Q5RJY2 · G2E3_MOUSE
- ProteinG2/M phase-specific E3 ubiquitin-protein ligase
- GeneG2e3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids716 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (By similarity).
Required for prevention of apoptotic death in early embryogenesis
Required for prevention of apoptotic death in early embryogenesis
Catalytic activity
Pathway
Protein modification; protein ubiquitination.
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 | cytoplasm | |
Cellular Component | nucleolus | |
Cellular Component | nucleus | |
Molecular Function | metal ion binding | |
Molecular Function | ubiquitin protein ligase activity | |
Biological Process | apoptotic process | |
Biological Process | blastocyst development | |
Biological Process | negative regulation of intrinsic apoptotic signaling pathway | |
Biological Process | protein polyubiquitination |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameG2/M phase-specific E3 ubiquitin-protein ligase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ5RJY2
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Shuttles between the nucleus and the cytoplasm. In the nucleus, delocalizes from the nucleolus to the nucleoplasm in response to DNA damage.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Embryos die prior to implantation due to massive apoptosis resulting in blastocyst involution.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 23 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000248345 | 1-716 | G2/M phase-specific E3 ubiquitin-protein ligase | |||
Sequence: MNENKPDNSQSLACVFCRKNDDCPNKYGEKKTYEKWNFSVHYYCLLMSSGIWQRGKEEEGVYGFLIEDIRKEVQRASKLKCTVCKKNGASIGCVVPTCKRSYHLPCGLQKECIFQFTDNFASFCWKHRPVQAITSNKYSSSLPCTICLEFVEPIPTYNILQSPCCKNAWFHRDCLQVQAINAGVFFFRCTLCNNTDIFQKEMLRMGIHIPEKDASWELEENAYQELLQSHDRCDIRRCHCKKGRDYNEPNSKWEVKRCQSCGSSGTHLACSSLQSWEQNWECLDCRRITYTSDFQKAPKHPLANSTNVTVTDCLLEESSSKLPRQSTVAQHKELLRQGSKFRRDISTILIELGFQIKKKTKTLYINKANVWRSALEQFQSQKFNPSCSIDVVYVNGNEVGSQHLGSKQEFLSHLMHHLENSSVFEGSLAKNLSLNSQAVKENLYYEVGKMLAISLVHGGPSPGFFSETLFNCLAYGPENTLPTLDDVSDIDVAQIIIKIDSATDLNILNSVISQHYNYLEVSGCLRLTTSLSDKFMLVKDILFYHVINRVKAPFESFKQGLKTLGVLEKIQTYPEAFYKILCHKPENLSAKNLSDLFTIHSVADVQTLRFWNSYLKAIEDGKSATTMEDILIFATGCSSVPPTGFKPSLSVECLHVDFPVADKYRNHLVLPATNTYEEFQENMDFTIRDTLRLEKEERSHILPRTLNVSSNEEMLI |
Proteomic databases
PTM databases
Expression
Tissue specificity
In the developing embryo, expressed predominantly in the central nervous system and early limb bud. In the adult, highest expression in Purkinje cell bodies and cells lining the ductus deferens.
Gene expression databases
Structure
Family & Domains
Features
Showing features for zinc finger, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Zinc finger | 11-51 | C2HC pre-PHD-type | ||||
Sequence: SLACVFCRKNDDCPNKYGEKKTYEKWNFSVHYYCLLMSSGI | ||||||
Zinc finger | 79-128 | PHD-type 1 | ||||
Sequence: LKCTVCKKNGASIGCVVPTCKRSYHLPCGLQKECIFQFTDNFASFCWKHR | ||||||
Zinc finger | 141-195 | PHD-type 2; degenerate | ||||
Sequence: SLPCTICLEFVEPIPTYNILQSPCCKNAWFHRDCLQVQAINAGVFFFRCTLCNNT | ||||||
Zinc finger | 237-286 | PHD-type 3 | ||||
Sequence: RCHCKKGRDYNEPNSKWEVKRCQSCGSSGTHLACSSLQSWEQNWECLDCR | ||||||
Domain | 369-696 | HECT | ||||
Sequence: NVWRSALEQFQSQKFNPSCSIDVVYVNGNEVGSQHLGSKQEFLSHLMHHLENSSVFEGSLAKNLSLNSQAVKENLYYEVGKMLAISLVHGGPSPGFFSETLFNCLAYGPENTLPTLDDVSDIDVAQIIIKIDSATDLNILNSVISQHYNYLEVSGCLRLTTSLSDKFMLVKDILFYHVINRVKAPFESFKQGLKTLGVLEKIQTYPEAFYKILCHKPENLSAKNLSDLFTIHSVADVQTLRFWNSYLKAIEDGKSATTMEDILIFATGCSSVPPTGFKPSLSVECLHVDFPVADKYRNHLVLPATNTYEEFQENMDFTIRDTLRLEKE |
Domain
Ubiquitin ligase activity is mediated by two distinct domains, PHD-type zinc fingers 2 and 3. The use of these distinct domains may allow ubiquitination of different targets by each domain. The HECT domain is catalytically inactive and does not contribute to this activity.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length716
- Mass (Da)81,784
- Last updated2011-07-27 v2
- Checksum9A3B7CE4A9F53A52
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 675 | in Ref. 3; AAH86455 | ||||
Sequence: T → A |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK129332 EMBL· GenBank· DDBJ | BAC98142.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AC161116 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC086455 EMBL· GenBank· DDBJ | AAH86455.1 EMBL· GenBank· DDBJ | mRNA | ||
AK084256 EMBL· GenBank· DDBJ | BAC39150.1 EMBL· GenBank· DDBJ | mRNA |