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P98179 (RBM3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative RNA-binding protein 3
Alternative name(s):
RNA-binding motif protein 3
RNPL
Gene names
Name:RBM3
Synonyms:RNPL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length157 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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

Subcellular location

Nucleus By similarity. Cytoplasm By similarity. Cell projectiondendrite By similarity. Note: Localizes in mRNA granules in dentrites By similarity.

Induction

Up-regulated by hypoxia. Ref.6

Post-translational modification

Arg-105 is dimethylated, probably to asymmetric dimethylarginine. Ref.4

Phosphorylated By similarity.

Sequence similarities

Contains 1 RRM (RNA recognition motif) domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

VLTF3P683182EBI-2949699,EBI-7366338From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 157157Putative RNA-binding protein 3
PRO_0000081752

Regions

Domain6 – 8479RRM
Compositional bias88 – 14962Gly-rich

Amino acid modifications

Modified residue1051Dimethylated arginine; in A2780 ovarian carcinoma cell line Ref.4
Modified residue1051Omega-N-methylated arginine Ref.4
Modified residue1471Phosphoserine Ref.7
Modified residue1551Phosphotyrosine Ref.5

Sequences

Sequence LengthMass (Da)Tools
P98179 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 91C12E2A3E32CFA4

FASTA15717,170
        10         20         30         40         50         60 
MSSEEGKLFV GGLNFNTDEQ ALEDHFSSFG PISEVVVVKD RETQRSRGFG FITFTNPEHA 

        70         80         90        100        110        120 
SVAMRAMNGE SLDGRQIRVD HAGKSARGTR GGGFGAHGRG RSYSRGGGDQ GYGSGRYYDS 

       130        140        150 
RPGGYGYGYG RSRDYNGRNQ GGYDRYSGGN YRDNYDN 

« Hide

References

« Hide 'large scale' references
[1]"RBM3, a novel human gene in Xp11.23 with a putative RNA-binding domain."
Derry J.M., Kerns J.A., Francke U.
Hum. Mol. Genet. 4:2307-2311(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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].
Tissue: Placenta.
[4]Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 48-75 AND 102-131, METHYLATION AT ARG-105, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Ovarian carcinoma.
[5]"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-155, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[6]"Oxygen-regulated expression of the RNA-binding proteins RBM3 and CIRP by a HIF-1-independent mechanism."
Wellmann S., Buehrer C., Moderegger E., Zelmer A., Kirschner R., Koehne P., Fujita J., Seeger K.
J. Cell Sci. 117:1785-1794(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY HYPOXIA.
[7]"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-147, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U28686 mRNA. Translation: AAB17212.1.
AF196969 Genomic DNA. No translation available.
BC006825 mRNA. Translation: AAH06825.1.
CCDSCCDS14301.1.
PIRG01859.
RefSeqNP_006734.1. NM_006743.4.
UniGeneHs.301404.

3D structure databases

ProteinModelPortalP98179.
SMRP98179. Positions 1-126.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111870. 18 interactions.
IntActP98179. 4 interactions.
MINTMINT-5002714.
STRING9606.ENSP00000365946.

PTM databases

PhosphoSiteP98179.

Polymorphism databases

DMDM1710620.

Proteomic databases

MaxQBP98179.
PaxDbP98179.
PeptideAtlasP98179.
PRIDEP98179.

Protocols and materials databases

DNASU5935.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000376755; ENSP00000365946; ENSG00000102317.
ENST00000376759; ENSP00000365950; ENSG00000102317.
ENST00000598825; ENSP00000470199; ENSG00000268489.
ENST00000600134; ENSP00000471507; ENSG00000268489.
GeneID5935.
KEGGhsa:5935.
UCSCuc004dkf.2. human.

Organism-specific databases

CTD5935.
GeneCardsGC0XP048432.
HGNCHGNC:9900. RBM3.
HPAHPA003624.
MIM300027. gene.
neXtProtNX_P98179.
PharmGKBPA34265.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0724.
HOGENOMHOG000276232.
HOVERGENHBG107480.
InParanoidP98179.
KOK13186.
OMAYDKYTRN.
PhylomeDBP98179.
TreeFamTF354331.

Gene expression databases

ArrayExpressP98179.
BgeeP98179.
CleanExHS_RBM3.
GenevestigatorP98179.

Family and domain databases

Gene3D3.30.70.330. 1 hit.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTSM00360. RRM. 1 hit.
[Graphical view]
PROSITEPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRBM3. human.
GeneWikiRBM3.
GenomeRNAi5935.
NextBio23136.
PROP98179.
SOURCESearch...

Entry information

Entry nameRBM3_HUMAN
AccessionPrimary (citable) accession number: P98179
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 120 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

MIM cross-references

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

Human chromosome X

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