTLICSIL SRSRFHVGDW MGTIRTLTGN TFSLADCIPL LRKTLKDESS VTCKLACTAV RNCVMSLCSS SYSELGLQLI IDVLTLRNSS YWLVRTELLE TLAEIDFRLV SFLEAKAENL HRGAHHYTGL LKLQERVLNN VVIHLLGDED PRVRHVAAAS LIRLVPKLFY KCDQGQADPV VAVARDQSSV YLKLLMHETQ PPSHFSVSTI TRIYRGYNLL PSITDVTMEN NLSRVIAAVS HELITSTTRA LTFGCCEALC LLSTAFPVCI WSLGWHCGVP PLSASDESRK SCTVGMATMI LTLLSSAWFP LDLSAHQDAL ILAGNLLAAS APKSLRSSWA SEEEANPAAT KQEEVWPALG DRALVPMVEQ LFSHLLKVIN ICAHVLDDVA PGPAIKAALP SLTNPPSLSP IRRKGKEKEP GEQASVPLSP KKGSEASAAS RQSDTSGPVT TSKSSSLGSF YHLPSYLKLH DVLKATHANY KVTLDLQNST EKFGGFLRSA LDVLSQILEL ATLQDIGKCV EEILGYLKSC FSREPMMATV CVQQLLKTLF GTNLASQFDG LSSNPSKSQG RAQRLGSSSV RPGLYHYCFM APYTHFTQAL ADASLRNMVQ AEQENDTSGW FDVLQKVSTQ LKTNLTSVTK NRADKNAIHN HIRLFEPLVI KALKQYTTTT CVQLQKQVLD LLAQLVQLRV NYCLLDSDQV FIGFVLKQFE YIEVGQFRES EAIIPNIFFF LVLLSYERYH SKQIIGIPKI IQLCDGIMAS GRKAVTHAIP ALQPIVHDLF VLRGTNKADA GKELETQKEV VVSMLLRLIQ YHQVLEMFIL VLQQCHKENE DKWKRLSRQI ADIILPMLAK QQMHIDSHEA LGVLNTLFEI LAPSSLRPVD MLLRSMFVTP NTMASVSTVQ LWISGILAIL RVLISQSTED IVLSRIQELS FSPYLISCTV INRLRDGDST STLEEHSEGK QIKNLPEETF SRFLLQLVGI LLEDIVTKQL KVEMSEQQHT FYCQELGTLL MCLIHIFKSG MFRRITAAAT RLFRSDGCGG SFYTLDSLNL RARSMITTHP ALVLLWCQIL LLVNHTDYRW WAEVQQTPKR HSLSSTKLLS PQMSGEEEDS DLAAKLGMCN REIVRRGALI LFCDYVCQNL HDSEHLTWLI VNHIQDLISL SHEPPVQDFI SAVHRNSAAS GLFIQAIQSR CENLSTPTML KKTLQCLEGI HLSQSGAVLT LYVDRLLCTP FRVLARMVDI LACRRVEMLL AANLQSSMAQ LPMEELNRIQ EYLQSSGLAQ RHQRLYSLLD RFRLSTMQDS LSPSPPVSSH PLDGDGHVSL ETVSPDKDWY VHLVKSQCWT RSDSALLEGA ELVNRIPAED MNAFMMNSEF NLSLLAPCLS LGMSEISGGQ KSALFEAARE VTLARVSGTV QQLPAVHHVF QPELPAEPAA YWSKLNDLFG DAALYQSLPT LARALAQYLV VVSKLPSHLH LPPEKEKDIV KFVVATLEAL SWHLIHEQIP LSLDLQAGLD CCCLALQLPG LWSVVSSTEF VTHACSLIYC VHFILEAVAV QPGEQLLSPE RRTNTPKAIS EEEEEVDPNT QNPKYITAAC EMVAEMVESL QSVLALGHKR NSGVPAFLTP LLRNIIISLA RLPLVNSYTR VPPLVWKLGW SPKPGGDFGT AFPEIPVEFL QEKEVFKEFI YRINTLGWTS RTQFEETWAT LLGVLVTQPL VMEQEESPPE EDTERTQINV LAVQAITSLV LSAMTVPVAG NPAVSCLEQQ PRNKPLKALD TRFGRKLSII RGIVEQEIQA MVSKRENIAT HHLYQAWDPV PSLSPATTGA LISHEKLLLQ INPERELGSM SYKLGQVSIH SVWLGNSITP LREEEWDEEE EEEADAPAPS SPPTSPVNSR KHRAGVDIHS CSQFLLELYS RWILPSSSAR RTPAILISEV VRSLLVVSDL FTERNQFELM YVTLTELRRV HPSEDEILAQ YLVPATCKAA AVLGMDKAVA EPVSRLLEST LRSSHLPSRV GALHGVLYVL ECDLLDDTAK QLIPVISDYL LSNLKGIAHC VNIHSQQHVL VMCATAFYLI ENYPLDVGPE FSASIIQMCG VMLSGSEEST PSIIYHCALR GLERLLLSEQ LSRLDAESLV KLSVDRVNVH SPHRAMAALG LMLTCMYTGK EKVSPGRTSD PNPAAPDSES VIVAMERVSV LFDRIRKGFP CEARVVARIL PQFLDDFFPP QDIMNKVIGE FLSNQQPYPQ FMATVVYKVF QTLHSTGQSS MVRDWVMLSL SNFTQRAPVA MATWSLSCFF VSASTSPWVA AILPHVISRM GKLEQVDVNL FCLVATDFYR HQIEEELDRR AFQSVLEVVA APGSPYHRLL TCLRNVHKVT TC // ID H3BMQ8_HUMAN Unreviewed; 140 AA. AC H3BMQ8; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 14-DEC-2022, entry version 69. DE RecName: Full=fructose-bisphosphate aldolase {ECO:0000256|ARBA:ARBA00013068}; DE EC=4.1.2.13 {ECO:0000256|ARBA:ARBA00013068}; DE Flags: Fragment; GN Name=ALDOA {ECO:0000313|Ensembl:ENSP00000454499.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000454499.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000454499.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [2] {ECO:0007829|PubMed:17081983} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [3] {ECO:0007829|PubMed:19413330} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [4] {ECO:0007829|PubMed:19608861} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [5] {ECO:0007829|PubMed:21269460} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [6] {ECO:0007829|PubMed:21406692} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [7] {ECO:0007829|PubMed:22905912} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22905912; DOI=10.1021/pr300539b; RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P., RA Mariman E.C., Renes J.; RT "Resveratrol-induced changes of the human adipocyte secretion profile."; RL J. Proteome Res. 11:4733-4743(2012). RN [8] {ECO:0007829|PubMed:22223895} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.M111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [9] {ECO:0007829|PubMed:22814378} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [10] {ECO:0007829|PubMed:23186163} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=23186163; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [11] {ECO:0007829|PubMed:24275569} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [12] {ECO:0007829|PubMed:25944712} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [13] {ECO:0000313|Ensembl:ENSP00000454499.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-2022) to UniProtKB. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 4/4. CC {ECO:0000256|ARBA:ARBA00004714}. CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase CC family. {ECO:0000256|ARBA:ARBA00010387}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC093512; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; H3BMQ8; -. DR SMR; H3BMQ8; -. DR SwissPalm; H3BMQ8; -. DR MaxQB; H3BMQ8; -. DR PeptideAtlas; H3BMQ8; -. DR ProteomicsDB; 40977; -. DR Antibodypedia; 1031; 709 antibodies from 37 providers. DR Ensembl; ENST00000566846.5; ENSP00000454499.1; ENSG00000149925.22. DR UCSC; uc059szj.1; human. DR HGNC; HGNC:414; ALDOA. DR VEuPathDB; HostDB:ENSG00000149925; -. DR GeneTree; ENSGT00950000182987; -. DR UniPathway; UPA00109; UER00183. DR ChiTaRS; ALDOA; human. DR Proteomes; UP000005640; Chromosome 16. DR Bgee; ENSG00000149925; Expressed in gastrocnemius and 94 other tissues. DR ExpressionAtlas; H3BMQ8; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000741; FBA_I. DR PANTHER; PTHR11627; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1. DR Pfam; PF00274; Glycolytic; 1. PE 1: Evidence at protein level; KW Proteomics identification {ECO:0007829|EPD:H3BMQ8, KW ECO:0007829|MaxQB:H3BMQ8}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}. FT NON_TER 140 FT /evidence="ECO:0000313|Ensembl:ENSP00000454499.1" SQ SEQUENCE 140 AA; 15463 MW; FAE94DFF0C029BB3 CRC64; MPYQYPALTP EQKKELSDIA HRIVAPGSIA KRLQSIGTEN TEENRRFYRQ LLLTADDRVN PCIGGVILFH ETLYQKADDG RPFPQVIKSK GGVVGIKVDK GVVPLAGTNG ETTTQGLDGL SERCAQYKKD GADFAKWRCV // ID H3BR68_HUMAN Unreviewed; 130 AA. AC H3BR68; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 14-DEC-2022, entry version 58. DE RecName: Full=fructose-bisphosphate aldolase {ECO:0000256|ARBA:ARBA00013068}; DE EC=4.1.2.13 {ECO:0000256|ARBA:ARBA00013068}; DE Flags: Fragment; GN Name=ALDOA {ECO:0000313|Ensembl:ENSP00000456098.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000456098.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000456098.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [2] {ECO:0007829|PubMed:19608861} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [3] {ECO:0007829|PubMed:21269460} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [4] {ECO:0007829|PubMed:22905912} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22905912; DOI=10.1021/pr300539b; RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P., RA Mariman E.C., Renes J.; RT "Resveratrol-induced changes of the human adipocyte secretion profile."; RL J. Proteome Res. 11:4733-4743(2012). RN [5] {ECO:0007829|PubMed:24275569} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [6] {ECO:0007829|PubMed:24129315} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=24129315; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [7] {ECO:0007829|PubMed:25944712} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [8] {ECO:0000313|Ensembl:ENSP00000456098.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-2022) to UniProtKB. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 4/4. CC {ECO:0000256|ARBA:ARBA00004714}. CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase CC family. {ECO:0000256|ARBA:ARBA00010387}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC093512; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR MetOSite; H3BR68; -. DR SwissPalm; H3BR68; -. DR MaxQB; H3BR68; -. DR PeptideAtlas; H3BR68; -. DR ProteomicsDB; 41985; -. DR Antibodypedia; 1031; 709 antibodies from 37 providers. DR Ensembl; ENST00000565355.1; ENSP00000456098.1; ENSG00000149925.22. DR UCSC; uc059szo.1; human. DR HGNC; HGNC:414; ALDOA. DR VEuPathDB; HostDB:ENSG00000149925; -. DR GeneTree; ENSGT00950000182987; -. DR HOGENOM; CLU_031243_4_0_1; -. DR UniPathway; UPA00109; UER00183. DR ChiTaRS; ALDOA; human. DR Proteomes; UP000005640; Chromosome 16. DR Bgee; ENSG00000149925; Expressed in gastrocnemius and 94 other tissues. DR ExpressionAtlas; H3BR68; baseline and differential. DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000741; FBA_I. DR PANTHER; PTHR11627; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1. DR Pfam; PF00274; Glycolytic; 1. PE 1: Evidence at protein level; KW Proteomics identification {ECO:0007829|EPD:H3BR68, KW ECO:0007829|MaxQB:H3BR68}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}. FT NON_TER 1 FT /evidence="ECO:0000313|Ensembl:ENSP00000456098.1" SQ SEQUENCE 130 AA; 13779 MW; FDAA97F6E33A4473 CRC64; XPGHACTQKF SHEEIAMATV TALRRTVPPA VTGITFLSGG QSEEEASINL NAINKCPLLK PWALTFSYGR ALQASALKAW GGKKENLKAA QEEYVKRALA NSLACQGKYT PSGQAGAAAS ESLFVSNHAY // ID H3BUH7_HUMAN Unreviewed; 155 AA. AC H3BUH7; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 14-DEC-2022, entry version 70. DE RecName: Full=fructose-bisphosphate aldolase {ECO:0000256|ARBA:ARBA00013068}; DE EC=4.1.2.13 {ECO:0000256|ARBA:ARBA00013068}; DE Flags: Fragment; GN Name=ALDOA {ECO:0000313|Ensembl:ENSP00000457643.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000457643.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000457643.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [2] {ECO:0007829|PubMed:17081983} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [3] {ECO:0007829|PubMed:18669648} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [4] {ECO:0007829|PubMed:19413330} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [5] {ECO:0007829|PubMed:19690332} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [6] {ECO:0007829|PubMed:19608861} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [7] {ECO:0007829|PubMed:20068231} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [8] {ECO:0007829|PubMed:21269460} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [9] {ECO:0007829|PubMed:21406692} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [10] {ECO:0007829|PubMed:22905912} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22905912; DOI=10.1021/pr300539b; RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P., RA Mariman E.C., Renes J.; RT "Resveratrol-induced changes of the human adipocyte secretion profile."; RL J. Proteome Res. 11:4733-4743(2012). RN [11] {ECO:0007829|PubMed:22223895} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.M111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [12] {ECO:0007829|PubMed:22814378} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [13] {ECO:0007829|PubMed:23186163} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=23186163; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [14] {ECO:0007829|PubMed:24275569} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [15] {ECO:0007829|PubMed:25114211} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [16] {ECO:0007829|PubMed:25944712} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [17] {ECO:0000313|Ensembl:ENSP00000457643.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-2022) to UniProtKB. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 4/4. CC {ECO:0000256|ARBA:ARBA00004714}. CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase CC family. {ECO:0000256|ARBA:ARBA00010387}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC093512; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; H3BUH7; -. DR SMR; H3BUH7; -. DR SwissPalm; H3BUH7; -. DR MaxQB; H3BUH7; -. DR PeptideAtlas; H3BUH7; -. DR ProteomicsDB; 42935; -. DR Antibodypedia; 1031; 709 antibodies from 37 providers. DR Ensembl; ENST00000563987.5; ENSP00000457643.1; ENSG00000149925.22. DR UCSC; uc059sze.1; human. DR HGNC; HGNC:414; ALDOA. DR VEuPathDB; HostDB:ENSG00000149925; -. DR GeneTree; ENSGT00950000182987; -. DR HOGENOM; CLU_031243_3_2_1; -. DR OMA; DYREMLF; -. DR UniPathway; UPA00109; UER00183. DR ChiTaRS; ALDOA; human. DR Proteomes; UP000005640; Chromosome 16. DR Bgee; ENSG00000149925; Expressed in gastrocnemius and 94 other tissues. DR ExpressionAtlas; H3BUH7; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000741; FBA_I. DR PANTHER; PTHR11627; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1. DR Pfam; PF00274; Glycolytic; 1. PE 1: Evidence at protein level; KW Proteomics identification {ECO:0007829|EPD:H3BUH7, KW ECO:0007829|MaxQB:H3BUH7}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}. FT NON_TER 155 FT /evidence="ECO:0000313|Ensembl:ENSP00000457643.1" SQ SEQUENCE 155 AA; 16917 MW; 46475A1C8DD97F38 CRC64; MPYQYPALTP EQKKELSDIA HRIVAPGKGI LAADESTGSI AKRLQSIGTE NTEENRRFYR QLLLTADDRV NPCIGGVILF HETLYQKADD GRPFPQVIKS KGGVVGIKVD KGVVPLAGTN GETTTQGLDG LSERCAQYKK DGADFAKWRC VLKIG // ID H3BPS8_HUMAN Unreviewed; 278 AA. AC H3BPS8; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 14-DEC-2022, entry version 72. DE RecName: Full=fructose-bisphosphate aldolase {ECO:0000256|ARBA:ARBA00013068}; DE EC=4.1.2.13 {ECO:0000256|ARBA:ARBA00013068}; DE Flags: Fragment; GN Name=ALDOA {ECO:0000313|Ensembl:ENSP00000455455.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000455455.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000455455.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [2] {ECO:0007829|PubMed:17081983} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [3] {ECO:0007829|PubMed:18669648} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [4] {ECO:0007829|PubMed:19413330} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [5] {ECO:0007829|PubMed:19690332} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [6] {ECO:0007829|PubMed:19608861} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [7] {ECO:0007829|PubMed:20068231} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [8] {ECO:0007829|PubMed:21269460} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [9] {ECO:0007829|PubMed:21406692} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [10] {ECO:0007829|PubMed:22905912} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22905912; DOI=10.1021/pr300539b; RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P., RA Mariman E.C., Renes J.; RT "Resveratrol-induced changes of the human adipocyte secretion profile."; RL J. Proteome Res. 11:4733-4743(2012). RN [11] {ECO:0007829|PubMed:22223895} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.M111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [12] {ECO:0007829|PubMed:22814378} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [13] {ECO:0007829|PubMed:23186163} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=23186163; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [14] {ECO:0007829|PubMed:24275569} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [15] {ECO:0007829|PubMed:25114211} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [16] {ECO:0007829|PubMed:25944712} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [17] {ECO:0000313|Ensembl:ENSP00000455455.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-2022) to UniProtKB. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 4/4. CC {ECO:0000256|ARBA:ARBA00004714}. CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase CC family. {ECO:0000256|ARBA:ARBA00010387}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC093512; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; H3BPS8; -. DR SMR; H3BPS8; -. DR IntAct; H3BPS8; 1. DR MINT; H3BPS8; -. DR MetOSite; H3BPS8; -. DR SwissPalm; H3BPS8; -. DR EPD; H3BPS8; -. DR MaxQB; H3BPS8; -. DR PeptideAtlas; H3BPS8; -. DR ProteomicsDB; 41583; -. DR Antibodypedia; 1031; 709 antibodies from 37 providers. DR Ensembl; ENST00000562679.5; ENSP00000455455.1; ENSG00000149925.22. DR UCSC; uc059szk.1; human. DR HGNC; HGNC:414; ALDOA. DR VEuPathDB; HostDB:ENSG00000149925; -. DR GeneTree; ENSGT00950000182987; -. DR HOGENOM; CLU_031243_3_0_1; -. DR OMA; DYREMLF; -. DR UniPathway; UPA00109; UER00183. DR ChiTaRS; ALDOA; human. DR Proteomes; UP000005640; Chromosome 16. DR Bgee; ENSG00000149925; Expressed in gastrocnemius and 94 other tissues. DR ExpressionAtlas; H3BPS8; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000741; FBA_I. DR PANTHER; PTHR11627; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1. DR Pfam; PF00274; Glycolytic; 1. PE 1: Evidence at protein level; KW Proteomics identification {ECO:0007829|EPD:H3BPS8, KW ECO:0007829|MaxQB:H3BPS8}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}. FT NON_TER 278 FT /evidence="ECO:0000313|Ensembl:ENSP00000455455.1" SQ SEQUENCE 278 AA; 30427 MW; 18B196C9A8ACBA37 CRC64; MARRKPEGSS FNMTHLSMAM AFSFPPVASG QLHPQLGNTQ HQTELGKELA TTSTMPYQYP ALTPEQKKEL SDIAHRIVAP GKGILAADES TGSIAKRLQS IGTENTEENR RFYRQLLLTA DDRVNPCIGG VILFHETLYQ KADDGRPFPQ VIKSKGGVVG IKVDKGVVPL AGTNGETTTQ GLDGLSERCA QYKKDGADFA KWRCVLKIGE HTPSALAIME NANVLARYAS ICQQNGIVPI VEPEILPDGD HDLKRCQYVT EKVLAAVYKA LSDHHIYL // ID H3BR04_HUMAN Unreviewed; 162 AA. AC H3BR04; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 14-DEC-2022, entry version 69. DE RecName: Full=fructose-bisphosphate aldolase {ECO:0000256|ARBA:ARBA00013068}; DE EC=4.1.2.13 {ECO:0000256|ARBA:ARBA00013068}; DE Flags: Fragment; GN Name=ALDOA {ECO:0000313|Ensembl:ENSP00000456020.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000456020.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000456020.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [2] {ECO:0007829|PubMed:17081983} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [3] {ECO:0007829|PubMed:19413330} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [4] {ECO:0007829|PubMed:19608861} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [5] {ECO:0007829|PubMed:21269460} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [6] {ECO:0007829|PubMed:21406692} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [7] {ECO:0007829|PubMed:22905912} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22905912; DOI=10.1021/pr300539b; RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P., RA Mariman E.C., Renes J.; RT "Resveratrol-induced changes of the human adipocyte secretion profile."; RL J. Proteome Res. 11:4733-4743(2012). RN [8] {ECO:0007829|PubMed:22223895} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.M111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [9] {ECO:0007829|PubMed:22814378} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [10] {ECO:0007829|PubMed:23186163} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=23186163; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [11] {ECO:0007829|PubMed:24275569} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [12] {ECO:0007829|PubMed:25944712} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [13] {ECO:0000313|Ensembl:ENSP00000456020.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-2022) to UniProtKB. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 4/4. CC {ECO:0000256|ARBA:ARBA00004714}. CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase CC family. {ECO:0000256|ARBA:ARBA00010387}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC093512; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; H3BR04; -. DR SMR; H3BR04; -. DR SwissPalm; H3BR04; -. DR MaxQB; H3BR04; -. DR PeptideAtlas; H3BR04; -. DR ProteomicsDB; 41937; -. DR Antibodypedia; 1031; 709 antibodies from 37 providers. DR Ensembl; ENST00000562168.5; ENSP00000456020.1; ENSG00000149925.22. DR UCSC; uc059sza.1; human. DR HGNC; HGNC:414; ALDOA. DR VEuPathDB; HostDB:ENSG00000149925; -. DR GeneTree; ENSGT00950000182987; -. DR UniPathway; UPA00109; UER00183. DR ChiTaRS; ALDOA; human. DR Proteomes; UP000005640; Chromosome 16. DR Bgee; ENSG00000149925; Expressed in gastrocnemius and 94 other tissues. DR ExpressionAtlas; H3BR04; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000741; FBA_I. DR PANTHER; PTHR11627; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1. DR Pfam; PF00274; Glycolytic; 1. PE 1: Evidence at protein level; KW Proteomics identification {ECO:0007829|EPD:H3BR04, KW ECO:0007829|MaxQB:H3BR04}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}. FT NON_TER 162 FT /evidence="ECO:0000313|Ensembl:ENSP00000456020.1" SQ SEQUENCE 162 AA; 17793 MW; 602E6C19147BEF89 CRC64; MPYQYPALTP EQKKELSDIA HRIVAPGSIA KRLQSIGTEN TEENRRFYRQ LLLTADDRVN PCIGGVILFH ETLYQKADDG RPFPQVIKSK GGVVGIKVDK GVVPLAGTNG ETTTQGLDGL SERCAQYKKD GADFAKWRCV LKIGEHTPSA LAIMENANVL AR // ID H3BU78_HUMAN Unreviewed; 204 AA. AC H3BU78; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 11-JUL-2012, sequence version 2. DT 14-DEC-2022, entry version 63. DE RecName: Full=Fructose-bisphosphate aldolase {ECO:0000256|RuleBase:RU003994}; DE EC=4.1.2.13 {ECO:0000256|RuleBase:RU003994}; DE Flags: Fragment; GN Name=ALDOA {ECO:0000313|Ensembl:ENSP00000457514.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000457514.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000457514.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [2] {ECO:0007829|PubMed:19608861} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [3] {ECO:0007829|PubMed:21269460} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [4] {ECO:0007829|PubMed:22905912} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22905912; DOI=10.1021/pr300539b; RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P., RA Mariman E.C., Renes J.; RT "Resveratrol-induced changes of the human adipocyte secretion profile."; RL J. Proteome Res. 11:4733-4743(2012). RN [5] {ECO:0007829|PubMed:24275569} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [6] {ECO:0007829|PubMed:25944712} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [7] {ECO:0000313|Ensembl:ENSP00000457514.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-2022) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3- CC phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729, CC ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13; CC Evidence={ECO:0000256|RuleBase:RU003994}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 4/4. CC {ECO:0000256|ARBA:ARBA00004714, ECO:0000256|RuleBase:RU004257}. CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase CC family. {ECO:0000256|ARBA:ARBA00010387, ECO:0000256|RuleBase:RU003994}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC093512; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; H3BU78; -. DR SMR; H3BU78; -. DR MetOSite; H3BU78; -. DR SwissPalm; H3BU78; -. DR MaxQB; H3BU78; -. DR PeptideAtlas; H3BU78; -. DR ProteomicsDB; 42854; -. DR Antibodypedia; 1031; 709 antibodies from 37 providers. DR Ensembl; ENST00000564688.1; ENSP00000457514.1; ENSG00000149925.22. DR UCSC; uc059szl.1; human. DR HGNC; HGNC:414; ALDOA. DR VEuPathDB; HostDB:ENSG00000149925; -. DR GeneTree; ENSGT00950000182987; -. DR HOGENOM; CLU_031243_2_1_1; -. DR UniPathway; UPA00109; UER00183. DR ChiTaRS; ALDOA; human. DR Proteomes; UP000005640; Chromosome 16. DR Bgee; ENSG00000149925; Expressed in gastrocnemius and 94 other tissues. DR ExpressionAtlas; H3BU78; baseline and differential. DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 2. DR InterPro; IPR029768; Aldolase_I_AS. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000741; FBA_I. DR PANTHER; PTHR11627; FRUCTOSE-BISPHOSPHATE ALDOLASE; 2. DR Pfam; PF00274; Glycolytic; 1. DR PROSITE; PS00158; ALDOLASE_CLASS_I; 1. PE 1: Evidence at protein level; KW Glycolysis {ECO:0000256|RuleBase:RU003994}; KW Lyase {ECO:0000256|RuleBase:RU003994}; KW Proteomics identification {ECO:0007829|EPD:H3BU78, KW ECO:0007829|MaxQB:H3BU78}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Schiff base {ECO:0000256|ARBA:ARBA00023270}. FT NON_TER 1 FT /evidence="ECO:0000313|Ensembl:ENSP00000457514.1" FT NON_TER 204 FT /evidence="ECO:0000313|Ensembl:ENSP00000457514.1" SQ SEQUENCE 204 AA; 22094 MW; 1105C7DD3543AD7A CRC64; RRFYRQLLLT ADDRVNPCIG GVILFHETLY QKADDGRPFP QVIKSKGGVV GIKVDKGVVP LAGTNGETTT QGLDGLSERC AQYKKDGADF AKWRCVLKIG EHTPSALAIM ENANVLARYA SICQQVLAAV YKALSDHHIY LEGTLLKPNM VTPGHACTQK FSHEEIAMAT VTALRRTVPP AVTGITFLSG GQSEEEASIN LNAI // ID H3BQN4_HUMAN Unreviewed; 361 AA. AC H3BQN4; DT 18-APR-2012, integrated into UniProtKB/TrEMBL. DT 18-APR-2012, sequence version 1. DT 14-DEC-2022, entry version 76. DE RecName: Full=Fructose-bisphosphate aldolase {ECO:0000256|RuleBase:RU003994}; DE EC=4.1.2.13 {ECO:0000256|RuleBase:RU003994}; GN Name=ALDOA {ECO:0000313|Ensembl:ENSP00000455857.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000455857.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000455857.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [2] {ECO:0007829|PubMed:17081983} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [3] {ECO:0007829|PubMed:18669648} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [4] {ECO:0007829|PubMed:19413330} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [5] {ECO:0007829|PubMed:19690332} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [6] {ECO:0007829|PubMed:19608861} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [7] {ECO:0007829|PubMed:20068231} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [8] {ECO:0007829|PubMed:21269460} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [9] {ECO:0007829|PubMed:21406692} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [10] {ECO:0007829|PubMed:22905912} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22905912; DOI=10.1021/pr300539b; RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P., RA Mariman E.C., Renes J.; RT "Resveratrol-induced changes of the human adipocyte secretion profile."; RL J. Proteome Res. 11:4733-4743(2012). RN [11] {ECO:0007829|PubMed:22223895} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.M111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [12] {ECO:0007829|PubMed:22814378} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [13] {ECO:0007829|PubMed:23186163} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=23186163; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [14] {ECO:0007829|PubMed:24275569} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [15] {ECO:0007829|PubMed:24129315} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=24129315; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [16] {ECO:0007829|PubMed:25114211} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [17] {ECO:0007829|PubMed:25944712} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [18] {ECO:0000313|Ensembl:ENSP00000455857.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-2022) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3- CC phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729, CC ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13; CC Evidence={ECO:0000256|RuleBase:RU003994}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 4/4. CC {ECO:0000256|ARBA:ARBA00004714, ECO:0000256|RuleBase:RU004257}. CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase CC family. {ECO:0000256|ARBA:ARBA00010387, ECO:0000256|RuleBase:RU003994}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC093512; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; H3BQN4; -. DR SMR; H3BQN4; -. DR SwissPalm; H3BQN4; -. DR MaxQB; H3BQN4; -. DR PeptideAtlas; H3BQN4; -. DR ProteomicsDB; 41829; -. DR Antibodypedia; 1031; 709 antibodies from 37 providers. DR Ensembl; ENST00000569798.5; ENSP00000455857.1; ENSG00000149925.22. DR UCSC; uc059szg.1; human. DR HGNC; HGNC:414; ALDOA. DR VEuPathDB; HostDB:ENSG00000149925; -. DR GeneTree; ENSGT00950000182987; -. DR UniPathway; UPA00109; UER00183. DR ChiTaRS; ALDOA; human. DR Proteomes; UP000005640; Chromosome 16. DR Bgee; ENSG00000149925; Expressed in gastrocnemius and 94 other tissues. DR ExpressionAtlas; H3BQN4; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR029768; Aldolase_I_AS. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000741; FBA_I. DR PANTHER; PTHR11627; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1. DR Pfam; PF00274; Glycolytic; 1. DR PROSITE; PS00158; ALDOLASE_CLASS_I; 1. PE 1: Evidence at protein level; KW Glycolysis {ECO:0000256|RuleBase:RU003994}; KW Lyase {ECO:0000256|RuleBase:RU003994}; KW Proteomics identification {ECO:0007829|EPD:H3BQN4, KW ECO:0007829|MaxQB:H3BQN4}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Schiff base {ECO:0000256|ARBA:ARBA00023270}. SQ SEQUENCE 361 AA; 39340 MW; CA08661BBDE6DE36 CRC64; MPYQYPALTP EQKKELSDIA HRIVAPGKGI LAADESTGSI AKRLQSIGTE NTEENRRFYR QLLLTADDRV NPCIGGVILF HETLYQKADD GRPFPQVIKS KGGVVGIKVD KGVVPLAGTN GETTTQGLDG LSERCAQYKK DGADFAKWRC VLKIGEHTPS ALAIMENANV LARYASICQQ NGIVPIVEPE ILPDGDHDLK RCQYVTEKVL AAVYKALSDH HIYLEGTLLK PNMVTPGHAC TQKFSHEEIA MATVTALRRT VPPAVTGITF LSGGQSEEEA SINLNAINKC PLLKPWALTF SYGRALQASA LKAWGGKKEN LKAAQEEYVK RALVRIGRRW AGCLGGWDSE KSPSHSTPLP A // ID J3KPS3_HUMAN Unreviewed; 368 AA. AC J3KPS3; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 14-DEC-2022, entry version 85. DE RecName: Full=Fructose-bisphosphate aldolase {ECO:0000256|RuleBase:RU003994}; DE EC=4.1.2.13 {ECO:0000256|RuleBase:RU003994}; GN Name=ALDOA {ECO:0000313|EMBL:EAW79936.1, GN ECO:0000313|Ensembl:ENSP00000378661.3}; GN ORFNames=hCG_1811258 {ECO:0000313|EMBL:EAW79936.1}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000378661.3, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|EMBL:EAW79936.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=11181995; DOI=10.1126/science.1058040; RA Venter J.C., Adams M.D., Myers E.W., Li P.W., Mural R.J., Sutton G.G., RA Smith H.O., Yandell M., Evans C.A., Holt R.A., Gocayne J.D., Amanatides P., RA Ballew R.M., Huson D.H., Wortman J.R., Zhang Q., Kodira C.D., Zheng X.H., RA Chen L., Skupski M., Subramanian G., Thomas P.D., Zhang J., RA Gabor Miklos G.L., Nelson C., Broder S., Clark A.G., Nadeau J., RA McKusick V.A., Zinder N., Levine A.J., Roberts R.J., Simon M., Slayman C., RA Hunkapiller M., Bolanos R., Delcher A., Dew I., Fasulo D., Flanigan M., RA Florea L., Halpern A., Hannenhalli S., Kravitz S., Levy S., Mobarry C., RA Reinert K., Remington K., Abu-Threideh J., Beasley E., Biddick K., RA Bonazzi V., Brandon R., Cargill M., Chandramouliswaran I., Charlab R., RA Chaturvedi K., Deng Z., Di Francesco V., Dunn P., Eilbeck K., RA Evangelista C., Gabrielian A.E., Gan W., Ge W., Gong F., Gu Z., Guan P., RA Heiman T.J., Higgins M.E., Ji R.R., Ke Z., Ketchum K.A., Lai Z., Lei Y., RA Li Z., Li J., Liang Y., Lin X., Lu F., Merkulov G.V., Milshina N., RA Moore H.M., Naik A.K., Narayan V.A., Neelam B., Nusskern D., Rusch D.B., RA Salzberg S., Shao W., Shue B., Sun J., Wang Z., Wang A., Wang X., Wang J., RA Wei M., Wides R., Xiao C., Yan C., Yao A., Ye J., Zhan M., Zhang W., RA Zhang H., Zhao Q., Zheng L., Zhong F., Zhong W., Zhu S., Zhao S., RA Gilbert D., Baumhueter S., Spier G., Carter C., Cravchik A., Woodage T., RA Ali F., An H., Awe A., Baldwin D., Baden H., Barnstead M., Barrow I., RA Beeson K., Busam D., Carver A., Center A., Cheng M.L., Curry L., RA Danaher S., Davenport L., Desilets R., Dietz S., Dodson K., Doup L., RA Ferriera S., Garg N., Gluecksmann A., Hart B., Haynes J., Haynes C., RA Heiner C., Hladun S., Hostin D., Houck J., Howland T., Ibegwam C., RA Johnson J., Kalush F., Kline L., Koduru S., Love A., Mann F., May D., RA McCawley S., McIntosh T., McMullen I., Moy M., Moy L., Murphy B., RA Nelson K., Pfannkoch C., Pratts E., Puri V., Qureshi H., Reardon M., RA Rodriguez R., Rogers Y.H., Romblad D., Ruhfel B., Scott R., Sitter C., RA Smallwood M., Stewart E., Strong R., Suh E., Thomas R., Tint N.N., Tse S., RA Vech C., Wang G., Wetter J., Williams S., Williams M., Windsor S., RA Winn-Deen E., Wolfe K., Zaveri J., Zaveri K., Abril J.F., Guigo R., RA Campbell M.J., Sjolander K.V., Karlak B., Kejariwal A., Mi H., Lazareva B., RA Hatton T., Narechania A., Diemer K., Muruganujan A., Guo N., Sato S., RA Bafna V., Istrail S., Lippert R., Schwartz R., Walenz B., Yooseph S., RA Allen D., Basu A., Baxendale J., Blick L., Caminha M., Carnes-Stine J., RA Caulk P., Chiang Y.H., Coyne M., Dahlke C., Mays A., Dombroski M., RA Donnelly M., Ely D., Esparham S., Fosler C., Gire H., Glanowski S., RA Glasser K., Glodek A., Gorokhov M., Graham K., Gropman B., Harris M., RA Heil J., Henderson S., Hoover J., Jennings D., Jordan C., Jordan J., RA Kasha J., Kagan L., Kraft C., Levitsky A., Lewis M., Liu X., Lopez J., RA Ma D., Majoros W., McDaniel J., Murphy S., Newman M., Nguyen T., Nguyen N., RA Nodell M., Pan S., Peck J., Peterson M., Rowe W., Sanders R., Scott J., RA Simpson M., Smith T., Sprague A., Stockwell T., Turner R., Venter E., RA Wang M., Wen M., Wu D., Wu M., Xia A., Zandieh A., Zhu X.; RT "The sequence of the human genome."; RL Science 291:1304-1351(2001). RN [2] {ECO:0000313|Ensembl:ENSP00000378661.3, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [3] {ECO:0000313|EMBL:EAW79936.1} RP NUCLEOTIDE SEQUENCE. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0007829|PubMed:17081983} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [5] {ECO:0007829|PubMed:18669648} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [6] {ECO:0007829|PubMed:19413330} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [7] {ECO:0007829|PubMed:19690332} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [8] {ECO:0007829|PubMed:19608861} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [9] {ECO:0007829|PubMed:20068231} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [10] {ECO:0007829|PubMed:21269460} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [11] {ECO:0007829|PubMed:21406692} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [12] {ECO:0007829|PubMed:22905912} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22905912; DOI=10.1021/pr300539b; RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P., RA Mariman E.C., Renes J.; RT "Resveratrol-induced changes of the human adipocyte secretion profile."; RL J. Proteome Res. 11:4733-4743(2012). RN [13] {ECO:0007829|PubMed:22223895} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.M111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [14] {ECO:0007829|PubMed:22814378} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [15] {ECO:0007829|PubMed:23186163} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=23186163; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [16] {ECO:0007829|PubMed:24275569} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [17] {ECO:0007829|PubMed:24129315} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=24129315; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [18] {ECO:0007829|PubMed:25114211} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [19] {ECO:0007829|PubMed:25944712} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [20] {ECO:0000313|Ensembl:ENSP00000378661.3} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-2022) to UniProtKB. CC -!- CATALYTIC ACTIVITY: CC Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3- CC phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729, CC ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13; CC Evidence={ECO:0000256|RuleBase:RU003994}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 4/4. CC {ECO:0000256|ARBA:ARBA00004714, ECO:0000256|RuleBase:RU004257}. CC -!- SIMILARITY: Belongs to the class I fructose-bisphosphate aldolase CC family. {ECO:0000256|ARBA:ARBA00010387, ECO:0000256|RuleBase:RU003994}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC093512; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471238; EAW79936.1; -; Genomic_DNA. DR SMR; J3KPS3; -. DR SwissPalm; J3KPS3; -. DR PRIDE; J3KPS3; -. DR Antibodypedia; 1031; 709 antibodies from 37 providers. DR Ensembl; ENST00000395240.7; ENSP00000378661.3; ENSG00000149925.22. DR UCSC; uc059sys.1; human. DR HGNC; HGNC:414; ALDOA. DR VEuPathDB; HostDB:ENSG00000149925; -. DR GeneTree; ENSGT00950000182987; -. DR UniPathway; UPA00109; UER00183. DR ChiTaRS; ALDOA; human. DR Proteomes; UP000005640; Chromosome 16. DR Bgee; ENSG00000149925; Expressed in gastrocnemius and 94 other tissues. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR029768; Aldolase_I_AS. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000741; FBA_I. DR PANTHER; PTHR11627; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1. DR Pfam; PF00274; Glycolytic; 1. DR PROSITE; PS00158; ALDOLASE_CLASS_I; 1. PE 1: Evidence at protein level; KW Glycolysis {ECO:0000256|RuleBase:RU003994}; KW Lyase {ECO:0000256|RuleBase:RU003994}; KW Proteomics identification {ECO:0007829|EPD:J3KPS3, KW ECO:0007829|MaxQB:J3KPS3}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Schiff base {ECO:0000256|ARBA:ARBA00023270}. SQ SEQUENCE 368 AA; 39817 MW; 6E24B9E9BC31C9EB CRC64; MPYQYPALTP EQKKELSDIA HRIVAPGKGI LAADESTGSI AKRLQSIGTE NTEENRRFYR QLLLTADDRV NPCIGGVILF HETLYQKADD GRPFPQVIKS KGGVVGIKVD KGVVPLAGTN GETTTQGLDG LSERCAQYKK DGADFAKWRC VLKIGEHTPS ALAIMENANV LARYASICQQ VGLQNGIVPI VEPEILPDGD HDLKRCQYVT EKVLAAVYKA LSDHHIYLEG TLLKPNMVTP GHACTQKFSH EEIAMATVTA LRRTVPPAVT GITFLSGGQS EEEASINLNA INKCPLLKPW ALTFSYGRAL QASALKAWGG KKENLKAAQE EYVKRALANS LACQGKYTPS GQAGAAASES LFVSNHAY //