Q7L622 · G2E3_HUMAN
- ProteinG2/M phase-specific E3 ubiquitin-protein ligase
- GeneG2E3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids706 (go to sequence)
- Protein existenceEvidence at protein 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. Essential in early embryonic development to prevent apoptotic death.
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 | cytosol | |
Cellular Component | Golgi apparatus | |
Cellular Component | intracellular membrane-bounded organelle | |
Cellular Component | nucleolus | |
Cellular Component | nucleus | |
Molecular Function | metal ion binding | |
Molecular Function | ubiquitin-protein transferase activity | |
Biological Process | apoptotic process | |
Biological Process | protein ubiquitination |
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
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ7L622
- 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
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 30-31 | Loss of nucleolar localization. No effect on nuclear localization. | ||||
Sequence: KK → AA | ||||||
Mutagenesis | 84 | Strong activity; when associated with A-258; A-261 and A-666. Strong activity; when associated with A-147 and A-666. No activity; when associated with A-147; A-258 and A-261. | ||||
Sequence: C → A | ||||||
Mutagenesis | 147 | Strong activity; when associated with A-84 and A-666. No activity; when associated with A-258; A-261 and A-666. No activity; when associated with A-84; A-258 and A-261. | ||||
Sequence: C → A | ||||||
Natural variant | VAR_027273 | 232 | in dbSNP:rs17096934 | |||
Sequence: R → H | ||||||
Mutagenesis | 258 | Strong activity; when associated with A-84; A-261 and A-666. No activity; when associated with A-147; A-261 and A-666. No activity; when associated with A-84; A-147 and A-261. | ||||
Sequence: C → A | ||||||
Mutagenesis | 261 | Strong activity; when associated with A-84; A-258 and A-666. No activity; when associated with A-84; A-147 and A-258. No activity; when associated with A-147; A-258 and A-666. | ||||
Sequence: C → A | ||||||
Mutagenesis | 666 | No effect on subcellular location. Strong activity; when associated with A-84; A-258 and A261. Strong activity; when associated with A-84 and A-147. No activity; when associated with A-147; A-258 and A-261. | ||||
Sequence: C → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 577 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 (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000248343 | 1-706 | UniProt | G2/M phase-specific E3 ubiquitin-protein ligase | |||
Sequence: MNESKPGDSQNLACVFCRKHDDCPNKYGEKKTKEKWNLTVHYYCLLMSSGIWQRGKEEEGVYGFLIEDIRKEVNRASKLKCCVCKKNGASIGCVAPRCKRSYHFPCGLQRECIFQFTGNFASFCWDHRPVQIITSNNYRESLPCTICLEFIEPIPSYNILRSPCCKNAWFHRDCLQVQAINAGVFFFRCTICNNSDIFQKEMLRMGIHIPEKDASWELEENAYQELLQHYERCDVRRCRCKEGRDYNAPDSKWEIKRCQCCGSSGTHLACSSLRSWEQNWECLECRGIIYNSGEFQKAKKHVLPNSNNVGITDCLLEESSPKLPRQSPGSQSKDLLRQGSKFRRNVSTLLIELGFQIKKKTKRLYINKANIWNSALDAFRNRNFNPSYAIEVAYVIENDNFGSEHPGSKQEFLSLLMQHLENSSLFEGSLSKNLSLNSQALKENLYYEAGKMLAISLVHGGPSPGFFSKTLFNCLVYGPENTQPILDDVSDFDVAQIIIRINTATTVADLKSIINECYNYLELIGCLRLITTLSDKYMLVKDILGYHVIQRVHTPFESFKQGLKTLGVLEKIQAYPEAFCSILCHKPESLSAKILSELFTVHTLPDVKALGFWNSYLQAVEDGKSTTTMEDILIFATGCSSIPPAGFKPTPSIECLHVDFPVGNKCNNCLAIPITNTYKEFQENMDFTIRNTLRLEKEESSHYIGH | |||||||
Modified residue (large scale data) | 292 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 320 | PRIDE | Phosphoserine | ||||
Sequence: S |
Proteomic databases
PTM databases
Expression
Tissue specificity
Predominantly expressed in brain, liver, kidney, testes and ovary.
Induction
Up-regulated approximately 4-fold in G2 when compared to S phase. Down-regulated approximately 3-fold by gamma-irradiation.
Gene expression databases
Organism-specific databases
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q7L622 | ATN1 Q86V38 | 3 | EBI-751757, EBI-11954292 | |
BINARY | Q7L622 | HTT P42858 | 6 | EBI-751757, EBI-466029 | |
BINARY | Q7L622 | KLK6 Q92876 | 3 | EBI-751757, EBI-2432309 | |
BINARY | Q7L622 | NEFL P07196 | 3 | EBI-751757, EBI-475646 | |
BINARY | Q7L622 | RPS15 P62841 | 3 | EBI-751757, EBI-372635 | |
BINARY | Q7L622 | SPECC1L Q69YQ0 | 2 | EBI-751757, EBI-351113 | |
BINARY | Q7L622 | SPRED1 Q7Z699 | 3 | EBI-751757, EBI-5235340 | |
BINARY | Q7L622 | WFS1 O76024 | 3 | EBI-751757, EBI-720609 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for zinc finger, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Zinc finger | 11-51 | C2HC pre-PHD-type | ||||
Sequence: NLACVFCRKHDDCPNKYGEKKTKEKWNLTVHYYCLLMSSGI | ||||||
Zinc finger | 79-128 | PHD-type 1 | ||||
Sequence: LKCCVCKKNGASIGCVAPRCKRSYHFPCGLQRECIFQFTGNFASFCWDHR | ||||||
Zinc finger | 143-193 | PHD-type 2; degenerate | ||||
Sequence: PCTICLEFIEPIPSYNILRSPCCKNAWFHRDCLQVQAINAGVFFFRCTICN | ||||||
Zinc finger | 237-286 | PHD-type 3 | ||||
Sequence: RCRCKEGRDYNAPDSKWEIKRCQCCGSSGTHLACSSLRSWEQNWECLECR | ||||||
Domain | 371-698 | HECT | ||||
Sequence: IWNSALDAFRNRNFNPSYAIEVAYVIENDNFGSEHPGSKQEFLSLLMQHLENSSLFEGSLSKNLSLNSQALKENLYYEAGKMLAISLVHGGPSPGFFSKTLFNCLVYGPENTQPILDDVSDFDVAQIIIRINTATTVADLKSIINECYNYLELIGCLRLITTLSDKYMLVKDILGYHVIQRVHTPFESFKQGLKTLGVLEKIQAYPEAFCSILCHKPESLSAKILSELFTVHTLPDVKALGFWNSYLQAVEDGKSTTTMEDILIFATGCSSIPPAGFKPTPSIECLHVDFPVGNKCNNCLAIPITNTYKEFQENMDFTIRNTLRLEKE |
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
- Length706
- Mass (Da)80,504
- Last updated2004-07-05 v1
- Checksum4B46ACF8782F941A
Computationally mapped potential isoform sequences
There are 9 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 184 | in Ref. 3; BAA91095 | ||||
Sequence: V → A | ||||||
Sequence conflict | 627 | in Ref. 3; BAB14280 | ||||
Sequence: T → A | ||||||
Sequence conflict | 665 | in Ref. 3; BAA91095 | ||||
Sequence: K → E |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB037754 EMBL· GenBank· DDBJ | BAA92571.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK000340 EMBL· GenBank· DDBJ | BAA91095.1 EMBL· GenBank· DDBJ | mRNA | ||
AK022867 EMBL· GenBank· DDBJ | BAB14280.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC000973 EMBL· GenBank· DDBJ | AAH00973.2 EMBL· GenBank· DDBJ | mRNA |