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   27-MAR-2024, entry version 184.
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; 251.
DR   IntAct; Q15434; 15.
DR   MINT; Q15434; -.
DR   STRING; 9606.ENSP00000262031; -.
DR   GlyCosmos; Q15434; 2 sites, 1 glycan.
DR   GlyGen; Q15434; 4 sites, 1 O-linked glycan (4 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; 9606-ENSP00000262031; -.
DR   PeptideAtlas; Q15434; -.
DR   ProteomicsDB; 60590; -.
DR   Pumba; Q15434; -.
DR   Antibodypedia; 28267; 237 antibodies from 24 providers.
DR   DNASU; 5939; -.
DR   Ensembl; ENST00000262031.10; ENSP00000262031.5; ENSG00000076067.14.
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   AGR; HGNC:9909; -.
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; XESSGQQ; -.
DR   OrthoDB; 129910at2759; -.
DR   PhylomeDB; Q15434; -.
DR   TreeFam; TF314644; -.
DR   PathwayCommons; Q15434; -.
DR   SignaLink; Q15434; -.
DR   BioGRID-ORCS; 5939; 19 hits in 1148 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 169 other cell types or tissues.
DR   ExpressionAtlas; Q15434; baseline and differential.
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   CDD; cd12471; RRM1_MSSP2; 1.
DR   CDD; cd12474; RRM2_MSSP2; 1.
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   PANTHER; PTHR48025; OS02G0815200 PROTEIN; 1.
DR   PANTHER; PTHR48025:SF22; OS02G0815200 PROTEIN; 1.
DR   Pfam; PF00076; RRM_1; 2.
DR   SMART; SM00360; RRM; 2.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   PROSITE; PS50102; RRM; 2.
DR   Genevisible; Q15434; HS.
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
//