O77666 · TRI26_PIG

  • Protein
    Tripartite motif-containing protein 26
  • Gene
    TRIM26
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

function

E3 ubiquitin-protein ligase which regulates the IFN-beta production and antiviral response downstream of various DNA-encoded pattern-recognition receptors (PRRs) (PubMed:33086712).
Plays also a central role in determining the response to different forms of oxidative stress by controlling levels of DNA glycosylases NEIL1, NEIL3 and NTH1 that are involved in repair of damaged DNA. Promotes nuclear IRF3 ubiquitination and proteasomal degradation. Bridges together TBK1 and NEMO during the innate response to viral infection leading to the activation of TBK1. Positively regulates LPS-mediated inflammatory innate immune response by catalyzing the 'Lys-11'-linked polyubiquitination of TAB1 to enhance its activation and subsequent NF-kappa-B and MAPK signalings. In a manner independent of its catalytic activity, inhibits WWP2, a SOX2-directed E3 ubiquitin ligase, and thus protects SOX2 from polyubiquitination and proteasomal degradation. Ubiquitinates the histone acetyltransferase protein complex component PHF20 and thereby triggers its degradation in the nucleus after its recruitment by the histone demethylase KDM6B, serving as a scaffold protein. Upon induction by TGF-beta, ubiquitinates the TFIID component TAF7 for proteasomal degradation (By similarity).
Induces ferroptosis by ubiquitinating SLC7A11, a critical protein for lipid reactive oxygen species (ROS) scavenging (By similarity).
Inhibitis Porcine reproductive and respiratory syndrome virus-2 by catalyzing the 'Lys-48'-linked polyubiquitination of the nucleocapsid protein N (PubMed:35077707).

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.

TypeIDPosition(s)Description
Binding site102Zn2+ (UniProtKB | ChEBI)
Binding site105Zn2+ (UniProtKB | ChEBI)
Binding site124Zn2+ (UniProtKB | ChEBI)
Binding site130Zn2+ (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentnucleus
Molecular Functionubiquitin protein ligase activity
Molecular Functionzinc ion binding
Biological Processinnate immune response
Biological Processnegative regulation of viral entry into host cell
Biological Processprotein ubiquitination

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Tripartite motif-containing protein 26
  • EC number
  • Alternative names
    • Zinc finger protein 173

Gene names

    • Name
      TRIM26
    • Synonyms
      ZNF173

Organism names

  • Taxonomic identifier
  • Strain
    • Large white
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Suina > Suidae > Sus

Accessions

  • Primary accession
    O77666

Proteomes

Subcellular Location

Cytoplasm
Nucleus
Note: Viral infection mediates TRIM26 nuclear translocation.

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000562381-545Tripartite motif-containing protein 26

Post-translational modification

Autoubiquitinates upon viral infection. In turn, autoubiquitinated TRIM26 recruits NEMO and bridges TBK1-NEMO interaction.

Keywords

Proteomic databases

Interaction

Subunit

Interacts with TBK1; this interaction bridges together TBK1 and NEMO in order to activate TBK1. Interacts with INCA1.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for zinc finger, coiled coil, domain, compositional bias, region.

TypeIDPosition(s)Description
Zinc finger16-57RING-type
Zinc finger97-138B box-type
Coiled coil172-226
Domain295-545B30.2/SPRY
Compositional bias376-402Acidic residues
Region376-440Disordered
Compositional bias414-440Acidic residues

Sequence similarities

Belongs to the TRIM/RBCC family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    545
  • Mass (Da)
    62,778
  • Last updated
    2000-05-01 v2
  • Checksum
    AF4E233309232C7E
MATSAPLRSLEEEVTCSICLDYLRDPVTIDCGHVFCRSCTTDIHPVSGGRPVCPLCKKPFTKENIRPVWQLASLVENIERLKVDTGRQPGEVAREQQDTRLCERHQEKLHYYCEDDGKLLCVMCRESREHRPHMAVLVEKAAQPHREKILNHLSTLRRDRDKIQGFQAKGEADILAELKKLQDQRQRILAAFEQGHQFLWEREQHLLDQLAKLEQEVTEGREKYKTRGDGELARLAQVISELEGKAQQPAAELMQDTRDFLTRYPRKKFWIGKPIARVVKKRTGEFSDKLLSLQRGLREFQGKLLRDLEYKTVSVTLDPQSASGYLQLSEDWKCVTYSGLYQSSYLHPQQFECEPGVLGSKGFTWGKVYWEVEVEREGWSEDEEEGDEEEEGEEEEEEEEAGYGAGFGYGDGYDDWGTDEDEESLGDEEEEEEEEEEEVLESCMVGVARDSVKRKGDLSLRPEDGVWALRLSSSGIWANTRPEAELFPAQRPRRVGIALDYEGGTVTFTNAESQELIYTFKATFTRRLLPFLWLRWPGTRLLLRP

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias376-402Acidic residues
Compositional bias414-440Acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJ251829
EMBL· GenBank· DDBJ
CAB63934.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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