ID   RBM6_HUMAN              Reviewed;        1123 AA.
AC   P78332; O60549; O75524;
DT   24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 5.
DT   14-DEC-2011, entry version 107.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lung;
RX   MEDLINE=98160103; PubMed=9500467;
RA   Gure A.O., Altorki N.K., Stockert E., Scanlan M.J., Old L.J.,
RA   Chen Y.-T.;
RT   "Human lung cancer antigens recognized by autologous antibodies:
RT   definition of a novel cDNA derived from the tumor suppressor gene
RT   locus on chromosome 3p21.3.";
RL   Cancer Res. 58:1034-1041(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=99281204; 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
RT   closely related flanking genes in a critical lung cancer region at
RT   3p21.3.";
RL   Eur. J. Hum. Genet. 7:478-486(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   MEDLINE=99280069; PubMed=10353602; DOI=10.1038/sj.onc.1202601;
RA   Drabkin H.A., West J.D., Hotfilder M., Heng Y.M., Erickson P.,
RA   Calvo R., Dalmau J., Gemmill R.M., Sablitzky F.;
RT   "DEF-3(g16/NY-LU-12), an RNA binding protein from the 3p21.3
RT   homozygous deletion region in SCLC.";
RL   Oncogene 18:2589-2597(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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   DISCUSSION OF SEQUENCE, AND VARIANT PHE-353.
RX   MEDLINE=20535986; PubMed=11085536;
RG   The international lung cancer chromosome 3p21.3 tumor suppressor gene
RG   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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-923, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=15302935; DOI=10.1073/pnas.0404720101;
RA   Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,
RA   Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
RT   "Large-scale characterization of HeLa cell nuclear phosphoproteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-891 AND SER-1025, AND
RP   MASS SPECTROMETRY.
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.,
RA   Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in
RT   signaling networks.";
RL   Cell 127:635-648(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1025, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein
RT   phosphorylation analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360 AND SER-362, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., 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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362; SER-891; SER-1022
RP   AND SER-1025, AND MASS SPECTROMETRY.
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
RT   the kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360; SER-362 AND
RP   SER-1025, AND MASS SPECTROMETRY.
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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND MASS
RP   SPECTROMETRY.
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   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360; SER-362 AND
RP   TYR-914, AND MASS SPECTROMETRY.
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).
CC   -!- FUNCTION: Specifically binds poly(G) RNA homopolymers in vitro.
CC   -!- SUBCELLULAR LOCATION: Nucleus (Probable).
CC   -!- TISSUE SPECIFICITY: Ubiquitous in adults.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
CC   -!- SIMILARITY: Contains 1 G-patch domain.
CC   -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
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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   IPI; IPI00297723; -.
DR   RefSeq; NP_005768.1; NM_005777.2.
DR   UniGene; Hs.696735; -.
DR   ProteinModelPortal; P78332; -.
DR   SMR; P78332; 454-564, 653-747.
DR   IntAct; P78332; 5.
DR   STRING; P78332; -.
DR   PhosphoSite; P78332; -.
DR   DMDM; 116242749; -.
DR   PRIDE; P78332; -.
DR   Ensembl; ENST00000266022; ENSP00000266022; ENSG00000004534.
DR   GeneID; 10180; -.
DR   KEGG; hsa:10180; -.
DR   UCSC; uc003cyc.1; human.
DR   CTD; 10180; -.
DR   GeneCards; GC03P049952; -.
DR   H-InvDB; HIX0003322; -.
DR   HGNC; HGNC:9903; RBM6.
DR   HPA; HPA026272; -.
DR   HPA; HPA027164; -.
DR   MIM; 606886; gene.
DR   neXtProt; NX_P78332; -.
DR   eggNOG; prNOG12886; -.
DR   HOGENOM; HBG278020; -.
DR   HOVERGEN; HBG007537; -.
DR   InParanoid; P78332; -.
DR   OMA; ERFAPGW; -.
DR   PhylomeDB; P78332; -.
DR   NextBio; 38538; -.
DR   ArrayExpress; P78332; -.
DR   Bgee; P78332; -.
DR   CleanEx; HS_RBM6; -.
DR   Genevestigator; P78332; -.
DR   GermOnline; ENSG00000004534; Homo sapiens.
DR   GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR   GO; GO:0003677; F:DNA binding; TAS:ProtInc.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006396; P:RNA processing; TAS:ProtInc.
DR   InterPro; IPR000467; G_patch.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR015880; Znf_C2H2-like.
DR   Gene3D; G3DSA:3.30.70.330; a_b_plait_nuc_bd; 2.
DR   Pfam; PF01585; G-patch; 1.
DR   SMART; SM00443; G_patch; 1.
DR   SMART; SM00360; RRM; 1.
DR   SMART; SM00355; ZnF_C2H2; 1.
DR   PROSITE; PS50174; G_PATCH; 1.
DR   PROSITE; PS50102; RRM; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Nucleus; Phosphoprotein; Polymorphism;
KW   Reference proteome; RNA-binding.
FT   CHAIN         1   1123       RNA-binding protein 6.
FT                                /FTId=PRO_0000081760.
FT   DOMAIN      456    536       RRM.
FT   DOMAIN     1051   1097       G-patch.
FT   COMPBIAS    826    829       Poly-Glu.
FT   COMPBIAS    892    895       Poly-Pro.
FT   COMPBIAS    915    921       Poly-Glu.
FT   MOD_RES     360    360       Phosphoserine.
FT   MOD_RES     362    362       Phosphoserine.
FT   MOD_RES     891    891       Phosphoserine.
FT   MOD_RES     914    914       Phosphotyrosine.
FT   MOD_RES     923    923       Phosphothreonine.
FT   MOD_RES    1022   1022       Phosphoserine.
FT   MOD_RES    1025   1025       Phosphoserine.
FT   VARIANT     353    353       S -> F (in a non-small cell lung cancer
FT                                cell line).
FT                                /FTId=VAR_014226.
FT   VARIANT     721    721       N -> T (in dbSNP:rs34707170).
FT                                /FTId=VAR_052216.
FT   CONFLICT    642    642       R -> K (in Ref. 2; AAC21578).
FT   CONFLICT    710    710       A -> V (in Ref. 1; AAC05826).
FT   CONFLICT    796    796       T -> S (in Ref. 1; AAC05826).
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
//