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Q9Y2W2

- WBP11_HUMAN

UniProt

Q9Y2W2 - WBP11_HUMAN

Protein

WW domain-binding protein 11

Gene

WBP11

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    Activates pre-mRNA splicing. May inhibit PP1 phosphatase activity.3 Publications

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. protein phosphatase type 1 regulator activity Source: Ensembl
    4. single-stranded DNA binding Source: ProtInc
    5. WW domain binding Source: UniProtKB

    GO - Biological processi

    1. mRNA processing Source: UniProtKB-KW
    2. RNA splicing Source: UniProtKB-KW
    3. rRNA processing Source: UniProtKB-KW

    Keywords - Biological processi

    mRNA processing, mRNA splicing, rRNA processing

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    WW domain-binding protein 11
    Short name:
    WBP-11
    Alternative name(s):
    Npw38-binding protein
    Short name:
    NpwBP
    SH3 domain-binding protein SNP70
    Splicing factor that interacts with PQBP-1 and PP1
    Gene namesi
    Name:WBP11
    Synonyms:NPWBP, SIPP1, SNP70
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:16461. WBP11.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: Predominantly located in the nucleus with granular heterogeneous distribution. Excluded from nucleoli in interphase cells, distributed throughout cytoplasm in dividing cells. Colocalized with SC35 and U2B in the nucleus. In the cytoplasm, associates with the intermediate filament protein vimentin.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. nuclear speck Source: Ensembl
    3. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi192 – 1921R → A: Loss of PQBP1-binding; when associated with A-197 and A-198. 1 Publication
    Mutagenesisi197 – 1971R → A: Loss of PQBP1-binding; when associated with A-192 and A-198. 1 Publication
    Mutagenesisi198 – 1981K → A: Loss of PQBP1-binding; when associated with A-192 and A-197. 1 Publication

    Organism-specific databases

    PharmGKBiPA38144.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 641641WW domain-binding protein 11PRO_0000065945Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei13 – 131N6-acetyllysine1 Publication
    Modified residuei181 – 1811Phosphoserine1 Publication
    Modified residuei237 – 2371Phosphoserine3 Publications
    Modified residuei279 – 2791Phosphoserine2 Publications
    Modified residuei283 – 2831Phosphoserine2 Publications
    Modified residuei353 – 3531Phosphoserine2 Publications
    Modified residuei361 – 3611Phosphoserine2 Publications
    Modified residuei364 – 3641Phosphoserine2 Publications
    Modified residuei565 – 5651N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y2W2.
    PaxDbiQ9Y2W2.
    PeptideAtlasiQ9Y2W2.
    PRIDEiQ9Y2W2.

    PTM databases

    PhosphoSiteiQ9Y2W2.

    Expressioni

    Tissue specificityi

    Ubiquitous. Highly expressed in the heart, pancreas, kidney skeletal muscle, placenta and brain (at protein level). Weakly expressed in liver and lung.1 Publication

    Gene expression databases

    ArrayExpressiQ9Y2W2.
    BgeeiQ9Y2W2.
    CleanExiHS_WBP11.
    GenevestigatoriQ9Y2W2.

    Organism-specific databases

    HPAiHPA040037.
    HPA046403.
    HPA049126.

    Interactioni

    Subunit structurei

    Interacts with PPP1CA, PPP1CB and PPP1CC By similarity. Interacts via the PGR motif with PQBP1 in the nucleus. Interacts with the WW domains of WBP4.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Q99IB83EBI-714455,EBI-6927928From a different organism.
    PCBP1Q153652EBI-714455,EBI-946095

    Protein-protein interaction databases

    BioGridi119702. 27 interactions.
    IntActiQ9Y2W2. 21 interactions.
    MINTiMINT-112641.
    STRINGi9606.ENSP00000261167.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y2W2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 4545Required for nuclear importBy similarityAdd
    BLAST
    Regioni217 – 2215Interaction with PP1By similarity
    Regioni306 – 3105Interaction with PP1By similarity

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili75 – 13359Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi455 – 46612PGRAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi140 – 20970Pro-richAdd
    BLAST
    Compositional biasi246 – 29752Asp-richAdd
    BLAST
    Compositional biasi319 – 3224Poly-Lys
    Compositional biasi393 – 538146Pro-richAdd
    BLAST

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG264066.
    HOGENOMiHOG000154840.
    HOVERGENiHBG056793.
    InParanoidiQ9Y2W2.
    KOiK12866.
    OMAiRGHDDDM.
    OrthoDBiEOG7RNK1J.
    PhylomeDBiQ9Y2W2.
    TreeFamiTF323226.

    Family and domain databases

    InterProiIPR019007. WW_dom-bd_prot_11.
    [Graphical view]
    PfamiPF09429. Wbp11. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9Y2W2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGRRSTSSTK SGKFMNPTDQ ARKEARKREL KKNKKQRMMV RAAVLKMKDP    50
    KQIIRDMEKL DEMEFNPVQQ PQLNEKVLKD KRKKLRETFE RILRLYEKEN 100
    PDIYKELRKL EVEYEQKRAQ LSQYFDAVKN AQHVEVESIP LPDMPHAPSN 150
    ILIQDIPLPG AQPPSILKKT SAYGPPTRAV SILPLLGHGV PRLPPGRKPP 200
    GPPPGPPPPQ VVQMYGRKVG FALDLPPRRR DEDMLYSPEL AQRGHDDDVS 250
    STSEDDGYPE DMDQDKHDDS TDDSDTDKSD GESDGDEFVH RDNGERDNNE 300
    EKKSGLSVRF ADMPGKSRKK KKNMKELTPL QAMMLRMAGQ EIPEEGREVE 350
    EFSEDDDEDD SDDSEAEKQS QKQHKEESHS DGTSTASSQQ QAPPQSVPPS 400
    QIQAPPMPGP PPLGPPPAPP LRPPGPPTGL PPGPPPGAPP FLRPPGMPGL 450
    RGPLPRLLPP GPPPGRPPGP PPGPPPGLPP GPPPRGPPPR LPPPAPPGIP 500
    PPRPGMMRPP LVPPLGPAPP GLFPPAPLPN PGVLSAPPNL IQRPKADDTS 550
    AATIEKKATA TISAKPQITN PKAEITRFVP TALRVRRENK GATAAPQRKS 600
    EDDSAVPLAK AAPKSGPSVP VSVQTKDDVY EAFMKEMEGL L 641
    Length:641
    Mass (Da):69,998
    Last modified:November 1, 1999 - v1
    Checksum:iC94F9687D132CE77
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB029309 mRNA. Translation: BAA88410.1.
    AF118023 mRNA. Translation: AAD30425.1.
    BC001621 mRNA. Translation: AAH01621.1.
    BC016441 mRNA. Translation: AAH16441.2.
    BC023532 mRNA. Translation: AAH23532.1.
    CCDSiCCDS8666.1.
    RefSeqiNP_057396.1. NM_016312.2.
    UniGeneiHs.655138.

    Genome annotation databases

    EnsembliENST00000261167; ENSP00000261167; ENSG00000084463.
    GeneIDi51729.
    KEGGihsa:51729.
    UCSCiuc001rci.3. human.

    Polymorphism databases

    DMDMi74735242.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB029309 mRNA. Translation: BAA88410.1 .
    AF118023 mRNA. Translation: AAD30425.1 .
    BC001621 mRNA. Translation: AAH01621.1 .
    BC016441 mRNA. Translation: AAH16441.2 .
    BC023532 mRNA. Translation: AAH23532.1 .
    CCDSi CCDS8666.1.
    RefSeqi NP_057396.1. NM_016312.2.
    UniGenei Hs.655138.

    3D structure databases

    ProteinModelPortali Q9Y2W2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119702. 27 interactions.
    IntActi Q9Y2W2. 21 interactions.
    MINTi MINT-112641.
    STRINGi 9606.ENSP00000261167.

    PTM databases

    PhosphoSitei Q9Y2W2.

    Polymorphism databases

    DMDMi 74735242.

    Proteomic databases

    MaxQBi Q9Y2W2.
    PaxDbi Q9Y2W2.
    PeptideAtlasi Q9Y2W2.
    PRIDEi Q9Y2W2.

    Protocols and materials databases

    DNASUi 51729.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000261167 ; ENSP00000261167 ; ENSG00000084463 .
    GeneIDi 51729.
    KEGGi hsa:51729.
    UCSCi uc001rci.3. human.

    Organism-specific databases

    CTDi 51729.
    GeneCardsi GC12M014939.
    HGNCi HGNC:16461. WBP11.
    HPAi HPA040037.
    HPA046403.
    HPA049126.
    neXtProti NX_Q9Y2W2.
    PharmGKBi PA38144.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG264066.
    HOGENOMi HOG000154840.
    HOVERGENi HBG056793.
    InParanoidi Q9Y2W2.
    KOi K12866.
    OMAi RGHDDDM.
    OrthoDBi EOG7RNK1J.
    PhylomeDBi Q9Y2W2.
    TreeFami TF323226.

    Miscellaneous databases

    ChiTaRSi WBP11. human.
    GeneWikii WBP11.
    GenomeRNAii 51729.
    NextBioi 55792.
    PROi Q9Y2W2.

    Gene expression databases

    ArrayExpressi Q9Y2W2.
    Bgeei Q9Y2W2.
    CleanExi HS_WBP11.
    Genevestigatori Q9Y2W2.

    Family and domain databases

    InterProi IPR019007. WW_dom-bd_prot_11.
    [Graphical view ]
    Pfami PF09429. Wbp11. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Association of two nuclear proteins, Npw38 and NpwBP, via the interaction between the WW domain and a novel proline-rich motif containing glycine and arginine."
      Komuro A., Saeki M., Kato S.
      J. Biol. Chem. 274:36513-36519(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-25, FUNCTION, INTERACTION WITH PQBP1, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-192; ARG-197 AND LYS-198.
    2. "A nuclear SH3 domain-binding protein that colocalizes with mRNA splicing factors and intermediate filament-containing perinuclear networks."
      Craggs G., Finan P.M., Lawson D., Wingfield J., Perera T., Gadher S., Totty N.F., Kellie S.
      J. Biol. Chem. 276:30552-30560(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
    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: Eye, Muscle and Placenta.
    4. "SIPP1, a novel pre-mRNA splicing factor and interactor of protein phosphatase-1."
      Llorian M., Beullens M., Andres I., Ortiz J.M., Bollen M.
      Biochem. J. 378:229-238(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    5. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-279 AND SER-283, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "Structure and function of the two tandem WW domains of the pre-mRNA splicing factor FBP21 (formin-binding protein 21)."
      Huang X., Beullens M., Zhang J., Zhou Y., Nicolaescu E., Lesage B., Hu Q., Wu J., Bollen M., Shi Y.
      J. Biol. Chem. 284:25375-25387(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH WBP4.
    8. "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-181; SER-353; SER-361 AND SER-364, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    9. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-13, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Y65C missense mutation in the WW domain of the Golabi-Ito-Hall syndrome protein PQBP1 affects its binding activity and deregulates pre-mRNA splicing."
      Tapia V.E., Nicolaescu E., McDonald C.B., Musi V., Oka T., Inayoshi Y., Satteson A.C., Mazack V., Humbert J., Gaffney C.J., Beullens M., Schwartz C.E., Landgraf C., Volkmer R., Pastore A., Farooq A., Bollen M., Sudol M.
      J. Biol. Chem. 285:19391-19401(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PQBP1.
    11. "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-237, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237; SER-279; SER-283; SER-353; SER-361 AND SER-364, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiWBP11_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y2W2
    Secondary accession number(s): Q96AY8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 13, 2005
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 110 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 12
      Human chromosome 12: entries, gene names and cross-references to MIM

    External Data

    Dasty 3