A0A0M3PSM2 · A0A0M3PSM2_CERCP

Function

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:2.3.2.27 (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 Componentcytosol
Cellular Componentnucleoplasm
Molecular Functionprotein homodimerization activity
Molecular Functionprotein kinase binding
Molecular Functionubiquitin protein ligase activity
Molecular Functionzinc ion binding
Biological Processautophagy
Biological Processdefense response to virus
Biological Processinnate immune response
Biological Processpositive regulation of autophagy
Biological Processpositive regulation of canonical NF-kappaB signal transduction
Biological Processpositive regulation of NF-kappaB transcription factor activity
Biological Processprotein polyubiquitination
Biological Processregulation of protein localization
Biological Processregulation of viral entry into host cell

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Tripartite motif-containing protein 5
  • EC number
  • Alternative names
    • RING-type E3 ubiquitin transferase TRIM5
    • TRIM5alpha

Gene names

    • Name
      TRIM5

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Cercopithecidae > Cercopithecinae > Cercopithecus

Accessions

  • Primary accession
    A0A0M3PSM2

Subcellular Location

Keywords

PTM/Processing

Keywords

Family & Domains

Features

Showing features for domain, coiled coil.

Type
IDPosition(s)Description
Domain15-60RING-type
Domain92-133B box-type
Coiled coil137-171
Domain283-495B30.2/SPRY

Sequence similarities

Belongs to the TRIM/RBCC family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    495
  • Mass (Da)
    56,956
  • Last updated
    2015-12-09 v1
  • Checksum
    AAF1590F9485759F
MASGILVNVKEEVTCPICLELLTEPLSLPCGHSFCQACITANQKKSMLYKEGERSCPVCRISYQPENIQPNRHVANIVEKLREVKLSPEEGQKVDHCARHGEKLLLFCQEDSKVICWLCERSQEHRGHHTFLMEEVAQEYHVKLQTALEMLRQKQQEAEKLEADIREEKASWKIQIDYDKTNVSADFEQLREVLDWEESNELQNLEKEEEDILKSLRKSETEMVQQTQYVRELISDLEHRLQGSMMELLQGVDGVIKRIENMTLKKPKTFHKNQRRVFRAPDLKGMLDMFRELTDVRRYWVDVTLAPNNISHAVIAEDKRQVSSRNSQIMYQAPGTLFGSLTNFNYCTGVLGSQSITSGKHYWEVDVSKKSAWILGVCAGFQPDATYNIEQNENYQPKYGYWVIGLQEGVKYSAFQDGSSYTTFAPFIVPLSVIICPDRVGVFVDYEACTVSFFNITNHGFLIYKFSQCSFSKPIFPYLNPRKCTVPMTLCSPSS

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KP743975
EMBL· GenBank· DDBJ
ALB36907.1
EMBL· GenBank· DDBJ
mRNA

Similar Proteins

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