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Protein

RNA-binding motif, single-stranded-interacting protein 2

Gene

RBMS2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB
  • RNA binding Source: ProtInc

GO - Biological processi

  • RNA processing Source: ProtInc
Complete GO annotation...

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
RNA-binding motif, single-stranded-interacting protein 2
Alternative name(s):
Suppressor of CDC2 with RNA-binding motif 3
Gene namesi
Name:RBMS2
Synonyms:SCR3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:9909. RBMS2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34275.

Polymorphism and mutation databases

BioMutaiRBMS2.
DMDMi55976301.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 407407RNA-binding motif, single-stranded-interacting protein 2PRO_0000081800Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei106 – 1061Phosphoserine3 Publications
Modified residuei269 – 2691Phosphothreonine1 Publication
Modified residuei280 – 2801Phosphoserine2 Publications
Modified residuei285 – 2851Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ15434.
PaxDbiQ15434.
PRIDEiQ15434.

PTM databases

PhosphoSiteiQ15434.

Expressioni

Gene expression databases

BgeeiQ15434.
CleanExiHS_RBMS2.
ExpressionAtlasiQ15434. baseline and differential.
GenevisibleiQ15434. HS.

Organism-specific databases

HPAiHPA039225.

Interactioni

Protein-protein interaction databases

BioGridi111874. 15 interactions.
IntActiQ15434. 3 interactions.
STRINGi9606.ENSP00000262031.

Structurei

Secondary structure

1
407
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi58 – 625Combined sources
Helixi69 – 735Combined sources
Turni77 – 793Combined sources
Beta strandi82 – 876Combined sources
Beta strandi91 – 933Combined sources
Beta strandi98 – 1058Combined sources
Helixi107 – 12014Combined sources
Beta strandi124 – 1263Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X4ENMR-A58-129[»]
ProteinModelPortaliQ15434.
SMRiQ15434. Positions 44-218.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15434.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini56 – 12974RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini135 – 22086RRM 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 2 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG320163.
GeneTreeiENSGT00760000118913.
HOGENOMiHOG000008467.
HOVERGENiHBG053108.
InParanoidiQ15434.
OMAiPGMDHPL.
PhylomeDBiQ15434.
TreeFamiTF314644.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q15434-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLSVTSRPG ISTFGYNRNN KKPYVSLAQQ MAPPSPSNST PNSSSGSNGN
60 70 80 90 100
DQLSKTNLYI RGLQPGTTDQ DLVKLCQPYG KIVSTKAILD KTTNKCKGYG
110 120 130 140 150
FVDFDSPSAA QKAVTALKAS GVQAQMAKQQ EQDPTNLYIS NLPLSMDEQE
160 170 180 190 200
LEGMLKPFGQ VISTRILRDT SGTSRGVGFA RMESTEKCEA IITHFNGKYI
210 220 230 240 250
KTPPGVPAPS DPLLCKFADG GPKKRQNQGK FVQNGRAWPR NADMGVMALT
260 270 280 290 300
YDPTTALQNG FYPAPYNITP NRMLAQSALS PYLSSPVSSY QRVTQTSPLQ
310 320 330 340 350
VPNPSWMHHH SYLMQPSGSV LTPGMDHPIS LQPASMMGPL TQQLGHLSLS
360 370 380 390 400
STGTYMPTAA AMQGAYISQY TPVPSSSVSV EESSGQQNQV AVDAPSEHGV

YSFQFNK
Length:407
Mass (Da):43,959
Last modified:November 1, 1996 - v1
Checksum:iBAFC794E2318BE0A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D28483 mRNA. Translation: BAA05842.1.
BC027863 mRNA. Translation: AAH27863.1.
BC072679 mRNA. Translation: AAH72679.1.
CCDSiCCDS8923.1.
PIRiS47660.
RefSeqiNP_002889.1. NM_002898.3.
XP_006719607.1. XM_006719544.2.
XP_011536942.1. XM_011538640.1.
UniGeneiHs.505729.
Hs.683360.

Genome annotation databases

EnsembliENST00000262031; ENSP00000262031; ENSG00000076067.
GeneIDi5939.
KEGGihsa:5939.
UCSCiuc001sln.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D28483 mRNA. Translation: BAA05842.1.
BC027863 mRNA. Translation: AAH27863.1.
BC072679 mRNA. Translation: AAH72679.1.
CCDSiCCDS8923.1.
PIRiS47660.
RefSeqiNP_002889.1. NM_002898.3.
XP_006719607.1. XM_006719544.2.
XP_011536942.1. XM_011538640.1.
UniGeneiHs.505729.
Hs.683360.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1X4ENMR-A58-129[»]
ProteinModelPortaliQ15434.
SMRiQ15434. Positions 44-218.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111874. 15 interactions.
IntActiQ15434. 3 interactions.
STRINGi9606.ENSP00000262031.

PTM databases

PhosphoSiteiQ15434.

Polymorphism and mutation databases

BioMutaiRBMS2.
DMDMi55976301.

Proteomic databases

MaxQBiQ15434.
PaxDbiQ15434.
PRIDEiQ15434.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000262031; ENSP00000262031; ENSG00000076067.
GeneIDi5939.
KEGGihsa:5939.
UCSCiuc001sln.2. human.

Organism-specific databases

CTDi5939.
GeneCardsiGC12P056915.
HGNCiHGNC:9909. RBMS2.
HPAiHPA039225.
MIMi602387. gene.
neXtProtiNX_Q15434.
PharmGKBiPA34275.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG320163.
GeneTreeiENSGT00760000118913.
HOGENOMiHOG000008467.
HOVERGENiHBG053108.
InParanoidiQ15434.
OMAiPGMDHPL.
PhylomeDBiQ15434.
TreeFamiTF314644.

Miscellaneous databases

ChiTaRSiRBMS2. human.
EvolutionaryTraceiQ15434.
GenomeRNAii5939.
NextBioi23154.
PROiQ15434.
SOURCEiSearch...

Gene expression databases

BgeeiQ15434.
CleanExiHS_RBMS2.
ExpressionAtlasiQ15434. baseline and differential.
GenevisibleiQ15434. HS.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
PROSITEiPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "SCR: novel human suppressors of cdc2/cdc13 mutants of Schizosaccharomyces pombe harbour motifs for RNA binding proteins."
    Kanaoka Y., Nojima H.
    Nucleic Acids Res. 22:2687-2693(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung and Skin.
  3. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; THR-269; SER-280 AND SER-285, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  5. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  8. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; SER-280 AND SER-285, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Solution structure of RRM domain in RNA binding motif, single-stranded interacting protein 2."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 58-129.

Entry informationi

Entry nameiRBMS2_HUMAN
AccessioniPrimary (citable) accession number: Q15434
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: November 1, 1996
Last modified: July 22, 2015
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.