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Q15434

- RBMS2_HUMAN

UniProt

Q15434 - RBMS2_HUMAN

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Protein

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

Gene

RBMS2

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

Functioni

GO - Molecular functioni

  1. nucleotide binding Source: InterPro
  2. poly(A) RNA binding Source: UniProtKB
  3. RNA binding Source: ProtInc

GO - Biological processi

  1. 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: Chromosome 12

Organism-specific databases

HGNCiHGNC:9909. RBMS2.

Subcellular locationi

Nucleus Curated

GO - Cellular componenti

  1. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34275.

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.
GenevestigatoriQ15434.

Organism-specific databases

HPAiHPA039225.

Interactioni

Protein-protein interaction databases

BioGridi111874. 11 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 – 625
Helixi69 – 735
Turni77 – 793
Beta strandi82 – 876
Beta strandi91 – 933
Beta strandi98 – 1058
Helixi107 – 12014
Beta strandi124 – 1263

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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:
EMBL
GenBank
DDBJ
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_006719544.1.
UniGeneiHs.505729.
Hs.683360.

Genome annotation databases

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

Polymorphism databases

DMDMi55976301.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D28483 mRNA. Translation: BAA05842.1 .
BC027863 mRNA. Translation: AAH27863.1 .
BC072679 mRNA. Translation: AAH72679.1 .
CCDSi CCDS8923.1.
PIRi S47660.
RefSeqi NP_002889.1. NM_002898.3.
XP_006719607.1. XM_006719544.1.
UniGenei Hs.505729.
Hs.683360.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1X4E NMR - A 58-129 [» ]
ProteinModelPortali Q15434.
SMRi Q15434. Positions 44-218.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111874. 11 interactions.
IntActi Q15434. 3 interactions.
STRINGi 9606.ENSP00000262031.

PTM databases

PhosphoSitei Q15434.

Polymorphism databases

DMDMi 55976301.

Proteomic databases

MaxQBi Q15434.
PaxDbi Q15434.
PRIDEi Q15434.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262031 ; ENSP00000262031 ; ENSG00000076067 .
GeneIDi 5939.
KEGGi hsa:5939.
UCSCi uc001sln.2. human.

Organism-specific databases

CTDi 5939.
GeneCardsi GC12P056915.
HGNCi HGNC:9909. RBMS2.
HPAi HPA039225.
MIMi 602387. gene.
neXtProti NX_Q15434.
PharmGKBi PA34275.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG320163.
GeneTreei ENSGT00760000118913.
HOGENOMi HOG000008467.
HOVERGENi HBG053108.
InParanoidi Q15434.
OMAi PGMDHPL.
PhylomeDBi Q15434.
TreeFami TF314644.

Miscellaneous databases

EvolutionaryTracei Q15434.
GenomeRNAii 5939.
NextBioi 23154.
PROi Q15434.
SOURCEi Search...

Gene expression databases

Bgeei Q15434.
CleanExi HS_RBMS2.
ExpressionAtlasi Q15434. baseline and differential.
Genevestigatori Q15434.

Family and domain databases

Gene3Di 3.30.70.330. 2 hits.
InterProi IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view ]
Pfami PF00076. RRM_1. 2 hits.
[Graphical view ]
SMARTi SM00360. RRM. 2 hits.
[Graphical view ]
PROSITEi PS50102. RRM. 2 hits.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 124 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