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O75554

- WBP4_HUMAN

UniProt

O75554 - WBP4_HUMAN

Protein

WW domain-binding protein 4

Gene

WBP4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 1 (01 Nov 1998)
      Previous versions | rss
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    Functioni

    Promotes pre-mRNA splicing. A spliceosome-associated protein; may play a role in cross-intron bridging of U1 and U2 snRNPs in the mammalian A complex.2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri11 – 4232Matrin-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. nucleic acid binding Source: InterPro
    2. proline-rich region binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. mRNA cis splicing, via spliceosome Source: UniProtKB

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    SignaLinkiO75554.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    WW domain-binding protein 4
    Short name:
    WBP-4
    Alternative name(s):
    Formin-binding protein 21
    WW domain-containing-binding protein 4
    Gene namesi
    Name:WBP4
    Synonyms:FBP21, FNBP21
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:12739. WBP4.

    Subcellular locationi

    Nucleus speckle 2 PublicationsPROSITE-ProRule annotation

    GO - Cellular componenti

    1. nuclear speck Source: UniProtKB
    2. nucleus Source: HPA
    3. plasma membrane Source: HPA
    4. spliceosomal complex Source: UniProtKB-KW

    Keywords - Cellular componenti

    Nucleus, Spliceosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi150 – 1501W → A: Nearly abolishes activation of pre-mRNA splicing. Abolishes interaction with WBP11. 1 Publication
    Mutagenesisi191 – 1911W → A: Nearly abolishes activation of pre-mRNA splicing. Abolishes interaction with WBP11. 1 Publication

    Organism-specific databases

    PharmGKBiPA37350.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 376376WW domain-binding protein 4PRO_0000076065Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei220 – 2201Phosphoserine2 Publications
    Modified residuei262 – 2621Phosphoserine1 Publication
    Modified residuei277 – 2771Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO75554.
    PaxDbiO75554.
    PRIDEiO75554.

    PTM databases

    PhosphoSiteiO75554.

    Expressioni

    Gene expression databases

    ArrayExpressiO75554.
    BgeeiO75554.
    CleanExiHS_WBP4.
    GenevestigatoriO75554.

    Organism-specific databases

    HPAiHPA038965.

    Interactioni

    Subunit structurei

    Associated with U2 snRNPs. Binds splicing factors SNRPB, SNRPC and SF1. Interacts via the WW domains with the Pro-rich domains of KHDRBS1/SAM68 By similarity. Interacts via the WW domains with the Pro-rich domains of WBP11.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    HTTP428583EBI-7251981,EBI-466029

    Protein-protein interaction databases

    BioGridi116363. 45 interactions.
    IntActiO75554. 2 interactions.
    MINTiMINT-127038.
    STRINGi9606.ENSP00000368801.

    Structurei

    Secondary structure

    1
    376
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi128 – 1303
    Turni134 – 1363
    Beta strandi140 – 1456
    Beta strandi148 – 1514
    Beta strandi161 – 1644
    Beta strandi168 – 1747
    Turni175 – 1773
    Beta strandi178 – 1836
    Turni184 – 1874
    Beta strandi188 – 1925

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DK1NMR-A127-163[»]
    2JXWNMR-A122-196[»]
    ProteinModelPortaliO75554.
    SMRiO75554. Positions 122-196.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO75554.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini122 – 15534WW 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini163 – 19634WW 2PROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi111 – 12515Lys-richAdd
    BLAST

    Domaini

    The WW domain recognizes the proline, glycine and methionine-rich (PGM) motif present in the splicing factors, as well as the Arg/Gly-rich-flanked Pro-rich domains found in several WW domain-binding proteins.By similarity

    Sequence similaritiesi

    Contains 1 matrin-type zinc finger.PROSITE-ProRule annotation
    Contains 2 WW domains.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri11 – 4232Matrin-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5104.
    HOGENOMiHOG000067962.
    HOVERGENiHBG053152.
    InParanoidiO75554.
    KOiK13220.
    OMAiESHEEVD.
    OrthoDBiEOG7H7930.
    PhylomeDBiO75554.
    TreeFamiTF316671.

    Family and domain databases

    InterProiIPR001202. WW_dom.
    IPR000690. Znf_C2H2_matrin.
    IPR003604. Znf_U1.
    IPR013085. Znf_U1-C.
    [Graphical view]
    PfamiPF00397. WW. 2 hits.
    PF06220. zf-U1. 1 hit.
    [Graphical view]
    SMARTiSM00456. WW. 2 hits.
    SM00451. ZnF_U1. 1 hit.
    [Graphical view]
    SUPFAMiSSF51045. SSF51045. 2 hits.
    PROSITEiPS01159. WW_DOMAIN_1. 2 hits.
    PS50020. WW_DOMAIN_2. 2 hits.
    PS50171. ZF_MATRIN. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O75554-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MADYWKSQPK KFCDYCKCWI ADNRPSVEFH ERGKNHKENV AKRISEIKQK    50
    SLDKAKEEEK ASKEFAAMEA AALKAYQEDL KRLGLESEIL EPSITPVTST 100
    IPPTSTSNQQ KEKKEKKKRK KDPSKGRWVE GITSEGYHYY YDLISGASQW 150
    EKPEGFQGDL KKTAVKTVWV EGLSEDGFTY YYNTETGESR WEKPDDFIPH 200
    TSDLPSSKVN ENSLGTLDES KSSDSHSDSD GEQEAEEGGV STETEKPKIK 250
    FKEKNKNSDG GSDPETQKEK SIQKQNSLGS NEEKSKTLKK SNPYGEWQEI 300
    KQEVESHEEV DLELPSTENE YVSTSEADGG GEPKVVFKEK TVTSLGVMAD 350
    GVAPVFKKRR TENGKSRNLR QRGDDQ 376
    Length:376
    Mass (Da):42,507
    Last modified:November 1, 1998 - v1
    Checksum:i7A122A29D4325D11
    GO
    Isoform 2 (identifier: O75554-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         26-46: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:355
    Mass (Da):40,030
    Checksum:iCB1274E9A8A9BE99
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti113 – 1131K → R in a breast cancer sample; somatic mutation. 1 Publication
    VAR_036352

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei26 – 4621Missing in isoform 2. 1 PublicationVSP_056413Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF071185 mRNA. Translation: AAC34811.1.
    AK297536 mRNA. Translation: BAH12608.1.
    AL157877 Genomic DNA. Translation: CAI13223.1.
    BC104879 mRNA. Translation: AAI04880.1.
    BC108310 mRNA. Translation: AAI08311.1.
    CCDSiCCDS9375.1.
    RefSeqiNP_009118.1. NM_007187.3.
    UniGeneiHs.411300.

    Genome annotation databases

    EnsembliENST00000379487; ENSP00000368801; ENSG00000120688.
    ENST00000542082; ENSP00000439301; ENSG00000120688.
    GeneIDi11193.
    KEGGihsa:11193.
    UCSCiuc001uxt.3. human.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF071185 mRNA. Translation: AAC34811.1 .
    AK297536 mRNA. Translation: BAH12608.1 .
    AL157877 Genomic DNA. Translation: CAI13223.1 .
    BC104879 mRNA. Translation: AAI04880.1 .
    BC108310 mRNA. Translation: AAI08311.1 .
    CCDSi CCDS9375.1.
    RefSeqi NP_009118.1. NM_007187.3.
    UniGenei Hs.411300.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DK1 NMR - A 127-163 [» ]
    2JXW NMR - A 122-196 [» ]
    ProteinModelPortali O75554.
    SMRi O75554. Positions 122-196.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116363. 45 interactions.
    IntActi O75554. 2 interactions.
    MINTi MINT-127038.
    STRINGi 9606.ENSP00000368801.

    PTM databases

    PhosphoSitei O75554.

    Proteomic databases

    MaxQBi O75554.
    PaxDbi O75554.
    PRIDEi O75554.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000379487 ; ENSP00000368801 ; ENSG00000120688 .
    ENST00000542082 ; ENSP00000439301 ; ENSG00000120688 .
    GeneIDi 11193.
    KEGGi hsa:11193.
    UCSCi uc001uxt.3. human.

    Organism-specific databases

    CTDi 11193.
    GeneCardsi GC13P041635.
    HGNCi HGNC:12739. WBP4.
    HPAi HPA038965.
    MIMi 604981. gene.
    neXtProti NX_O75554.
    PharmGKBi PA37350.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5104.
    HOGENOMi HOG000067962.
    HOVERGENi HBG053152.
    InParanoidi O75554.
    KOi K13220.
    OMAi ESHEEVD.
    OrthoDBi EOG7H7930.
    PhylomeDBi O75554.
    TreeFami TF316671.

    Enzyme and pathway databases

    SignaLinki O75554.

    Miscellaneous databases

    EvolutionaryTracei O75554.
    GeneWikii WBP4.
    GenomeRNAii 11193.
    NextBioi 42605.
    PROi O75554.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75554.
    Bgeei O75554.
    CleanExi HS_WBP4.
    Genevestigatori O75554.

    Family and domain databases

    InterProi IPR001202. WW_dom.
    IPR000690. Znf_C2H2_matrin.
    IPR003604. Znf_U1.
    IPR013085. Znf_U1-C.
    [Graphical view ]
    Pfami PF00397. WW. 2 hits.
    PF06220. zf-U1. 1 hit.
    [Graphical view ]
    SMARTi SM00456. WW. 2 hits.
    SM00451. ZnF_U1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51045. SSF51045. 2 hits.
    PROSITEi PS01159. WW_DOMAIN_1. 2 hits.
    PS50020. WW_DOMAIN_2. 2 hits.
    PS50171. ZF_MATRIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "WW domain-mediated interactions reveal a spliceosome-associated protein that binds a third class of proline-rich motif: the proline glycine and methionine-rich motif."
      Bedford M.T., Reed R., Leder P.
      Proc. Natl. Acad. Sci. U.S.A. 95:10602-10607(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SNRPB; SNRPC; SF1 AND U2.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    3. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] (ISOFORM 1).
      Tissue: Brain and Testis.
    5. "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-220, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. "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-220; SER-262 AND SER-277, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "Solution structure of WW domain in WW domain binding protein 4 (WBP-4)."
      RIKEN structural genomics initiative (RSGI)
      Submitted (OCT-2006) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 124-164.
    8. "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: STRUCTURE BY NMR OF 122-196, FUNCTION, MUTAGENESIS OF TRP-150 AND TRP-191, SUBCELLULAR LOCATION, INTERACTION WITH WBP11.
    9. Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-113.

    Entry informationi

    Entry nameiWBP4_HUMAN
    AccessioniPrimary (citable) accession number: O75554
    Secondary accession number(s): B7Z4M2, Q32P29
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: November 1, 1998
    Last modified: October 1, 2014
    This is version 116 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 13
      Human chromosome 13: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3