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Q05086

- UBE3A_HUMAN

UniProt

Q05086 - UBE3A_HUMAN

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Protein
Ubiquitin-protein ligase E3A
Gene
UBE3A, E6AP, EPVE6AP, HPVE6A
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 K48-linked ubiquitination Source: UniProtKB
  8. protein autoubiquitination Source: FlyBase
  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
Complete GO annotation...

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 Inferred

GO - Cellular componenti

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

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
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 E3A
PRO_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 PSMD4.4 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. 117 interactions.
DIPiDIP-6002N.
IntActiQ05086. 39 interactions.
MINTiMINT-147444.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiQ05086.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini776 – 875100HECT
Add
BLAST

Region

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

Compositional bias

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

Sequence similaritiesi

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.

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.
VSP_006705Add
BLAST
Alternative sequencei1 – 1010MEKLHQCYWK → MATACKR in isoform III.
VSP_006706

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti359 – 3591R → RNLVNEFNSR AA sequence 1 Publication
Sequence conflicti423 – 4231P → L in AAA35542. 1 Publication
Sequence conflicti647 – 6493TFR → LFV in AAA35542. 1 Publication
Sequence conflicti669 – 6691E → V in AAA35542. 1 Publication
Sequence conflicti686 – 6861D → N in AAA35542. 1 Publication

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. 117 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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 149 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

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