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Q9H0M0

- WWP1_HUMAN

UniProt

Q9H0M0 - WWP1_HUMAN

Protein

NEDD4-like E3 ubiquitin-protein ligase WWP1

Gene

WWP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Ubiquitinates ERBB4 isoforms JM-A CYT-1 and JM-B CYT-1, KLF2, KLF5 and TP63 and promotes their proteasomal degradation. Ubiquitinates RNF11 without targeting it for degradation. Ubiquitinates and promotes degradation of TGFBR1; the ubiquitination is enhanced by SMAD7. Ubiquitinates SMAD6 and SMAD7. Ubiquitinates and promotes degradation of SMAD2 in response to TGF-beta signaling, which requires interaction with TGIF.3 Publications

    Enzyme regulationi

    Activated by NDFIP1- and NDFIP2-binding.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei890 – 8901Glycyl thioester intermediatePROSITE-ProRule annotation
    Sitei890 – 8901Required for ubiquitin-thioester formationBy similarity

    GO - Molecular functioni

    1. ligase activity Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. ubiquitin-protein transferase activity Source: UniProtKB

    GO - Biological processi

    1. central nervous system development Source: UniProtKB
    2. ion transmembrane transport Source: Reactome
    3. negative regulation of transcription, DNA-templated Source: UniProtKB
    4. proteasome-mediated ubiquitin-dependent protein catabolic process Source: Ensembl
    5. protein ubiquitination Source: UniProtKB
    6. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: RefGenome
    7. signal transduction Source: UniProtKB
    8. transmembrane transport Source: Reactome
    9. viral entry into host cell Source: UniProtKB

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Host-virus interaction, Ubl conjugation pathway

    Enzyme and pathway databases

    ReactomeiREACT_115828. Downregulation of ERBB4 signaling.
    REACT_160189. Stimuli-sensing channels.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinkiQ9H0M0.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NEDD4-like E3 ubiquitin-protein ligase WWP1 (EC:6.3.2.-)
    Alternative name(s):
    Atrophin-1-interacting protein 5
    Short name:
    AIP5
    TGIF-interacting ubiquitin ligase 1
    Short name:
    Tiul1
    WW domain-containing protein 1
    Gene namesi
    Name:WWP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:17004. WWP1.

    Subcellular locationi

    Cytoplasm By similarity. Cell membrane By similarity; Peripheral membrane protein By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. cytoplasm Source: RefGenome
    2. cytosol Source: Reactome
    3. nucleus Source: RefGenome
    4. plasma membrane Source: UniProtKB-SubCell
    5. ubiquitin ligase complex Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi614 – 6141E → A: Reduces ubiquitin transfer. 1 Publication
    Mutagenesisi621 – 6211H → A: Strongly reduces ubiquitin transfer. 1 Publication
    Mutagenesisi675 – 6751D → A: Reduces ubiquitin transfer. 1 Publication
    Mutagenesisi798 – 7981E → A: Reduces ubiquitin transfer. Strongly reduces ubiquitin transfer; when associated with A-845. 1 Publication
    Mutagenesisi804 – 8041M → P: Strongly reduces ubiquitin transfer; when associated with P-806. 1 Publication
    Mutagenesisi806 – 8061E → P: Strongly reduces ubiquitin transfer; when associated with P-804. 1 Publication
    Mutagenesisi845 – 8451R → A: No effect. 1 Publication
    Mutagenesisi848 – 8481Q → A: Abolishes ubiquitin transfer; when associated with A-855. 1 Publication
    Mutagenesisi855 – 8551R → A: Abolishes ubiquitin transfer; when associated with A-848. 1 Publication

    Organism-specific databases

    PharmGKBiPA134960138.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 922922NEDD4-like E3 ubiquitin-protein ligase WWP1PRO_0000120336Add
    BLAST

    Post-translational modificationi

    Auto-ubiquitinated and ubiquitinated by RNF11.3 Publications

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    MaxQBiQ9H0M0.
    PaxDbiQ9H0M0.
    PRIDEiQ9H0M0.

    PTM databases

    PhosphoSiteiQ9H0M0.

    Expressioni

    Tissue specificityi

    Detected in heart, placenta, pancreas, kidney, liver, skeletal muscle, bone marrow, fetal brain, and at much lower levels in adult brain and lung. Isoform 1 and isoform 5 predominate in all tissues tested, except in testis and bone marrow, where isoform 5 is expressed at much higher levels than isoform 1.2 Publications

    Gene expression databases

    ArrayExpressiQ9H0M0.
    BgeeiQ9H0M0.
    CleanExiHS_WWP1.
    GenevestigatoriQ9H0M0.

    Organism-specific databases

    HPAiHPA023180.

    Interactioni

    Subunit structurei

    Binds KLF2 AND HIVEP3 By similarity. Binds SCNN1A, SCNN1B, SCNN1G, WBP1, WBP2, DRPLA and adenovirus type 2 PIII. Interacts with RNF11 By similarity. Interacts with SPG20. Interacts with ERBB4 isoforms JM-B CYT-1 and JM-A CYT-1. Interacts with SMAD1, SMAD2, SMAD3, SMAD5, SMAD6, SMAD7, TGFBR1 AND TGFBR2. Associates with the TGFBR1:TGFBR2 receptor complex in presence of SMAD7. Interacts with SKIL isoform 1. Interacts with TP63 isoform 1 and isoform 2. Interacts with STAMBP and RNF11. Interacts with NDFIP1 and NDFIP2 Probable; this interaction activates the E3 ubiquitin-protein ligase. Interacts with TGIF.By similarity7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CPSF6Q166303EBI-742157,EBI-358410

    Protein-protein interaction databases

    BioGridi116243. 57 interactions.
    IntActiQ9H0M0. 22 interactions.
    MINTiMINT-199541.
    STRINGi9606.ENSP00000265428.

    Structurei

    Secondary structure

    1
    922
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi500 – 5056
    Turni509 – 5113
    Beta strandi513 – 5186
    Beta strandi521 – 5233
    Helixi547 – 56014
    Beta strandi564 – 5718
    Turni573 – 5753
    Helixi576 – 58510
    Helixi589 – 5935
    Beta strandi594 – 6007
    Turni601 – 6033
    Helixi610 – 62314
    Helixi626 – 6283
    Beta strandi629 – 63810
    Beta strandi641 – 6433
    Helixi645 – 6495
    Helixi653 – 66917
    Helixi680 – 6867
    Helixi693 – 6975
    Helixi701 – 71111
    Beta strandi723 – 7264
    Beta strandi730 – 7334
    Beta strandi737 – 7404
    Helixi743 – 7453
    Turni750 – 7523
    Helixi753 – 76614
    Turni767 – 7693
    Helixi770 – 78314
    Helixi786 – 7894
    Helixi794 – 8029
    Helixi809 – 8146
    Beta strandi816 – 8205
    Helixi826 – 83712
    Helixi840 – 85112
    Helixi861 – 8633
    Beta strandi873 – 8764
    Beta strandi886 – 8883
    Helixi889 – 8913
    Beta strandi893 – 8953
    Helixi902 – 91413

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ND7X-ray2.10A546-917[»]
    2OP7NMR-A494-532[»]
    ProteinModelPortaliQ9H0M0.
    SMRiQ9H0M0. Positions 19-145, 351-919.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9H0M0.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 9894C2PROSITE-ProRule annotationAdd
    BLAST
    Domaini349 – 38234WW 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini381 – 41434WW 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini456 – 48934WW 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini496 – 52934WW 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini588 – 922335HECTPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 C2 domain.PROSITE-ProRule annotation
    Contains 1 HECT (E6AP-type E3 ubiquitin-protein ligase) domain.PROSITE-ProRule annotation
    Contains 4 WW domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5021.
    HOGENOMiHOG000208453.
    HOVERGENiHBG004134.
    InParanoidiQ9H0M0.
    KOiK05633.
    OMAiKNGIVQT.
    OrthoDBiEOG7RFTGT.
    PhylomeDBiQ9H0M0.
    TreeFamiTF323658.

    Family and domain databases

    Gene3Di2.60.40.150. 1 hit.
    InterProiIPR000008. C2_dom.
    IPR024928. E3_ub_ligase_SMURF1.
    IPR000569. HECT.
    IPR001202. WW_dom.
    [Graphical view]
    PfamiPF00168. C2. 1 hit.
    PF00632. HECT. 1 hit.
    PF00397. WW. 4 hits.
    [Graphical view]
    PIRSFiPIRSF001569. E3_ub_ligase_SMURF1. 1 hit.
    SMARTiSM00239. C2. 1 hit.
    SM00119. HECTc. 1 hit.
    SM00456. WW. 4 hits.
    [Graphical view]
    SUPFAMiSSF49562. SSF49562. 1 hit.
    SSF51045. SSF51045. 4 hits.
    SSF56204. SSF56204. 1 hit.
    PROSITEiPS50004. C2. 1 hit.
    PS50237. HECT. 1 hit.
    PS01159. WW_DOMAIN_1. 4 hits.
    PS50020. WW_DOMAIN_2. 4 hits.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: Q9H0M0-1) [UniParc]FASTAAdd to Basket

    Also known as: A

    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

    MATASPRSDT SNNHSGRLQL QVTVSSAKLK RKKNWFGTAI YTEVVVDGEI    50
    TKTAKSSSSS NPKWDEQLTV NVTPQTTLEF QVWSHRTLKA DALLGKATID 100
    LKQALLIHNR KLERVKEQLK LSLENKNGIA QTGELTVVLD GLVIEQENIT 150
    NCSSSPTIEI QENGDALHEN GEPSARTTAR LAVEGTNGID NHVPTSTLVQ 200
    NSCCSYVVNG DNTPSSPSQV AARPKNTPAP KPLASEPADD TVNGESSSFA 250
    PTDNASVTGT PVVSEENALS PNCTSTTVED PPVQEILTSS ENNECIPSTS 300
    AELESEARSI LEPDTSNSRS SSAFEAAKSR QPDGCMDPVR QQSGNANTET 350
    LPSGWEQRKD PHGRTYYVDH NTRTTTWERP QPLPPGWERR VDDRRRVYYV 400
    DHNTRTTTWQ RPTMESVRNF EQWQSQRNQL QGAMQQFNQR YLYSASMLAA 450
    ENDPYGPLPP GWEKRVDSTD RVYFVNHNTK TTQWEDPRTQ GLQNEEPLPE 500
    GWEIRYTREG VRYFVDHNTR TTTFKDPRNG KSSVTKGGPQ IAYERGFRWK 550
    LAHFRYLCQS NALPSHVKIN VSRQTLFEDS FQQIMALKPY DLRRRLYVIF 600
    RGEEGLDYGG LAREWFFLLS HEVLNPMYCL FEYAGKNNYC LQINPASTIN 650
    PDHLSYFCFI GRFIAMALFH GKFIDTGFSL PFYKRMLSKK LTIKDLESID 700
    TEFYNSLIWI RDNNIEECGL EMYFSVDMEI LGKVTSHDLK LGGSNILVTE 750
    ENKDEYIGLM TEWRFSRGVQ EQTKAFLDGF NEVVPLQWLQ YFDEKELEVM 800
    LCGMQEVDLA DWQRNTVYRH YTRNSKQIIW FWQFVKETDN EVRMRLLQFV 850
    TGTCRLPLGG FAELMGSNGP QKFCIEKVGK DTWLPRSHTC FNRLDLPPYK 900
    SYEQLKEKLL FAIEETEGFG QE 922
    Length:922
    Mass (Da):105,202
    Last modified:March 1, 2001 - v1
    Checksum:i35B6E1C03A3147DA
    GO
    Isoform 2 (identifier: Q9H0M0-2) [UniParc]FASTAAdd to Basket

    Also known as: B

    The sequence of this isoform differs from the canonical sequence as follows:
         112-120: LERVKEQLK → CWLLKARME
         121-922: Missing.

    Show »
    Length:120
    Mass (Da):13,453
    Checksum:i952B6A78C5D4B93D
    GO
    Isoform 3 (identifier: Q9H0M0-3) [UniParc]FASTAAdd to Basket

    Also known as: C

    The sequence of this isoform differs from the canonical sequence as follows:
         112-242: LERVKEQLKL...LASEPADDTV → F

    Show »
    Length:792
    Mass (Da):91,548
    Checksum:i833D351CC08D9998
    GO
    Isoform 4 (identifier: Q9H0M0-4)

    Also known as: D

    Sequence is not available
    Length:
    Mass (Da):
    Isoform 5 (identifier: Q9H0M0-5)

    Also known as: E

    Sequence is not available
    Length:
    Mass (Da):
    Isoform 6 (identifier: Q9H0M0-6) [UniParc]FASTAAdd to Basket

    Also known as: F

    The sequence of this isoform differs from the canonical sequence as follows:
         23-240: Missing.

    Show »
    Length:704
    Mass (Da):81,649
    Checksum:iB39DCB6841290CF0
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti852 – 8521G → V.
    Corresponds to variant rs1059901 [ dbSNP | Ensembl ].
    VAR_052960

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei23 – 240218Missing in isoform 6. 1 PublicationVSP_007600Add
    BLAST
    Alternative sequencei112 – 242131LERVK…ADDTV → F in isoform 3. 1 PublicationVSP_007602Add
    BLAST
    Alternative sequencei112 – 1209LERVKEQLK → CWLLKARME in isoform 2. 1 PublicationVSP_007601
    Alternative sequencei121 – 922802Missing in isoform 2. 1 PublicationVSP_007603Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL136739 mRNA. Translation: CAB66673.1.
    AY043361 mRNA. Translation: AAK94668.1.
    AY345857 mRNA. Translation: AAQ22764.1.
    AC083845 Genomic DNA. No translation available.
    AC103817 Genomic DNA. No translation available.
    BC015380 mRNA. Translation: AAH15380.2.
    BC036065 mRNA. Translation: AAH36065.1.
    U96113 mRNA. Translation: AAC51324.1.
    CCDSiCCDS6242.1. [Q9H0M0-1]
    RefSeqiNP_008944.1. NM_007013.3. [Q9H0M0-1]
    XP_005250817.1. XM_005250760.2. [Q9H0M0-1]
    UniGeneiHs.655189.

    Genome annotation databases

    EnsembliENST00000265428; ENSP00000265428; ENSG00000123124. [Q9H0M0-1]
    ENST00000517970; ENSP00000427793; ENSG00000123124. [Q9H0M0-1]
    GeneIDi11059.
    KEGGihsa:11059.
    UCSCiuc003ydt.3. human. [Q9H0M0-1]

    Polymorphism databases

    DMDMi32171908.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL136739 mRNA. Translation: CAB66673.1 .
    AY043361 mRNA. Translation: AAK94668.1 .
    AY345857 mRNA. Translation: AAQ22764.1 .
    AC083845 Genomic DNA. No translation available.
    AC103817 Genomic DNA. No translation available.
    BC015380 mRNA. Translation: AAH15380.2 .
    BC036065 mRNA. Translation: AAH36065.1 .
    U96113 mRNA. Translation: AAC51324.1 .
    CCDSi CCDS6242.1. [Q9H0M0-1 ]
    RefSeqi NP_008944.1. NM_007013.3. [Q9H0M0-1 ]
    XP_005250817.1. XM_005250760.2. [Q9H0M0-1 ]
    UniGenei Hs.655189.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ND7 X-ray 2.10 A 546-917 [» ]
    2OP7 NMR - A 494-532 [» ]
    ProteinModelPortali Q9H0M0.
    SMRi Q9H0M0. Positions 19-145, 351-919.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116243. 57 interactions.
    IntActi Q9H0M0. 22 interactions.
    MINTi MINT-199541.
    STRINGi 9606.ENSP00000265428.

    PTM databases

    PhosphoSitei Q9H0M0.

    Polymorphism databases

    DMDMi 32171908.

    Proteomic databases

    MaxQBi Q9H0M0.
    PaxDbi Q9H0M0.
    PRIDEi Q9H0M0.

    Protocols and materials databases

    DNASUi 11059.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265428 ; ENSP00000265428 ; ENSG00000123124 . [Q9H0M0-1 ]
    ENST00000517970 ; ENSP00000427793 ; ENSG00000123124 . [Q9H0M0-1 ]
    GeneIDi 11059.
    KEGGi hsa:11059.
    UCSCi uc003ydt.3. human. [Q9H0M0-1 ]

    Organism-specific databases

    CTDi 11059.
    GeneCardsi GC08P087424.
    HGNCi HGNC:17004. WWP1.
    HPAi HPA023180.
    MIMi 602307. gene.
    neXtProti NX_Q9H0M0.
    PharmGKBi PA134960138.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5021.
    HOGENOMi HOG000208453.
    HOVERGENi HBG004134.
    InParanoidi Q9H0M0.
    KOi K05633.
    OMAi KNGIVQT.
    OrthoDBi EOG7RFTGT.
    PhylomeDBi Q9H0M0.
    TreeFami TF323658.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_115828. Downregulation of ERBB4 signaling.
    REACT_160189. Stimuli-sensing channels.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    SignaLinki Q9H0M0.

    Miscellaneous databases

    ChiTaRSi WWP1. human.
    EvolutionaryTracei Q9H0M0.
    GeneWikii WWP1.
    GenomeRNAii 11059.
    NextBioi 42019.
    PROi Q9H0M0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H0M0.
    Bgeei Q9H0M0.
    CleanExi HS_WWP1.
    Genevestigatori Q9H0M0.

    Family and domain databases

    Gene3Di 2.60.40.150. 1 hit.
    InterProi IPR000008. C2_dom.
    IPR024928. E3_ub_ligase_SMURF1.
    IPR000569. HECT.
    IPR001202. WW_dom.
    [Graphical view ]
    Pfami PF00168. C2. 1 hit.
    PF00632. HECT. 1 hit.
    PF00397. WW. 4 hits.
    [Graphical view ]
    PIRSFi PIRSF001569. E3_ub_ligase_SMURF1. 1 hit.
    SMARTi SM00239. C2. 1 hit.
    SM00119. HECTc. 1 hit.
    SM00456. WW. 4 hits.
    [Graphical view ]
    SUPFAMi SSF49562. SSF49562. 1 hit.
    SSF51045. SSF51045. 4 hits.
    SSF56204. SSF56204. 1 hit.
    PROSITEi PS50004. C2. 1 hit.
    PS50237. HECT. 1 hit.
    PS01159. WW_DOMAIN_1. 4 hits.
    PS50020. WW_DOMAIN_2. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Testis.
    2. "Alternative splicing determines the domain structure of WWP1, a Nedd4 family protein."
      Flasza M., Gorman P., Roylance R., Canfield A.E., Baron M.
      Biochem. Biophys. Res. Commun. 290:431-437(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6), TISSUE SPECIFICITY.
      Tissue: Mammary cancer.
    3. "The novel E3 ubiquitin ligase Tiul1 associates with TGIF to target Smad2 for degradation."
      Seo S.R., Lallemand F., Ferrand N., Pessah M., L'Hoste S., Camonis J., Atfi A.
      EMBO J. 23:3780-3792(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, UBIQUITINATION OF SMAD2 AND TGFBR1, INTERACTION WITH SMAD7 AND TGIF.
    4. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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: Lung and Testis.
    6. "Identification of novel human WW domain-containing proteins by cloning of ligand targets."
      Pirozzi G., McConnell S.J., Uveges A.J., Carter J.M., Sparks A.B., Kay B.K., Fowlkes D.M.
      J. Biol. Chem. 272:14611-14616(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 191-870, INTERACTION WITH WBP1; WBP2; SCNN1A; SCNN1B AND SCNN1G.
      Tissue: Bone marrow and Brain.
    7. "Atrophin-1, the DRPLA gene product, interacts with two families of WW domain-containing proteins."
      Wood J.D., Yuan J., Margolis R.L., Colomer V., Duan K., Kushi J., Kaminsky Z., Kleiderlein J.J. Jr., Sharp A.H., Ross C.A.
      Mol. Cell. Neurosci. 11:149-160(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DRPLA, TISSUE SPECIFICITY.
    8. "Adenovirus protein involved in virus internalization recruits ubiquitin-protein ligases."
      Galinier R., Gout E., Lortat-Jacob H., Wood J., Chroboczek J.
      Biochemistry 41:14299-14305(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PIII.
    9. "Negative regulation of transforming growth factor-beta (TGF-beta) signaling by WW domain-containing protein 1 (WWP1)."
      Komuro A., Imamura T., Saitoh M., Yoshida Y., Yamori T., Miyazono K., Miyazawa K.
      Oncogene 23:6914-6923(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN UBIQUITINATION OF TGFBR1; SMAD6 AND SMAD7, INTERACTION WITH SMAD1; SMAD2; SMAD3; SMAD5; SMAD6; SMAD7; TGFBR1; TGFBR2 AND SKIL.
    10. "The WW domain containing E3 ubiquitin protein ligase 1 upregulates ErbB2 and EGFR through RING finger protein 11."
      Chen C., Zhou Z., Liu R., Li Y., Azmi P.B., Seth A.K.
      Oncogene 27:6845-6855(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: AUTOUBIQUITINATION.
    11. "Endogenous spartin (SPG20) is recruited to endosomes and lipid droplets and interacts with the ubiquitin E3 ligases AIP4 and AIP5."
      Edwards T.L., Clowes V.E., Tsang H.T., Connell J.W., Sanderson C.M., Luzio J.P., Reid E.
      Biochem. J. 423:31-39(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SPG20.
    12. "Control of the activity of WW-HECT domain E3 ubiquitin ligases by NDFIP proteins."
      Mund T., Pelham H.R.
      EMBO Rep. 10:501-507(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVATION BY NDFIP1 AND NDFIP2, AUTOUBIQUITINATION.
    13. "WW domain containing E3 ubiquitin protein ligase 1 targets the full-length ErbB4 for ubiquitin-mediated degradation in breast cancer."
      Li Y., Zhou Z., Alimandi M., Chen C.
      Oncogene 28:2948-2958(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ERBB4.
    14. "Conformational flexibility underlies ubiquitin ligation mediated by the WWP1 HECT domain E3 ligase."
      Verdecia M.A., Joazeiro C.A.P., Wells N.J., Ferrer J.-L., Bowman M.E., Hunter T., Noel J.P.
      Mol. Cell 11:249-259(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 546-917, MUTAGENESIS OF GLU-614; HIS-621; ASP-675; GLU-798; MET-804; GLU-806; ARG-845; GLN-848 AND ARG-855, FUNCTION.

    Entry informationi

    Entry nameiWWP1_HUMAN
    AccessioniPrimary (citable) accession number: Q9H0M0
    Secondary accession number(s): O00307, Q5YLC1, Q96BP4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2003
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 135 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 8
      Human chromosome 8: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

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