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O08759 (UBE3A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-protein ligase E3A
EC=6.3.2.-
Alternative name(s):
Oncogenic protein-associated protein E6-AP
Gene names
Name:Ube3a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length885 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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. 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 By similarity.

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Binds UBQLN1 and UBQLN2. Interacts with the 26S proteasome. Interacts with BPY2 By similarity. Interacts with HIF1AN, MAPK6 AND NEURL4; interaction with MAPK6 may be mediated by NEURL4 By similarity. Interacts with the proteasomal subunit PSMD4 By similarity.

Subcellular location

Cytoplasm. Nucleus.

Tissue specificity

Most abundant in brain, heart and thymus.

Miscellaneous

A cysteine residue is required for ubiquitin-thioester formation.

Sequence similarities

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

Caution

It is uncertain whether Met-1 or Met-38 is the initiator.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentCytoplasm
Nucleus
Proteasome
   Molecular functionLigase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processandrogen receptor signaling pathway

Inferred from physical interaction PubMed 16254014. Source: MGI

ovarian follicle development

Inferred from mutant phenotype PubMed 11756548. Source: MGI

positive regulation of phosphatidylinositol 3-kinase cascade

Inferred from mutant phenotype PubMed 16254014. Source: MGI

positive regulation of transcription from RNA polymerase II promoter

Inferred from genetic interaction PubMed 16254014. Source: MGI

prostate gland growth

Inferred from mutant phenotype PubMed 11756548PubMed 16254014. Source: MGI

protein K48-linked ubiquitination

Inferred from sequence or structural similarity. Source: UniProtKB

protein ubiquitination involved in ubiquitin-dependent protein catabolic process

Inferred from Biological aspect of Ancestor. Source: RefGenome

sperm entry

Inferred from mutant phenotype PubMed 11756548. Source: MGI

   Cellular_componentcytosol

Inferred from direct assay Ref.1. Source: MGI

nucleus

Inferred from direct assay Ref.1. Source: MGI

proteasome complex

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functiontranscription coactivator activity

Inferred from direct assay PubMed 16254014. Source: MGI

ubiquitin-protein ligase activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 885885Ubiquitin-protein ligase E3A
PRO_0000194981

Regions

Domain786 – 885100HECT
Compositional bias405 – 4106Asp/Glu-rich (acidic)

Sites

Active site8531Glycyl thioester intermediate By similarity

Amino acid modifications

Modified residue2291Phosphoserine By similarity

Experimental info

Sequence conflict1871D → E in AAB47756. Ref.2
Sequence conflict3011L → V in AAB47756. Ref.2
Sequence conflict3431T → S in AAB47756. Ref.2
Sequence conflict3841N → K in AAB47756. Ref.2
Sequence conflict4601S → F in AAB47756. Ref.2
Sequence conflict4861G → F in AAB47756. Ref.2
Sequence conflict5351T → R in AAB47756. Ref.2
Sequence conflict577 – 5826DEGGVS → MREAFP Ref.2
Sequence conflict5841E → S Ref.2
Sequence conflict587 – 5882QL → SW Ref.2
Sequence conflict5971D → N in AAB47756. Ref.2
Sequence conflict623 – 6275FTLIG → VYSDWH in AAB47756. Ref.2
Sequence conflict725 – 7262IS → NL in AAB47756. Ref.2
Sequence conflict8171L → Q in AAB47756. Ref.2
Sequence conflict869 – 8702NV → KE in AAB47756. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O08759 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 55D885E080CCB699

FASTA885101,176
        10         20         30         40         50         60 
MFLISDSKLL SPSCHRMATA CKSSPGESQS EDIEASRMKR AAAKHLIERY YHQLTEGCGN 

        70         80         90        100        110        120 
EACTNEFCAS CPTFLRMDNN AAAIKALELY KINAKLCDPH PSKKGASSAY LENSKGASNN 

       130        140        150        160        170        180 
SEIKMNKKEG KDFKDVIYLT EEKVYEIYEF CRESEDYSPL IRVIGRIFSS AEALVLSFRK 

       190        200        210        220        230        240 
VKQHTKDELK SLQEKDEDKD EDEKEKAACS AAAMEEDSEA SSSRMGDSSQ GDNNVQKLGP 

       250        260        270        280        290        300 
DDVTVDIDAI RRVYSSLLAN EKLETAFLNA LVYLSPNVEC DLTYHNVYTR DPNYLNLFII 

       310        320        330        340        350        360 
LMENSNLHSP EYLEMALPLF CKAMCKLPLE AQGKLIRLWS KYTADQIRRM METFQQLITY 

       370        380        390        400        410        420 
KVISNEFNSR NLVNDDDAIV AASNCLKMVY YANVVGGDVD TNHNEEDDEE PIPESSELTL 

       430        440        450        460        470        480 
QELLGDERRN KKGPRVDPLE TELGVKTLDC RKPLISFEES INEPLNDVLE MDKDYTFFKV 

       490        500        510        520        530        540 
ETENKGSFMT CPFILNAVTK NLGLYYDNRI RMYSERRITV LYSLVQGQQL NPYLTLKVRR 

       550        560        570        580        590        600 
DHIIDDALVR LEMIAMENPA DLKKQLYVEF EGEQGVDEGG VSKEFFQLVV EEIFNPDIGM 

       610        620        630        640        650        660 
FTYDEATKLF WFNPSSFETE GQFTLIGILG LAIYNNCILD VHFPMVVYRK LMGKKGTFRD 

       670        680        690        700        710        720 
LGDSHPVLYQ SLKDLLEYEG SVEDDMMITF QISQTDLFGN PMMYDLKENG DKIPITNENR 

       730        740        750        760        770        780 
KEFVISYSDY ILNKSVEKQF KAFRRGFHMV TNESPLKYLF RPEEIELLIC GSRNLDFQAL 

       790        800        810        820        830        840 
EETTEYDGGY TRESVVIREF WEIVHSFTDE QKRLFLLFTT GTDRAPVGGL GKLKMIIAKN 

       850        860        870        880 
GPDTERLPTS HTCFNVLLLP EYSSKEKLNV RLLKAITYAK GFGML

« Hide

References

[1]"Subcellular localization and ubiquitin-conjugating enzyme (E2) interactions of mammalian HECT family ubiquitin protein ligases."
Hatakeyama S., Jensen J.P., Weissman A.M.
J. Biol. Chem. 272:15085-15092(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6 X CBA.
[2]"The E6-Ap ubiquitin-protein ligase (UBE3A) gene is localized within a narrowed Angelman syndrome critical region."
Sutcliffe J.S., Jiang Y.-H., Galjaard R.-J., Matsuura T., Fang P., Kubota T., Christian S.L., Bressler J., Cattanach B., Ledbetter D.H., Beaudet A.L.
Genome Res. 7:368-377(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U96636 mRNA. Translation: AAB63361.1.
U82122 mRNA. Translation: AAB47756.1.
IPIIPI00115595.
UniGeneMm.9002.

3D structure databases

ProteinModelPortalO08759.
SMRO08759. Positions 38-101, 531-879.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-4139156.
STRING10090.ENSMUSP00000082326.

PTM databases

PhosphoSiteO08759.

Proteomic databases

PaxDbO08759.
PRIDEO08759.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

MGIMGI:105098. Ube3a.

Phylogenomic databases

eggNOGCOG5021.
HOGENOMHOG000261634.
HOVERGENHBG059326.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

CleanExMM_UBE3A.
GenevestigatorO08759.

Family and domain databases

InterProIPR000569. HECT.
IPR017134. Ubiquitin-protein_ligase_E6-AP.
[Graphical view]
PfamPF00632. HECT. 1 hit.
[Graphical view]
PIRSFPIRSF037201. Ubiquitin-protein_ligase_E6-AP. 1 hit.
SMARTSM00119. HECTc. 1 hit.
[Graphical view]
SUPFAMSSF56204. HECT. 1 hit.
PROSITEPS50237. HECT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUBE3A. mouse.
SOURCESearch...

Entry information

Entry nameUBE3A_MOUSE
AccessionPrimary (citable) accession number: O08759
Secondary accession number(s): P97482
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 1, 1997
Last modified: May 29, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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