P62839 · UB2D2_RAT
- ProteinUbiquitin-conjugating enzyme E2 D2
- GeneUbe2d2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids147 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and SQSTM1 and autoubiquitination of STUB1 and TRAF6. Involved in the signal-induced conjugation and subsequent degradation of NFKBIA, FBXW2-mediated GCM1 ubiquitination and degradation, MDM2-dependent degradation of p53/TP53 and the activation of MAVS in the mitochondria by RIGI in response to viral infection. Essential for viral activation of IRF3 (By similarity).
Mediates ubiquitination of PEX5
Mediates ubiquitination of PEX5
Catalytic activity
Pathway
Protein modification; protein ubiquitination.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 85 | Glycyl thioester intermediate | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | nucleus | |
Cellular Component | protein-containing complex | |
Cellular Component | ubiquitin ligase complex | |
Molecular Function | ATP binding | |
Molecular Function | ubiquitin conjugating enzyme activity | |
Molecular Function | ubiquitin protein ligase activity | |
Molecular Function | ubiquitin protein ligase binding | |
Molecular Function | ubiquitin-protein transferase activity | |
Biological Process | protein autoubiquitination | |
Biological Process | protein K48-linked ubiquitination | |
Biological Process | protein polyubiquitination | |
Biological Process | protein ubiquitination | |
Biological Process | ubiquitin-dependent protein catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameUbiquitin-conjugating enzyme E2 D2
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionP62839
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000082464 | 1-147 | Ubiquitin-conjugating enzyme E2 D2 | |||
Sequence: MALKRIHKELNDLARDPPAQCSAGPVGDDMFHWQATIMGPNDSPYQGGVFFLTIHFPTDYPFKPPKVAFTTRIYHPNINSNGSICLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLVPEIARIYKTDREKYNRIAREWTQKYAM |
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly expressed in testis.
Interaction
Subunit
Interacts with SCF (SKP1-CUL1-F-box protein) E3 ubiquitin ligase complex. Interacts with CNOT4 (via RING domain). Interacts with E3 ubiquitin-protein ligases CBLC, PJA1 and PJA2. Interacts with PDZRN3. Interacts with PPP1R11.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-147 | UBC core | ||||
Sequence: MALKRIHKELNDLARDPPAQCSAGPVGDDMFHWQATIMGPNDSPYQGGVFFLTIHFPTDYPFKPPKVAFTTRIYHPNINSNGSICLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLVPEIARIYKTDREKYNRIAREWTQKYAM |
Sequence similarities
Belongs to the ubiquitin-conjugating enzyme family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length147
- Mass (Da)16,735
- Last updated2004-08-16 v1
- ChecksumC942BE7853CBC355
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U13176 EMBL· GenBank· DDBJ | AAA85101.1 EMBL· GenBank· DDBJ | mRNA |