Q5RJY2 · G2E3_MOUSE

  • Protein
    G2/M phase-specific E3 ubiquitin-protein ligase
  • Gene
    G2e3
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    5/5

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

Catalytic activity

  • S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.
    EC:2.3.2.26 (UniProtKB | ENZYME | Rhea)

Pathway

Protein modification; protein ubiquitination.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componentnucleolus
Cellular Componentnucleus
Molecular Functionmetal ion binding
Molecular Functionubiquitin protein ligase activity
Biological Processapoptotic process
Biological Processblastocyst development
Biological Processnegative regulation of intrinsic apoptotic signaling pathway
Biological Processprotein polyubiquitination

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    G2/M phase-specific E3 ubiquitin-protein ligase
  • EC number
  • Alternative names
    • G2/M phase-specific HECT-type E3 ubiquitin transferase

Gene names

    • Name
      G2e3
    • Synonyms
      Kiaa1333

Organism names

  • Taxonomic identifier
  • Strain
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q5RJY2
  • Secondary accessions
    • E9QK24
    • Q6ZPT7
    • Q8BNA4

Proteomes

Organism-specific databases

Subcellular Location

Nucleus, nucleolus
Cytoplasm
Note: Shuttles between the nucleus and the cytoplasm. In the nucleus, delocalizes from the nucleolus to the nucleoplasm in response to DNA damage.

Keywords

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.

Go to variant viewer

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002483451-716G2/M phase-specific E3 ubiquitin-protein ligase

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

Interaction

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for zinc finger, domain.

TypeIDPosition(s)Description
Zinc finger11-51C2HC pre-PHD-type
Zinc finger79-128PHD-type 1
Zinc finger141-195PHD-type 2; degenerate
Zinc finger237-286PHD-type 3
Domain369-696HECT

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    716
  • Mass (Da)
    81,784
  • Last updated
    2011-07-27 v2
  • Checksum
    9A3B7CE4A9F53A52
MNENKPDNSQSLACVFCRKNDDCPNKYGEKKTYEKWNFSVHYYCLLMSSGIWQRGKEEEGVYGFLIEDIRKEVQRASKLKCTVCKKNGASIGCVVPTCKRSYHLPCGLQKECIFQFTDNFASFCWKHRPVQAITSNKYSSSLPCTICLEFVEPIPTYNILQSPCCKNAWFHRDCLQVQAINAGVFFFRCTLCNNTDIFQKEMLRMGIHIPEKDASWELEENAYQELLQSHDRCDIRRCHCKKGRDYNEPNSKWEVKRCQSCGSSGTHLACSSLQSWEQNWECLDCRRITYTSDFQKAPKHPLANSTNVTVTDCLLEESSSKLPRQSTVAQHKELLRQGSKFRRDISTILIELGFQIKKKTKTLYINKANVWRSALEQFQSQKFNPSCSIDVVYVNGNEVGSQHLGSKQEFLSHLMHHLENSSVFEGSLAKNLSLNSQAVKENLYYEVGKMLAISLVHGGPSPGFFSETLFNCLAYGPENTLPTLDDVSDIDVAQIIIKIDSATDLNILNSVISQHYNYLEVSGCLRLTTSLSDKFMLVKDILFYHVINRVKAPFESFKQGLKTLGVLEKIQTYPEAFYKILCHKPENLSAKNLSDLFTIHSVADVQTLRFWNSYLKAIEDGKSATTMEDILIFATGCSSVPPTGFKPSLSVECLHVDFPVADKYRNHLVLPATNTYEEFQENMDFTIRDTLRLEKEERSHILPRTLNVSSNEEMLI

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
E9Q7C2E9Q7C2_MOUSEG2e3739
E9Q7E5E9Q7E5_MOUSEG2e3622

Sequence caution

The sequence BAC98142.1 differs from that shown. Reason: Erroneous initiation Extended N-terminus.

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict675in Ref. 3; AAH86455

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

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