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Q05086

- UBE3A_HUMAN

UniProt

Q05086 - UBE3A_HUMAN

Protein

Ubiquitin-protein ligase E3A

Gene

UBE3A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 4 (25 Nov 2008)
      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 transfers it to its substrates. Several substrates have been identified including the RAD23A and RAD23B, MCM7 (which is involved in DNA replication), annexin A1, the PML tumor suppressor, and the cell cycle regulator CDKN1B. Catalyzes the high-risk human papilloma virus E6-mediated ubiquitination of p53/TP53, contributing to the neoplastic progression of cells infected by these viruses. Additionally, may function as a cellular quality control ubiquitin ligase by helping the degradation of the cytoplasmic misfolded proteins. Finally, UBE3A also promotes its own degradation in vivo.6 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei843 – 8431Glycyl thioester intermediate

    GO - Molecular functioni

    1. ligase activity Source: UniProtKB-KW
    2. protein binding Source: IntAct
    3. transcription coactivator activity Source: Ensembl
    4. ubiquitin-protein transferase activity Source: UniProtKB

    GO - Biological processi

    1. androgen receptor signaling pathway Source: RefGenome
    2. brain development Source: ProtInc
    3. ovarian follicle development Source: Ensembl
    4. positive regulation of phosphatidylinositol 3-kinase signaling Source: Ensembl
    5. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
    6. prostate gland growth Source: Ensembl
    7. protein autoubiquitination Source: FlyBase
    8. protein K48-linked ubiquitination Source: UniProtKB
    9. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: RefGenome
    10. proteolysis Source: ProtInc
    11. sperm entry Source: Ensembl
    12. ubiquitin-dependent protein catabolic process Source: ProtInc
    13. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Host-virus interaction, Ubl conjugation pathway

    Enzyme and pathway databases

    ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin-protein ligase E3A (EC:6.3.2.-)
    Alternative name(s):
    E6AP ubiquitin-protein ligase
    Human papillomavirus E6-associated protein
    Oncogenic protein-associated protein E6-AP
    Renal carcinoma antigen NY-REN-54
    Gene namesi
    Name:UBE3A
    Synonyms:E6AP, EPVE6AP, HPVE6A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:12496. UBE3A.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. cytoplasm Source: RefGenome
    2. cytosol Source: Ensembl
    3. nucleus Source: RefGenome
    4. proteasome complex Source: UniProtKB-KW

    Keywords - Cellular componenti

    Nucleus, Proteasome

    Pathology & Biotechi

    Involvement in diseasei

    Angelman syndrome (AS) [MIM:105830]: A neurodevelopmental disorder characterized by severe motor and intellectual retardation, ataxia, frequent jerky limb movements and flapping of the arms and hands, hypotonia, seizures, absence of speech, frequent smiling and episodes of paroxysmal laughter, open-mouthed expression revealing the tongue.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti826 – 8261I → II in AS. 1 Publication
    VAR_008144

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi105830. phenotype.
    Orphaneti72. Angelman syndrome.
    PharmGKBiPA37144.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 875875Ubiquitin-protein ligase E3APRO_0000194980Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei218 – 2181Phosphoserine2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ05086.
    PaxDbiQ05086.
    PRIDEiQ05086.

    PTM databases

    PhosphoSiteiQ05086.

    Expressioni

    Gene expression databases

    ArrayExpressiQ05086.
    BgeeiQ05086.
    GenevestigatoriQ05086.

    Organism-specific databases

    HPAiHPA039410.

    Interactioni

    Subunit structurei

    Binds UBQLN1 and UBQLN2. Interacts with the 26S proteasome. Interacts with HCV core protein and targets it to degradation. Interacts with the E6 protein of the cancer-associated human papillomavirus types 16 and 18. The E6/E6-AP complex binds to and targets the p53/TP53 tumor-suppressor protein for ubiquitin-mediated proteolysis. Interacts with BPY2. Interacts with HIF1AN, MAPK6 AND NEURL4; interaction with MAPK6 may be mediated by NEURL4. Interacts with the proteasomal subunit PSMD4.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    E6P031262EBI-954357,EBI-1177242From a different organism.
    E6P040193EBI-954357,EBI-1177232From a different organism.
    E6P064633EBI-954357,EBI-1186926From a different organism.
    E6P069312EBI-954357,EBI-7281937From a different organism.
    E6Q77E163EBI-954357,EBI-7011359From a different organism.
    TP53P046373EBI-954357,EBI-366083

    Protein-protein interaction databases

    BioGridi113185. 119 interactions.
    DIPiDIP-6002N.
    IntActiQ05086. 39 interactions.
    MINTiMINT-147444.

    Structurei

    Secondary structure

    1
    875
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi27 – 4115
    Helixi65 – 7814
    Helixi403 – 4108
    Beta strandi525 – 5273
    Beta strandi529 – 5313
    Helixi532 – 54514
    Helixi548 – 5525
    Beta strandi557 – 5593
    Helixi569 – 58214
    Helixi585 – 5873
    Beta strandi589 – 5924
    Turni594 – 5963
    Beta strandi599 – 6013
    Helixi609 – 62416
    Helixi635 – 6417
    Helixi648 – 6547
    Helixi656 – 66712
    Helixi672 – 6754
    Beta strandi679 – 6846
    Turni687 – 6893
    Beta strandi692 – 6976
    Turni698 – 7025
    Turni707 – 7093
    Helixi710 – 72213
    Helixi727 – 74115
    Beta strandi742 – 7443
    Helixi753 – 7608
    Turni768 – 7703
    Beta strandi775 – 7795
    Helixi785 – 79511
    Helixi799 – 80911
    Beta strandi810 – 8156
    Helixi820 – 8234
    Beta strandi826 – 8338
    Beta strandi839 – 8413
    Helixi842 – 8443
    Beta strandi846 – 8516
    Helixi855 – 86814

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1C4ZX-ray2.60A/B/C518-875[»]
    1D5FX-ray2.80A/B/C518-875[»]
    1EQXNMR-A401-418[»]
    2KR1NMR-A24-87[»]
    4GIZX-ray2.55A/B403-414[»]
    ProteinModelPortaliQ05086.
    SMRiQ05086. Positions 24-87, 520-869.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ05086.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini776 – 875100HECTPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni401 – 41818E6-bindingAdd
    BLAST
    Regioni418 – 517100Interaction with HCV core proteinAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi394 – 3996Asp/Glu-rich (acidic)

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5021.
    HOVERGENiHBG059326.
    InParanoidiQ05086.
    KOiK10587.
    OMAiNEPLNDV.
    OrthoDBiEOG7NKKJP.
    PhylomeDBiQ05086.
    TreeFamiTF315189.

    Family and domain databases

    InterProiIPR000569. HECT.
    IPR017134. Ubiquitin-protein_ligase_E6-AP.
    [Graphical view]
    PfamiPF00632. HECT. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037201. Ubiquitin-protein_ligase_E6-AP. 1 hit.
    SMARTiSM00119. HECTc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56204. SSF56204. 1 hit.
    PROSITEiPS50237. HECT. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform II (identifier: Q05086-1) [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

    MEKLHQCYWK SGEPQSDDIE ASRMKRAAAK HLIERYYHQL TEGCGNEACT    50
    NEFCASCPTF LRMDNNAAAI KALELYKINA KLCDPHPSKK GASSAYLENS 100
    KGAPNNSCSE IKMNKKGARI DFKDVTYLTE EKVYEILELC REREDYSPLI 150
    RVIGRVFSSA EALVQSFRKV KQHTKEELKS LQAKDEDKDE DEKEKAACSA 200
    AAMEEDSEAS SSRIGDSSQG DNNLQKLGPD DVSVDIDAIR RVYTRLLSNE 250
    KIETAFLNAL VYLSPNVECD LTYHNVYSRD PNYLNLFIIV MENRNLHSPE 300
    YLEMALPLFC KAMSKLPLAA QGKLIRLWSK YNADQIRRMM ETFQQLITYK 350
    VISNEFNSRN LVNDDDAIVA ASKCLKMVYY ANVVGGEVDT NHNEEDDEEP 400
    IPESSELTLQ ELLGEERRNK KGPRVDPLET ELGVKTLDCR KPLIPFEEFI 450
    NEPLNEVLEM DKDYTFFKVE TENKFSFMTC PFILNAVTKN LGLYYDNRIR 500
    MYSERRITVL YSLVQGQQLN PYLRLKVRRD HIIDDALVRL EMIAMENPAD 550
    LKKQLYVEFE GEQGVDEGGV SKEFFQLVVE EIFNPDIGMF TYDESTKLFW 600
    FNPSSFETEG QFTLIGIVLG LAIYNNCILD VHFPMVVYRK LMGKKGTFRD 650
    LGDSHPVLYQ SLKDLLEYEG NVEDDMMITF QISQTDLFGN PMMYDLKENG 700
    DKIPITNENR KEFVNLYSDY ILNKSVEKQF KAFRRGFHMV TNESPLKYLF 750
    RPEEIELLIC GSRNLDFQAL EETTEYDGGY TRDSVLIREF WEIVHSFTDE 800
    QKRLFLQFTT GTDRAPVGGL GKLKMIIAKN GPDTERLPTS HTCFNVLLLP 850
    EYSSKEKLKE RLLKAITYAK GFGML 875
    Length:875
    Mass (Da):100,688
    Last modified:November 25, 2008 - v4
    Checksum:iF80F0502B3B3838A
    GO
    Isoform I (identifier: Q05086-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-23: Missing.

    Show »
    Length:852
    Mass (Da):97,968
    Checksum:i3C061DA8D216055A
    GO
    Isoform III (identifier: Q05086-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-10: MEKLHQCYWK → MATACKR

    Show »
    Length:872
    Mass (Da):100,102
    Checksum:iAB4C9B22356C9556
    GO

    Sequence cautioni

    The sequence AAA35542.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti359 – 3591R → RNLVNEFNSR AA sequence (PubMed:8380895)Curated
    Sequence conflicti423 – 4231P → L in AAA35542. (PubMed:8380895)Curated
    Sequence conflicti647 – 6493TFR → LFV in AAA35542. (PubMed:8380895)Curated
    Sequence conflicti669 – 6691E → V in AAA35542. (PubMed:8380895)Curated
    Sequence conflicti686 – 6861D → N in AAA35542. (PubMed:8380895)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti44 – 441C → Y Probable polymorphism. 1 Publication
    VAR_007852
    Natural varianti62 – 621R → H.1 Publication
    VAR_008142
    Natural varianti201 – 2011A → T.2 Publications
    Corresponds to variant rs147145506 [ dbSNP | Ensembl ].
    VAR_007853
    Natural varianti290 – 2901V → G.3 Publications
    Corresponds to variant rs1059383 [ dbSNP | Ensembl ].
    VAR_047516
    Natural varianti372 – 3721S → P.1 Publication
    VAR_008143
    Natural varianti826 – 8261I → II in AS. 1 Publication
    VAR_008144

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2323Missing in isoform I. 2 PublicationsVSP_006705Add
    BLAST
    Alternative sequencei1 – 1010MEKLHQCYWK → MATACKR in isoform III. 2 PublicationsVSP_006706

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X98021
    , X98027, X98022, X98023, X98024, X98025, X98026, X98028, X98029, X98030 Genomic DNA. Translation: CAA66653.1.
    X98031 mRNA. Translation: CAA66654.1.
    X98032 mRNA. Translation: CAA66655.1.
    X98033 mRNA. Translation: CAA66656.1.
    AC100774 Genomic DNA. No translation available.
    AK292514 mRNA. Translation: BAF85203.1.
    AC124997 Genomic DNA. No translation available.
    CH471151 Genomic DNA. Translation: EAW57645.1.
    L07557 mRNA. Translation: AAA35542.1. Different initiation.
    AF016708
    , AF016703, AF016704, AF016705, AF016706, AF016707 Genomic DNA. Translation: AAB69154.1.
    U84404 mRNA. Translation: AAB49301.1.
    AJ001107 Genomic DNA. Translation: CAA04534.1.
    AJ001108 Genomic DNA. Translation: CAA04535.1.
    AJ001109 Genomic DNA. Translation: CAA04536.1.
    AJ001110 Genomic DNA. Translation: CAA04537.1.
    AJ001111 Genomic DNA. Translation: CAA04538.1.
    AJ001112 Genomic DNA. Translation: CAA04539.1.
    CCDSiCCDS32177.1. [Q05086-2]
    CCDS45191.1. [Q05086-3]
    CCDS45192.1. [Q05086-1]
    RefSeqiNP_000453.2. NM_000462.3. [Q05086-1]
    NP_570853.1. NM_130838.1. [Q05086-2]
    NP_570854.1. NM_130839.2. [Q05086-3]
    XP_005268324.1. XM_005268267.2. [Q05086-2]
    XP_005268325.1. XM_005268268.2. [Q05086-2]
    XP_005268326.1. XM_005268269.2. [Q05086-2]
    XP_005268327.1. XM_005268270.2. [Q05086-2]
    XP_005268328.1. XM_005268271.2. [Q05086-2]
    XP_006720736.1. XM_006720673.1. [Q05086-3]
    XP_006720737.1. XM_006720674.1. [Q05086-3]
    XP_006720738.1. XM_006720675.1. [Q05086-2]
    XP_006720739.1. XM_006720676.1. [Q05086-2]
    UniGeneiHs.598862.

    Genome annotation databases

    EnsembliENST00000232165; ENSP00000232165; ENSG00000114062. [Q05086-3]
    ENST00000397954; ENSP00000381045; ENSG00000114062. [Q05086-1]
    ENST00000428984; ENSP00000401265; ENSG00000114062. [Q05086-2]
    ENST00000438097; ENSP00000411258; ENSG00000114062. [Q05086-2]
    ENST00000566215; ENSP00000457771; ENSG00000114062. [Q05086-2]
    GeneIDi7337.
    KEGGihsa:7337.
    UCSCiuc001zaq.3. human. [Q05086-1]
    uc001zas.3. human. [Q05086-3]

    Polymorphism databases

    DMDMi215274240.

    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
    X98021
    , X98027 , X98022 , X98023 , X98024 , X98025 , X98026 , X98028 , X98029 , X98030 Genomic DNA. Translation: CAA66653.1 .
    X98031 mRNA. Translation: CAA66654.1 .
    X98032 mRNA. Translation: CAA66655.1 .
    X98033 mRNA. Translation: CAA66656.1 .
    AC100774 Genomic DNA. No translation available.
    AK292514 mRNA. Translation: BAF85203.1 .
    AC124997 Genomic DNA. No translation available.
    CH471151 Genomic DNA. Translation: EAW57645.1 .
    L07557 mRNA. Translation: AAA35542.1 . Different initiation.
    AF016708
    , AF016703 , AF016704 , AF016705 , AF016706 , AF016707 Genomic DNA. Translation: AAB69154.1 .
    U84404 mRNA. Translation: AAB49301.1 .
    AJ001107 Genomic DNA. Translation: CAA04534.1 .
    AJ001108 Genomic DNA. Translation: CAA04535.1 .
    AJ001109 Genomic DNA. Translation: CAA04536.1 .
    AJ001110 Genomic DNA. Translation: CAA04537.1 .
    AJ001111 Genomic DNA. Translation: CAA04538.1 .
    AJ001112 Genomic DNA. Translation: CAA04539.1 .
    CCDSi CCDS32177.1. [Q05086-2 ]
    CCDS45191.1. [Q05086-3 ]
    CCDS45192.1. [Q05086-1 ]
    RefSeqi NP_000453.2. NM_000462.3. [Q05086-1 ]
    NP_570853.1. NM_130838.1. [Q05086-2 ]
    NP_570854.1. NM_130839.2. [Q05086-3 ]
    XP_005268324.1. XM_005268267.2. [Q05086-2 ]
    XP_005268325.1. XM_005268268.2. [Q05086-2 ]
    XP_005268326.1. XM_005268269.2. [Q05086-2 ]
    XP_005268327.1. XM_005268270.2. [Q05086-2 ]
    XP_005268328.1. XM_005268271.2. [Q05086-2 ]
    XP_006720736.1. XM_006720673.1. [Q05086-3 ]
    XP_006720737.1. XM_006720674.1. [Q05086-3 ]
    XP_006720738.1. XM_006720675.1. [Q05086-2 ]
    XP_006720739.1. XM_006720676.1. [Q05086-2 ]
    UniGenei Hs.598862.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1C4Z X-ray 2.60 A/B/C 518-875 [» ]
    1D5F X-ray 2.80 A/B/C 518-875 [» ]
    1EQX NMR - A 401-418 [» ]
    2KR1 NMR - A 24-87 [» ]
    4GIZ X-ray 2.55 A/B 403-414 [» ]
    ProteinModelPortali Q05086.
    SMRi Q05086. Positions 24-87, 520-869.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113185. 119 interactions.
    DIPi DIP-6002N.
    IntActi Q05086. 39 interactions.
    MINTi MINT-147444.

    PTM databases

    PhosphoSitei Q05086.

    Polymorphism databases

    DMDMi 215274240.

    Proteomic databases

    MaxQBi Q05086.
    PaxDbi Q05086.
    PRIDEi Q05086.

    Protocols and materials databases

    DNASUi 7337.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000232165 ; ENSP00000232165 ; ENSG00000114062 . [Q05086-3 ]
    ENST00000397954 ; ENSP00000381045 ; ENSG00000114062 . [Q05086-1 ]
    ENST00000428984 ; ENSP00000401265 ; ENSG00000114062 . [Q05086-2 ]
    ENST00000438097 ; ENSP00000411258 ; ENSG00000114062 . [Q05086-2 ]
    ENST00000566215 ; ENSP00000457771 ; ENSG00000114062 . [Q05086-2 ]
    GeneIDi 7337.
    KEGGi hsa:7337.
    UCSCi uc001zaq.3. human. [Q05086-1 ]
    uc001zas.3. human. [Q05086-3 ]

    Organism-specific databases

    CTDi 7337.
    GeneCardsi GC15M025582.
    GeneReviewsi UBE3A.
    HGNCi HGNC:12496. UBE3A.
    HPAi HPA039410.
    MIMi 105830. phenotype.
    601623. gene.
    neXtProti NX_Q05086.
    Orphaneti 72. Angelman syndrome.
    PharmGKBi PA37144.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5021.
    HOVERGENi HBG059326.
    InParanoidi Q05086.
    KOi K10587.
    OMAi NEPLNDV.
    OrthoDBi EOG7NKKJP.
    PhylomeDBi Q05086.
    TreeFami TF315189.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    ChiTaRSi UBE3A. human.
    EvolutionaryTracei Q05086.
    GeneWikii UBE3A.
    GenomeRNAii 7337.
    NextBioi 28722.
    PROi Q05086.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q05086.
    Bgeei Q05086.
    Genevestigatori Q05086.

    Family and domain databases

    InterProi IPR000569. HECT.
    IPR017134. Ubiquitin-protein_ligase_E6-AP.
    [Graphical view ]
    Pfami PF00632. HECT. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037201. Ubiquitin-protein_ligase_E6-AP. 1 hit.
    SMARTi SM00119. HECTc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56204. SSF56204. 1 hit.
    PROSITEi PS50237. HECT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The human E6-AP gene (UBE3A) encodes three potential protein isoforms generated by differential splicing."
      Yamamoto Y., Huibregtse J.M., Howley P.M.
      Genomics 41:263-266(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS I; II AND III), VARIANT GLY-290.
      Tissue: Keratinocyte.
    2. "UBE3A/E6-AP mutations cause Angelman syndrome."
      Kishino T., Lalande M., Wagstaff J.
      Nat. Genet. 15:70-73(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM I).
      Tissue: Fetal brain.
    3. "De novo truncating mutations in E6-AP ubiquitin-protein ligase gene (UBE3A) in Angelman syndrome."
      Matsuura T., Sutcliffe J.S., Fang P., Galjaard R.-J., Jiang Y.-H., Benton C.S., Rommens J.M., Beaudet A.L.
      Nat. Genet. 15:74-77(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM I), VARIANTS TYR-44 AND THR-201.
    4. "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 III).
      Tissue: Testis.
    5. "Analysis of the DNA sequence and duplication history of human chromosome 15."
      Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
      , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
      Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "Cloning and expression of the cDNA for E6-AP, a protein that mediates the interaction of the human papillomavirus E6 oncoprotein with p53."
      Huibregtse J.M., Scheffner M., Howley P.M.
      Mol. Cell. Biol. 13:775-784(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-875, PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION, VARIANT GLY-290.
      Tissue: Keratinocyte.
    8. "The ubiquitin-protein ligase E6-associated protein (E6-AP) serves as its own substrate."
      Nuber U., Schwarz S.E., Scheffner M.
      Eur. J. Biochem. 254:643-649(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    9. "Mutations in the E6-AP gene (UBE3A) in patients with Angelman syndrome."
      Hennies H.C., Buerger J., Sperling K., Reis A.
      Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-787, VARIANT GLY-290.
    10. Cited for: IDENTIFICATION AS A RENAL CANCER ANTIGEN.
      Tissue: Renal cell carcinoma.
    11. "Identification of HHR23A as a substrate for E6-associated protein-mediated ubiquitination."
      Kumar S., Talis A.L., Howley P.M.
      J. Biol. Chem. 274:18785-18792(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "The hPLIC proteins may provide a link between the ubiquitination machinery and the proteasome."
      Kleijnen M.F., Shih A.H., Zhou P., Kumar S., Soccio R.E., Kedersha N.L., Gill G., Howley P.M.
      Mol. Cell 6:409-419(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UBQLN1 AND UBQLN2.
    13. "VCY2 protein interacts with the HECT domain of ubiquitin-protein ligase E3A."
      Wong E.Y., Tse J.Y., Yao K.M., Tam P.C., Yeung W.S.
      Biochem. Biophys. Res. Commun. 296:1104-1111(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BPY2.
    14. "Mass spectrometric characterization of the affinity-purified human 26S proteasome complex."
      Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.
      Biochemistry 46:3553-3565(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    15. Cited for: INTERACTION WITH HCV CORE PROTEIN.
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    17. Cited for: FUNCTION.
    18. "The ubiquitin ligase E6-AP is induced and recruited to aggresomes in response to proteasome inhibition and may be involved in the ubiquitination of Hsp70-bound misfolded proteins."
      Mishra A., Godavarthi S.K., Maheshwari M., Goswami A., Jana N.R.
      J. Biol. Chem. 284:10537-10545(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    19. Cited for: FUNCTION.
    20. "UBE3A/E6-AP regulates cell proliferation by promoting proteasomal degrADation of p27."
      Mishra A., Godavarthi S.K., Jana N.R.
      Neurobiol. Dis. 36:26-34(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    21. "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-218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "Identification and proteomic analysis of distinct UBE3A/E6AP protein complexes."
      Martinez-Noel G., Galligan J.T., Sowa M.E., Arndt V., Overton T.M., Harper J.W., Howley P.M.
      Mol. Cell. Biol. 32:3095-3106(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH HIF1AN; MAPK6; NEURL4 AND PSMD4.
    24. "Structure of an E6AP-UbcH7 complex: insights into ubiquitination by the E2-E3 enzyme cascade."
      Huang L., Kinnucan E., Wang G., Beaudenon S., Howley P.M., Huibregtse J.M., Pavletich N.P.
      Science 286:1321-1326(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 495-852 IN COMPLEX WITH UBE2L3.
    25. "Solution structure determination and mutational analysis of the papillomavirus E6 interacting peptide of E6AP."
      Be X., Hong Y., Wei J., Androphy E.J., Chen J.J., Baleja J.D.
      Biochemistry 40:1293-1299(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 401-418.
    26. Cited for: VARIANT AS ILE-826 INS, VARIANTS HIS-62; THR-201 AND PRO-372.

    Entry informationi

    Entry nameiUBE3A_HUMAN
    AccessioniPrimary (citable) accession number: Q05086
    Secondary accession number(s): A8K8Z9
    , P78355, Q93066, Q9UEP4, Q9UEP5, Q9UEP6, Q9UEP7, Q9UEP8, Q9UEP9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 150 of the entry and version 4 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: 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

    Dasty 3