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Protein

RNA-binding protein 3

Gene

Rbm3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cold-inducible mRNA binding protein that enhances global protein synthesis at both physiological and mild hypothermic temperatures. Reduces the relative abundance of microRNAs, when overexpressed. Enhances phosphorylation of translation initiation factors and active polysome formation.1 Publication

GO - Molecular functioni

  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: MGI
  • ribosomal large subunit binding Source: MGI

GO - Biological processi

  • positive regulation of translation Source: UniProtKB
  • production of miRNAs involved in gene silencing by miRNA Source: MGI
  • regulation of translation Source: UniProtKB
  • response to cold Source: MGI
  • translation Source: MGI
Complete GO annotation...

Keywords - Biological processi

Stress response

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
RNA-binding protein 3
Alternative name(s):
RNA-binding motif protein 3
Gene namesi
Name:Rbm3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:1099460. Rbm3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 153153RNA-binding protein 3PRO_0000081753Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei103 – 1031Dimethylated arginine; alternateBy similarity
Modified residuei103 – 1031Omega-N-methylated arginine; alternateBy similarity
Modified residuei133 – 1331PhosphoserineCombined sources
Modified residuei143 – 1431PhosphoserineBy similarity
Modified residuei151 – 1511PhosphotyrosineBy similarity

Post-translational modificationi

Arg-103 is dimethylated, probably to asymmetric dimethylarginine.By similarity
Phosphorylated.By similarity

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

EPDiO89086.
PaxDbiO89086.
PRIDEiO89086.

2D gel databases

REPRODUCTION-2DPAGEIPI00130883.

PTM databases

iPTMnetiO89086.
PhosphoSiteiO89086.

Expressioni

Gene expression databases

BgeeiO89086.
CleanExiMM_RBM3.
ExpressionAtlasiO89086. baseline and differential.
GenevisibleiO89086. MM.

Interactioni

Subunit structurei

Interacts with RPL4. Associates with the 60S ribosomal subunits in an RNA-independent manner.

Protein-protein interaction databases

BioGridi202821. 2 interactions.
IntActiO89086. 3 interactions.
MINTiMINT-1649273.
STRINGi10090.ENSMUSP00000038964.

Structurei

3D structure databases

ProteinModelPortaliO89086.
SMRiO89086. Positions 1-123.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 8479RRMPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi88 – 14558Gly-richAdd
BLAST

Sequence similaritiesi

Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IQVN. Eukaryota.
ENOG410YRZ9. LUCA.
HOGENOMiHOG000276232.
HOVERGENiHBG107480.
InParanoidiO89086.
KOiK13186.
OrthoDBiEOG780RPD.
PhylomeDBiO89086.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O89086-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSEEGKLFV GGLNFNTDEQ ALEDHFSSFG PISEVVVVKD RETQRSRGFG
60 70 80 90 100
FITFTNPEHA SDAMRAMNGE SLDGRQIRVD HAGKSARGSR GGAFGGRGRS
110 120 130 140 150
YSRGGGDQGY GSGRYDSRPG GYGYGYGRSR DYSGSQGGYD RYSGGNYRDN

YDN
Length:153
Mass (Da):16,605
Last modified:November 1, 1998 - v1
Checksum:iC54A66A1A9E4FF3D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB016424 mRNA. Translation: BAA32060.1.
AY052560 mRNA. Translation: AAL10707.1.
BC006580 mRNA. Translation: AAH06580.1.
CCDSiCCDS52988.1.
RefSeqiNP_001159882.1. NM_001166410.2.
NP_001159883.1. NM_001166411.2.
UniGeneiMm.128512.
Mm.360569.

Genome annotation databases

EnsembliENSMUST00000115615; ENSMUSP00000111277; ENSMUSG00000031167.
ENSMUST00000115619; ENSMUSP00000111282; ENSMUSG00000031167.
ENSMUST00000115621; ENSMUSP00000111284; ENSMUSG00000031167.
GeneIDi19652.
KEGGimmu:19652.
UCSCiuc009sob.3. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB016424 mRNA. Translation: BAA32060.1.
AY052560 mRNA. Translation: AAL10707.1.
BC006580 mRNA. Translation: AAH06580.1.
CCDSiCCDS52988.1.
RefSeqiNP_001159882.1. NM_001166410.2.
NP_001159883.1. NM_001166411.2.
UniGeneiMm.128512.
Mm.360569.

3D structure databases

ProteinModelPortaliO89086.
SMRiO89086. Positions 1-123.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202821. 2 interactions.
IntActiO89086. 3 interactions.
MINTiMINT-1649273.
STRINGi10090.ENSMUSP00000038964.

PTM databases

iPTMnetiO89086.
PhosphoSiteiO89086.

2D gel databases

REPRODUCTION-2DPAGEIPI00130883.

Proteomic databases

EPDiO89086.
PaxDbiO89086.
PRIDEiO89086.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000115615; ENSMUSP00000111277; ENSMUSG00000031167.
ENSMUST00000115619; ENSMUSP00000111282; ENSMUSG00000031167.
ENSMUST00000115621; ENSMUSP00000111284; ENSMUSG00000031167.
GeneIDi19652.
KEGGimmu:19652.
UCSCiuc009sob.3. mouse.

Organism-specific databases

CTDi5935.
MGIiMGI:1099460. Rbm3.

Phylogenomic databases

eggNOGiENOG410IQVN. Eukaryota.
ENOG410YRZ9. LUCA.
HOGENOMiHOG000276232.
HOVERGENiHBG107480.
InParanoidiO89086.
KOiK13186.
OrthoDBiEOG780RPD.
PhylomeDBiO89086.

Miscellaneous databases

PROiO89086.
SOURCEiSearch...

Gene expression databases

BgeeiO89086.
CleanExiMM_RBM3.
ExpressionAtlasiO89086. baseline and differential.
GenevisibleiO89086. MM.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Decreased expression of mouse Rbm3, a cold-shock protein, in Sertoli cells of cryptorchid testis."
    Danno S., Itoh K., Matsuda T., Fujita J.
    Am. J. Pathol. 156:1685-1692(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "A 5' leader of Rbm3, a cold stress-induced mRNA, mediates internal initiation of translation with increased efficiency under conditions of mild hypothermia."
    Chappell S.A., Owens G.C., Mauro V.P.
    J. Biol. Chem. 276:36917-36922(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: ICR.
  3. "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].
    Strain: Czech II.
    Tissue: Mammary gland.
  4. "Cold stress-induced protein Rbm3 binds 60S ribosomal subunits, alters microRNA levels, and enhances global protein synthesis."
    Dresios J., Aschrafi A., Owens G.C., Vanderklish P.W., Edelman G.M., Mauro V.P.
    Proc. Natl. Acad. Sci. U.S.A. 102:1865-1870(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ASSOCIATION WITH RIBOSOMES.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiRBM3_MOUSE
AccessioniPrimary (citable) accession number: O89086
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: June 8, 2016
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

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.