RBMS2_HUMAN
ID RBMS2_HUMAN Reviewed; 407 AA.
AC Q15434;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=RNA-binding motif, single-stranded-interacting protein 2;
DE AltName: Full=Suppressor of CDC2 with RNA-binding motif 3;
GN Name=RBMS2; Synonyms=SCR3;
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].
RX PubMed=8041632; DOI=10.1093/nar/22.13.2687;
RA Kanaoka Y., Nojima H.;
RT "SCR: novel human suppressors of cdc2/cdc13 mutants of Schizosaccharomyces
RT pombe harbour motifs for RNA binding proteins.";
RL Nucleic Acids Res. 22:2687-2693(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Skin;
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 [3]
RP IDENTIFICATION BY 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; THR-269; SER-280 AND
RP SER-285, 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 [5]
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 [6]
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]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND IDENTIFICATION BY
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; SER-280 AND SER-285, 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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [11]
RP STRUCTURE BY NMR OF 58-129.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RRM domain in RNA binding motif, single-stranded
RT interacting protein 2.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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DR EMBL; D28483; BAA05842.1; -; mRNA.
DR EMBL; BC027863; AAH27863.1; -; mRNA.
DR EMBL; BC072679; AAH72679.1; -; mRNA.
DR CCDS; CCDS8923.1; -.
DR PIR; S47660; S47660.
DR RefSeq; NP_002889.1; NM_002898.3.
DR RefSeq; XP_006719607.1; XM_006719544.3.
DR RefSeq; XP_011536942.1; XM_011538640.2.
DR PDB; 1X4E; NMR; -; A=58-129.
DR PDBsum; 1X4E; -.
DR AlphaFoldDB; Q15434; -.
DR SMR; Q15434; -.
DR BioGRID; 111874; 237.
DR IntAct; Q15434; 15.
DR MINT; Q15434; -.
DR STRING; 9606.ENSP00000262031; -.
DR GlyGen; Q15434; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q15434; -.
DR PhosphoSitePlus; Q15434; -.
DR BioMuta; RBMS2; -.
DR DMDM; 55976301; -.
DR EPD; Q15434; -.
DR jPOST; Q15434; -.
DR MassIVE; Q15434; -.
DR MaxQB; Q15434; -.
DR PaxDb; Q15434; -.
DR PeptideAtlas; Q15434; -.
DR PRIDE; Q15434; -.
DR ProteomicsDB; 60590; -.
DR Antibodypedia; 28267; 212 antibodies from 24 providers.
DR DNASU; 5939; -.
DR Ensembl; ENST00000262031.10; ENSP00000262031.5; ENSG00000076067.13.
DR GeneID; 5939; -.
DR KEGG; hsa:5939; -.
DR MANE-Select; ENST00000262031.10; ENSP00000262031.5; NM_002898.4; NP_002889.1.
DR UCSC; uc001sln.3; human.
DR CTD; 5939; -.
DR DisGeNET; 5939; -.
DR GeneCards; RBMS2; -.
DR HGNC; HGNC:9909; RBMS2.
DR HPA; ENSG00000076067; Low tissue specificity.
DR MIM; 602387; gene.
DR neXtProt; NX_Q15434; -.
DR OpenTargets; ENSG00000076067; -.
DR PharmGKB; PA34275; -.
DR VEuPathDB; HostDB:ENSG00000076067; -.
DR eggNOG; KOG4733; Eukaryota.
DR GeneTree; ENSGT00940000155250; -.
DR InParanoid; Q15434; -.
DR OMA; DHGIYSF; -.
DR OrthoDB; 810893at2759; -.
DR PhylomeDB; Q15434; -.
DR TreeFam; TF314644; -.
DR PathwayCommons; Q15434; -.
DR SignaLink; Q15434; -.
DR BioGRID-ORCS; 5939; 11 hits in 1072 CRISPR screens.
DR ChiTaRS; RBMS2; human.
DR EvolutionaryTrace; Q15434; -.
DR GenomeRNAi; 5939; -.
DR Pharos; Q15434; Tbio.
DR PRO; PR:Q15434; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q15434; protein.
DR Bgee; ENSG00000076067; Expressed in sural nerve and 167 other tissues.
DR ExpressionAtlas; Q15434; baseline and differential.
DR Genevisible; Q15434; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:0003730; F:mRNA 3'-UTR binding; IBA:GO_Central.
DR GO; GO:0008143; F:poly(A) binding; IBA:GO_Central.
DR GO; GO:0008266; F:poly(U) RNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006396; P:RNA processing; TAS:ProtInc.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; RNA-binding.
FT CHAIN 1..407
FT /note="RNA-binding motif, single-stranded-interacting
FT protein 2"
FT /id="PRO_0000081800"
FT DOMAIN 56..129
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 135..220
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 29..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 269
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:1X4E"
FT HELIX 69..73
FT /evidence="ECO:0007829|PDB:1X4E"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:1X4E"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:1X4E"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:1X4E"
FT STRAND 98..105
FT /evidence="ECO:0007829|PDB:1X4E"
FT HELIX 107..120
FT /evidence="ECO:0007829|PDB:1X4E"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:1X4E"
SQ SEQUENCE 407 AA; 43959 MW; BAFC794E2318BE0A CRC64;
MLLSVTSRPG ISTFGYNRNN KKPYVSLAQQ MAPPSPSNST PNSSSGSNGN DQLSKTNLYI
RGLQPGTTDQ DLVKLCQPYG KIVSTKAILD KTTNKCKGYG FVDFDSPSAA QKAVTALKAS
GVQAQMAKQQ EQDPTNLYIS NLPLSMDEQE LEGMLKPFGQ VISTRILRDT SGTSRGVGFA
RMESTEKCEA IITHFNGKYI KTPPGVPAPS DPLLCKFADG GPKKRQNQGK FVQNGRAWPR
NADMGVMALT YDPTTALQNG FYPAPYNITP NRMLAQSALS PYLSSPVSSY QRVTQTSPLQ
VPNPSWMHHH SYLMQPSGSV LTPGMDHPIS LQPASMMGPL TQQLGHLSLS STGTYMPTAA
AMQGAYISQY TPVPSSSVSV EESSGQQNQV AVDAPSEHGV YSFQFNK
