Q712K3 · UB2R2_HUMAN
- ProteinUbiquitin-conjugating enzyme E2 R2
- GeneUBE2R2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids238 (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 monoubiquitination and 'Lys-48'-linked polyubiquitination. May be involved in degradation of katenin.
Catalytic activity
Pathway
Protein modification; protein ubiquitination.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 93 | Glycyl thioester intermediate | ||||
Sequence: C |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | ATP binding | |
Molecular Function | ubiquitin conjugating enzyme activity | |
Molecular Function | ubiquitin-protein transferase activity | |
Biological Process | protein K48-linked ubiquitination | |
Biological Process | protein monoubiquitination | |
Biological Process | protein polyubiquitination | |
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 R2
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ712K3
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 93 | Loss of function. | ||||
Sequence: C → S | ||||||
Mutagenesis | 97 | Loss of function. | ||||
Sequence: L → S | ||||||
Mutagenesis | 233 | Abolishes phosphorylation by CK2. | ||||
Sequence: S → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 125 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000280513 | 1-238 | Ubiquitin-conjugating enzyme E2 R2 | |||
Sequence: MAQQQMTSSQKALMLELKSLQEEPVEGFRITLVDESDLYNWEVAIFGPPNTLYEGGYFKAHIKFPIDYPYSPPTFRFLTKMWHPNIYENGDVCISILHPPVDDPQSGELPSERWNPTQNVRTILLSVISLLNEPNTFSPANVDASVMFRKWRDSKGKDKEYAEIIRKQVSATKAEAEKDGVKVPTTLAEYCIKTKVPSNDNSSDLLYDDLYDDDIDDEDEEEEDADCYDDDDSGNEES | ||||||
Modified residue | 233 | Phosphoserine; by CK2 | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
When phosphorylated, interacts with beta-TrCP (BTRC).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q712K3 | APPBP2 Q92624 | 3 | EBI-2340879, EBI-743771 | |
BINARY | Q712K3 | GSC2 O15499 | 3 | EBI-2340879, EBI-19954058 | |
BINARY | Q712K3 | MEOX1 P50221 | 6 | EBI-2340879, EBI-2864512 | |
BINARY | Q712K3 | SDCBP O00560 | 3 | EBI-2340879, EBI-727004 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 8-174 | UBC core | ||||
Sequence: SSQKALMLELKSLQEEPVEGFRITLVDESDLYNWEVAIFGPPNTLYEGGYFKAHIKFPIDYPYSPPTFRFLTKMWHPNIYENGDVCISILHPPVDDPQSGELPSERWNPTQNVRTILLSVISLLNEPNTFSPANVDASVMFRKWRDSKGKDKEYAEIIRKQVSATKA | ||||||
Region | 194-238 | Disordered | ||||
Sequence: TKVPSNDNSSDLLYDDLYDDDIDDEDEEEEDADCYDDDDSGNEES | ||||||
Compositional bias | 206-238 | Acidic residues | ||||
Sequence: LYDDLYDDDIDDEDEEEEDADCYDDDDSGNEES |
Sequence similarities
Belongs to the ubiquitin-conjugating enzyme family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length238
- Mass (Da)27,166
- Last updated2004-07-05 v1
- ChecksumE896CF0116A56308
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 39 | in Ref. 2; BAA91156 | ||||
Sequence: Y → H | ||||||
Sequence conflict | 127 | in Ref. 2; BAA91156 | ||||
Sequence: V → A | ||||||
Compositional bias | 206-238 | Acidic residues | ||||
Sequence: LYDDLYDDDIDDEDEEEEDADCYDDDDSGNEES |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ240087 EMBL· GenBank· DDBJ | CAC80336.1 EMBL· GenBank· DDBJ | mRNA | ||
AK000426 EMBL· GenBank· DDBJ | BAA91156.1 EMBL· GenBank· DDBJ | mRNA | ||
CR457233 EMBL· GenBank· DDBJ | CAG33514.1 EMBL· GenBank· DDBJ | mRNA | ||
AL139113 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471071 EMBL· GenBank· DDBJ | EAW58479.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471071 EMBL· GenBank· DDBJ | EAW58480.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC004862 EMBL· GenBank· DDBJ | AAH04862.1 EMBL· GenBank· DDBJ | mRNA | ||
BC047584 EMBL· GenBank· DDBJ | AAH47584.1 EMBL· GenBank· DDBJ | mRNA |