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 18-JUN-2025, entry version 264. DE RecName: Full=Fructose-bisphosphate aldolase A {ECO:0000305}; DE EC=4.1.2.13 {ECO:0000269|PubMed:14766013, ECO:0000269|PubMed:2204832}; 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 CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=2204832; DOI=10.1016/0166-6851(90)90189-s; RA Doebeli H., Trzeciak A., Gillessen D., Matile H., Srivastava I.K., RA Perrin L.H., Jakob P.E., Certa U.; RT "Expression, purification, biochemical characterization and inhibition of RT recombinant Plasmodium falciparum aldolase."; RL Mol. Biochem. Parasitol. 41:259-268(1990). RN [18] 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 [19] 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 [20] 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 [21] 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 [22] 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 [23] 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 [24] 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 [25] 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 [26] 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 [27] 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 [28] 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 [29] 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 [30] 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 [31] 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 [32] 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 [33] 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 [34] 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 [35] 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 [36] 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 [37] 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 [38] 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 [39] 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 [40] 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 [41] 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 [42] 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 [43] 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 [44] 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 [45] 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 [46] 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, ECO:0000269|PubMed:2204832}; 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 KM=24 uM for fructose-l,6-bisphosphate {ECO:0000269|PubMed:2204832}; 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; P05062: ALDOB; NbExp=3; IntAct=EBI-709613, EBI-1045507; CC P04075; P09972: ALDOC; NbExp=5; IntAct=EBI-709613, EBI-2952751; CC P04075; Q86X55: CARM1; NbExp=2; IntAct=EBI-709613, EBI-2339854; 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_001243177.4. [P04075-2] DR RefSeq; NP_908930.1; NM_184041.5. [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; 342. DR FunCoup; P04075; 1506. DR IntAct; P04075; 92. DR MINT; P04075; -. DR STRING; 9606.ENSP00000496166; -. 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; 3 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P04075; -. DR MetOSite; P04075; -. DR PhosphoSitePlus; P04075; -. DR SwissPalm; P04075; -. DR BioMuta; ALDOA; -. DR DMDM; 113606; -. DR OGP; P04075; -. DR REPRODUCTION-2DPAGE; IPI00465439; -. DR REPRODUCTION-2DPAGE; P04075; -. DR CPTAC; CPTAC-2718; -. DR CPTAC; CPTAC-2719; -. DR CPTAC; CPTAC-459; -. DR jPOST; P04075; -. DR MassIVE; P04075; -. DR PaxDb; 9606-ENSP00000378669; -. DR PeptideAtlas; P04075; -. DR PRIDE; P04075; -. DR ProteomicsDB; 51647; -. [P04075-1] DR Pumba; P04075; -. DR TopDownProteomics; P04075-1; -. [P04075-1] DR Antibodypedia; 1031; 702 antibodies from 38 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 AGR; HGNC:414; -. 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; WRAVITI; -. DR OrthoDB; 36455at2759; -. DR PAN-GO; P04075; 4 GO annotations based on evolutionary models. DR PhylomeDB; P04075; -. DR TreeFam; TF314203; -. DR BioCyc; MetaCyc:HS07647-MONOMER; -. 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; 801 hits in 1177 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 96 other cell types or tissues. DR ExpressionAtlas; P04075; baseline and differential. DR GO; GO:0015629; C:actin cytoskeleton; IDA:BHF-UCL. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. 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 CDD; cd00948; FBP_aldolase_I_a; 1. DR FunFam; 3.20.20.70:FF:000021; Fructose-bisphosphate aldolase; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR InterPro; IPR029768; Aldolase_I_AS. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000741; FBA_I. DR NCBIfam; NF033379; FrucBisAld_I; 1. DR PANTHER; PTHR11627; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1. DR Pfam; PF00274; Glycolytic; 1. DR SUPFAM; SSF51569; Aldolase; 1. DR PROSITE; PS00158; ALDOLASE_CLASS_I; 1. 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; Proteomics identification; Reference proteome; KW 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|UniProtKB:P00883" FT ACT_SITE 230 FT /note="Schiff-base intermediate with dihydroxyacetone-P" FT /evidence="ECO:0000250|UniProtKB:P00883" FT BINDING 43 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /evidence="ECO:0000250|UniProtKB:P00883" FT BINDING 272..274 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /evidence="ECO:0000250|UniProtKB:P00883" FT BINDING 301 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /evidence="ECO:0000250|UniProtKB:P00883" FT BINDING 304 FT /ligand="beta-D-fructose 1,6-bisphosphate" FT /ligand_id="ChEBI:CHEBI:32966" FT /evidence="ECO:0000250|UniProtKB:P00883" 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; does not affect FT thermal stability; 4-fold decrease in catalytic efficiency FT due to reduced enzyme activity; 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 //