Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q15434 (RBMS2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
RNA-binding motif, single-stranded-interacting protein 2
Alternative name(s):
Suppressor of CDC2 with RNA-binding motif 3
Gene names
Name:RBMS2
Synonyms:SCR3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length407 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Subcellular location

Nucleus Potential.

Sequence similarities

Contains 2 RRM (RNA recognition motif) domains.

Ontologies

Keywords
   Cellular componentNucleus
   DomainRepeat
   LigandRNA-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA processing

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionRNA binding

Traceable author statement Ref.1. Source: ProtInc

nucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 407407RNA-binding motif, single-stranded-interacting protein 2
PRO_0000081800

Regions

Domain56 – 12974RRM 1
Domain135 – 22086RRM 2

Amino acid modifications

Modified residue11N-acetylmethionine Ref.9
Modified residue1061Phosphoserine Ref.4 Ref.7 Ref.8
Modified residue2691Phosphothreonine Ref.4
Modified residue2801Phosphoserine Ref.4 Ref.8
Modified residue2851Phosphoserine Ref.4 Ref.8

Secondary structure

................. 407
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q15434 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: BAFC794E2318BE0A

FASTA40743,959
        10         20         30         40         50         60 
MLLSVTSRPG ISTFGYNRNN KKPYVSLAQQ MAPPSPSNST PNSSSGSNGN DQLSKTNLYI 

        70         80         90        100        110        120 
RGLQPGTTDQ DLVKLCQPYG KIVSTKAILD KTTNKCKGYG FVDFDSPSAA QKAVTALKAS 

       130        140        150        160        170        180 
GVQAQMAKQQ EQDPTNLYIS NLPLSMDEQE LEGMLKPFGQ VISTRILRDT SGTSRGVGFA 

       190        200        210        220        230        240 
RMESTEKCEA IITHFNGKYI KTPPGVPAPS DPLLCKFADG GPKKRQNQGK FVQNGRAWPR 

       250        260        270        280        290        300 
NADMGVMALT YDPTTALQNG FYPAPYNITP NRMLAQSALS PYLSSPVSSY QRVTQTSPLQ 

       310        320        330        340        350        360 
VPNPSWMHHH SYLMQPSGSV LTPGMDHPIS LQPASMMGPL TQQLGHLSLS STGTYMPTAA 

       370        380        390        400 
AMQGAYISQY TPVPSSSVSV EESSGQQNQV AVDAPSEHGV YSFQFNK 

« Hide

References

« Hide 'large scale' references
[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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D28483 mRNA. Translation: BAA05842.1.
BC027863 mRNA. Translation: AAH27863.1.
BC072679 mRNA. Translation: AAH72679.1.
CCDSCCDS8923.1.
PIRS47660.
RefSeqNP_002889.1. NM_002898.3.
XP_006719607.1. XM_006719544.1.
UniGeneHs.505729.
Hs.683360.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1X4ENMR-A58-129[»]
ProteinModelPortalQ15434.
SMRQ15434. Positions 44-218.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111874. 11 interactions.
IntActQ15434. 3 interactions.
STRING9606.ENSP00000262031.

PTM databases

PhosphoSiteQ15434.

Polymorphism databases

DMDM55976301.

Proteomic databases

MaxQBQ15434.
PaxDbQ15434.
PRIDEQ15434.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262031; ENSP00000262031; ENSG00000076067.
GeneID5939.
KEGGhsa:5939.
UCSCuc001sln.2. human.

Organism-specific databases

CTD5939.
GeneCardsGC12P056915.
HGNCHGNC:9909. RBMS2.
HPAHPA039225.
MIM602387. gene.
neXtProtNX_Q15434.
PharmGKBPA34275.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG320163.
HOGENOMHOG000008467.
HOVERGENHBG053108.
InParanoidQ15434.
OMAPGMDHPL.
PhylomeDBQ15434.
TreeFamTF314644.

Gene expression databases

ArrayExpressQ15434.
BgeeQ15434.
CleanExHS_RBMS2.
GenevestigatorQ15434.

Family and domain databases

Gene3D3.30.70.330. 2 hits.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00076. RRM_1. 2 hits.
[Graphical view]
SMARTSM00360. RRM. 2 hits.
[Graphical view]
PROSITEPS50102. RRM. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ15434.
GenomeRNAi5939.
NextBio23154.
PROQ15434.
SOURCESearch...

Entry information

Entry nameRBMS2_HUMAN
AccessionPrimary (citable) accession number: Q15434
Entry history
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM