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O00308

- WWP2_HUMAN

UniProt

O00308 - WWP2_HUMAN

Protein

NEDD4-like E3 ubiquitin-protein ligase WWP2

Gene

WWP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 2 (20 Jun 2003)
      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. Polyubiquitinates POU5F1 by 'Lys-63'-linked conjugation and promotes it to proteasomal degradation; in embryonic stem cells (ESCs) the ubiquitination is proposed to regulate POU5F1 protein level. Ubiquitinates EGR2 and promotes it to proteasomal degradation; in T-cells the ubiquitination inhibits activation-induced cell death. Ubiquitinates SLC11A2; the ubiquitination is enhanced by presence of NDFIP1 and NDFIP2. Ubiquitinates RPB1 and promotes it to proteasomal degradation.2 Publications

    Enzyme regulationi

    Activated by NDFIP1- and NDFIP2-binding.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei838 – 8381Glycyl thioester intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

    1. ligase activity Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. RNA polymerase II transcription factor binding Source: BHF-UCL
    4. transcription factor binding Source: UniProtKB
    5. ubiquitin-protein transferase activity Source: UniProtKB

    GO - Biological processi

    1. cellular protein modification process Source: ProtInc
    2. negative regulation of gene expression Source: UniProtKB
    3. negative regulation of protein transport Source: UniProtKB
    4. negative regulation of sequence-specific DNA binding transcription factor activity Source: BHF-UCL
    5. negative regulation of transcription, DNA-templated Source: BHF-UCL
    6. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    7. negative regulation of transporter activity Source: UniProtKB
    8. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
    9. protein autoubiquitination Source: FlyBase
    10. protein K63-linked ubiquitination Source: UniProtKB
    11. protein ubiquitination Source: UniProtKB
    12. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: RefGenome
    13. regulation of ion transmembrane transport Source: BHF-UCL
    14. regulation of membrane potential Source: BHF-UCL
    15. regulation of potassium ion transmembrane transporter activity Source: BHF-UCL
    16. viral entry into host cell Source: UniProtKB

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Host-virus interaction, Ubl conjugation pathway

    Enzyme and pathway databases

    SignaLinkiO00308.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NEDD4-like E3 ubiquitin-protein ligase WWP2 (EC:6.3.2.-)
    Alternative name(s):
    Atrophin-1-interacting protein 2
    Short name:
    AIP2
    WW domain-containing protein 2
    Gene namesi
    Name:WWP2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:16804. WWP2.

    Subcellular locationi

    Nucleus 2 Publications

    GO - Cellular componenti

    1. cytoplasm Source: BHF-UCL
    2. membrane Source: UniProtKB
    3. nucleus Source: UniProtKB
    4. ubiquitin ligase complex Source: ProtInc

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi498 – 4981K → R: Does not affect FBXL15-mediated ubiquitination. 1 Publication
    Mutagenesisi500 – 5001H → K: Does not affect FBXL15-mediated ubiquitination. 1 Publication
    Mutagenesisi838 – 8381C → A: Abolishes ubiquitination of POU5F1. 1 Publication

    Organism-specific databases

    PharmGKBiPA134946925.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 870870NEDD4-like E3 ubiquitin-protein ligase WWP2PRO_0000120338Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei211 – 2111Phosphoserine2 Publications

    Post-translational modificationi

    Autoubiquitinated. Ubiquitinated by the SCF(FBXL15) complex, leading to its degradation by the proteasome.2 Publications

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiO00308.
    PaxDbiO00308.
    PRIDEiO00308.

    PTM databases

    PhosphoSiteiO00308.

    Expressioni

    Tissue specificityi

    Detected in heart, throughout the brain, placenta, lung, liver, muscle, kidney and pancreas. Also detected in spleen and peripheral blood leukocytes.2 Publications

    Developmental stagei

    Highly expressed in undifferentiated embryonic stem cells and expression is reduced after embryoid body (EB) formation. Not detectable at day 13 of EB formation; low levels are again detected at day 18 of EB formation.1 Publication

    Gene expression databases

    ArrayExpressiO00308.
    BgeeiO00308.
    CleanExiHS_WWP2.
    GenevestigatoriO00308.

    Organism-specific databases

    HPAiHPA041682.

    Interactioni

    Subunit structurei

    Interacts with POU5F1, RBP1, EGR2 and SLC11A2 By similarity. Interacts with SCNN1A, SCNN1B, SCNN1G, WBP1, WBP2, ATN1 and adenovirus type 2 PIII. Interacts with ERBB4, NDFIP1 AND NDFIP2.By similarity8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ADARB1P785635EBI-743923,EBI-2967304
    POU5F1Q018604EBI-743923,EBI-475687
    SMAD2Q157964EBI-743923,EBI-1040141
    SMAD3P840224EBI-743923,EBI-347161
    SMAD7O151055EBI-743923,EBI-3861591

    Protein-protein interaction databases

    BioGridi116244. 54 interactions.
    IntActiO00308. 21 interactions.
    MINTiMINT-148449.
    STRINGi9606.ENSP00000348283.

    Structurei

    3D structure databases

    ProteinModelPortaliO00308.
    SMRiO00308. Positions 17-143, 302-867.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini20 – 10081C2Add
    BLAST
    Domaini300 – 33334WW 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini330 – 36334WW 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini405 – 43733WW 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini444 – 47734WW 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini536 – 870335HECTPROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The C2 domain is involved in autoinhibition of the catalytic activity by interacting with the HECT domain.By similarity

    Sequence similaritiesi

    Contains 1 C2 domain.Curated
    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.
    InParanoidiO00308.
    KOiK05630.
    OMAiINSYVEV.
    OrthoDBiEOG7RFTGT.
    PhylomeDBiO00308.
    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]
    PfamiPF00632. 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.
    PROSITEiPS50237. HECT. 1 hit.
    PS01159. WW_DOMAIN_1. 4 hits.
    PS50020. WW_DOMAIN_2. 4 hits.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O00308-1) [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

    MASASSSRAG VALPFEKSQL TLKVVSAKPK VHNRQPRINS YVEVAVDGLP    50
    SETKKTGKRI GSSELLWNEI IILNVTAQSH LDLKVWSCHT LRNELLGTAS 100
    VNLSNVLKNN GGKMENMQLT LNLQTENKGS VVSGGELTIF LDGPTVDLGN 150
    VPNGSALTDG SQLPSRDSSG TAVAPENRHQ PPSTNCFGGR SRTHRHSGAS 200
    ARTTPATGEQ SPGARSRHRQ PVKNSGHSGL ANGTVNDEPT TATDPEEPSV 250
    VGVTSPPAAP LSVTPNPNTT SLPAPATPAE GEEPSTSGTQ QLPAAAQAPD 300
    ALPAGWEQRE LPNGRVYYVD HNTKTTTWER PLPPGWEKRT DPRGRFYYVD 350
    HNTRTTTWQR PTAEYVRNYE QWQSQRNQLQ GAMQHFSQRF LYQSSSASTD 400
    HDPLGPLPPG WEKRQDNGRV YYVNHNTRTT QWEDPRTQGM IQEPALPPGW 450
    EMKYTSEGVR YFVDHNTRTT TFKDPRPGFE SGTKQGSPGA YDRSFRWKYH 500
    QFRFLCHSNA LPSHVKISVS RQTLFEDSFQ QIMNMKPYDL RRRLYIIMRG 550
    EEGLDYGGIA REWFFLLSHE VLNPMYCLFE YAGKNNYCLQ INPASSINPD 600
    HLTYFRFIGR FIAMALYHGK FIDTGFTLPF YKRMLNKRPT LKDLESIDPE 650
    FYNSIVWIKE NNLEECGLEL YFIQDMEILG KVTTHELKEG GESIRVTEEN 700
    KEEYIMLLTD WRFTRGVEEQ TKAFLDGFNE VAPLEWLRYF DEKELELMLC 750
    GMQEIDMSDW QKSTIYRHYT KNSKQIQWFW QVVKEMDNEK RIRLLQFVTG 800
    TCRLPVGGFA ELIGSNGPQK FCIDKVGKET WLPRSHTCFN RLDLPPYKSY 850
    EQLREKLLYA IEETEGFGQE 870
    Length:870
    Mass (Da):98,912
    Last modified:June 20, 2003 - v2
    Checksum:iFCCD75CBA61F2204
    GO
    Isoform 2 (identifier: O00308-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-116: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:754
    Mass (Da):86,308
    Checksum:iEB1D2F174EEE0676
    GO
    Isoform 3 (identifier: O00308-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-439: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:431
    Mass (Da):51,079
    Checksum:i31464D3E9B6A8F77
    GO
    Isoform 4 (identifier: O00308-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         336-870: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:335
    Mass (Da):35,248
    Checksum:i4FDE005EDF329841
    GO

    Sequence cautioni

    The sequence BAC86528.1 differs from that shown. Reason: Frameshift at position 757.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti136 – 1361E → K in AAC51325. (PubMed:9169421)Curated
    Sequence conflicti390 – 3901F → L in BAG62027. (PubMed:14702039)Curated
    Sequence conflicti394 – 3952SS → FW in AAC51325. (PubMed:9169421)Curated
    Sequence conflicti545 – 5451Y → F in BAC86528. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 439439Missing in isoform 3. 1 PublicationVSP_046461Add
    BLAST
    Alternative sequencei1 – 116116Missing in isoform 2. 1 PublicationVSP_044706Add
    BLAST
    Alternative sequencei336 – 870535Missing in isoform 4. 1 PublicationVSP_054711Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U96114 mRNA. Translation: AAC51325.1.
    JN712744 mRNA. Translation: AFK29253.1.
    AK126332 mRNA. Translation: BAC86528.1. Frameshift.
    AK300266 mRNA. Translation: BAG62027.1.
    AK312792 mRNA. Translation: BAG35653.1.
    AC026468 Genomic DNA. No translation available.
    AC092115 Genomic DNA. No translation available.
    CH471092 Genomic DNA. Translation: EAW83287.1.
    BC000108 mRNA. Translation: AAH00108.1.
    BC013645 mRNA. Translation: AAH13645.1.
    BC064531 mRNA. Translation: AAH64531.1.
    CCDSiCCDS10885.1. [O00308-1]
    CCDS58475.1. [O00308-4]
    CCDS58476.1. [O00308-2]
    CCDS58477.1. [O00308-3]
    RefSeqiNP_001257382.1. NM_001270453.1. [O00308-2]
    NP_001257383.1. NM_001270454.1. [O00308-1]
    NP_001257384.1. NM_001270455.1. [O00308-4]
    NP_008945.2. NM_007014.4. [O00308-1]
    NP_955456.1. NM_199424.2. [O00308-3]
    XP_005255835.1. XM_005255778.2. [O00308-1]
    UniGeneiHs.408458.

    Genome annotation databases

    EnsembliENST00000356003; ENSP00000348283; ENSG00000198373. [O00308-1]
    ENST00000359154; ENSP00000352069; ENSG00000198373. [O00308-1]
    ENST00000568684; ENSP00000456216; ENSG00000198373. [O00308-3]
    ENST00000569174; ENSP00000455311; ENSG00000198373. [O00308-4]
    GeneIDi11060.
    KEGGihsa:11060.
    UCSCiuc002exu.2. human. [O00308-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U96114 mRNA. Translation: AAC51325.1 .
    JN712744 mRNA. Translation: AFK29253.1 .
    AK126332 mRNA. Translation: BAC86528.1 . Frameshift.
    AK300266 mRNA. Translation: BAG62027.1 .
    AK312792 mRNA. Translation: BAG35653.1 .
    AC026468 Genomic DNA. No translation available.
    AC092115 Genomic DNA. No translation available.
    CH471092 Genomic DNA. Translation: EAW83287.1 .
    BC000108 mRNA. Translation: AAH00108.1 .
    BC013645 mRNA. Translation: AAH13645.1 .
    BC064531 mRNA. Translation: AAH64531.1 .
    CCDSi CCDS10885.1. [O00308-1 ]
    CCDS58475.1. [O00308-4 ]
    CCDS58476.1. [O00308-2 ]
    CCDS58477.1. [O00308-3 ]
    RefSeqi NP_001257382.1. NM_001270453.1. [O00308-2 ]
    NP_001257383.1. NM_001270454.1. [O00308-1 ]
    NP_001257384.1. NM_001270455.1. [O00308-4 ]
    NP_008945.2. NM_007014.4. [O00308-1 ]
    NP_955456.1. NM_199424.2. [O00308-3 ]
    XP_005255835.1. XM_005255778.2. [O00308-1 ]
    UniGenei Hs.408458.

    3D structure databases

    ProteinModelPortali O00308.
    SMRi O00308. Positions 17-143, 302-867.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116244. 54 interactions.
    IntActi O00308. 21 interactions.
    MINTi MINT-148449.
    STRINGi 9606.ENSP00000348283.

    PTM databases

    PhosphoSitei O00308.

    Proteomic databases

    MaxQBi O00308.
    PaxDbi O00308.
    PRIDEi O00308.

    Protocols and materials databases

    DNASUi 11060.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000356003 ; ENSP00000348283 ; ENSG00000198373 . [O00308-1 ]
    ENST00000359154 ; ENSP00000352069 ; ENSG00000198373 . [O00308-1 ]
    ENST00000568684 ; ENSP00000456216 ; ENSG00000198373 . [O00308-3 ]
    ENST00000569174 ; ENSP00000455311 ; ENSG00000198373 . [O00308-4 ]
    GeneIDi 11060.
    KEGGi hsa:11060.
    UCSCi uc002exu.2. human. [O00308-1 ]

    Organism-specific databases

    CTDi 11060.
    GeneCardsi GC16P069796.
    HGNCi HGNC:16804. WWP2.
    HPAi HPA041682.
    MIMi 602308. gene.
    neXtProti NX_O00308.
    PharmGKBi PA134946925.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5021.
    HOGENOMi HOG000208453.
    HOVERGENi HBG004134.
    InParanoidi O00308.
    KOi K05630.
    OMAi INSYVEV.
    OrthoDBi EOG7RFTGT.
    PhylomeDBi O00308.
    TreeFami TF323658.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    SignaLinki O00308.

    Miscellaneous databases

    ChiTaRSi WWP2. human.
    GeneWikii WWP2.
    GenomeRNAii 11060.
    NextBioi 13633274.
    PROi O00308.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O00308.
    Bgeei O00308.
    CleanExi HS_WWP2.
    Genevestigatori O00308.

    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 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 PS50237. HECT. 1 hit.
    PS01159. WW_DOMAIN_1. 4 hits.
    PS50020. WW_DOMAIN_2. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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] (ISOFORM 1), INTERACTION WITH WBP1; WBP2; SCNN1A; SCNN1B AND SCNN1G.
      Tissue: Bone marrow and Brain.
    2. "Bioinformatic analysis of E3 ligase WWP2 in 14 different vertebrates."
      Jiang G.Y., Yang J.H., Liu S.F.
      Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "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] (ISOFORMS 1; 2 AND 3).
      Tissue: Placenta, Testis and Trachea.
    4. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORMS 1 AND 4).
      Tissue: Brain, Ovary and Placenta.
    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 ATN1, TISSUE SPECIFICITY.
    8. "Ubiquitin-protein ligase WWP2 binds to and downregulates the epithelial Na(+) channel."
      McDonald F.J., Western A.H., McNeil J.D., Thomas B.C., Olson D.R., Snyder P.M.
      Am. J. Physiol. 283:F431-F436(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SCNN1A; SCNN1B AND SCNN1G.
    9. "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 ADENOVIRUS TYPE 2 PIII.
    10. "N4WBP5, a potential target for ubiquitination by the Nedd4 family of proteins, is a novel Golgi-associated protein."
      Harvey K.F., Shearwin-Whyatt L.M., Fotia A., Parton R.G., Kumar S.
      J. Biol. Chem. 277:9307-9317(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NDFIP1.
    11. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Autoinhibition of the HECT-type ubiquitin ligase Smurf2 through its C2 domain."
      Wiesner S., Ogunjimi A.A., Wang H.R., Rotin D., Sicheri F., Wrana J.L., Forman-Kay J.D.
      Cell 130:651-662(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: AUTOINHIBITION BY C2 DOMAIN.
    13. "WWP2 promotes degradation of transcription factor OCT4 in human embryonic stem cells."
      Xu H., Wang W., Li C., Yu H., Yang A., Wang B., Jin Y.
      Cell Res. 19:561-573(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN UBIQUITINATION OF POU5F1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INTERACTION WITH POU5F1, MUTAGENESIS OF CYS-838.
    14. "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.
    15. "The HECT-type E3 ubiquitin ligase AIP2 inhibits activation-induced T-cell death by catalyzing EGR2 ubiquitination."
      Chen A., Gao B., Zhang J., McEwen T., Ye S.Q., Zhang D., Fang D.
      Mol. Cell. Biol. 29:5348-5356(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN UBIQUITINATION OF EGR2, INTERACTION WITH EGR2.
    16. "Interactions of ErbB4 and Kap1 connect the growth factor and DNA damage response pathways."
      Gilmore-Hebert M., Ramabhadran R., Stern D.F.
      Mol. Cancer Res. 8:1388-1398(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ERBB4, SUBCELLULAR LOCATION.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "SCF(FBXL15) regulates BMP signalling by directing the degradation of HECT-type ubiquitin ligase Smurf1."
      Cui Y., He S., Xing C., Lu K., Wang J., Xing G., Meng A., Jia S., He F., Zhang L.
      EMBO J. 30:2675-2689(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, MUTAGENESIS OF LYS-498 AND HIS-500.
    19. "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-211, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiWWP2_HUMAN
    AccessioniPrimary (citable) accession number: O00308
    Secondary accession number(s): A6NEP1
    , B2R706, B4DTL5, F5H213, H3BRF3, I3RSG8, Q6ZTQ5, Q96CZ2, Q9BWN6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2003
    Last sequence update: June 20, 2003
    Last modified: October 1, 2014
    This is version 140 of the entry and version 2 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

    Miscellaneous

    A cysteine residue is required for ubiquitin-thioester formation.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3