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 26-FEB-2020, entry version 183. 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 P26641-2:EEF1G; NbExp=3; IntAct=EBI-2692323, EBI-10177695; 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 SMR; P78332; -. DR BioGrid; 115479; 38. DR IntAct; P78332; 32. 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 PRIDE; P78332; -. DR ProteomicsDB; 5671; -. DR ProteomicsDB; 57570; -. [P78332-1] DR ProteomicsDB; 69630; -. DR DNASU; 10180; -. DR Ensembl; ENST00000266022; ENSP00000266022; ENSG00000004534. [P78332-1] DR Ensembl; ENST00000422955; ENSP00000392939; ENSG00000004534. [P78332-2] DR Ensembl; ENST00000425608; ENSP00000408665; ENSG00000004534. [P78332-3] DR Ensembl; ENST00000442092; ENSP00000393530; ENSG00000004534. [P78332-2] DR GeneID; 10180; -. DR KEGG; hsa:10180; -. 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; HPA026272; -. DR HPA; HPA027164; -. DR MIM; 606886; gene. DR neXtProt; NX_P78332; -. DR OpenTargets; ENSG00000004534; -. DR PharmGKB; PA34268; -. DR eggNOG; ENOG410IQDR; Eukaryota. DR eggNOG; ENOG4111TS3; LUCA. DR GeneTree; ENSGT00940000157976; -. DR HOGENOM; CLU_010527_0_0_1; -. DR InParanoid; P78332; -. DR OMA; SQMDFRG; -. DR OrthoDB; 786674at2759; -. DR PhylomeDB; P78332; -. DR TreeFam; TF315789; -. 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 myometrium and 228 other tissues. DR ExpressionAtlas; P78332; baseline and differential. DR Genevisible; P78332; HS. DR GO; GO:0005634; C:nucleus; TAS:ProtInc. DR GO; GO:0003677; F:DNA binding; TAS:ProtInc. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. 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; PTHR13948:SF22; 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; SSF54928; 2. DR PROSITE; PS50174; G_PATCH; 1. DR PROSITE; PS50102; RRM; 1. PE 1: Evidence at protein level; KW Alternative splicing; Isopeptide bond; Nucleus; Phosphoprotein; KW Polymorphism; 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 COMPBIAS 826..829 FT /note="Poly-Glu" FT COMPBIAS 892..895 FT /note="Poly-Pro" FT COMPBIAS 915..921 FT /note="Poly-Glu" FT MOD_RES 17 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:23186163" FT MOD_RES 240 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:23186163" FT MOD_RES 344 FT /note="Phosphothreonine" FT /evidence="ECO:0000244|PubMed:23186163" FT MOD_RES 360 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:17525332, FT ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:23186163, ECO:0000244|PubMed:24275569" FT MOD_RES 362 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:17525332, FT ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:23186163, ECO:0000244|PubMed:24275569" FT MOD_RES 891 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:24275569" FT MOD_RES 1022 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:23186163" FT MOD_RES 1025 FT /note="Phosphoserine" FT /evidence="ECO:0000244|PubMed:17081983, FT ECO:0000244|PubMed:18669648, ECO:0000244|PubMed:18691976, FT ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:23186163, FT ECO:0000244|PubMed:24275569" FT CROSSLNK 36 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000244|PubMed:28112733" FT CROSSLNK 331 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000244|PubMed:28112733" FT CROSSLNK 386 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000244|PubMed:25218447, FT ECO:0000244|PubMed:28112733" FT CROSSLNK 453 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000244|PubMed:25218447, FT ECO:0000244|PubMed:25755297, ECO:0000244|PubMed:25772364, FT ECO:0000244|PubMed:28112733" FT CROSSLNK 469 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000244|PubMed:28112733" FT CROSSLNK 569 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000244|PubMed:25218447, FT ECO:0000244|PubMed:25755297, ECO:0000244|PubMed:25772364, FT ECO:0000244|PubMed:28112733" FT CROSSLNK 871 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000244|PubMed:28112733" FT CROSSLNK 879 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000244|PubMed:28112733" FT CROSSLNK 887 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000244|PubMed:28112733" FT CROSSLNK 935 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000244|PubMed:28112733" FT CROSSLNK 948 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000244|PubMed:28112733" FT CROSSLNK 991 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000244|PubMed:28112733" FT CROSSLNK 1019 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000244|PubMed:28112733" FT CROSSLNK 1042 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000244|PubMed:28112733" FT CROSSLNK 1046 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000244|PubMed:25218447, FT ECO:0000244|PubMed:28112733" FT CROSSLNK 1066 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000244|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 //