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Q15434

- RBMS2_HUMAN

UniProt

Q15434 - RBMS2_HUMAN

Protein

RNA-binding motif, single-stranded-interacting protein 2

Gene

RBMS2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    GO - Molecular functioni

    1. nucleotide binding Source: InterPro
    2. poly(A) RNA binding Source: UniProtKB
    3. RNA binding Source: ProtInc

    GO - Biological processi

    1. RNA processing Source: ProtInc

    Keywords - Ligandi

    RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    RNA-binding motif, single-stranded-interacting protein 2
    Alternative name(s):
    Suppressor of CDC2 with RNA-binding motif 3
    Gene namesi
    Name:RBMS2
    Synonyms:SCR3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:9909. RBMS2.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34275.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 407407RNA-binding motif, single-stranded-interacting protein 2PRO_0000081800Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei106 – 1061Phosphoserine3 Publications
    Modified residuei269 – 2691Phosphothreonine1 Publication
    Modified residuei280 – 2801Phosphoserine2 Publications
    Modified residuei285 – 2851Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ15434.
    PaxDbiQ15434.
    PRIDEiQ15434.

    PTM databases

    PhosphoSiteiQ15434.

    Expressioni

    Gene expression databases

    ArrayExpressiQ15434.
    BgeeiQ15434.
    CleanExiHS_RBMS2.
    GenevestigatoriQ15434.

    Organism-specific databases

    HPAiHPA039225.

    Interactioni

    Protein-protein interaction databases

    BioGridi111874. 11 interactions.
    IntActiQ15434. 3 interactions.
    STRINGi9606.ENSP00000262031.

    Structurei

    Secondary structure

    1
    407
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi58 – 625
    Helixi69 – 735
    Turni77 – 793
    Beta strandi82 – 876
    Beta strandi91 – 933
    Beta strandi98 – 1058
    Helixi107 – 12014
    Beta strandi124 – 1263

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1X4ENMR-A58-129[»]
    ProteinModelPortaliQ15434.
    SMRiQ15434. Positions 44-218.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ15434.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini56 – 12974RRM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini135 – 22086RRM 2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 2 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG320163.
    HOGENOMiHOG000008467.
    HOVERGENiHBG053108.
    InParanoidiQ15434.
    OMAiPGMDHPL.
    PhylomeDBiQ15434.
    TreeFamiTF314644.

    Family and domain databases

    Gene3Di3.30.70.330. 2 hits.
    InterProiIPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view]
    PfamiPF00076. RRM_1. 2 hits.
    [Graphical view]
    SMARTiSM00360. RRM. 2 hits.
    [Graphical view]
    PROSITEiPS50102. RRM. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q15434-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLLSVTSRPG ISTFGYNRNN KKPYVSLAQQ MAPPSPSNST PNSSSGSNGN    50
    DQLSKTNLYI RGLQPGTTDQ DLVKLCQPYG KIVSTKAILD KTTNKCKGYG 100
    FVDFDSPSAA QKAVTALKAS GVQAQMAKQQ EQDPTNLYIS NLPLSMDEQE 150
    LEGMLKPFGQ VISTRILRDT SGTSRGVGFA RMESTEKCEA IITHFNGKYI 200
    KTPPGVPAPS DPLLCKFADG GPKKRQNQGK FVQNGRAWPR NADMGVMALT 250
    YDPTTALQNG FYPAPYNITP NRMLAQSALS PYLSSPVSSY QRVTQTSPLQ 300
    VPNPSWMHHH SYLMQPSGSV LTPGMDHPIS LQPASMMGPL TQQLGHLSLS 350
    STGTYMPTAA AMQGAYISQY TPVPSSSVSV EESSGQQNQV AVDAPSEHGV 400
    YSFQFNK 407
    Length:407
    Mass (Da):43,959
    Last modified:November 1, 1996 - v1
    Checksum:iBAFC794E2318BE0A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D28483 mRNA. Translation: BAA05842.1.
    BC027863 mRNA. Translation: AAH27863.1.
    BC072679 mRNA. Translation: AAH72679.1.
    CCDSiCCDS8923.1.
    PIRiS47660.
    RefSeqiNP_002889.1. NM_002898.3.
    XP_006719607.1. XM_006719544.1.
    UniGeneiHs.505729.
    Hs.683360.

    Genome annotation databases

    EnsembliENST00000262031; ENSP00000262031; ENSG00000076067.
    GeneIDi5939.
    KEGGihsa:5939.
    UCSCiuc001sln.2. human.

    Polymorphism databases

    DMDMi55976301.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D28483 mRNA. Translation: BAA05842.1 .
    BC027863 mRNA. Translation: AAH27863.1 .
    BC072679 mRNA. Translation: AAH72679.1 .
    CCDSi CCDS8923.1.
    PIRi S47660.
    RefSeqi NP_002889.1. NM_002898.3.
    XP_006719607.1. XM_006719544.1.
    UniGenei Hs.505729.
    Hs.683360.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1X4E NMR - A 58-129 [» ]
    ProteinModelPortali Q15434.
    SMRi Q15434. Positions 44-218.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111874. 11 interactions.
    IntActi Q15434. 3 interactions.
    STRINGi 9606.ENSP00000262031.

    PTM databases

    PhosphoSitei Q15434.

    Polymorphism databases

    DMDMi 55976301.

    Proteomic databases

    MaxQBi Q15434.
    PaxDbi Q15434.
    PRIDEi Q15434.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262031 ; ENSP00000262031 ; ENSG00000076067 .
    GeneIDi 5939.
    KEGGi hsa:5939.
    UCSCi uc001sln.2. human.

    Organism-specific databases

    CTDi 5939.
    GeneCardsi GC12P056915.
    HGNCi HGNC:9909. RBMS2.
    HPAi HPA039225.
    MIMi 602387. gene.
    neXtProti NX_Q15434.
    PharmGKBi PA34275.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG320163.
    HOGENOMi HOG000008467.
    HOVERGENi HBG053108.
    InParanoidi Q15434.
    OMAi PGMDHPL.
    PhylomeDBi Q15434.
    TreeFami TF314644.

    Miscellaneous databases

    EvolutionaryTracei Q15434.
    GenomeRNAii 5939.
    NextBioi 23154.
    PROi Q15434.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q15434.
    Bgeei Q15434.
    CleanExi HS_RBMS2.
    Genevestigatori Q15434.

    Family and domain databases

    Gene3Di 3.30.70.330. 2 hits.
    InterProi IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view ]
    Pfami PF00076. RRM_1. 2 hits.
    [Graphical view ]
    SMARTi SM00360. RRM. 2 hits.
    [Graphical view ]
    PROSITEi PS50102. RRM. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "SCR: novel human suppressors of cdc2/cdc13 mutants of Schizosaccharomyces pombe harbour motifs for RNA binding proteins."
      Kanaoka Y., Nojima H.
      Nucleic Acids Res. 22:2687-2693(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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: Lung and Skin.
    3. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; THR-269; SER-280 AND SER-285, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    5. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    8. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; SER-280 AND SER-285, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Solution structure of RRM domain in RNA binding motif, single-stranded interacting protein 2."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 58-129.

    Entry informationi

    Entry nameiRBMS2_HUMAN
    AccessioniPrimary (citable) accession number: Q15434
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 23, 2004
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 123 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3