A0A8R2H7G9 · A0A8R2H7G9_ACYPI

Function

function

Functions within a multiprotein E3 ubiquitin ligase complex, catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins.

Catalytic activity

  • [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N6-ubiquitinyl-L-lysine.
    EC:2.3.2.31 (UniProtKB | ENZYME | Rhea)

Pathway

Protein modification; protein ubiquitination.

Features

Showing features for active site.

144650100150200250300350400
TypeIDPosition(s)Description
Active site415

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 Componentcytosol
Cellular Componentendoplasmic reticulum
Cellular ComponentGolgi apparatus
Cellular Componentmitochondrion
Cellular Componentubiquitin ligase complex
Molecular Functionubiquitin conjugating enzyme binding
Molecular Functionubiquitin protein ligase activity
Molecular Functionzinc ion binding
Biological Processautophagy of mitochondrion
Biological Processnegative regulation of protein phosphorylation
Biological Processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
Biological Processprotein polyubiquitination
Biological Processregulation of apoptotic process
Biological Processregulation of cellular response to oxidative stress
Biological Processregulation of mitochondrion organization
Biological Processubiquitin-dependent protein catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    E3 ubiquitin-protein ligase parkin
  • EC number

Organism names

  • Taxonomic identifier
  • Strain
    • LSR1
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Paraneoptera > Hemiptera > Sternorrhyncha > Aphidomorpha > Aphidoidea > Aphididae > Macrosiphini > Acyrthosiphon

Accessions

  • Primary accession
    A0A8R2H7G9

Proteomes

Subcellular Location

Keywords

PTM/Processing

Keywords

Interaction

Subunit

Forms an E3 ubiquitin ligase complex.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain28-103Ubiquitin-like
Domain222-446RING-type

Sequence similarities

Belongs to the RBR family. Parkin subfamily.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    446
  • Mass (Da)
    50,966
  • Last updated
    2022-10-12 v1
  • Checksum
    2A0088948B901C64
MMYMLDCLLNFIRRVLDTIFSRRITNSLLIFVKTNTGTVVPVGLDPKWEVRDVKEFVAPKLGMTPEELMIIFAGKELQDSELLEEYNLAEQTVLHAVKSRRRSFKRKPRVSTCIEEDEEFDDTKRAAVNFYVYCTSPCANTTVGKIRVRCFKCKSGAFTVDGDPKNWNDVLKPKRITGHCEISQCTDGEVGWSEFYFKCSEHVTKGENDEAVALHLIRNNLHDIQCLACTDVRSKVFVYPCDDGHVTCLECFCEYAVSRLRERRFVFDNNIGYTLPCPVGCPNSLINQPYHFKVLSKDHFEMYERFATEEYVLKNGGVLCPQPNCGAGILVDDDCDKVSCINGCGYVFCKKCLQGYHIGECLPKEEQLIIDITGYSVDPKLVSQSKWDDASKVKIKVSTKPCPKCRTATERDGGCMHMVCTRCSFPWCWLCQTEWTRECMGSHWFS

Keywords

Sequence databases

Genome annotation databases

Similar Proteins

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