O77666 · TRI26_PIG
- ProteinTripartite motif-containing protein 26
- GeneTRIM26
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids545 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
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).
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
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Molecular Function | ubiquitin protein ligase activity | |
Molecular Function | zinc ion binding | |
Biological Process | innate immune response | |
Biological Process | negative regulation of viral entry into host cell | |
Biological Process | protein ubiquitination |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTripartite motif-containing protein 26
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Suina > Suidae > Sus
Accessions
- Primary accessionO77666
Proteomes
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000056238 | 1-545 | Tripartite motif-containing protein 26 | |||
Sequence: MATSAPLRSLEEEVTCSICLDYLRDPVTIDCGHVFCRSCTTDIHPVSGGRPVCPLCKKPFTKENIRPVWQLASLVENIERLKVDTGRQPGEVAREQQDTRLCERHQEKLHYYCEDDGKLLCVMCRESREHRPHMAVLVEKAAQPHREKILNHLSTLRRDRDKIQGFQAKGEADILAELKKLQDQRQRILAAFEQGHQFLWEREQHLLDQLAKLEQEVTEGREKYKTRGDGELARLAQVISELEGKAQQPAAELMQDTRDFLTRYPRKKFWIGKPIARVVKKRTGEFSDKLLSLQRGLREFQGKLLRDLEYKTVSVTLDPQSASGYLQLSEDWKCVTYSGLYQSSYLHPQQFECEPGVLGSKGFTWGKVYWEVEVEREGWSEDEEEGDEEEEGEEEEEEEEAGYGAGFGYGDGYDDWGTDEDEESLGDEEEEEEEEEEEVLESCMVGVARDSVKRKGDLSLRPEDGVWALRLSSSGIWANTRPEAELFPAQRPRRVGIALDYEGGTVTFTNAESQELIYTFKATFTRRLLPFLWLRWPGTRLLLRP |
Post-translational modification
Autoubiquitinates upon viral infection. In turn, autoubiquitinated TRIM26 recruits NEMO and bridges TBK1-NEMO interaction.
Keywords
- PTM
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Zinc finger | 16-57 | RING-type | ||||
Sequence: CSICLDYLRDPVTIDCGHVFCRSCTTDIHPVSGGRPVCPLCK | ||||||
Zinc finger | 97-138 | B box-type | ||||
Sequence: QDTRLCERHQEKLHYYCEDDGKLLCVMCRESREHRPHMAVLV | ||||||
Coiled coil | 172-226 | |||||
Sequence: ADILAELKKLQDQRQRILAAFEQGHQFLWEREQHLLDQLAKLEQEVTEGREKYKT | ||||||
Domain | 295-545 | B30.2/SPRY | ||||
Sequence: RGLREFQGKLLRDLEYKTVSVTLDPQSASGYLQLSEDWKCVTYSGLYQSSYLHPQQFECEPGVLGSKGFTWGKVYWEVEVEREGWSEDEEEGDEEEEGEEEEEEEEAGYGAGFGYGDGYDDWGTDEDEESLGDEEEEEEEEEEEVLESCMVGVARDSVKRKGDLSLRPEDGVWALRLSSSGIWANTRPEAELFPAQRPRRVGIALDYEGGTVTFTNAESQELIYTFKATFTRRLLPFLWLRWPGTRLLLRP | ||||||
Compositional bias | 376-402 | Acidic residues | ||||
Sequence: REGWSEDEEEGDEEEEGEEEEEEEEAG | ||||||
Region | 376-440 | Disordered | ||||
Sequence: REGWSEDEEEGDEEEEGEEEEEEEEAGYGAGFGYGDGYDDWGTDEDEESLGDEEEEEEEEEEEVL | ||||||
Compositional bias | 414-440 | Acidic residues | ||||
Sequence: DDWGTDEDEESLGDEEEEEEEEEEEVL |
Sequence similarities
Belongs to the TRIM/RBCC family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length545
- Mass (Da)62,778
- Last updated2000-05-01 v2
- ChecksumAF4E233309232C7E
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 376-402 | Acidic residues | ||||
Sequence: REGWSEDEEEGDEEEEGEEEEEEEEAG | ||||||
Compositional bias | 414-440 | Acidic residues | ||||
Sequence: DDWGTDEDEESLGDEEEEEEEEEEEVL |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ251829 EMBL· GenBank· DDBJ | CAB63934.1 EMBL· GenBank· DDBJ | Genomic DNA |