Essential maintenance is planned to begin on Fri Jan 24 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ in case of any outage.

A6I748 · A6I748_RAT

  • Protein
    RING-type E3 ubiquitin transferase
  • Gene
    Trim21
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    5/5

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 Componentcytoplasm
Cellular Componentcytoplasmic stress granule
Cellular Componentcytosol
Cellular Componentnucleoplasm
Cellular Componentnucleus
Cellular ComponentSCF ubiquitin ligase complex
Molecular Functionidentical protein binding
Molecular Functionprotein homodimerization activity
Molecular Functionprotein kinase binding
Molecular Functiontranscription coactivator activity
Molecular Functionubiquitin protein ligase activity
Molecular Functionubiquitin-protein transferase activity
Molecular Functionzinc ion binding
Biological Processinnate immune response
Biological Processnegative regulation of innate immune response
Biological Processnegative regulation of protein deubiquitination
Biological Processnegative regulation of viral transcription
Biological Processpositive regulation of autophagy
Biological Processpositive regulation of canonical NF-kappaB signal transduction
Biological Processpositive regulation of cell cycle
Biological Processpositive regulation of viral entry into host cell
Biological Processproteasomal protein catabolic process
Biological Processprotein autoubiquitination
Biological Processprotein destabilization
Biological Processprotein K27-linked ubiquitination
Biological Processprotein K48-linked ubiquitination
Biological Processprotein K6-linked ubiquitination
Biological Processprotein K63-linked ubiquitination
Biological Processprotein monoubiquitination
Biological Processprotein polyubiquitination
Biological Processprotein ubiquitination
Biological Processpyroptotic inflammatory response
Biological Processregulation of protein localization
Biological Processregulation of viral entry into host cell
Biological Processresponse to type II interferon
Biological Processstress granule disassembly
Biological Processsuppression of viral release by host

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    RING-type E3 ubiquitin transferase
  • EC number

Gene names

    • Name
      Trim21
    • Synonyms
      Trim21_predicted
    • ORF names
      rCG_40392

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • BN
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus

Accessions

  • Primary accession
    A6I748

Proteomes

Organism-specific databases

Family & Domains

Features

Showing features for domain, coiled coil.

Type
IDPosition(s)Description
Domain20-59RING-type
Domain91-132B box-type
Coiled coil187-246
Domain272-471B30.2/SPRY

Sequence similarities

Belongs to the TRIM/RBCC family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    471
  • Mass (Da)
    54,127
  • Last updated
    2023-06-28 v1
  • MD5 Checksum
    6BEF06E5AA59903133C3093657175956
MSHSTTSKMSLEKMWEEVTCSICLEPMVEPMSIECGHCFCKECISEVGGNGGGSCPVCRQHFLLRNLRPNRHIANMVENLKQEAQNTKKGTQEVHCMKHGEILHLFCEEDGQALCWVCAQSGKHRDHTKVPIEEAAKIYQEKIHKALEKLRKGKELAEKLEMDLAMQRTDWKRNIDTQKSRIHEEFAHQNSLLAQEEQRQLQRLEKDEREHLRLLGEKEAELAEKNQALQELISELERRSRGSELELLKEVRIVLERSVSWKLDTVDVDSPDLTSTCHVPGRKKMLRTCWVHITLDRDTANSCLIISKDRRQVRMGDTYQNVSENAERFNNYPMVLGAQRFSSGKMYWEVDVTQKQAWDLGVCRDSVQRKGHFSLSPENGFWTIWLWQKDNYEAGTSPQTTLHIQVPPCQIGIFVDYEAGIVSFYNITDHGSLIYTFSECAFIGPLRPFFSVGFNDDGGNSAPLKLCPLKI

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CH473956
EMBL· GenBank· DDBJ
EDM18181.1
EMBL· GenBank· DDBJ
Genomic DNA
CH473956
EMBL· GenBank· DDBJ
EDM18183.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help