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

Contribute

Send feedback

Read comments (?) or add your own

Q15434 (RBMS2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 111. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	407 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Subcellular location	Nucleus Potential.
Sequence similarities	Contains 2 RRM (RNA recognition motif) domains.

Ontologies

Keywords
Cellular component	Nucleus
Domain	Repeat
Ligand	RNA-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA processing Traceable author statement Ref.1. Source: ProtInc
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	RNA binding Traceable author statement Ref.1. Source: ProtInc nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 407

407

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

PRO_0000081800

Regions

Domain

56 – 129

RRM 1

Domain

135 – 220

RRM 2

Amino acid modifications

Modified residue

106

Phosphoserine Ref.4 Ref.6 Ref.7

Modified residue

269

Phosphothreonine Ref.4

Modified residue

280

Phosphoserine Ref.4 Ref.7

Modified residue

285

Phosphoserine Ref.4 Ref.7

Secondary structure

407

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q15434 [UniParc].

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

FASTA

407

43,959

        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' referencesShow '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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[5]	"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].
[6]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[7]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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.

IPI

IPI00003706.

PIR

S47660.

RefSeq

NP_002889.1. NM_002898.3.

UniGene

Hs.505729.
Hs.683360.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1X4E	NMR	-	A	58-129	[»]

ProteinModelPortal

Q15434.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q15434. 2 interactions.

STRING

9606.ENSP00000262031.

PTM databases

PhosphoSite

Q15434.

Polymorphism databases

DMDM

55976301.

Proteomic databases

PaxDb

Q15434.

PRIDE

Q15434.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000262031; ENSP00000262031; ENSG00000076067.

GeneID

5939.

KEGG

hsa:5939.

UCSC

uc001sln.2. human.

Organism-specific databases

CTD

5939.

GeneCards

GC12P056915.

HGNC

HGNC:9909. RBMS2.

HPA

HPA039225.

MIM

602387. gene.

neXtProt

NX_Q15434.

PharmGKB

PA34275.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG320163.

HOGENOM

HOG000008467.

HOVERGEN

HBG053108.

InParanoid

Q15434.

OMA

SQQMAPP.

OrthoDB

EOG469QV2.

PhylomeDB

Q15434.

Gene expression databases

ArrayExpress

Q15434.

Bgee

Q15434.

CleanEx

HS_RBMS2.

Genevestigator

Q15434.

GermOnline

ENSG00000076067. Homo sapiens.

Family and domain databases

Gene3D

3.30.70.330. 2 hits.

InterPro

IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]

Pfam

PF00076. RRM_1. 2 hits.
[Graphical view]

SMART

SM00360. RRM. 2 hits.
[Graphical view]

PROSITE

PS50102. RRM. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q15434.

GenomeRNAi

5939.

NextBio

23154.

SOURCE

Search...

Entry information

Entry name

RBMS2_HUMAN

Accession

Primary (citable) accession number: Q15434

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 23, 2004
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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

Human chromosome 12

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

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents