Q6P9F5 · TRI40_HUMAN

  • Protein
    E3 ubiquitin ligase TRIM40
  • Gene
    TRIM40
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

E3 ubiquitin-protein ligase that plays a role in the limitation of the innate immune response (PubMed:21474709, PubMed:29117565).
Mediates inhibition of the RLR signaling pathway by ubiquitinating RIGI and IFIH1 receptors, leading to their proteasomal degradation (PubMed:21474709).
Promotes also the neddylation of IKBKG/NEMO, stabilizing NFKBIA, and thereby inhibiting of NF-kappa-B nuclear translocation and activation (PubMed:21474709).

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)

Features

Showing features for binding site.

125820406080100120140160180200220240
TypeIDPosition(s)Description
Binding site71Zn2+ (UniProtKB | ChEBI)
Binding site74Zn2+ (UniProtKB | ChEBI)
Binding site93Zn2+ (UniProtKB | ChEBI)
Binding site99Zn2+ (UniProtKB | ChEBI)

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 ComponentIkappaB kinase complex
Molecular Functionubiquitin protein ligase activity
Molecular Functionzinc ion binding
Biological Processinnate immune response
Biological Processnegative regulation of cell growth
Biological Processnegative regulation of NF-kappaB transcription factor activity
Biological Processnegative regulation of non-canonical NF-kappaB signal transduction
Biological Processnegative regulation of protein catabolic process
Biological Processnegative regulation of protein localization to nucleus
Biological Processprotein neddylation
Biological Processprotein ubiquitination

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    E3 ubiquitin ligase TRIM40
  • EC number
  • Alternative names
    • Probable E3 NEDD8-protein ligase
    • RING finger protein 35

Gene names

    • Name
      TRIM40
    • Synonyms
      RNF35

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q6P9F5
  • Secondary accessions
    • Q5SRJ6
    • Q5SS36
    • Q8TD96

Proteomes

Organism-specific databases

Subcellular Location

Disease & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_055309142in dbSNP:rs12528473
Natural variantVAR_055310215in dbSNP:rs757259
Natural variantVAR_057222244in dbSNP:rs757259

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 551 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000562601-258E3 ubiquitin ligase TRIM40

Proteomic databases

PTM databases

Expression

Tissue specificity

Highly expressed in normal gastrointestinal epithelia but that is down-regulated in gastrointestinal carcinomas and chronic inflammatory lesions of the gastrointestinal tract.

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts with NEDD8.

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for zinc finger, coiled coil.

TypeIDPosition(s)Description
Zinc finger14-56RING-type
Zinc finger66-107B box-type
Coiled coil107-159

Sequence similarities

Belongs to the TRIM/RBCC family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

Q6P9F5-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    258
  • Mass (Da)
    29,336
  • Last updated
    2009-05-05 v3
  • Checksum
    C360BECD4411F1DB
MIPLQKDNQEEGVCPICQESLKEAVSTNCGHLFCRVCLTQHVEKASASGVFCCPLCRKPCSEEVLGTGYICPNHQKRVCRFCEESRLLLCVECLVSPEHMSHHELTIENALSHYKERLNRRSRKLRKDIAELQRLKAQQEKKLQALQFQVDHGNHRLEAGPESQHQTREQLGALPQQWLGQLEHMPAEAARILDISRAVTQLRSLVIDLERTAKELDTNTLKNAGDLLNRSAPQKLEVIYPQLEKGVSELLLQPPQKL

Q6P9F5-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A140T9D5A0A140T9D5_HUMANTRIM40229
A0A0G2JMU7A0A0G2JMU7_HUMANTRIM40258
A0A0G2JK97A0A0G2JK97_HUMANTRIM40229
A0A0G2JIV5A0A0G2JIV5_HUMANTRIM40258

Features

Showing features for alternative sequence.

TypeIDPosition(s)Description
Alternative sequenceVSP_012131148-176in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF489517
EMBL· GenBank· DDBJ
AAM09503.1
EMBL· GenBank· DDBJ
mRNA
AB110939
EMBL· GenBank· DDBJ
BAD13705.1
EMBL· GenBank· DDBJ
Genomic DNA
AB110940
EMBL· GenBank· DDBJ
BAD13706.1
EMBL· GenBank· DDBJ
Genomic DNA
AB202084
EMBL· GenBank· DDBJ
BAE78604.1
EMBL· GenBank· DDBJ
Genomic DNA
AL669914
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BX322644
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AL671859
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CR788282
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BX927221
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CH471081
EMBL· GenBank· DDBJ
EAX03265.1
EMBL· GenBank· DDBJ
Genomic DNA
CH471081
EMBL· GenBank· DDBJ
EAX03266.1
EMBL· GenBank· DDBJ
Genomic DNA
BC060785
EMBL· GenBank· DDBJ
AAH60785.1
EMBL· GenBank· DDBJ
mRNA

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.
FeedbackHelp