RBM6_HUMAN
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 03-AUG-2022, entry version 194.
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.
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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; 85.
DR IntAct; P78332; 43.
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 PRIDE; P78332; -.
DR ProteomicsDB; 5671; -.
DR ProteomicsDB; 57570; -. [P78332-1]
DR ProteomicsDB; 69630; -.
DR Antibodypedia; 13824; 190 antibodies from 27 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; 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 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
