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Protein

RNA-binding protein 3

Gene

RBM3

Organism
Homo sapiens (Human)
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 (By similarity).By similarity

GO - Molecular functioni

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

GO - Biological processi

  • positive regulation of translation Source: UniProtKB
  • regulation of translation Source: UniProtKB
  • RNA processing Source: ProtInc

Keywordsi

Molecular functionRNA-binding
Biological processStress response

Names & Taxonomyi

Protein namesi
Recommended name:
RNA-binding protein 3
Alternative name(s):
RNA-binding motif protein 3
RNPL
Gene namesi
Name:RBM3
Synonyms:RNPL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:9900. RBM3.

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cell projection, Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi5935.
OpenTargetsiENSG00000102317.
PharmGKBiPA34265.

Polymorphism and mutation databases

BioMutaiRBM3.
DMDMi1710620.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000817521 – 157RNA-binding protein 3Add BLAST157

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei47Omega-N-methylarginineCombined sources1
Modified residuei105Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei105Dimethylated arginine; in A2780 ovarian carcinoma cell line1 Publication1
Modified residuei105Omega-N-methylarginine; alternateCombined sources1
Modified residuei121Omega-N-methylarginineCombined sources1
Modified residuei131Omega-N-methylarginineCombined sources1
Modified residuei147PhosphoserineCombined sources1
Modified residuei155PhosphotyrosineCombined sources1

Post-translational modificationi

Arg-105 is dimethylated, probably to asymmetric dimethylarginine.
Phosphorylated.By similarity

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

EPDiP98179.
MaxQBiP98179.
PaxDbiP98179.
PeptideAtlasiP98179.
PRIDEiP98179.
TopDownProteomicsiP98179.

PTM databases

iPTMnetiP98179.
PhosphoSitePlusiP98179.

Expressioni

Inductioni

Up-regulated by hypoxia.1 Publication

Gene expression databases

BgeeiENSG00000102317.
CleanExiHS_RBM3.
ExpressionAtlasiP98179. baseline and differential.
GenevisibleiP98179. HS.

Organism-specific databases

HPAiCAB062559.
HPA003624.

Interactioni

Subunit structurei

Interacts with RPL4. Associates with the 60S ribosomal subunits in an RNA-independent manner. Associates with ribosomes (By similarity).By similarity

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi111870. 46 interactors.
IntActiP98179. 23 interactors.
MINTiMINT-5002714.
STRINGi9606.ENSP00000365946.

Structurei

3D structure databases

ProteinModelPortaliP98179.
SMRiP98179.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini6 – 84RRMPROSITE-ProRule annotationAdd BLAST79

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi88 – 149Gly-richAdd BLAST62

Phylogenomic databases

eggNOGiKOG0118. Eukaryota.
COG0724. LUCA.
GeneTreeiENSGT00710000106295.
HOGENOMiHOG000276232.
HOVERGENiHBG107480.
InParanoidiP98179.
KOiK13186.
OMAiNFNTDER.
OrthoDBiEOG090A0FPM.
PhylomeDBiP98179.
TreeFamiTF354331.

Family and domain databases

CDDicd12449. RRM_CIRBP_RBM3. 1 hit.
Gene3Di3.30.70.330. 1 hit.
InterProiView protein in InterPro
IPR012677. Nucleotide-bd_a/b_plait.
IPR034278. RBM3/CIRBP_RRM.
IPR000504. RRM_dom.
PfamiView protein in Pfam
PF00076. RRM_1. 1 hit.
SMARTiView protein in SMART
SM00360. RRM. 1 hit.
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiView protein in PROSITE
PS50102. RRM. 1 hit.

Sequencei

Sequence statusi: Complete.

P98179-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSEEGKLFV GGLNFNTDEQ ALEDHFSSFG PISEVVVVKD RETQRSRGFG
60 70 80 90 100
FITFTNPEHA SVAMRAMNGE SLDGRQIRVD HAGKSARGTR GGGFGAHGRG
110 120 130 140 150
RSYSRGGGDQ GYGSGRYYDS RPGGYGYGYG RSRDYNGRNQ GGYDRYSGGN

YRDNYDN
Length:157
Mass (Da):17,170
Last modified:October 1, 1996 - v1
Checksum:i91C12E2A3E32CFA4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28686 mRNA. Translation: AAB17212.1.
AF196969 Genomic DNA. No translation available.
BC006825 mRNA. Translation: AAH06825.1.
CCDSiCCDS14301.1.
PIRiG01859.
RefSeqiNP_006734.1. NM_006743.4.
UniGeneiHs.301404.

Genome annotation databases

EnsembliENST00000376755; ENSP00000365946; ENSG00000102317.
ENST00000376759; ENSP00000365950; ENSG00000102317.
GeneIDi5935.
KEGGihsa:5935.
UCSCiuc004dkf.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U28686 mRNA. Translation: AAB17212.1.
AF196969 Genomic DNA. No translation available.
BC006825 mRNA. Translation: AAH06825.1.
CCDSiCCDS14301.1.
PIRiG01859.
RefSeqiNP_006734.1. NM_006743.4.
UniGeneiHs.301404.

3D structure databases

ProteinModelPortaliP98179.
SMRiP98179.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111870. 46 interactors.
IntActiP98179. 23 interactors.
MINTiMINT-5002714.
STRINGi9606.ENSP00000365946.

PTM databases

iPTMnetiP98179.
PhosphoSitePlusiP98179.

Polymorphism and mutation databases

BioMutaiRBM3.
DMDMi1710620.

Proteomic databases

EPDiP98179.
MaxQBiP98179.
PaxDbiP98179.
PeptideAtlasiP98179.
PRIDEiP98179.
TopDownProteomicsiP98179.

Protocols and materials databases

DNASUi5935.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000376755; ENSP00000365946; ENSG00000102317.
ENST00000376759; ENSP00000365950; ENSG00000102317.
GeneIDi5935.
KEGGihsa:5935.
UCSCiuc004dkf.3. human.

Organism-specific databases

CTDi5935.
DisGeNETi5935.
GeneCardsiRBM3.
HGNCiHGNC:9900. RBM3.
HPAiCAB062559.
HPA003624.
MIMi300027. gene.
neXtProtiNX_P98179.
OpenTargetsiENSG00000102317.
PharmGKBiPA34265.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0118. Eukaryota.
COG0724. LUCA.
GeneTreeiENSGT00710000106295.
HOGENOMiHOG000276232.
HOVERGENiHBG107480.
InParanoidiP98179.
KOiK13186.
OMAiNFNTDER.
OrthoDBiEOG090A0FPM.
PhylomeDBiP98179.
TreeFamiTF354331.

Miscellaneous databases

ChiTaRSiRBM3. human.
GeneWikiiRBM3.
GenomeRNAii5935.
PROiP98179.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000102317.
CleanExiHS_RBM3.
ExpressionAtlasiP98179. baseline and differential.
GenevisibleiP98179. HS.

Family and domain databases

CDDicd12449. RRM_CIRBP_RBM3. 1 hit.
Gene3Di3.30.70.330. 1 hit.
InterProiView protein in InterPro
IPR012677. Nucleotide-bd_a/b_plait.
IPR034278. RBM3/CIRBP_RRM.
IPR000504. RRM_dom.
PfamiView protein in Pfam
PF00076. RRM_1. 1 hit.
SMARTiView protein in SMART
SM00360. RRM. 1 hit.
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiView protein in PROSITE
PS50102. RRM. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRBM3_HUMAN
AccessioniPrimary (citable) accession number: P98179
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: February 15, 2017
This is version 144 of the entry and version 1 of the sequence. See 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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.