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   02-OCT-2024, entry version 206.
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.
DR   RefSeq; XP_016860990.1; XM_017005501.1.
DR   RefSeq; XP_016860991.1; XM_017005502.1.
DR   AlphaFoldDB; P78332; -.
DR   BioGRID; 115479; 128.
DR   IntAct; P78332; 87.
DR   MINT; P78332; -.
DR   STRING; 9606.ENSP00000266022; -.
DR   GlyGen; P78332; 3 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; P78332; -.
DR   PhosphoSitePlus; P78332; -.
DR   BioMuta; RBM6; -.
DR   DMDM; 116242749; -.
DR   jPOST; P78332; -.
DR   MassIVE; P78332; -.
DR   PaxDb; 9606-ENSP00000266022; -.
DR   PeptideAtlas; P78332; -.
DR   ProteomicsDB; 5671; -.
DR   ProteomicsDB; 57570; -. [P78332-1]
DR   ProteomicsDB; 69630; -.
DR   Pumba; P78332; -.
DR   Antibodypedia; 13824; 211 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   AGR; HGNC:9903; -.
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   OrthoDB; 298711at2759; -.
DR   PhylomeDB; P78332; -.
DR   TreeFam; TF315789; -.
DR   PathwayCommons; P78332; -.
DR   SignaLink; P78332; -.
DR   BioGRID-ORCS; 10180; 18 hits in 1166 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 204 other cell types or tissues.
DR   ExpressionAtlas; P78332; baseline and differential.
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   Gene3D; 2.160.20.80; E3 ubiquitin-protein ligase SopA; 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; IPR035617; RBM6_OCRE.
DR   InterPro; IPR034123; RBM6_RRM1.
DR   InterPro; IPR034125; RBM6_RRM2.
DR   InterPro; IPR000504; RRM_dom.
DR   PANTHER; PTHR13948; RNA-BINDING PROTEIN; 1.
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   SMART; SM00360; RRM; 2.
DR   SUPFAM; SSF141571; Pentapeptide repeat-like; 1.
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   Alternative splicing; Isopeptide bond; Nucleus; Phosphoprotein;
KW   Proteomics identification; Reference proteome; RNA-binding;
KW   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
//