ID RBM6_HUMAN Reviewed; 1123 AA. AC P78332; B4E0G6; O60549; O75524; Q86SS3; DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 5. DT 14-DEC-2022, entry version 196. DE RecName: Full=RNA-binding protein 6; DE AltName: Full=Lung cancer antigen NY-LU-12; DE AltName: Full=Protein G16; DE AltName: Full=RNA-binding motif protein 6; DE AltName: Full=RNA-binding protein DEF-3; GN Name=RBM6; Synonyms=DEF3; 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=Lung; RX PubMed=9500467; RA Gure A.O., Altorki N.K., Stockert E., Scanlan M.J., Old L.J., Chen Y.-T.; RT "Human lung cancer antigens recognized by autologous antibodies: definition RT of a novel cDNA derived from the tumor suppressor gene locus on chromosome RT 3p21.3."; RL Cancer Res. 58:1034-1041(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=10352938; DOI=10.1038/sj.ejhg.5200334; RA Timmer T., Terpstra P., van den Berg A., Veldhuis P.M., Ter Elst A., RA Voutsinas G., Hulsbeek M.M.F., Draaijers T.G., Looman M.W.G., Kok K., RA Naylor S.L., Buys C.H.C.M.; RT "A comparison of genomic structures and expression patterns of two closely RT related flanking genes in a critical lung cancer region at 3p21.3."; RL Eur. J. Hum. Genet. 7:478-486(1999). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=10353602; DOI=10.1038/sj.onc.1202601; RA Drabkin H.A., West J.D., Hotfilder M., Heng Y.M., Erickson P., Calvo R., RA Dalmau J., Gemmill R.M., Sablitzky F.; RT "DEF-3(g16/NY-LU-12), an RNA binding protein from the 3p21.3 homozygous RT deletion region in SCLC."; RL Oncogene 18:2589-2597(1999). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Latif F., Duh F.-M., Wei M.H., Sekido Y., Forgacs E., Minna J.D., RA Lerman M.I.; RT "A highly conserved and universally expressed gene is interrupted by a RT homozygous deletion in a small cell lung cancer cell line NCI-H740."; RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Thymus; 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 GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 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 [8] RP DISCUSSION OF SEQUENCE, AND VARIANT PHE-353. RX PubMed=11085536; RG The international lung cancer chromosome 3p21.3 tumor suppressor gene consortium; RA Lerman M.I., Minna J.D.; RT "The 630-kb lung cancer homozygous deletion region on human chromosome RT 3p21.3: identification and evaluation of the resident candidate tumor RT suppressor genes."; RL Cancer Res. 60:6116-6133(2000). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1025, 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360 AND SER-362, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1025, 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360; SER-362 AND SER-1025, 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 [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360 AND SER-362, 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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-891 AND SER-1025, 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 [16] RP INTERACTION WITH FAM168B. RX PubMed=20716133; DOI=10.1111/j.1582-4934.2010.01134.x; RA Mishra M., Akatsu H., Heese K.; RT "The novel protein MANI modulates neurogenesis and neurite-cone growth."; RL J. Cell. Mol. Med. 15:1713-1725(2011). RN [17] 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-240; THR-344; RP SER-360; SER-362; SER-1022 AND SER-1025, AND IDENTIFICATION BY MASS RP 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 [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360; SER-362; SER-891 AND RP SER-1025, AND 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 [20] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-386; LYS-453; LYS-569 AND RP LYS-1046, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [21] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-453 AND LYS-569, AND RP IDENTIFICATION BY MASS 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 [22] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-453 AND LYS-569, AND RP IDENTIFICATION BY MASS 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 [23] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-36; LYS-331; LYS-386; LYS-453; RP LYS-469; LYS-569; LYS-871; LYS-879; LYS-887; LYS-935; LYS-948; LYS-991; RP LYS-1019; LYS-1042; LYS-1046 AND LYS-1066, AND IDENTIFICATION BY MASS RP 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). CC -!- FUNCTION: Specifically binds poly(G) RNA homopolymers in vitro. CC -!- SUBUNIT: May interact with FAM168B. CC -!- INTERACTION: CC P78332; P26641-2: EEF1G; NbExp=3; IntAct=EBI-2692323, EBI-10177695; CC P78332-2; Q15555: MAPRE2; NbExp=3; IntAct=EBI-14150298, EBI-739717; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=P78332-1; Sequence=Displayed; CC Name=2; CC IsoId=P78332-2; Sequence=VSP_045202; CC Name=3; CC IsoId=P78332-3; Sequence=VSP_057401, VSP_057402; CC -!- TISSUE SPECIFICITY: Ubiquitous in adults. 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; AF042857; AAC05826.1; -; mRNA. DR EMBL; AF069517; AAC21578.1; -; mRNA. DR EMBL; AF091264; AAD04160.1; -; mRNA. DR EMBL; U50839; AAC35207.1; -; mRNA. DR EMBL; AK303371; BAG64428.1; -; mRNA. DR EMBL; AC104450; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC105935; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC046643; AAH46643.1; -; mRNA. DR CCDS; CCDS2809.1; -. [P78332-1] DR CCDS; CCDS54586.1; -. [P78332-2] DR RefSeq; NP_001161054.1; NM_001167582.1. [P78332-2] DR RefSeq; NP_005768.1; NM_005777.2. [P78332-1] DR RefSeq; XP_005264843.1; XM_005264786.1. DR RefSeq; XP_005264844.1; XM_005264787.2. DR RefSeq; XP_016860988.1; XM_017005499.1. DR RefSeq; XP_016860989.1; XM_017005500.1. [P78332-2] DR RefSeq; XP_016860990.1; XM_017005501.1. [P78332-2] DR RefSeq; XP_016860991.1; XM_017005502.1. [P78332-2] DR AlphaFoldDB; P78332; -. DR BioGRID; 115479; 114. DR IntAct; P78332; 44. DR MINT; P78332; -. DR STRING; 9606.ENSP00000266022; -. DR iPTMnet; P78332; -. DR PhosphoSitePlus; P78332; -. DR BioMuta; RBM6; -. DR DMDM; 116242749; -. DR EPD; P78332; -. DR jPOST; P78332; -. DR MassIVE; P78332; -. DR MaxQB; P78332; -. DR PaxDb; P78332; -. DR PeptideAtlas; P78332; -. DR ProteomicsDB; 5671; -. DR ProteomicsDB; 57570; -. [P78332-1] DR ProteomicsDB; 69630; -. DR Antibodypedia; 13824; 188 antibodies from 26 providers. DR DNASU; 10180; -. DR Ensembl; ENST00000266022.9; ENSP00000266022.4; ENSG00000004534.15. [P78332-1] DR Ensembl; ENST00000422955.5; ENSP00000392939.1; ENSG00000004534.15. [P78332-2] DR Ensembl; ENST00000425608.5; ENSP00000408665.1; ENSG00000004534.15. [P78332-3] DR Ensembl; ENST00000442092.5; ENSP00000393530.1; ENSG00000004534.15. [P78332-2] DR GeneID; 10180; -. DR KEGG; hsa:10180; -. DR MANE-Select; ENST00000266022.9; ENSP00000266022.4; NM_005777.3; NP_005768.1. DR UCSC; uc003cyc.4; human. [P78332-1] DR UCSC; uc062jzu.1; human. DR CTD; 10180; -. DR DisGeNET; 10180; -. DR GeneCards; RBM6; -. DR HGNC; HGNC:9903; RBM6. DR HPA; ENSG00000004534; Low tissue specificity. DR MIM; 606886; gene. DR neXtProt; NX_P78332; -. DR OpenTargets; ENSG00000004534; -. DR PharmGKB; PA34268; -. DR VEuPathDB; HostDB:ENSG00000004534; -. DR eggNOG; KOG0154; Eukaryota. DR GeneTree; ENSGT00940000157976; -. DR HOGENOM; CLU_010527_0_0_1; -. DR InParanoid; P78332; -. DR OMA; REVGSCM; -. DR PhylomeDB; P78332; -. DR TreeFam; TF315789; -. DR PathwayCommons; P78332; -. DR SignaLink; P78332; -. DR BioGRID-ORCS; 10180; 16 hits in 1087 CRISPR screens. DR ChiTaRS; RBM6; human. DR GeneWiki; RBM6; -. DR GenomeRNAi; 10180; -. DR Pharos; P78332; Tbio. DR PRO; PR:P78332; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; P78332; protein. DR Bgee; ENSG00000004534; Expressed in lower esophagus mucosa and 202 other tissues. DR ExpressionAtlas; P78332; baseline and differential. DR Genevisible; P78332; HS. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; TAS:ProtInc. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central. DR GO; GO:0006396; P:RNA processing; TAS:ProtInc. DR CDD; cd16163; OCRE_RBM6; 1. DR CDD; cd12314; RRM1_RBM6; 1. DR CDD; cd12563; RRM2_RBM6; 1. DR Gene3D; 3.30.70.330; -; 2. DR InterPro; IPR000467; G_patch_dom. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf. DR InterPro; IPR041591; OCRE. DR InterPro; IPR035979; RBD_domain_sf. DR InterPro; IPR028806; RBM6. DR InterPro; IPR035617; RBM6_OCRE. DR InterPro; IPR034123; RBM6_RRM1. DR InterPro; IPR034125; RBM6_RRM2. DR InterPro; IPR000504; RRM_dom. DR PANTHER; PTHR13948:SF22; RNA-BINDING PROTEIN 6; 3. DR Pfam; PF01585; G-patch; 1. DR Pfam; PF17780; OCRE; 1. DR SMART; SM00443; G_patch; 1. DR SMART; SM00360; RRM; 2. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2. DR PROSITE; PS50174; G_PATCH; 1. DR PROSITE; PS50102; RRM; 1. DR AGR; HGNC:9903; -. PE 1: Evidence at protein level; KW Alternative splicing; Isopeptide bond; Nucleus; Phosphoprotein; KW Reference proteome; RNA-binding; Ubl conjugation. FT CHAIN 1..1123 FT /note="RNA-binding protein 6" FT /id="PRO_0000081760" FT DOMAIN 456..536 FT /note="RRM" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT DOMAIN 1051..1097 FT /note="G-patch" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00092" FT REGION 1..391 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 413..454 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 574..654 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 741..787 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 827..948 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1004..1106 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 111..134 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 141..234 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 241..288 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 306..347 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 354..369 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 431..453 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 574..588 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 594..654 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 742..771 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 772..787 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 827..864 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 872..886 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 934..948 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1004..1052 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 17 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 240 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 344 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 360 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17525332, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 362 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17525332, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 891 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:24275569" FT MOD_RES 1022 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1025 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT CROSSLNK 36 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 331 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 386 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 453 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 469 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 569 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 871 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 879 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 887 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 935 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 948 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 991 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1019 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1042 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 1046 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 1066 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..522 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_045202" FT VAR_SEQ 496..520 FT /note="YDYGYVCVEFSLLEDAIGCMEANQG -> NSNDPGQRSYPGVCIKPGFLVLQ FT TM (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_057401" FT VAR_SEQ 521..1123 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_057402" FT VARIANT 353 FT /note="S -> F (in a non-small cell lung cancer cell line; FT dbSNP:rs61731329)" FT /evidence="ECO:0000269|PubMed:11085536" FT /id="VAR_014226" FT VARIANT 721 FT /note="N -> T (in dbSNP:rs34707170)" FT /id="VAR_052216" FT CONFLICT 642 FT /note="R -> K (in Ref. 2; AAC21578)" FT /evidence="ECO:0000305" FT CONFLICT 710 FT /note="A -> V (in Ref. 1; AAC05826)" FT /evidence="ECO:0000305" FT CONFLICT 796 FT /note="T -> S (in Ref. 1; AAC05826)" FT /evidence="ECO:0000305" SQ SEQUENCE 1123 AA; 128644 MW; 2952ED1BAA839DE4 CRC64; MWGDSRPANR TGPFRGSQEE RFAPGWNRDY PPPPLKSHAQ ERHSGNFPGR DSLPFDFQGH SGPPFANVEE HSFSYGARDG PHGDYRGGEG PGHDFRGGDF SSSDFQSRDS SQLDFRGRDI HSGDFRDREG PPMDYRGGDG TSMDYRGREA PHMNYRDRDA HAVDFRGRDA PPSDFRGRGT YDLDFRGRDG SHADFRGRDL SDLDFRAREQ SRSDFRNRDV SDLDFRDKDG TQVDFRGRGS GTTDLDFRDR DTPHSDFRGR HRSRTDQDFR GREMGSCMEF KDREMPPVDP NILDYIQPST QDREHSGMNV NRREESTHDH TIERPAFGIQ KGEFEHSETR EGETQGVAFE HESPADFQNS QSPVQDQDKS QLSGREEQSS DAGLFKEEGG LDFLGRQDTD YRSMEYRDVD HRLPGSQMFG YGQSKSFPEG KTARDAQRDL QDQDYRTGPS EEKPSRLIRL SGVPEDATKE EILNAFRTPD GMPVKNLQLK EYNTGYDYGY VCVEFSLLED AIGCMEANQG TLMIQDKEVT LEYVSSLDFW YCKRCKANIG GHRSSCSFCK NPREVTEAKQ ELITYPQPQK TSIPAPLEKQ PNQPLRPADK EPEPRKREEG QESRLGHQKR EAERYLPPSR REGPTFRRDR ERESWSGETR QDGESKTIML KRIYRSTPPE VIVEVLEPYV RLTTANVRII KNRTGPMGHT YGFIDLDSHA EALRVVKILQ NLDPPFSIDG KMVAVNLATG KRRNDSGDHS DHMHYYQGKK YFRDRRGGGR NSDWSSDTNR QGQQSSSDCY IYDSATGYYY DPLAGTYYDP NTQQEVYVPQ DPGLPEEEEI KEKKPTSQGK SSSKKEMSKR DGKEKKDRGV TRFQENASEG KAPAEDVFKK PLPPTVKKEE SPPPPKVVNP LIGLLGEYGG DSDYEEEEEE EQTPPPQPRT AQPQKREEQT KKENEEDKLT DWNKLACLLC RRQFPNKEVL IKHQQLSDLH KQNLEIHRKI KQSEQELAYL ERREREGKFK GRGNDRREKL QSFDSPERKR IKYSRETDSD RKLVDKEDID TSSKGGCVQQ ATGWRKGTGL GYGHPGLASS EEAEGRMRGP SVGASGRTSK RQSNETYRDA VRRVMFARYK ELD // ID EF1G_HUMAN Reviewed; 437 AA. AC P26641; B4DTG2; Q6PJ62; Q6PK31; Q96CU2; Q9P196; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 14-DEC-2022, entry version 234. DE RecName: Full=Elongation factor 1-gamma; DE Short=EF-1-gamma; DE AltName: Full=eEF-1B gamma; GN Name=EEF1G; Synonyms=EF1G; ORFNames=PRO1608; 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). RX PubMed=1461723; DOI=10.1093/nar/20.22.5907; RA Sanders J., Maassen J.A., Moeller W.; RT "Elongation factor-1 messenger-RNA levels in cultured cells are high RT compared to tissue and are not drastically affected further by oncogenic RT transformation."; RL Nucleic Acids Res. 20:5907-5910(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=1598220; DOI=10.1093/nar/20.10.2598; RA Kumabe T., Schma Y., Yamamoto T.; RT "Human cDNAs encoding elongation factor 1 gamma and the ribosomal protein RT L19."; RL Nucleic Acids Res. 20:2598-2598(1992). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Placenta; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Bone marrow, Eye, Liver, Lung, Muscle, 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 [6] RP PROTEIN SEQUENCE OF 2-14. 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 [7] RP PROTEIN SEQUENCE OF 2-14, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT RP ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=B-cell lymphoma; RA Bienvenut W.V.; RL Submitted (OCT-2004) to UniProtKB. RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 80-437 (ISOFORM 1). RC TISSUE=Pancreatic carcinoma; RX PubMed=1372736; DOI=10.1097/00006676-199203000-00003; RA Lew Y., Jones D.V., Mars W.M., Evans D., Byrd D., Frazier M.L.; RT "Expression of elongation factor-1 gamma-related sequence in human RT pancreatic cancer."; RL Pancreas 7:144-152(1992). RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 121-437 (ISOFORM 1). RC TISSUE=Fetal liver; RA Zhang C., Yu Y., Zhang S., Wei H., Zhang Y., Zhou G., Bi J., Liu M., He F.; RT "Functional prediction of the coding sequences of 79 new genes deduced by RT analysis of cDNA clones from human fetal liver."; RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases. RN [10] 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 [11] RP INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=16548883; DOI=10.1111/j.1462-5822.2005.00644.x; RA Leong W.F., Chow V.T.; RT "Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal RT differential cellular gene expression in response to enterovirus 71 RT infection."; RL Cell. Microbiol. 8:565-580(2006). RN [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-147 AND LYS-434, 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 [14] 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 [15] RP MALONYLATION AT LYS-434. 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 [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [17] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [18] 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 [19] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-253, 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 [20] 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 [21] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-285, AND IDENTIFICATION BY MASS RP 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 [22] RP STRUCTURE BY NMR OF 276-437. RX PubMed=12766415; DOI=10.1023/a:1023504611632; RA Vanwetswinkel S., Kriek J., Andersen G.R., Dijk J., Siegal G.; RT "1H, 15N and 13C resonance assignments of the highly conserved 19 kDa C- RT terminal domain from human elongation factor 1Bgamma."; RL J. Biomol. NMR 26:189-190(2003). CC -!- FUNCTION: Probably plays a role in anchoring the complex to other CC cellular components. CC -!- SUBUNIT: EF-1 is composed of four subunits: alpha, beta, delta, and CC gamma. CC -!- INTERACTION: CC P26641; Q8WUW1: BRK1; NbExp=3; IntAct=EBI-351467, EBI-2837444; CC P26641; P24534: EEF1B2; NbExp=9; IntAct=EBI-351467, EBI-354334; CC P26641; P29692: EEF1D; NbExp=4; IntAct=EBI-351467, EBI-358607; CC P26641; P29692-2: EEF1D; NbExp=4; IntAct=EBI-351467, EBI-5280572; CC P26641; Q04695: KRT17; NbExp=2; IntAct=EBI-351467, EBI-297873; CC P26641; Q9HB07: MYG1; NbExp=3; IntAct=EBI-351467, EBI-709754; CC P26641; Q16512: PKN1; NbExp=3; IntAct=EBI-351467, EBI-602382; CC P26641; Q969Q1: TRIM63; NbExp=2; IntAct=EBI-351467, EBI-5661333; CC P26641; P14679-2: TYR; NbExp=3; IntAct=EBI-351467, EBI-25894402; CC P26641; P31930: UQCRC1; NbExp=3; IntAct=EBI-351467, EBI-1052596; CC P26641-2; P24534: EEF1B2; NbExp=3; IntAct=EBI-10177695, EBI-354334; CC P26641-2; P29692: EEF1D; NbExp=3; IntAct=EBI-10177695, EBI-358607; CC P26641-2; P29692-2: EEF1D; NbExp=3; IntAct=EBI-10177695, EBI-5280572; CC P26641-2; Q658K8: EEF1DP3; NbExp=4; IntAct=EBI-10177695, EBI-10248874; CC P26641-2; O94889: KLHL18; NbExp=3; IntAct=EBI-10177695, EBI-2510096; CC P26641-2; Q9HBL7: PLGRKT; NbExp=3; IntAct=EBI-10177695, EBI-714824; CC P26641-2; P78332: RBM6; NbExp=3; IntAct=EBI-10177695, EBI-2692323; CC P26641-2; F4ZW62; NbExp=3; IntAct=EBI-10177695, EBI-10177680; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P26641-1; Sequence=Displayed; CC Name=2; CC IsoId=P26641-2; Sequence=VSP_056204; CC -!- TISSUE SPECIFICITY: Highly expressed in pancreatic tumor tissue and to CC a lesser extent in normal kidney, intestine, pancreas, stomach, lung, CC brain, spleen and liver. CC -!- INDUCTION: Down-regulated in response to enterovirus 71 (EV71) CC infection. {ECO:0000269|PubMed:16548883}. 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; X63526; CAA45089.1; -; mRNA. DR EMBL; Z11531; CAA77630.1; -; mRNA. DR EMBL; AK300203; BAG61974.1; -; mRNA. DR EMBL; AP001363; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AP002990; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC000384; AAH00384.1; -; mRNA. DR EMBL; BC006509; AAH06509.1; -; mRNA. DR EMBL; BC006520; AAH06520.1; -; mRNA. DR EMBL; BC007949; AAH07949.2; -; mRNA. DR EMBL; BC009865; AAH09865.1; -; mRNA. DR EMBL; BC013918; AAH13918.1; -; mRNA. DR EMBL; BC015813; AAH15813.1; -; mRNA. DR EMBL; BC021974; AAH21974.2; -; mRNA. DR EMBL; BC028179; AAH28179.1; -; mRNA. DR EMBL; BC031012; AAH31012.1; -; mRNA. DR EMBL; BC067738; AAH67738.1; -; mRNA. DR EMBL; M55409; AAC18414.1; -; mRNA. DR EMBL; AF119850; AAF69604.1; -; mRNA. DR CCDS; CCDS44626.1; -. [P26641-1] DR PIR; S22655; S22655. DR RefSeq; NP_001395.1; NM_001404.4. [P26641-1] DR PDB; 1PBU; NMR; -; A=276-437. DR PDB; 5DQS; X-ray; 2.10 A; A=2-218. DR PDB; 5JPO; X-ray; 2.00 A; A/B/C/D=1-218. DR PDBsum; 1PBU; -. DR PDBsum; 5DQS; -. DR PDBsum; 5JPO; -. DR AlphaFoldDB; P26641; -. DR BMRB; P26641; -. DR SMR; P26641; -. DR BioGRID; 108257; 388. DR CORUM; P26641; -. DR DIP; DIP-32516N; -. DR IntAct; P26641; 220. DR MINT; P26641; -. DR STRING; 9606.ENSP00000331901; -. DR ChEMBL; CHEMBL4295735; -. DR GlyGen; P26641; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P26641; -. DR MetOSite; P26641; -. DR PhosphoSitePlus; P26641; -. DR SwissPalm; P26641; -. DR BioMuta; EEF1G; -. DR DMDM; 119165; -. DR OGP; P26641; -. DR EPD; P26641; -. DR jPOST; P26641; -. DR MassIVE; P26641; -. DR MaxQB; P26641; -. DR PaxDb; P26641; -. DR PeptideAtlas; P26641; -. DR ProteomicsDB; 5107; -. DR ProteomicsDB; 54359; -. [P26641-1] DR TopDownProteomics; P26641-1; -. [P26641-1] DR Antibodypedia; 52234; 377 antibodies from 29 providers. DR DNASU; 1937; -. DR Ensembl; ENST00000329251.5; ENSP00000331901.4; ENSG00000254772.10. [P26641-1] DR GeneID; 1937; -. DR KEGG; hsa:1937; -. DR MANE-Select; ENST00000329251.5; ENSP00000331901.4; NM_001404.5; NP_001395.1. DR CTD; 1937; -. DR DisGeNET; 1937; -. DR GeneCards; EEF1G; -. DR HGNC; HGNC:3213; EEF1G. DR HPA; ENSG00000254772; Low tissue specificity. DR MIM; 130593; gene. DR neXtProt; NX_P26641; -. DR OpenTargets; ENSG00000254772; -. DR PharmGKB; PA27649; -. DR VEuPathDB; HostDB:ENSG00000254772; -. DR eggNOG; KOG0867; Eukaryota. DR eggNOG; KOG1627; Eukaryota. DR GeneTree; ENSGT00390000007552; -. DR HOGENOM; CLU_011226_3_1_1; -. DR InParanoid; P26641; -. DR OMA; TRWYETI; -. DR PhylomeDB; P26641; -. DR TreeFam; TF314343; -. DR PathwayCommons; P26641; -. DR Reactome; R-HSA-156842; Eukaryotic Translation Elongation. DR Reactome; R-HSA-9725370; Signaling by ALK fusions and activated point mutants. DR SignaLink; P26641; -. DR SIGNOR; P26641; -. DR BioGRID-ORCS; 1937; 565 hits in 1084 CRISPR screens. DR ChiTaRS; EEF1G; human. DR EvolutionaryTrace; P26641; -. DR GeneWiki; EEF1G; -. DR GenomeRNAi; 1937; -. DR Pharos; P26641; Tbio. DR PRO; PR:P26641; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; P26641; protein. DR Bgee; ENSG00000254772; Expressed in cortical plate and 101 other tissues. DR ExpressionAtlas; P26641; baseline and differential. DR Genevisible; P26641; HS. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005634; C:nucleus; HDA:UniProtKB. DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL. DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW. DR GO; GO:0009615; P:response to virus; IEP:UniProtKB. DR GO; GO:0006414; P:translational elongation; IBA:GO_Central. DR Gene3D; 3.30.70.1010; -; 1. DR InterPro; IPR001662; EF1B_G_C. DR InterPro; IPR036433; EF1B_G_C_sf. DR InterPro; IPR010987; Glutathione-S-Trfase_C-like. DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf. DR InterPro; IPR040079; Glutathione_S-Trfase. DR InterPro; IPR004045; Glutathione_S-Trfase_N. DR InterPro; IPR004046; GST_C. DR InterPro; IPR036249; Thioredoxin-like_sf. DR Pfam; PF00647; EF1G; 1. DR Pfam; PF00043; GST_C; 1. DR Pfam; PF02798; GST_N; 1. DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1. DR SMART; SM01183; EF1G; 1. DR SUPFAM; SSF89942; eEF1-gamma domain; 1. DR SUPFAM; SSF47616; GST C-terminal domain-like; 1. DR SUPFAM; SSF52833; Thioredoxin-like; 1. DR PROSITE; PS50040; EF1G_C; 1. DR PROSITE; PS50405; GST_CTER; 1. DR PROSITE; PS50404; GST_NTER; 1. DR AGR; HGNC:3213; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing; KW Elongation factor; Isopeptide bond; Protein biosynthesis; KW Reference proteome; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:12665801, ECO:0000269|Ref.7, FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, FT ECO:0007744|PubMed:22814378" FT CHAIN 2..437 FT /note="Elongation factor 1-gamma" FT /id="PRO_0000208813" FT DOMAIN 2..87 FT /note="GST N-terminal" FT DOMAIN 88..216 FT /note="GST C-terminal" FT DOMAIN 276..437 FT /note="EF-1-gamma C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00519" FT REGION 221..268 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 221..260 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378" FT MOD_RES 147 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 212 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9D8N0" FT MOD_RES 401 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q9D8N0" FT MOD_RES 434 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 434 FT /note="N6-malonyllysine; alternate" FT /evidence="ECO:0000269|PubMed:21908771" FT CROSSLNK 253 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1)" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 285 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..4 FT /note="MAAG -> MAERWVAPAVLRRARFASTFFLSPQIYAHKDGDLRSAFFILSFK FT RGEFIPFLNW (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056204" FT CONFLICT 102 FT /note="A -> V (in Ref. 5; AAH13918)" FT /evidence="ECO:0000305" FT STRAND 3..7 FT /evidence="ECO:0007829|PDB:5JPO" FT HELIX 13..25 FT /evidence="ECO:0007829|PDB:5JPO" FT STRAND 28..32 FT /evidence="ECO:0007829|PDB:5JPO" FT TURN 35..37 FT /evidence="ECO:0007829|PDB:5JPO" FT TURN 40..42 FT /evidence="ECO:0007829|PDB:5JPO" FT HELIX 43..45 FT /evidence="ECO:0007829|PDB:5JPO" FT HELIX 47..52 FT /evidence="ECO:0007829|PDB:5JPO" FT STRAND 58..63 FT /evidence="ECO:0007829|PDB:5JPO" FT HELIX 72..78 FT /evidence="ECO:0007829|PDB:5JPO" FT HELIX 82..85 FT /evidence="ECO:0007829|PDB:5JPO" FT HELIX 89..105 FT /evidence="ECO:0007829|PDB:5JPO" FT HELIX 107..117 FT /evidence="ECO:0007829|PDB:5JPO" FT HELIX 125..145 FT /evidence="ECO:0007829|PDB:5JPO" FT TURN 146..148 FT /evidence="ECO:0007829|PDB:5JPO" FT STRAND 150..153 FT /evidence="ECO:0007829|PDB:5JPO" FT HELIX 159..174 FT /evidence="ECO:0007829|PDB:5JPO" FT HELIX 178..181 FT /evidence="ECO:0007829|PDB:5JPO" FT HELIX 185..195 FT /evidence="ECO:0007829|PDB:5JPO" FT HELIX 198..204 FT /evidence="ECO:0007829|PDB:5JPO" FT HELIX 279..281 FT /evidence="ECO:0007829|PDB:1PBU" FT HELIX 290..299 FT /evidence="ECO:0007829|PDB:1PBU" FT HELIX 302..304 FT /evidence="ECO:0007829|PDB:1PBU" FT HELIX 306..311 FT /evidence="ECO:0007829|PDB:1PBU" FT TURN 316..318 FT /evidence="ECO:0007829|PDB:1PBU" FT STRAND 320..324 FT /evidence="ECO:0007829|PDB:1PBU" FT HELIX 329..331 FT /evidence="ECO:0007829|PDB:1PBU" FT HELIX 338..348 FT /evidence="ECO:0007829|PDB:1PBU" FT HELIX 349..351 FT /evidence="ECO:0007829|PDB:1PBU" FT HELIX 353..355 FT /evidence="ECO:0007829|PDB:1PBU" FT STRAND 356..358 FT /evidence="ECO:0007829|PDB:1PBU" FT STRAND 361..364 FT /evidence="ECO:0007829|PDB:1PBU" FT STRAND 370..381 FT /evidence="ECO:0007829|PDB:1PBU" FT HELIX 384..386 FT /evidence="ECO:0007829|PDB:1PBU" FT HELIX 388..390 FT /evidence="ECO:0007829|PDB:1PBU" FT HELIX 394..396 FT /evidence="ECO:0007829|PDB:1PBU" FT HELIX 408..418 FT /evidence="ECO:0007829|PDB:1PBU" FT TURN 424..426 FT /evidence="ECO:0007829|PDB:1PBU" SQ SEQUENCE 437 AA; 50119 MW; A6110663110CF3FC CRC64; MAAGTLYTYP ENWRAFKALI AAQYSGAQVR VLSAPPHFHF GQTNRTPEFL RKFPAGKVPA FEGDDGFCVF ESNAIAYYVS NEELRGSTPE AAAQVVQWVS FADSDIVPPA STWVFPTLGI MHHNKQATEN AKEEVRRILG LLDAYLKTRT FLVGERVTLA DITVVCTLLW LYKQVLEPSF RQAFPNTNRW FLTCINQPQF RAVLGEVKLC EKMAQFDAKK FAETQPKKDT PRKEKGSREE KQKPQAERKE EKKAAAPAPE EEMDECEQAL AAEPKAKDPF AHLPKSTFVL DEFKRKYSNE DTLSVALPYF WEHFDKDGWS LWYSEYRFPE ELTQTFMSCN LITGMFQRLD KLRKNAFASV ILFGTNNSSS ISGVWVFRGQ ELAFPLSPDW QVDYESYTWR KLDPGSEETQ TLVREYFSWE GAFQHVGKAF NQGKIFK // ID MARE2_HUMAN Reviewed; 327 AA. AC Q15555; B2RE21; B3KR39; B4DJV4; B7Z2L3; E9PHR3; F5H1V8; G5E9I6; Q9UQ33; DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 14-DEC-2022, entry version 193. DE RecName: Full=Microtubule-associated protein RP/EB family member 2; DE AltName: Full=APC-binding protein EB2; DE AltName: Full=End-binding protein 2; DE Short=EB2; GN Name=MAPRE2; Synonyms=RP1; 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), INDUCTION, TISSUE SPECIFICITY, AND RP INTERACTION WITH APC. RX PubMed=9233623; RA Renner C., Pfitzenmeier J.-P., Gerlach K., Held G., Ohnesorge S., Sahin U., RA Bauer S., Pfreundschuh M.; RT "RP1, a new member of the adenomatous polyposis coli-binding EB1-like gene RT family, is differentially expressed in activated T cells."; RL J. Immunol. 159:1276-1283(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Brain; RA Oishi N.; RT "RP1, a member of the APC-binding EB1 family, alternative form."; RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases. RN [3] 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 (OCT-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3; 4 AND 5). RC TISSUE=Amygdala, Brain, and Trachea; 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 GENOMIC DNA]. RX PubMed=16177791; DOI=10.1038/nature03983; RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J., RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.; RT "DNA sequence and analysis of human chromosome 18."; RL Nature 437:551-555(2005). RN [7] 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [9] RP INTERACTION WITH TUBULIN, AND SUBCELLULAR LOCATION. RX PubMed=10188731; RX DOI=10.1002/(sici)1097-0215(19990412)81:2<275::aid-ijc18>3.0.co;2-z; RA Juwana J.-P., Henderikx P., Mischo A., Wadle A., Fadle N., Gerlach K., RA Arends J.W., Hoogenboom H., Pfreundschuh M., Renner C.; RT "EB/RP gene family encodes tubulin binding proteins."; RL Int. J. Cancer 81:275-284(1999). RN [10] RP CHARACTERIZATION, AND INTERACTION WITH TUBULIN; APC AND DCTN1. RX PubMed=14514668; DOI=10.1074/jbc.m306194200; RA Bu W., Su L.-K.; RT "Characterization of functional domains of human EB1 family proteins."; RL J. Biol. Chem. 278:49721-49731(2003). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-167, 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 [12] RP IDENTIFICATION BY 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 [13] 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, AND IDENTIFICATION BY RP 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 [15] 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 [16] 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 [17] 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 [18] RP INTERACTION WITH SLAIN1. RX PubMed=21646404; DOI=10.1083/jcb.201012179; RA van der Vaart B., Manatschal C., Grigoriev I., Olieric V., Gouveia S.M., RA Bjelic S., Demmers J., Vorobjev I., Hoogenraad C.C., Steinmetz M.O., RA Akhmanova A.; RT "SLAIN2 links microtubule plus end-tracking proteins and controls RT microtubule growth in interphase."; RL J. Cell Biol. 193:1083-1099(2011). RN [19] 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 [20] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORM 5), CLEAVAGE OF RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 5), AND IDENTIFICATION RP 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 [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY MASS RP 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 [22] RP INVOLVEMENT IN CSCSC2, VARIANTS CSCSC2 SER-68; CYS-87 AND CYS-143, RP CHARACTERIZATION OF VARIANTS CSCSC2 SER-68; CYS-87 AND CYS-143, AND RP INTERACTION WITH TUBULIN. RX PubMed=26637975; DOI=10.1016/j.ajhg.2015.10.014; RA Isrie M., Breuss M., Tian G., Hansen A.H., Cristofoli F., Morandell J., RA Kupchinsky Z.A., Sifrim A., Rodriguez-Rodriguez C.M., Dapena E.P., RA Doonanco K., Leonard N., Tinsa F., Moortgat S., Ulucan H., Koparir E., RA Karaca E., Katsanis N., Marton V., Vermeesch J.R., Davis E.E., Cowan N.J., RA Keays D.A., Van Esch H.; RT "Mutations in Either TUBB or MAPRE2 Cause Circumferential Skin Creases RT Kunze Type."; RL Am. J. Hum. Genet. 97:790-800(2015). CC -!- FUNCTION: May be involved in microtubule polymerization, and spindle CC function by stabilizing microtubules and anchoring them at centrosomes. CC May play a role in cell migration (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Interacts with DCTN1 (PubMed:14514668). Interacts with APC CC (via C-terminal) (PubMed:9233623, PubMed:14514668). Interacts with CC monomeric and polymerized tubulin (PubMed:10188731, PubMed:14514668, CC PubMed:26637975). Interacts with SLAIN1 (PubMed:21646404). CC {ECO:0000269|PubMed:10188731, ECO:0000269|PubMed:14514668, CC ECO:0000269|PubMed:21646404, ECO:0000269|PubMed:26637975, CC ECO:0000269|PubMed:9233623}. CC -!- INTERACTION: CC Q15555; Q9NQ79: CRTAC1; NbExp=7; IntAct=EBI-739717, EBI-10205543; CC Q15555; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-739717, EBI-742054; CC Q15555; Q8NHY3: GAS2L2; NbExp=3; IntAct=EBI-739717, EBI-7960826; CC Q15555; P25791: LMO2; NbExp=5; IntAct=EBI-739717, EBI-739696; CC Q15555; P25791-3: LMO2; NbExp=7; IntAct=EBI-739717, EBI-11959475; CC Q15555; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-739717, EBI-739832; CC Q15555; Q15691: MAPRE1; NbExp=8; IntAct=EBI-739717, EBI-1004115; CC Q15555; Q15555: MAPRE2; NbExp=5; IntAct=EBI-739717, EBI-739717; CC Q15555; Q9UPY8: MAPRE3; NbExp=7; IntAct=EBI-739717, EBI-726739; CC Q15555; Q6ZW49-2: PAXIP1; NbExp=3; IntAct=EBI-739717, EBI-10236271; CC Q15555; P78332-2: RBM6; NbExp=3; IntAct=EBI-739717, EBI-14150298; CC Q15555; Q13077: TRAF1; NbExp=9; IntAct=EBI-739717, EBI-359224; CC Q15555; Q9BWF2: TRAIP; NbExp=10; IntAct=EBI-739717, EBI-1756205; CC Q15555; Q99757: TXN2; NbExp=6; IntAct=EBI-739717, EBI-2932492; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton CC {ECO:0000269|PubMed:10188731}. Note=Associated with the microtubule CC network. Accumulates at the plus end of microtubules. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=Q15555-1; Sequence=Displayed; CC Name=2; CC IsoId=Q15555-2; Sequence=VSP_012944, VSP_012945; CC Name=3; CC IsoId=Q15555-3; Sequence=VSP_045710; CC Name=5; CC IsoId=Q15555-5; Sequence=VSP_055671; CC Name=4; CC IsoId=Q15555-4; Sequence=VSP_046041; CC -!- TISSUE SPECIFICITY: Expressed in different tumor cell lines. Up- CC regulated in activated B- and T-lymphocytes. CC {ECO:0000269|PubMed:9233623}. CC -!- DOMAIN: Composed of two functionally independent domains. The N- CC terminal domain forms a hydrophobic cleft involved in microtubule CC binding and the C-terminal is involved in the formation of mutually CC exclusive complexes with APC and DCTN1. CC -!- DISEASE: Skin creases, congenital symmetric circumferential, 2 (CSCSC2) CC [MIM:616734]: An autosomal dominant disease characterized by multiple, CC symmetric, circumferential rings of folded skin, affecting primarily CC the limbs. Affected individuals also exhibit intellectual disability, CC cleft palate, and dysmorphic features. {ECO:0000269|PubMed:26637975}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- SIMILARITY: Belongs to the MAPRE family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA83375.1; Type=Erroneous initiation; Note=Truncated N-terminus.; 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; X94232; CAA63923.1; -; mRNA. DR EMBL; AB016823; BAA83375.1; ALT_INIT; mRNA. DR EMBL; CR536545; CAG38782.1; -; mRNA. DR EMBL; BT020086; AAV38889.1; -; mRNA. DR EMBL; AK090945; BAG52251.1; -; mRNA. DR EMBL; AK296251; BAG58966.1; -; mRNA. DR EMBL; AK294833; BAH11899.1; -; mRNA. DR EMBL; AK315766; BAG38118.1; -; mRNA. DR EMBL; AC009277; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC015967; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471088; EAX01336.1; -; Genomic_DNA. DR EMBL; CH471088; EAX01338.1; -; Genomic_DNA. DR EMBL; BC007318; AAH07318.1; -; mRNA. DR CCDS; CCDS11910.1; -. [Q15555-1] DR CCDS; CCDS45850.1; -. [Q15555-3] DR CCDS; CCDS45851.1; -. [Q15555-5] DR CCDS; CCDS58619.1; -. [Q15555-4] DR PIR; G01037; G01037. DR RefSeq; NP_001137298.1; NM_001143826.2. [Q15555-5] DR RefSeq; NP_001137299.1; NM_001143827.2. [Q15555-3] DR RefSeq; NP_001243349.1; NM_001256420.1. [Q15555-4] DR RefSeq; NP_055083.1; NM_014268.3. [Q15555-1] DR AlphaFoldDB; Q15555; -. DR SMR; Q15555; -. DR BioGRID; 116178; 112. DR IntAct; Q15555; 37. DR MINT; Q15555; -. DR STRING; 9606.ENSP00000300249; -. DR Allergome; 8363; Hom s RP1. DR GlyGen; Q15555; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q15555; -. DR PhosphoSitePlus; Q15555; -. DR BioMuta; MAPRE2; -. DR DMDM; 60390165; -. DR OGP; Q15555; -. DR EPD; Q15555; -. DR jPOST; Q15555; -. DR MassIVE; Q15555; -. DR MaxQB; Q15555; -. DR PaxDb; Q15555; -. DR PeptideAtlas; Q15555; -. DR ProteomicsDB; 20585; -. DR ProteomicsDB; 25777; -. DR ProteomicsDB; 33949; -. DR ProteomicsDB; 60631; -. [Q15555-1] DR ProteomicsDB; 60632; -. [Q15555-2] DR Antibodypedia; 8544; 429 antibodies from 30 providers. DR DNASU; 10982; -. DR Ensembl; ENST00000300249.10; ENSP00000300249.4; ENSG00000166974.13. [Q15555-1] DR Ensembl; ENST00000413393.5; ENSP00000396074.1; ENSG00000166974.13. [Q15555-5] DR Ensembl; ENST00000436190.6; ENSP00000407723.1; ENSG00000166974.13. [Q15555-3] DR Ensembl; ENST00000538170.6; ENSP00000446343.1; ENSG00000166974.13. [Q15555-4] DR Ensembl; ENST00000588910.5; ENSP00000468588.1; ENSG00000166974.13. [Q15555-2] DR Ensembl; ENST00000589699.1; ENSP00000464921.1; ENSG00000166974.13. [Q15555-5] DR GeneID; 10982; -. DR KEGG; hsa:10982; -. DR MANE-Select; ENST00000300249.10; ENSP00000300249.4; NM_014268.4; NP_055083.1. DR UCSC; uc002kyf.3; human. [Q15555-1] DR CTD; 10982; -. DR DisGeNET; 10982; -. DR GeneCards; MAPRE2; -. DR HGNC; HGNC:6891; MAPRE2. DR HPA; ENSG00000166974; Low tissue specificity. DR MalaCards; MAPRE2; -. DR MIM; 605789; gene. DR MIM; 616734; phenotype. DR neXtProt; NX_Q15555; -. DR OpenTargets; ENSG00000166974; -. DR Orphanet; 2505; Multiple benign circumferential skin creases on limbs. DR PharmGKB; PA30635; -. DR VEuPathDB; HostDB:ENSG00000166974; -. DR eggNOG; KOG3000; Eukaryota. DR GeneTree; ENSGT00490000043329; -. DR HOGENOM; CLU_041744_1_0_1; -. DR InParanoid; Q15555; -. DR OMA; EQCGTGG; -. DR PhylomeDB; Q15555; -. DR TreeFam; TF313620; -. DR PathwayCommons; Q15555; -. DR SignaLink; Q15555; -. DR BioGRID-ORCS; 10982; 8 hits in 1079 CRISPR screens. DR ChiTaRS; MAPRE2; human. DR GeneWiki; MAPRE2; -. DR GenomeRNAi; 10982; -. DR Pharos; Q15555; Tbio. DR PRO; PR:Q15555; -. DR Proteomes; UP000005640; Chromosome 18. DR RNAct; Q15555; protein. DR Bgee; ENSG00000166974; Expressed in cortical plate and 211 other tissues. DR ExpressionAtlas; Q15555; baseline and differential. DR Genevisible; Q15555; HS. DR GO; GO:0005737; C:cytoplasm; HDA:UniProtKB. DR GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central. DR GO; GO:0005925; C:focal adhesion; IDA:ARUK-UCL. DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:LIFEdb. DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central. DR GO; GO:0035371; C:microtubule plus-end; IBA:GO_Central. DR GO; GO:0051233; C:spindle midzone; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0008017; F:microtubule binding; IDA:ARUK-UCL. DR GO; GO:0051010; F:microtubule plus-end binding; IBA:GO_Central. DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0032014; P:positive regulation of ARF protein signal transduction; ISS:ARUK-UCL. DR GO; GO:0120183; P:positive regulation of focal adhesion disassembly; ISS:ARUK-UCL. DR GO; GO:0043547; P:positive regulation of GTPase activity; ISS:ARUK-UCL. DR GO; GO:0051549; P:positive regulation of keratinocyte migration; ISS:ARUK-UCL. DR GO; GO:1904825; P:protein localization to microtubule plus-end; IBA:GO_Central. DR GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; IBA:GO_Central. DR GO; GO:0051225; P:spindle assembly; IBA:GO_Central. DR Gene3D; 1.10.418.10; -; 1. DR InterPro; IPR001715; CH-domain. DR InterPro; IPR036872; CH_dom_sf. DR InterPro; IPR004953; EB1_C. DR InterPro; IPR036133; EB1_C_sf. DR InterPro; IPR027328; MAPRE. DR InterPro; IPR027735; RP1/EB2_vertebrate. DR PANTHER; PTHR10623; MICROTUBULE-ASSOCIATED PROTEIN RP/EB FAMILY MEMBER; 1. DR PANTHER; PTHR10623:SF7; MICROTUBULE-ASSOCIATED PROTEIN RP/EB FAMILY MEMBER 2; 1. DR Pfam; PF00307; CH; 1. DR Pfam; PF03271; EB1; 1. DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1. DR SUPFAM; SSF140612; EB1 dimerisation domain-like; 1. DR PROSITE; PS50021; CH; 1. DR PROSITE; PS51230; EB1_C; 1. DR AGR; HGNC:6891; -. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Cell cycle; Cell division; Cytoplasm; KW Cytoskeleton; Microtubule; Mitosis; Phosphoprotein; Reference proteome. FT CHAIN 1..327 FT /note="Microtubule-associated protein RP/EB family member FT 2" FT /id="PRO_0000213424" FT DOMAIN 57..159 FT /note="Calponin-homology (CH)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044" FT DOMAIN 236..306 FT /note="EB1 C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00576" FT REGION 1..21 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 171..240 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 187..327 FT /note="DCTN1-binding" FT REGION 259..302 FT /note="APC-binding" FT REGION 299..327 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 193..240 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 9 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 167 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:15592455" FT MOD_RES 219 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT VAR_SEQ 1..83 FT /note="MPGPTQTLSPNGENNNDIIQDNNGTIIPFRKHTVRGERSYSWGMAVNVYSTS FT ITQETMSRHDIIAWVNDIVSLNYTKVEQLCS -> MARTTTTSSRIITGPSFLSGSTQC FT AGSVPT (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046041" FT VAR_SEQ 1..43 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055671" FT VAR_SEQ 1..40 FT /note="MPGPTQTLSPNGENNNDIIQDNNGTIIPFRKHTVRGERSY -> MKQNRDQK FT CPVSQRNSSFQQPGRKPGCS (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045710" FT VAR_SEQ 252..259 FT /note="HSLKLALE -> MHQLWPRL (in isoform 2)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_012944" FT VAR_SEQ 260..327 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_012945" FT VARIANT 68 FT /note="N -> S (in CSCSC2; enhances binding to microtubules; FT dbSNP:rs864309719)" FT /evidence="ECO:0000269|PubMed:26637975" FT /id="VAR_076540" FT VARIANT 87 FT /note="Y -> C (in CSCSC2; enhances binding to microtubules; FT dbSNP:rs864309717)" FT /evidence="ECO:0000269|PubMed:26637975" FT /id="VAR_076541" FT VARIANT 143 FT /note="R -> C (in CSCSC2; enhances binding to microtubules; FT dbSNP:rs864309720)" FT /evidence="ECO:0000269|PubMed:26637975" FT /id="VAR_076542" FT VARIANT 162 FT /note="Y -> C (in dbSNP:rs11538993)" FT /id="VAR_050018" FT CONFLICT 65 FT /note="A -> G (in Ref. 8; BAA83375)" FT /evidence="ECO:0000305" FT CONFLICT 100 FT /note="S -> N (in Ref. 5; BAG58966)" FT /evidence="ECO:0000305" FT CONFLICT 128 FT /note="M -> K (in Ref. 5; BAG58966)" FT /evidence="ECO:0000305" FT CONFLICT 209 FT /note="S -> G (in Ref. 5; BAG52251)" FT /evidence="ECO:0000305" FT CONFLICT 235 FT /note="K -> I (in Ref. 5; BAH11899)" FT /evidence="ECO:0000305" FT INIT_MET Q15555-5:1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES Q15555-5:2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:22814378" SQ SEQUENCE 327 AA; 37031 MW; 2BE99E9F9EFA83C3 CRC64; MPGPTQTLSP NGENNNDIIQ DNNGTIIPFR KHTVRGERSY SWGMAVNVYS TSITQETMSR HDIIAWVNDI VSLNYTKVEQ LCSGAAYCQF MDMLFPGCIS LKKVKFQAKL EHEYIHNFKL LQASFKRMNV DKVIPVEKLV KGRFQDNLDF IQWFKKFYDA NYDGKEYDPV EARQGQDAIP PPDPGEQIFN LPKKSHHANS PTAGAAKSSP AAKPGSTPSR PSSAKRASSS GSASKSDKDL ETQVIQLNEQ VHSLKLALEG VEKERDFYFG KLREIELLCQ EHGQENDDLV QRLMDILYAS EEHEGHTEEP EAEEQAHEQQ PPQQEEY // ID F168B_HUMAN Reviewed; 195 AA. AC A1KXE4; Q2TAZ6; Q6NZ40; DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot. DT 20-FEB-2007, sequence version 1. DT 14-DEC-2022, entry version 110. DE RecName: Full=Myelin-associated neurite-outgrowth inhibitor; DE Short=Mani; DE AltName: Full=p20; GN Name=FAM168B; Synonyms=KIAA0280L, MANI; 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), HOMODIMERIZATION, INTERACTION WITH RP CDC27; PRDX6 AND RBM6, AND TISSUE SPECIFICITY. RX PubMed=20716133; DOI=10.1111/j.1582-4934.2010.01134.x; RA Mishra M., Akatsu H., Heese K.; RT "The novel protein MANI modulates neurogenesis and neurite-cone growth."; RL J. Cell. Mol. Med. 15:1713-1725(2011). RN [2] 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Brain, and Eye; 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 [4] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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 [5] RP INTERACTION WITH DAZAP2; FAM168A; TMTC1 AND YPEL2. RX PubMed=22771904; DOI=10.1016/j.febslet.2012.06.043; RA Mishra M., Lee S., Lin M.K., Yamashita T., Heese K.; RT "Characterizing the neurite outgrowth inhibitory effect of Mani."; RL FEBS Lett. 586:3018-3023(2012). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND IDENTIFICATION BY MASS RP 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). CC -!- FUNCTION: Inhibitor of neuronal axonal outgrowth. Acts as a negative CC regulator of CDC42 and STAT3 and a positive regulator of STMN2. CC Positive regulator of CDC27. {ECO:0000250|UniProtKB:D4AEP3}. CC -!- SUBUNIT: May form homodimers. May interact with DAZAP2, FAM168A, PRDX6, CC RBM6, TMTC1 and YPEL2. Interacts with CDC27. CC {ECO:0000269|PubMed:20716133, ECO:0000269|PubMed:22771904}. CC -!- INTERACTION: CC A1KXE4-2; P21549: AGXT; NbExp=3; IntAct=EBI-12193763, EBI-727098; CC A1KXE4-2; Q03989: ARID5A; NbExp=3; IntAct=EBI-12193763, EBI-948603; CC A1KXE4-2; O95817: BAG3; NbExp=3; IntAct=EBI-12193763, EBI-747185; CC A1KXE4-2; Q9UQM7: CAMK2A; NbExp=3; IntAct=EBI-12193763, EBI-1383687; CC A1KXE4-2; O75909-2: CCNK; NbExp=3; IntAct=EBI-12193763, EBI-12010594; CC A1KXE4-2; P33240: CSTF2; NbExp=3; IntAct=EBI-12193763, EBI-711360; CC A1KXE4-2; Q9H0L4: CSTF2T; NbExp=3; IntAct=EBI-12193763, EBI-747012; CC A1KXE4-2; Q9H6Z9: EGLN3; NbExp=3; IntAct=EBI-12193763, EBI-1175354; CC A1KXE4-2; Q92567-2: FAM168A; NbExp=3; IntAct=EBI-12193763, EBI-11978259; CC A1KXE4-2; Q8WU58: FAM222B; NbExp=3; IntAct=EBI-12193763, EBI-2807642; CC A1KXE4-2; P22607: FGFR3; NbExp=3; IntAct=EBI-12193763, EBI-348399; CC A1KXE4-2; O75593: FOXH1; NbExp=3; IntAct=EBI-12193763, EBI-1759806; CC A1KXE4-2; Q12951-2: FOXI1; NbExp=3; IntAct=EBI-12193763, EBI-12018822; CC A1KXE4-2; Q9BZE0: GLIS2; NbExp=3; IntAct=EBI-12193763, EBI-7251368; CC A1KXE4-2; Q13227: GPS2; NbExp=3; IntAct=EBI-12193763, EBI-713355; CC A1KXE4-2; P17482: HOXB9; NbExp=3; IntAct=EBI-12193763, EBI-745290; CC A1KXE4-2; Q9ULV5-2: HSF4; NbExp=3; IntAct=EBI-12193763, EBI-12056251; CC A1KXE4-2; O14901: KLF11; NbExp=3; IntAct=EBI-12193763, EBI-948266; CC A1KXE4-2; Q6PEX3: KRTAP26-1; NbExp=3; IntAct=EBI-12193763, EBI-3957672; CC A1KXE4-2; Q14847-2: LASP1; NbExp=3; IntAct=EBI-12193763, EBI-9088686; CC A1KXE4-2; Q71SY5: MED25; NbExp=3; IntAct=EBI-12193763, EBI-394558; CC A1KXE4-2; Q8IXL7-2: MSRB3; NbExp=3; IntAct=EBI-12193763, EBI-10699187; CC A1KXE4-2; Q8TDC0: MYOZ3; NbExp=3; IntAct=EBI-12193763, EBI-5662487; CC A1KXE4-2; Q14511-2: NEDD9; NbExp=3; IntAct=EBI-12193763, EBI-11746523; CC A1KXE4-2; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-12193763, EBI-2811583; CC A1KXE4-2; P32242: OTX1; NbExp=3; IntAct=EBI-12193763, EBI-740446; CC A1KXE4-2; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-12193763, EBI-11022007; CC A1KXE4-2; P78337: PITX1; NbExp=3; IntAct=EBI-12193763, EBI-748265; CC A1KXE4-2; Q7Z3K3: POGZ; NbExp=3; IntAct=EBI-12193763, EBI-1389308; CC A1KXE4-2; Q96HA1-2: POM121; NbExp=3; IntAct=EBI-12193763, EBI-11956563; CC A1KXE4-2; Q7Z5V6-2: PPP1R32; NbExp=3; IntAct=EBI-12193763, EBI-12000762; CC A1KXE4-2; P0CG20: PRR35; NbExp=3; IntAct=EBI-12193763, EBI-11986293; CC A1KXE4-2; Q9BTL3: RAMAC; NbExp=3; IntAct=EBI-12193763, EBI-744023; CC A1KXE4-2; O43251-10: RBFOX2; NbExp=3; IntAct=EBI-12193763, EBI-11963050; CC A1KXE4-2; Q9BQY4: RHOXF2; NbExp=3; IntAct=EBI-12193763, EBI-372094; CC A1KXE4-2; Q01974: ROR2; NbExp=3; IntAct=EBI-12193763, EBI-6422642; CC A1KXE4-2; Q7Z3H4: SAMD7; NbExp=3; IntAct=EBI-12193763, EBI-12148649; CC A1KXE4-2; P14678-2: SNRPB; NbExp=3; IntAct=EBI-12193763, EBI-372475; CC A1KXE4-2; P09234: SNRPC; NbExp=3; IntAct=EBI-12193763, EBI-766589; CC A1KXE4-2; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-12193763, EBI-11959123; CC A1KXE4-2; Q9NQB0-10: TCF7L2; NbExp=3; IntAct=EBI-12193763, EBI-11746252; CC A1KXE4-2; Q96A09: TENT5B; NbExp=3; IntAct=EBI-12193763, EBI-752030; CC A1KXE4-2; Q01085-2: TIAL1; NbExp=3; IntAct=EBI-12193763, EBI-11064654; CC A1KXE4-2; Q08117-2: TLE5; NbExp=3; IntAct=EBI-12193763, EBI-11741437; CC A1KXE4-2; O43711: TLX3; NbExp=3; IntAct=EBI-12193763, EBI-3939165; CC A1KXE4-2; Q5T6F2: UBAP2; NbExp=3; IntAct=EBI-12193763, EBI-2514383; CC A1KXE4-2; O95231: VENTX; NbExp=3; IntAct=EBI-12193763, EBI-10191303; CC A1KXE4-2; Q14119: VEZF1; NbExp=3; IntAct=EBI-12193763, EBI-11980193; CC A1KXE4-2; A8MV65-2: VGLL3; NbExp=3; IntAct=EBI-12193763, EBI-11957216; CC A1KXE4-2; A5D8V6: VPS37C; NbExp=3; IntAct=EBI-12193763, EBI-2559305; CC A1KXE4-2; Q64LD2-2: WDR25; NbExp=3; IntAct=EBI-12193763, EBI-12032042; CC A1KXE4-2; Q96K80: ZC3H10; NbExp=3; IntAct=EBI-12193763, EBI-742550; CC A1KXE4-2; Q15915: ZIC1; NbExp=3; IntAct=EBI-12193763, EBI-11963196; CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region CC {ECO:0000250|UniProtKB:D4AEP3}. Cell membrane CC {ECO:0000250|UniProtKB:Q80XQ8}; Multi-pass membrane protein CC {ECO:0000250|UniProtKB:Q80XQ8}. Cell projection, axon CC {ECO:0000250|UniProtKB:Q80XQ8}. Note=Expressed in neuronal cell bodies CC and axonal fibers. {ECO:0000250|UniProtKB:Q80XQ8}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=A1KXE4-1; Sequence=Displayed; CC Name=2; CC IsoId=A1KXE4-2; Sequence=VSP_032508; CC -!- TISSUE SPECIFICITY: Expressed in the brain, within neuronal axonal CC fibers and associated with myelin sheets (at protein level). Expression CC tends to be lower in the brain of Alzheimer disease patients compared CC to healthy individuals (at protein level). CC {ECO:0000269|PubMed:20716133}. CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:D4AEP3}. CC -!- SIMILARITY: Belongs to the FAM168 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; AY253283; AAP79599.1; -; mRNA. DR EMBL; CH471250; EAW51267.1; -; Genomic_DNA. DR EMBL; BC066347; AAH66347.1; -; mRNA. DR EMBL; BC110642; AAI10643.1; -; mRNA. DR CCDS; CCDS42755.1; -. [A1KXE4-1] DR RefSeq; NP_001009993.2; NM_001009993.3. [A1KXE4-1] DR RefSeq; NP_001308672.1; NM_001321743.1. [A1KXE4-1] DR RefSeq; NP_001308673.1; NM_001321744.1. [A1KXE4-1] DR RefSeq; NP_001308674.1; NM_001321745.1. [A1KXE4-1] DR RefSeq; NP_001308675.1; NM_001321746.1. [A1KXE4-1] DR RefSeq; NP_001308676.1; NM_001321747.1. [A1KXE4-1] DR RefSeq; NP_001308677.1; NM_001321748.1. [A1KXE4-1] DR RefSeq; XP_016858816.1; XM_017003327.1. [A1KXE4-1] DR AlphaFoldDB; A1KXE4; -. DR BioGRID; 126221; 56. DR IntAct; A1KXE4; 58. DR MINT; A1KXE4; -. DR STRING; 9606.ENSP00000387051; -. DR GlyGen; A1KXE4; 1 site. DR iPTMnet; A1KXE4; -. DR PhosphoSitePlus; A1KXE4; -. DR BioMuta; FAM168B; -. DR EPD; A1KXE4; -. DR jPOST; A1KXE4; -. DR MassIVE; A1KXE4; -. DR MaxQB; A1KXE4; -. DR PaxDb; A1KXE4; -. DR PeptideAtlas; A1KXE4; -. DR ProteomicsDB; 124; -. [A1KXE4-1] DR ProteomicsDB; 125; -. [A1KXE4-2] DR Antibodypedia; 50282; 57 antibodies from 15 providers. DR DNASU; 130074; -. DR Ensembl; ENST00000389915.4; ENSP00000374565.3; ENSG00000152102.18. [A1KXE4-1] DR Ensembl; ENST00000409185.5; ENSP00000387051.1; ENSG00000152102.18. [A1KXE4-1] DR GeneID; 130074; -. DR KEGG; hsa:130074; -. DR MANE-Select; ENST00000389915.4; ENSP00000374565.3; NM_001009993.4; NP_001009993.2. DR UCSC; uc002tsd.4; human. [A1KXE4-1] DR CTD; 130074; -. DR DisGeNET; 130074; -. DR GeneCards; FAM168B; -. DR HGNC; HGNC:27016; FAM168B. DR HPA; ENSG00000152102; Low tissue specificity. DR neXtProt; NX_A1KXE4; -. DR OpenTargets; ENSG00000152102; -. DR PharmGKB; PA162387098; -. DR VEuPathDB; HostDB:ENSG00000152102; -. DR eggNOG; ENOG502QQDS; Eukaryota. DR GeneTree; ENSGT00390000005140; -. DR HOGENOM; CLU_065824_1_0_1; -. DR InParanoid; A1KXE4; -. DR OMA; AMYAPHI; -. DR PhylomeDB; A1KXE4; -. DR TreeFam; TF331128; -. DR PathwayCommons; A1KXE4; -. DR SignaLink; A1KXE4; -. DR BioGRID-ORCS; 130074; 14 hits in 1087 CRISPR screens. DR ChiTaRS; FAM168B; human. DR GenomeRNAi; 130074; -. DR Pharos; A1KXE4; Tdark. DR PRO; PR:A1KXE4; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; A1KXE4; protein. DR Bgee; ENSG00000152102; Expressed in lateral globus pallidus and 210 other tissues. DR ExpressionAtlas; A1KXE4; baseline and differential. DR Genevisible; A1KXE4; HS. DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR029247; FAM168A/MANI. DR PANTHER; PTHR31844; MYELIN-ASSOCIATED NEURITE-OUTGROWTH INHIBITOR-RELATED; 1. DR Pfam; PF14944; TCRP1; 2. DR AGR; HGNC:27016; -. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Cell membrane; Cell projection; KW Cytoplasm; Glycoprotein; Membrane; Phosphoprotein; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1..195 FT /note="Myelin-associated neurite-outgrowth inhibitor" FT /id="PRO_0000325978" FT TOPO_DOM 1..18 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 19..42 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 43..142 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 143..164 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 165..195 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0007744|PubMed:19413330" FT MOD_RES 6 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CARBOHYD 46 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT VAR_SEQ 78..195 FT /note="NPYQTAVYPVRSAYPQQSPYAQQGTYYTQPLYAAPPHVIHHTTVVQPNGMPA FT TVYPAPIPPPRGNGVTMGMVAGTTMAMSAGTLLTAHSPTPVAPHPVTVPTYRAPGTPTY FT SYVPPQW -> QAVPMSPCADQWARQLGQISGQPFVLLAGLLCWPHGEALESLMDCN FT (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_032508" FT CONFLICT 7 FT /note="P -> L (in Ref. 3; AAI10643)" FT /evidence="ECO:0000305" SQ SEQUENCE 195 AA; 20324 MW; 27A0D0D74AB44A10 CRC64; MNPVYSPGSS GVPYANAKGI GYPAGFPMGY AAAAPAYSPN MYPGANPTFQ TGYTPGTPYK VSCSPTSGAV PPYSSSPNPY QTAVYPVRSA YPQQSPYAQQ GTYYTQPLYA APPHVIHHTT VVQPNGMPAT VYPAPIPPPR GNGVTMGMVA GTTMAMSAGT LLTAHSPTPV APHPVTVPTY RAPGTPTYSY VPPQW // ID E9PGM9_HUMAN Unreviewed; 991 AA. AC E9PGM9; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 14-DEC-2022, entry version 91. DE SubName: Full=RNA-binding protein 6 {ECO:0000313|Ensembl:ENSP00000396466.1}; GN Name=RBM6 {ECO:0000313|Ensembl:ENSP00000396466.1}; 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:ENSP00000396466.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {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 [2] {ECO:0000313|Ensembl:ENSP00000396466.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [3] {ECO:0007829|PubMed:17525332} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R., Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [4] {ECO:0007829|PubMed:18691976} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [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:19369195} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(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: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 [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: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:25218447} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [13] {ECO:0007829|PubMed:25772364} RP IDENTIFICATION BY MASS 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 [14] {ECO:0007829|PubMed:25755297} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.O114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurethsson 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 [15] {ECO:0007829|PubMed:28112733} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; 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 [16] {ECO:0000313|Ensembl:ENSP00000396466.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-2022) to UniProtKB. 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; AC104450; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC105935; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; XP_005264841.1; XM_005264784.1. DR RefSeq; XP_006712979.1; XM_006712916.1. DR AlphaFoldDB; E9PGM9; -. DR IntAct; E9PGM9; 1. DR MINT; E9PGM9; -. DR EPD; E9PGM9; -. DR MaxQB; E9PGM9; -. DR PeptideAtlas; E9PGM9; -. DR ProteomicsDB; 20352; -. DR Antibodypedia; 13824; 188 antibodies from 26 providers. DR DNASU; 10180; -. DR Ensembl; ENST00000443081.5; ENSP00000396466.1; ENSG00000004534.15. DR GeneID; 10180; -. DR UCSC; uc062jzp.1; human. DR CTD; 10180; -. DR HGNC; HGNC:9903; RBM6. DR VEuPathDB; HostDB:ENSG00000004534; -. DR GeneTree; ENSGT00940000157976; -. DR BioGRID-ORCS; 10180; 16 hits in 1087 CRISPR screens. DR ChiTaRS; RBM6; human. DR GenomeRNAi; 10180; -. DR Proteomes; UP000005640; Chromosome 3. DR Bgee; ENSG00000004534; Expressed in lower esophagus mucosa and 202 other tissues. DR ExpressionAtlas; E9PGM9; baseline and differential. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule. DR CDD; cd16163; OCRE_RBM6; 1. DR CDD; cd12314; RRM1_RBM6; 1. DR CDD; cd12563; RRM2_RBM6; 1. DR Gene3D; 3.30.70.330; -; 2. DR InterPro; IPR000467; G_patch_dom. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf. DR InterPro; IPR041591; OCRE. DR InterPro; IPR035979; RBD_domain_sf. DR InterPro; IPR028806; RBM6. DR InterPro; IPR035617; RBM6_OCRE. DR InterPro; IPR034123; RBM6_RRM1. DR InterPro; IPR034125; RBM6_RRM2. DR InterPro; IPR000504; RRM_dom. DR PANTHER; PTHR13948:SF22; RNA-BINDING PROTEIN 6; 2. DR Pfam; PF01585; G-patch; 1. DR Pfam; PF17780; OCRE; 1. DR SMART; SM00443; G_patch; 1. DR SMART; SM00360; RRM; 2. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2. DR PROSITE; PS50174; G_PATCH; 1. DR PROSITE; PS50102; RRM; 1. PE 1: Evidence at protein level; KW Proteomics identification {ECO:0007829|EPD:E9PGM9, KW ECO:0007829|MaxQB:E9PGM9}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176}. FT DOMAIN 324..404 FT /note="RRM" FT /evidence="ECO:0000259|PROSITE:PS50102" FT DOMAIN 919..965 FT /note="G-patch" FT /evidence="ECO:0000259|PROSITE:PS50174" FT REGION 1..60 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 89..259 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 281..322 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 442..522 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 609..655 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 695..816 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 872..974 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 109..156 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 174..215 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 222..237 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 299..321 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 442..456 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 462..522 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 610..639 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 640..655 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 695..732 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 740..754 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 802..816 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 872..920 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 991 AA; 113929 MW; 161813C30591FD00 CRC64; MDYRGGDGTS MDYRGREAPH MNYRDRDAHA VDFRGRDAPP SDFRGRGTYD LDFRGRDGSH ADFRGRDLSD LDFRAREQSR SDFRNRDVSD LDFRDKDGTQ VDFRGRGSGT TDLDFRDRDT PHSDFRGRHR SRTDQDFRGR EMGSCMEFKD REMPPVDPNI LDYIQPSTQD REHSGMNVNR REESTHDHTI ERPAFGIQKG EFEHSETREG ETQGVAFEHE SPADFQNSQS PVQDQDKSQL SGREEQSSDA GLFKEEGGLD FLGRQDTDYR SMEYRDVDHR LPGSQMFGYG QSKSFPEGKT ARDAQRDLQD QDYRTGPSEE KPSRLIRLSG VPEDATKEEI LNAFRTPDGM PVKNLQLKEY NTGYDYGYVC VEFSLLEDAI GCMEANQGTL MIQDKEVTLE YVSSLDFWYC KRCKANIGGH RSSCSFCKNP REVTEAKQEL ITYPQPQKTS IPAPLEKQPN QPLRPADKEP EPRKREEGQE SRLGHQKREA ERYLPPSRRE GPTFRRDRER ESWSGETRQD GESKTIMLKR IYRSTPPEVI VEVLEPYVRL TTANVRIIKN RTGPMGHTYG FIDLDSHAEA LRVVKILQNL DPPFSIDGKM VAVNLATGKR RNDSGDHSDH MHYYQGKKYF RDRRGGGRNS DWSSDTNRQG QQSSSDCYIY DSATGYYYDP LAGTYYDPNT QQEVYVPQDP GLPEEEEIKE KKPTSQGKSS SKKEMSKRDG KEKKDRGVTR FQENASEGKA PAEDVFKKPL PPTVKKEESP PPPKVVNPLI GLLGEYGGDS DYEEEEEEEQ TPPPQPRTAQ PQKREEQTKK ENEEDKLTDW NKLACLLCRR QFPNKEVLIK HQQLSDLHKQ NLEIHRKIKQ SEQELAYLER REREGKFKGR GNDRREKLQS FDSPERKRIK YSRETDSDRK LVDKEDIDTS SKGGCVQQAT GWRKGTGLGY GHPGLASSEE AEGRMRGPSV GASGRTSKRQ SNETYRDAVR RVMFARYKEL D // ID A8K6Q4_HUMAN Unreviewed; 1123 AA. AC A8K6Q4; DT 04-DEC-2007, integrated into UniProtKB/TrEMBL. DT 04-DEC-2007, sequence version 1. DT 14-DEC-2022, entry version 83. DE SubName: Full=cDNA FLJ76888, highly similar to Homo sapiens RNA binding motif protein 6 (RBM6), mRNA {ECO:0000313|EMBL:BAF84408.1}; 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|EMBL:BAF84408.1}; RN [1] {ECO:0000313|EMBL:BAF84408.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Placenta {ECO:0000313|EMBL:BAF84408.1}; RA Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A., RA Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y., RA Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T., RA Sugano S., Nomura N., Isogai T.; RT "NEDO human cDNA sequencing project."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. 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; AK291719; BAF84408.1; -; mRNA. DR RefSeq; NP_001161054.1; NM_001167582.1. DR RefSeq; NP_005768.1; NM_005777.2. DR AlphaFoldDB; A8K6Q4; -. DR PeptideAtlas; A8K6Q4; -. DR DNASU; 10180; -. DR GeneID; 10180; -. DR KEGG; hsa:10180; -. DR CTD; 10180; -. DR PharmGKB; PA34268; -. DR OrthoDB; 786674at2759; -. DR BioGRID-ORCS; 10180; 16 hits in 1087 CRISPR screens. DR GenomeRNAi; 10180; -. DR Genevisible; A8K6Q4; HS. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule. DR CDD; cd16163; OCRE_RBM6; 1. DR CDD; cd12314; RRM1_RBM6; 1. DR CDD; cd12563; RRM2_RBM6; 1. DR Gene3D; 3.30.70.330; -; 2. DR InterPro; IPR000467; G_patch_dom. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf. DR InterPro; IPR041591; OCRE. DR InterPro; IPR035979; RBD_domain_sf. DR InterPro; IPR028806; RBM6. DR InterPro; IPR035617; RBM6_OCRE. DR InterPro; IPR034123; RBM6_RRM1. DR InterPro; IPR034125; RBM6_RRM2. DR InterPro; IPR000504; RRM_dom. DR PANTHER; PTHR13948:SF22; RNA-BINDING PROTEIN 6; 3. DR Pfam; PF01585; G-patch; 1. DR Pfam; PF17780; OCRE; 1. DR SMART; SM00443; G_patch; 1. DR SMART; SM00360; RRM; 2. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2. DR PROSITE; PS50174; G_PATCH; 1. DR PROSITE; PS50102; RRM; 1. PE 2: Evidence at transcript level; KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176}. FT DOMAIN 456..536 FT /note="RRM" FT /evidence="ECO:0000259|PROSITE:PS50102" FT DOMAIN 1051..1097 FT /note="G-patch" FT /evidence="ECO:0000259|PROSITE:PS50174" FT REGION 1..391 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 412..454 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 574..654 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 741..787 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 827..948 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1004..1106 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 75..93 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 111..134 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 141..234 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 241..288 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 306..347 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 354..369 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 431..453 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 574..588 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 594..654 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 742..771 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 772..787 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 827..864 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 872..886 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 934..948 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1004..1052 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 1123 AA; 128618 MW; 52DD0C606C9E4C94 CRC64; MWGDSRPANR TGPFRGSQEE RFAPGWNRDY PPPPLKSHAQ ERHSGNFPGR DSLPFDFQGH SGPPFANVEE HSFSYGARDG PHDDYRGGEG PGHDFRGGDF SSSDFQSRDS SQLDFRGRDI HSGDFRDREG PPMDYRGGDG TSMDYRGREA PHMNYRDRDA HAVDFRGRDA PPSDFRGRGT YDLDFRGRDG SHADFRGRDL SDLDFRAREQ SRSDFRNRDV SDLDFRDKDG TQVDFRGRGS GTTDLDFRDR DTPHSDFRGR HRSRTDQDFR GREMGSCMEF KDREMPPVDP NILDYIQPST QDREHSGMNV NRREESTHDH TIERPAFGIQ KGEFEHSETR EGETQGVAFE HESPADFQNS QSPVQDQDKS QLSGREEQSS DAGLFKEEGG LDFLGRQDTD YRSMEYRDVG HRLPGSQMFG YGQSKSFPEG KTARDAQRDL QDQDYRTGPS EEKPSRLIRL SGVPEDATKE EILNAFRTPD GMPVKNLQLK EYNTGYDYGY VCVEFSLLED AIGCMEANQG TLMIQDKEVT LEYVSSLDFW YCKRCKANIG GHRSSCSFCK NPREVTEAKQ ELITYPQPQK TSIPAPLEKQ PNQPLRPADK EPEPRKREEG QESRLGHQKR EAERYLAPSR REGPTFRRDR ERESWSGETR QDGESKTIML KRIYRSTPPE VIVEVLEPYV RLTTANVRII KNRTGPMGHT YGFIDLDSHA EALRVVKILQ NLDPPFSIDG KMVAVNLATG KRRNDSGDHS DHMHYYQGKK YFRDRRGGGR NSDWSSDTNR QGQQSSSDCY IYDSATGYYY DPLAGTYYDP NTQQEVYVPQ DPGLPEEEEI KEKKPTSQGK SSSKKEMSKR DGKEKKDRGV TRFQENASEG KAPAEDVFKK PLPPTVKKEE SPPPPKVVNP LIGLLGEYGG DSDYEEEEEE EQTPPPQPRT AQPQKREEQT KKENEEDKLT DWNKLACLLC RRQFPNKEVL IKHQQLSDLH KQNLEIHRKI KQSEQELAYL ERREREGKFK GRGNDRREKL QSFDSPERKR IKYSRETDSD RKLVDKEDID TSSKGGCVQQ ATGWRKGTGL GYGHPGLASS EEAEGRMRGP SVGASGRTSK RQSNETYRDA VRRVMFARYK ELD // ID F8WCA5_HUMAN Unreviewed; 697 AA. AC F8WCA5; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 14-DEC-2022, entry version 82. DE SubName: Full=RNA-binding protein 6 {ECO:0000313|Ensembl:ENSP00000406548.1}; GN Name=RBM6 {ECO:0000313|Ensembl:ENSP00000406548.1}; 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:ENSP00000406548.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000406548.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [2] {ECO:0007829|PubMed:17525332} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R., Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [3] {ECO:0007829|PubMed:18691976} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [4] {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 [5] {ECO:0007829|PubMed:19369195} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [6] {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 [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: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 [9] {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 [10] {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 [11] {ECO:0007829|PubMed:25218447} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [12] {ECO:0007829|PubMed:25772364} RP IDENTIFICATION BY MASS 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 [13] {ECO:0007829|PubMed:25755297} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.O114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurethsson 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 [14] {ECO:0007829|PubMed:28112733} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; 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 [15] {ECO:0000313|Ensembl:ENSP00000406548.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-2022) to UniProtKB. 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; AC104450; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC105935; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; F8WCA5; -. DR MaxQB; F8WCA5; -. DR PeptideAtlas; F8WCA5; -. DR ProteomicsDB; 31085; -. DR Ensembl; ENST00000454079.5; ENSP00000406548.1; ENSG00000004534.15. DR UCSC; uc062jzt.1; human. DR HGNC; HGNC:9903; RBM6. DR VEuPathDB; HostDB:ENSG00000004534; -. DR GeneTree; ENSGT00940000157976; -. DR HOGENOM; CLU_395306_0_0_1; -. DR ChiTaRS; RBM6; human. DR Proteomes; UP000005640; Chromosome 3. DR Bgee; ENSG00000004534; Expressed in lower esophagus mucosa and 202 other tissues. DR ExpressionAtlas; F8WCA5; baseline and differential. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule. DR CDD; cd12314; RRM1_RBM6; 1. DR CDD; cd12563; RRM2_RBM6; 1. DR Gene3D; 3.30.70.330; -; 2. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf. DR InterPro; IPR041591; OCRE. DR InterPro; IPR035979; RBD_domain_sf. DR InterPro; IPR028806; RBM6. DR InterPro; IPR034123; RBM6_RRM1. DR InterPro; IPR034125; RBM6_RRM2. DR InterPro; IPR000504; RRM_dom. DR PANTHER; PTHR13948:SF22; RNA-BINDING PROTEIN 6; 3. DR Pfam; PF17780; OCRE; 1. DR SMART; SM00360; RRM; 2. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2. DR PROSITE; PS50102; RRM; 1. PE 1: Evidence at protein level; KW Proteomics identification {ECO:0007829|EPD:F8WCA5, KW ECO:0007829|MaxQB:F8WCA5}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176}. FT DOMAIN 324..404 FT /note="RRM" FT /evidence="ECO:0000259|PROSITE:PS50102" FT REGION 1..60 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 89..259 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 281..322 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 442..522 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 630..654 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 109..156 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 174..215 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 222..237 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 299..321 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 442..456 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 462..522 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 640..654 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 697 AA; 80390 MW; 92E4E87BDAA2632E CRC64; MDYRGGDGTS MDYRGREAPH MNYRDRDAHA VDFRGRDAPP SDFRGRGTYD LDFRGRDGSH ADFRGRDLSD LDFRAREQSR SDFRNRDVSD LDFRDKDGTQ VDFRGRGSGT TDLDFRDRDT PHSDFRGRHR SRTDQDFRGR EMGSCMEFKD REMPPVDPNI LDYIQPSTQD REHSGMNVNR REESTHDHTI ERPAFGIQKG EFEHSETREG ETQGVAFEHE SPADFQNSQS PVQDQDKSQL SGREEQSSDA GLFKEEGGLD FLGRQDTDYR SMEYRDVDHR LPGSQMFGYG QSKSFPEGKT ARDAQRDLQD QDYRTGPSEE KPSRLIRLSG VPEDATKEEI LNAFRTPDGM PVKNLQLKEY NTGYDYGYVC VEFSLLEDAI GCMEANQGTL MIQDKEVTLE YVSSLDFWYC KRCKANIGGH RSSCSFCKNP REVTEAKQEL ITYPQPQKTS IPAPLEKQPN QPLRPADKEP EPRKREEGQE SRLGHQKREA ERYLPPSRRE GPTFRRDRER ESWSGETRQD GESKTIMLKR IYRSTPPEVI VEVLEPYVRL TTANVRIIKN RTGPMGHTYG FIDLDSHAEA LRVVKILQNL DPPFSIDGKM VAVNLATGKR RNDSGDHSDH MHYYQGKKYF RDRRGGGRNS DWSSDTNRQG QQSSSDCYIY DSATGYYYDP LAGTYYDPNT QVSLGLFFFF FFFYLCQ // ID B3KSK6_HUMAN Unreviewed; 601 AA. AC B3KSK6; DT 02-SEP-2008, integrated into UniProtKB/TrEMBL. DT 02-SEP-2008, sequence version 1. DT 14-DEC-2022, entry version 67. DE SubName: Full=cDNA FLJ36517 fis, clone TRACH2002043, highly similar to RNA-binding protein 6 {ECO:0000313|EMBL:BAG52768.1}; 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|EMBL:BAG52768.1}; RN [1] {ECO:0000313|EMBL:BAG52768.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Trachea {ECO:0000313|EMBL:BAG52768.1}; 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., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., RA Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., RA Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., RA Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., RA Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., RA Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., RA Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., RA Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., RA Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., RA Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., RA Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., RA Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., RA Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., RA Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., RA Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). 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; AK093836; BAG52768.1; -; mRNA. DR AlphaFoldDB; B3KSK6; -. DR PeptideAtlas; B3KSK6; -. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR CDD; cd16163; OCRE_RBM6; 1. DR CDD; cd12563; RRM2_RBM6; 1. DR Gene3D; 3.30.70.330; -; 1. DR InterPro; IPR000467; G_patch_dom. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf. DR InterPro; IPR041591; OCRE. DR InterPro; IPR035979; RBD_domain_sf. DR InterPro; IPR028806; RBM6. DR InterPro; IPR035617; RBM6_OCRE. DR InterPro; IPR034125; RBM6_RRM2. DR PANTHER; PTHR13948:SF22; RNA-BINDING PROTEIN 6; 1. DR Pfam; PF01585; G-patch; 1. DR Pfam; PF17780; OCRE; 1. DR SMART; SM00443; G_patch; 1. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1. DR PROSITE; PS50174; G_PATCH; 1. PE 2: Evidence at transcript level; FT DOMAIN 529..575 FT /note="G-patch" FT /evidence="ECO:0000259|PROSITE:PS50174" FT REGION 52..132 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 219..265 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 305..426 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 482..584 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 52..66 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 72..132 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 220..249 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 250..265 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 305..342 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 350..364 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 412..426 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 482..530 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 601 AA; 69152 MW; 30098565D497D2A4 CRC64; MIQDKEVTLE YVSSLDFWYC KRCKANIGGH RSSCSFCKNP REVTEAKQEL ITYPQPQKTS IPAPLEKQPN QPLRPADKEP EPRKREEGQE SRLGHQKREA ERYLPPSRRE GPTFRRDRER ESWSGETRQD GESKTIMLKR IYRSTPPEVI VEVLEPYVRL TTANVRIIKN RTGPMGHTYG FIDLDSHAEA LRVVKILQNL DPPFSIDGKM VAVNLATGKR RSDSGDHSDH MHYYQGKKYF RDRRGGGRNS DWSSDTNRQG QQSSSDCYIY DSATGYYYDP LAGTYYDPNT QQEVYVPQDP GLPEEEEIKE KKPTSQGKSS SKKEMSKRDG KEKKDRGVTR FQENASEGKA PAEDVFKKPL PPTVKKEESP PPPKVVNPLI GLLGEYGGDS DYEEEEEEEQ TPPPQPRTAQ PQKREEQTKK ENEEDKLTDW NKLACLLCRR QFPNKEVLIK HQQLSDLHKQ NLEIHRKIKQ SEQELAYLER REREGKFKGR GNDRREKLQS FDSPERKRIK YSRETDSDRK LVDKEDIDTS SKGGCVQQAT GWRKGTGLGY GHPGLASSEE AEGRMRGPSV GASGRTSKRQ SNETYRDAVR RVMFARYKEL D // ID B4DNY1_HUMAN Unreviewed; 465 AA. AC B4DNY1; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 14-DEC-2022, entry version 81. DE SubName: Full=cDNA FLJ60318, highly similar to RNA-binding protein 6 {ECO:0000313|EMBL:BAG60393.1}; 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|EMBL:BAG60393.1}; RN [1] {ECO:0000313|EMBL:BAG60393.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Lung {ECO:0000313|EMBL:BAG60393.1}; RA Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A., RA Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y., RA Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T., RA Sugano S., Nomura N., Isogai T.; RT "NEDO human cDNA sequencing project focused on splicing variants."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. 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; AK298108; BAG60393.1; -; mRNA. DR AlphaFoldDB; B4DNY1; -. DR MaxQB; B4DNY1; -. DR PeptideAtlas; B4DNY1; -. DR ProteomicsDB; 4736; -. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR CDD; cd16163; OCRE_RBM6; 1. DR CDD; cd12563; RRM2_RBM6; 1. DR Gene3D; 3.30.70.330; -; 1. DR InterPro; IPR000467; G_patch_dom. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf. DR InterPro; IPR041591; OCRE. DR InterPro; IPR035979; RBD_domain_sf. DR InterPro; IPR028806; RBM6. DR InterPro; IPR035617; RBM6_OCRE. DR InterPro; IPR034125; RBM6_RRM2. DR PANTHER; PTHR13948:SF22; RNA-BINDING PROTEIN 6; 1. DR Pfam; PF01585; G-patch; 1. DR Pfam; PF17780; OCRE; 1. DR SMART; SM00443; G_patch; 1. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1. DR PROSITE; PS50174; G_PATCH; 1. PE 2: Evidence at transcript level; FT DOMAIN 393..439 FT /note="G-patch" FT /evidence="ECO:0000259|PROSITE:PS50174" FT REGION 83..129 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 169..290 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 346..448 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 84..113 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 114..129 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 169..206 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 214..228 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 276..290 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 346..394 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 465 AA; 53252 MW; 8E33EBBEE7F7C691 CRC64; MLKRIYRSTP PEVIVEVLEP YVRLTTANVR IIKNRTGPMG HTYGFIDLDS HAEALRVVKI LQNLDPPFSI DGKMVAVNLA TGKRRNDSGD HSDHMHYYQG KKYFRDRRGG GRNSDWSSDT NRQGQQSSSD CYIYDSATGY YYDPLAGTYY DPNTQQEVYV PQDPGLPEEE EIKEKKPTSQ GKSSSKKEMS KRDGKEKKDR GVTRFQENAS EGKAPAEDVF KKPLPPTVKK EESPPPPKVV NPLIGLLGEY GGDSDYEEEE EEEQTPPPQP RTAQPQKREE QTKKENEEDK LTDWNKLACL LCRRQFPNKE VLIKHQQLSD LHKQNLEIHR KIKQSEQELA YLERREREGK FKGRGNDRRE KLQSFDSPER KRIKYSRETD SDRKLVDKED IDTSSKGGCV QQATGWRKGT GLGYGHPGLA SSEEAEGRMR GPSVGASGRT SKRQSNETYR DAVRRVMFAR YKELD // ID F8WCT0_HUMAN Unreviewed; 35 AA. AC F8WCT0; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 14-DEC-2022, entry version 41. DE SubName: Full=RNA-binding protein 6 {ECO:0000313|Ensembl:ENSP00000396410.1}; GN Name=RBM6 {ECO:0000313|Ensembl:ENSP00000396410.1}; 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:ENSP00000396410.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000396410.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [2] {ECO:0000313|Ensembl:ENSP00000396410.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-2022) to UniProtKB. 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; AC104450; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC105935; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; F8WCT0; -. DR PeptideAtlas; F8WCT0; -. DR Ensembl; ENST00000419610.5; ENSP00000396410.1; ENSG00000004534.15. DR UCSC; uc062jzq.1; human. DR HGNC; HGNC:9903; RBM6. DR VEuPathDB; HostDB:ENSG00000004534; -. DR GeneTree; ENSGT00940000157976; -. DR HOGENOM; CLU_3368305_0_0_1; -. DR ChiTaRS; RBM6; human. DR Proteomes; UP000005640; Chromosome 3. DR Bgee; ENSG00000004534; Expressed in lower esophagus mucosa and 202 other tissues. DR ExpressionAtlas; F8WCT0; baseline and differential. PE 4: Predicted; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}. FT REGION 1..35 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 35 AA; 3965 MW; 760C44336E22B35E CRC64; MWGDSRPANR TGPFRVRQTL VGTDLPVHSA RTQEK // ID C9JMC8_HUMAN Unreviewed; 76 AA. AC C9JMC8; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 14-DEC-2022, entry version 74. DE SubName: Full=RNA-binding protein 6 {ECO:0000313|Ensembl:ENSP00000389763.1}; DE Flags: Fragment; GN Name=RBM6 {ECO:0000313|Ensembl:ENSP00000389763.1}; 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:ENSP00000389763.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000389763.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [2] {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 [3] {ECO:0007829|PubMed:28112733} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; 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 [4] {ECO:0000313|Ensembl:ENSP00000389763.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-2022) to UniProtKB. 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; AC104450; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC105935; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; C9JMC8; -. DR MaxQB; C9JMC8; -. DR PeptideAtlas; C9JMC8; -. DR ProteomicsDB; 10827; -. DR Antibodypedia; 13824; 188 antibodies from 26 providers. DR Ensembl; ENST00000433811.1; ENSP00000389763.1; ENSG00000004534.15. DR UCSC; uc062jzw.1; human. DR HGNC; HGNC:9903; RBM6. DR VEuPathDB; HostDB:ENSG00000004534; -. DR GeneTree; ENSGT00940000157976; -. DR HOGENOM; CLU_199411_0_0_1; -. DR OMA; REVGSCM; -. DR ChiTaRS; RBM6; human. DR Proteomes; UP000005640; Chromosome 3. DR Bgee; ENSG00000004534; Expressed in lower esophagus mucosa and 202 other tissues. DR ExpressionAtlas; C9JMC8; baseline and differential. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR InterPro; IPR028806; RBM6. DR PANTHER; PTHR13948:SF22; RNA-BINDING PROTEIN 6; 1. PE 1: Evidence at protein level; KW Proteomics identification {ECO:0007829|PeptideAtlas:C9JMC8, KW ECO:0007829|ProteomicsDB:C9JMC8}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}. FT REGION 1..76 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 76 FT /evidence="ECO:0000313|Ensembl:ENSP00000389763.1" SQ SEQUENCE 76 AA; 8584 MW; 174381B3D4CE6A10 CRC64; MWGDSRPANR TGPFRGSQEE RFAPGWNRDY PPPPLKSHAQ ERHSGNFPGR DSLPFDFQGH SGPPFANVEE HSFSYG // ID F8WF63_HUMAN Unreviewed; 199 AA. AC F8WF63; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 14-DEC-2022, entry version 73. DE SubName: Full=RNA-binding protein 6 {ECO:0000313|Ensembl:ENSP00000399942.1}; GN Name=RBM6 {ECO:0000313|Ensembl:ENSP00000399942.1}; 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:ENSP00000399942.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000399942.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [2] {ECO:0007829|PubMed:25218447} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [3] {ECO:0007829|PubMed:25772364} RP IDENTIFICATION BY MASS 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 [4] {ECO:0007829|PubMed:25755297} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.O114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurethsson 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 [5] {ECO:0007829|PubMed:28112733} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; 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 [6] {ECO:0000313|Ensembl:ENSP00000399942.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-2022) to UniProtKB. 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; AC104450; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC105935; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; F8WF63; -. DR MaxQB; F8WF63; -. DR PeptideAtlas; F8WF63; -. DR ProteomicsDB; 32078; -. DR Ensembl; ENST00000434592.5; ENSP00000399942.1; ENSG00000004534.15. DR UCSC; uc062jzv.1; human. DR HGNC; HGNC:9903; RBM6. DR VEuPathDB; HostDB:ENSG00000004534; -. DR GeneTree; ENSGT00940000157976; -. DR HOGENOM; CLU_118638_0_0_1; -. DR ChiTaRS; RBM6; human. DR Proteomes; UP000005640; Chromosome 3. DR Bgee; ENSG00000004534; Expressed in lower esophagus mucosa and 202 other tissues. DR ExpressionAtlas; F8WF63; baseline and differential. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR InterPro; IPR028806; RBM6. DR PANTHER; PTHR13948:SF22; RNA-BINDING PROTEIN 6; 1. PE 1: Evidence at protein level; KW Proteomics identification {ECO:0007829|EPD:F8WF63, KW ECO:0007829|MaxQB:F8WF63}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}. FT REGION 52..130 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 52..66 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 72..130 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 199 AA; 23426 MW; 03609399154AB08F CRC64; MIQDKEVTLE YVSSLDFWYC KRCKANIGGH RSSCSFCKNP REVTEAKQEL ITYPQPQKTS IPAPLEKQPN QPLRPADKEP EPRKREEGQE SRLGHQKREA ERYLPPSRRE GPTFRRDRER ESWSGETRQD GESKTIMLKR IYRSTPPEVI VEVLEPYVRL TTANVRIIKN RTGPMGHTYG FIDLDSHACV WFYRKLFVW // ID C9JSL1_HUMAN Unreviewed; 156 AA. AC C9JSL1; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 14-DEC-2022, entry version 84. DE SubName: Full=RNA-binding protein 6 {ECO:0000313|Ensembl:ENSP00000394336.1}; DE Flags: Fragment; GN Name=RBM6 {ECO:0000313|Ensembl:ENSP00000394336.1}; 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:ENSP00000394336.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000394336.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [2] {ECO:0007829|PubMed:25218447} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [3] {ECO:0007829|PubMed:25772364} RP IDENTIFICATION BY MASS 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 [4] {ECO:0007829|PubMed:25755297} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.O114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurethsson 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 [5] {ECO:0007829|PubMed:28112733} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; 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 [6] {ECO:0000313|Ensembl:ENSP00000394336.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-2022) to UniProtKB. 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; AC104450; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC105935; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; C9JSL1; -. DR SMR; C9JSL1; -. DR MaxQB; C9JSL1; -. DR PeptideAtlas; C9JSL1; -. DR ProteomicsDB; 11494; -. DR Antibodypedia; 13824; 188 antibodies from 26 providers. DR Ensembl; ENST00000446471.1; ENSP00000394336.1; ENSG00000004534.15. DR UCSC; uc062kab.1; human. DR HGNC; HGNC:9903; RBM6. DR VEuPathDB; HostDB:ENSG00000004534; -. DR GeneTree; ENSGT00940000157976; -. DR OMA; REVGSCM; -. DR ChiTaRS; RBM6; human. DR Proteomes; UP000005640; Chromosome 3. DR Bgee; ENSG00000004534; Expressed in lower esophagus mucosa and 202 other tissues. DR ExpressionAtlas; C9JSL1; baseline and differential. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR InterPro; IPR028806; RBM6. DR PANTHER; PTHR13948:SF22; RNA-BINDING PROTEIN 6; 1. PE 1: Evidence at protein level; KW Proteomics identification {ECO:0007829|EPD:C9JSL1, KW ECO:0007829|MaxQB:C9JSL1}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}. FT REGION 48..135 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 50..66 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 72..135 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 156 FT /evidence="ECO:0000313|Ensembl:ENSP00000394336.1" SQ SEQUENCE 156 AA; 18297 MW; 056C2A1A1CDF36DE CRC64; MIQDKEVTLE YVSSLDFWYC KRCKANIGGH RSSCSFCKNP REVTEAKQEL ITYPQPQKTS IPAPLEKQPN QPLRPADKEP EPRKREEGQE SRLGHQKREA ERYLPPSRRE GPTFRRDRER ESWSGETRQD GESKTIMLKR IYRSTPPEVI VEVLEP // ID C9J250_HUMAN Unreviewed; 119 AA. AC C9J250; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 14-DEC-2022, entry version 75. DE SubName: Full=RNA-binding protein 6 {ECO:0000313|Ensembl:ENSP00000392475.1}; GN Name=RBM6 {ECO:0000313|Ensembl:ENSP00000392475.1}; 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:ENSP00000392475.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000392475.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [2] {ECO:0007829|PubMed:25218447} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [3] {ECO:0007829|PubMed:28112733} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; 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 [4] {ECO:0000313|Ensembl:ENSP00000392475.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-2022) to UniProtKB. 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; AC104450; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC105935; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; C9J250; -. DR MaxQB; C9J250; -. DR PeptideAtlas; C9J250; -. DR ProteomicsDB; 8160; -. DR Antibodypedia; 13824; 188 antibodies from 26 providers. DR Ensembl; ENST00000421682.1; ENSP00000392475.1; ENSG00000004534.15. DR UCSC; uc062kaf.1; human. DR HGNC; HGNC:9903; RBM6. DR VEuPathDB; HostDB:ENSG00000004534; -. DR GeneTree; ENSGT00940000157976; -. DR HOGENOM; CLU_2060686_0_0_1; -. DR ChiTaRS; RBM6; human. DR Proteomes; UP000005640; Chromosome 3. DR Bgee; ENSG00000004534; Expressed in lower esophagus mucosa and 202 other tissues. DR ExpressionAtlas; C9J250; baseline and differential. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR InterPro; IPR000467; G_patch_dom. DR InterPro; IPR028806; RBM6. DR PANTHER; PTHR13948:SF22; RNA-BINDING PROTEIN 6; 1. DR Pfam; PF01585; G-patch; 1. DR SMART; SM00443; G_patch; 1. DR PROSITE; PS50174; G_PATCH; 1. PE 1: Evidence at protein level; KW Proteomics identification {ECO:0007829|EPD:C9J250, KW ECO:0007829|MaxQB:C9J250}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}. FT DOMAIN 47..93 FT /note="G-patch" FT /evidence="ECO:0000259|PROSITE:PS50174" FT REGION 1..24 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 65..103 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..23 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 119 AA; 12695 MW; 6260137840346C5E CRC64; MIAGKSSSLL TLQKGNGLST PGKLTGSDGV CFFCSDRKLV DKEDIDTSSK GGCVQQATGW RKGTGLGYGH PGLASSEEAE GRMRGPSVGA SGRTSKRQSN ETYRDAVRRV MFARYKELD // ID C9JII0_HUMAN Unreviewed; 120 AA. AC C9JII0; DT 03-NOV-2009, integrated into UniProtKB/TrEMBL. DT 03-NOV-2009, sequence version 1. DT 14-DEC-2022, entry version 73. DE SubName: Full=RNA-binding protein 6 {ECO:0000313|Ensembl:ENSP00000403865.1}; DE Flags: Fragment; GN Name=RBM6 {ECO:0000313|Ensembl:ENSP00000403865.1}; 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:ENSP00000403865.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000403865.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [2] {ECO:0000313|Ensembl:ENSP00000403865.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-2022) to UniProtKB. 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; AC104450; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC105935; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; C9JII0; -. DR SMR; C9JII0; -. DR MaxQB; C9JII0; -. DR PeptideAtlas; C9JII0; -. DR ProteomicsDB; 10340; -. DR Antibodypedia; 13824; 188 antibodies from 26 providers. DR Ensembl; ENST00000438912.1; ENSP00000403865.1; ENSG00000004534.15. DR UCSC; uc062kae.1; human. DR HGNC; HGNC:9903; RBM6. DR VEuPathDB; HostDB:ENSG00000004534; -. DR GeneTree; ENSGT00940000157976; -. DR HOGENOM; CLU_2055010_0_0_1; -. DR OMA; REVGSCM; -. DR ChiTaRS; RBM6; human. DR Proteomes; UP000005640; Chromosome 3. DR Bgee; ENSG00000004534; Expressed in lower esophagus mucosa and 202 other tissues. DR ExpressionAtlas; C9JII0; baseline and differential. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR InterPro; IPR041591; OCRE. DR InterPro; IPR028806; RBM6. DR PANTHER; PTHR13948:SF22; RNA-BINDING PROTEIN 6; 1. DR Pfam; PF17780; OCRE; 1. PE 1: Evidence at protein level; KW Proteomics identification {ECO:0007829|EPD:C9JII0, KW ECO:0007829|MaxQB:C9JII0}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}. FT DOMAIN 35..85 FT /note="OCRE" FT /evidence="ECO:0000259|Pfam:PF17780" FT REGION 1..36 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 58..120 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..19 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 20..36 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 72..120 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 120 FT /evidence="ECO:0000313|Ensembl:ENSP00000403865.1" SQ SEQUENCE 120 AA; 13804 MW; AF92B07739B60A95 CRC64; MHYYQGKKYF RDRRGGGRNS DWSSDTNRQG QQSSSDCYIY DSATGYYYDP LAGTYYDPNT QQEVYVPQDP GLPEEEEIKE KKPTSQGKSS SKKEMSKRDG KEKKDRGVTR FQENASEGKA //