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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
  • ribosomal large subunit binding Source: Ensembl
  • RNA binding Source: ProtInc

GO - Biological processi

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
RNPL
Gene namesi
Name:RBM3
Synonyms:RNPL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:9900. RBM3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34265.

Polymorphism and mutation databases

BioMutaiRBM3.
DMDMi1710620.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 157157RNA-binding protein 3PRO_0000081752Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei105 – 1051Dimethylated arginine; in A2780 ovarian carcinoma cell line1 Publication
Modified residuei147 – 1471Phosphoserine1 Publication
Modified residuei155 – 1551Phosphotyrosine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

MaxQBiP98179.
PaxDbiP98179.
PeptideAtlasiP98179.
PRIDEiP98179.

PTM databases

PhosphoSiteiP98179.

Expressioni

Inductioni

Up-regulated by hypoxia.1 Publication

Gene expression databases

BgeeiP98179.
CleanExiHS_RBM3.
ExpressionAtlasiP98179. baseline and differential.
GenevestigatoriP98179.

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

WithEntry#Exp.IntActNotes
HNRNPKP619783EBI-2949699,EBI-304185
HNRPKQ6IBN13EBI-2949699,EBI-3440248
KHDRBS2Q5VWX13EBI-2949699,EBI-742808
RBMXP381593EBI-2949699,EBI-743526
RBMY1A1P0DJD33EBI-2949699,EBI-8638511
RBMY1JQ154153EBI-2949699,EBI-8642021
SNRPAP090123EBI-2949699,EBI-607085
VLTF3P683182EBI-2949699,EBI-7366338From a different organism.

Protein-protein interaction databases

BioGridi111870. 27 interactions.
IntActiP98179. 11 interactions.
MINTiMINT-5002714.
STRINGi9606.ENSP00000365946.

Structurei

3D structure databases

ProteinModelPortaliP98179.
SMRiP98179. Positions 1-126.
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 – 14962Gly-richAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0724.
GeneTreeiENSGT00710000106295.
HOGENOMiHOG000276232.
HOVERGENiHBG107480.
InParanoidiP98179.
KOiK13186.
OMAiNFNTDER.
PhylomeDBiP98179.
TreeFamiTF354331.

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]
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

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.2. 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. Positions 1-126.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111870. 27 interactions.
IntActiP98179. 11 interactions.
MINTiMINT-5002714.
STRINGi9606.ENSP00000365946.

PTM databases

PhosphoSiteiP98179.

Polymorphism and mutation databases

BioMutaiRBM3.
DMDMi1710620.

Proteomic databases

MaxQBiP98179.
PaxDbiP98179.
PeptideAtlasiP98179.
PRIDEiP98179.

Protocols and materials databases

DNASUi5935.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000376755; ENSP00000365946; ENSG00000102317.
ENST00000376759; ENSP00000365950; ENSG00000102317.
GeneIDi5935.
KEGGihsa:5935.
UCSCiuc004dkf.2. human.

Organism-specific databases

CTDi5935.
GeneCardsiGC0XP048432.
HGNCiHGNC:9900. RBM3.
HPAiCAB062559.
HPA003624.
MIMi300027. gene.
neXtProtiNX_P98179.
PharmGKBiPA34265.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0724.
GeneTreeiENSGT00710000106295.
HOGENOMiHOG000276232.
HOVERGENiHBG107480.
InParanoidiP98179.
KOiK13186.
OMAiNFNTDER.
PhylomeDBiP98179.
TreeFamiTF354331.

Miscellaneous databases

ChiTaRSiRBM3. human.
GeneWikiiRBM3.
GenomeRNAii5935.
NextBioi23136.
PROiP98179.
SOURCEiSearch...

Gene expression databases

BgeeiP98179.
CleanExiHS_RBM3.
ExpressionAtlasiP98179. baseline and differential.
GenevestigatoriP98179.

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]
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiRBM3_HUMAN
AccessioniPrimary (citable) accession number: P98179
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 29, 2015
This is version 127 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

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
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.