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P98179

- RBM3_HUMAN

UniProt

P98179 - RBM3_HUMAN

Protein

Putative RNA-binding protein 3

Gene

RBM3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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

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

    GO - Biological processi

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

    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

    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 3PRO_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.
    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.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.
    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.
    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.
    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...
    MobiDBi 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 .
    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

    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: October 1, 2014
    This is version 122 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