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P98179

- RBM3_HUMAN

UniProt

P98179 - RBM3_HUMAN

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Protein
Putative RNA-binding protein 3
Gene
RBM3, RNPL
Organism
Homo sapiens (Human)
Status
Reviewed - 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.

GO - Molecular functioni

  1. RNA binding Source: ProtInc
  2. nucleotide binding Source: InterPro
  3. poly(A) RNA binding Source: UniProtKB
  4. protein binding Source: IntAct
  5. ribosomal large subunit binding Source: Ensembl
Complete GO annotation...

GO - Biological processi

  1. RNA processing Source: ProtInc
  2. positive regulation of translation Source: UniProtKB
  3. production of miRNAs involved in gene silencing by miRNA Source: Ensembl
  4. regulation of translation Source: UniProtKB
  5. response to cold Source: Ensembl
  6. translation Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Stress response

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Putative 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: Chromosome X

Organism-specific databases

HGNCiHGNC:9900. RBM3.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. dendrite Source: UniProtKB
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34265.

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei105 – 1051Dimethylated arginine; in A2780 ovarian carcinoma cell line1 Publication
Modified residuei105 – 1051Omega-N-methylated arginine1 Publication
Modified residuei147 – 1471Phosphoserine1 Publication
Modified residuei155 – 1551Phosphotyrosine1 Publication

Post-translational modificationi

Arg-105 is dimethylated, probably to asymmetric dimethylarginine.1 Publication
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

ArrayExpressiP98179.
BgeeiP98179.
CleanExiHS_RBM3.
GenevestigatoriP98179.

Organism-specific databases

HPAiHPA003624.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
VLTF3P683182EBI-2949699,EBI-7366338From a different organism.

Protein-protein interaction databases

BioGridi111870. 19 interactions.
IntActiP98179. 4 interactions.
MINTiMINT-5002714.
STRINGi9606.ENSP00000365946.

Structurei

3D structure databases

ProteinModelPortaliP98179.
SMRiP98179. Positions 1-126.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 8479RRM
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi88 – 14962Gly-rich
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0724.
HOGENOMiHOG000276232.
HOVERGENiHBG107480.
InParanoidiP98179.
KOiK13186.
OMAiYDKYTRN.
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

MSSEEGKLFV GGLNFNTDEQ ALEDHFSSFG PISEVVVVKD RETQRSRGFG    50
FITFTNPEHA SVAMRAMNGE SLDGRQIRVD HAGKSARGTR GGGFGAHGRG 100
RSYSRGGGDQ GYGSGRYYDS RPGGYGYGYG RSRDYNGRNQ GGYDRYSGGN 150
YRDNYDN 157
Length:157
Mass (Da):17,170
Last modified:October 1, 1996 - v1
Checksum:i91C12E2A3E32CFA4
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
ENST00000598825; ENSP00000470199; ENSG00000268489.
ENST00000600134; ENSP00000471507; ENSG00000268489.
GeneIDi5935.
KEGGihsa:5935.
UCSCiuc004dkf.2. human.

Polymorphism databases

DMDMi1710620.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U28686 mRNA. Translation: AAB17212.1 .
AF196969 Genomic DNA. No translation available.
BC006825 mRNA. Translation: AAH06825.1 .
CCDSi CCDS14301.1.
PIRi G01859.
RefSeqi NP_006734.1. NM_006743.4.
UniGenei Hs.301404.

3D structure databases

ProteinModelPortali P98179.
SMRi P98179. Positions 1-126.
ModBasei Search...

Protein-protein interaction databases

BioGridi 111870. 19 interactions.
IntActi P98179. 4 interactions.
MINTi MINT-5002714.
STRINGi 9606.ENSP00000365946.

PTM databases

PhosphoSitei P98179.

Polymorphism databases

DMDMi 1710620.

Proteomic databases

MaxQBi P98179.
PaxDbi P98179.
PeptideAtlasi P98179.
PRIDEi P98179.

Protocols and materials databases

DNASUi 5935.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000376755 ; ENSP00000365946 ; ENSG00000102317 .
ENST00000376759 ; ENSP00000365950 ; ENSG00000102317 .
ENST00000598825 ; ENSP00000470199 ; ENSG00000268489 .
ENST00000600134 ; ENSP00000471507 ; ENSG00000268489 .
GeneIDi 5935.
KEGGi hsa:5935.
UCSCi uc004dkf.2. human.

Organism-specific databases

CTDi 5935.
GeneCardsi GC0XP048432.
HGNCi HGNC:9900. RBM3.
HPAi HPA003624.
MIMi 300027. gene.
neXtProti NX_P98179.
PharmGKBi PA34265.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0724.
HOGENOMi HOG000276232.
HOVERGENi HBG107480.
InParanoidi P98179.
KOi K13186.
OMAi YDKYTRN.
PhylomeDBi P98179.
TreeFami TF354331.

Miscellaneous databases

ChiTaRSi RBM3. human.
GeneWikii RBM3.
GenomeRNAii 5935.
NextBioi 23136.
PROi P98179.
SOURCEi Search...

Gene expression databases

ArrayExpressi P98179.
Bgeei P98179.
CleanExi HS_RBM3.
Genevestigatori P98179.

Family and domain databases

Gene3Di 3.30.70.330. 1 hit.
InterProi IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view ]
Pfami PF00076. RRM_1. 1 hit.
[Graphical view ]
SMARTi SM00360. RRM. 1 hit.
[Graphical view ]
PROSITEi PS50102. RRM. 1 hit.
[Graphical view ]
ProtoNeti Search...

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].

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: September 3, 2014
This is version 121 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

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