Q8WV44 · TRI41_HUMAN
- ProteinE3 ubiquitin-protein ligase TRIM41
- GeneTRIM41
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids630 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Directly binds to influenza A virus or vesicular stomatitis virus nucleoproteins and targets them for ubiquitination and proteasomal degradation, thereby limiting viral infections (PubMed:28169297, PubMed:29899090, PubMed:31979016).
Activates the innate antiviral response by catalyzing monoubiquitination of CGAS, thereby activating CGAS (PubMed:29760876).
Also involved in innate antiviral response by mediating 'Lys-63'-linked polyubiquitylation of BCL10 which in turn hubs NEMO for activation of NF-kappa-B and IRF3 pathways (By similarity).
Catalyzes the ubiquitin-mediated degradation of other substrates including protein kinase C, ZSCAN21 or TOP3B suggesting additional roles besides its function in immune response (PubMed:17893151, PubMed:33378676).
Catalytic activity
Pathway
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nuclear body | |
Cellular Component | nucleolus | |
Molecular Function | identical protein binding | |
Molecular Function | ubiquitin protein ligase activity | |
Molecular Function | zinc ion binding | |
Biological Process | cellular response to lipopolysaccharide | |
Biological Process | cellular response to muramyl dipeptide | |
Biological Process | defense response to virus | |
Biological Process | positive regulation of type I interferon-mediated signaling pathway | |
Biological Process | protein monoubiquitination | |
Biological Process | protein ubiquitination |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameE3 ubiquitin-protein ligase TRIM41
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ8WV44
- Secondary accessions
Proteomes
Organism-specific databases
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 20 | Abolishes E3 ligase activity. | ||||
Sequence: C → A | ||||||
Natural variant | VAR_027914 | 78 | in dbSNP:rs6601178 | |||
Sequence: A → T | ||||||
Natural variant | VAR_027915 | 438 | in dbSNP:rs2241371 | |||
Sequence: D → G |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 734 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, cross-link, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000056262 | 1-630 | UniProt | E3 ubiquitin-protein ligase TRIM41 | |||
Sequence: MAAVAMTPNPVQTLQEEAVCAICLDYFTDPVSIGCGHNFCRVCVTQLWGGEDEEDRDELDREEEEEDGEEEEVEAVGAGAGWDTPMRDEDYEGDMEEEVEEEEEGVFWTSGMSRSSWDNMDYVWEEEDEEEDLDYYLGDMEEEDLRGEDEEDEEEVLEEVEEEDLDPVTPLPPPPAPRRCFTCPQCRKSFPRRSFRPNLQLANMVQVIRQMHPTPGRGSRVTDQGICPKHQEALKLFCEVDEEAICVVCRESRSHKQHSVVPLEEVVQEYKAKLQGHVEPLRKHLEAVQKMKAKEERRVTELKSQMKSELAAVASEFGRLTRFLAEEQAGLERRLREMHEAQLGRAGAAASRLAEQAAQLSRLLAEAQERSQQGGLRLLQDIKETFNRCEEVQLQPPEVWSPDPCQPHSHDFLTDAIVRKMSRMFCQAARVDLTLDPDTAHPALMLSPDRRGVRLAERRQEVADHPKRFSADCCVLGAQGFRSGRHYWEVEVGGRRGWAVGAARESTHHKEKVGPGGSSVGSGDASSSRHHHRRRRLHLPQQPLLQREVWCVGTNGKRYQAQSSTEQTLLSPSEKPRRFGVYLDYEAGRLGFYNAETLAHVHTFSAAFLGERVFPFFRVLSKGTRIKLCP | |||||||
Modified residue | 84 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Cross-link | 256 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 401 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 439 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 447 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 447 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 571 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Induction
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with NOD2 (PubMed:27812135).
Interacts with TRIM17; this interaction prevents TRIM41 activity on ZSCAN2 (By similarity).
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for zinc finger, compositional bias, region, coiled coil, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Zinc finger | 20-61 | RING-type; degenerate | ||||
Sequence: CAICLDYFTDPVSIGCGHNFCRVCVTQLWGGEDEEDRDELDR | ||||||
Compositional bias | 51-76 | Acidic residues | ||||
Sequence: EDEEDRDELDREEEEEDGEEEEVEAV | ||||||
Region | 51-86 | Disordered | ||||
Sequence: EDEEDRDELDREEEEEDGEEEEVEAVGAGAGWDTPM | ||||||
Compositional bias | 143-166 | Acidic residues | ||||
Sequence: EDLRGEDEEDEEEVLEEVEEEDLD | ||||||
Region | 143-176 | Disordered | ||||
Sequence: EDLRGEDEEDEEEVLEEVEEEDLDPVTPLPPPPA | ||||||
Zinc finger | 222-263 | B box-type | ||||
Sequence: TDQGICPKHQEALKLFCEVDEEAICVVCRESRSHKQHSVVPL | ||||||
Coiled coil | 264-373 | |||||
Sequence: EEVVQEYKAKLQGHVEPLRKHLEAVQKMKAKEERRVTELKSQMKSELAAVASEFGRLTRFLAEEQAGLERRLREMHEAQLGRAGAAASRLAEQAAQLSRLLAEAQERSQQ | ||||||
Domain | 413-630 | B30.2/SPRY | ||||
Sequence: LTDAIVRKMSRMFCQAARVDLTLDPDTAHPALMLSPDRRGVRLAERRQEVADHPKRFSADCCVLGAQGFRSGRHYWEVEVGGRRGWAVGAARESTHHKEKVGPGGSSVGSGDASSSRHHHRRRRLHLPQQPLLQREVWCVGTNGKRYQAQSSTEQTLLSPSEKPRRFGVYLDYEAGRLGFYNAETLAHVHTFSAAFLGERVFPFFRVLSKGTRIKLCP | ||||||
Region | 503-538 | Disordered | ||||
Sequence: ARESTHHKEKVGPGGSSVGSGDASSSRHHHRRRRLH |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
Q8WV44-1
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.
- Name1
- SynonymsTRIM41a, TRIM41alpha
- Length630
- Mass (Da)71,670
- Last updated2006-10-17 v3
- Checksum8E704CBEAB928BF5
Q8WV44-2
- Name2
- SynonymsTRIM41b, TRIM41beta, RINCK1
Q8WV44-3
- Name3
- Differences from canonical
- 1-420: Missing
Q8WV44-4
- Name4
- SynonymsRINCK2
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_012515 | 1-420 | in isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 51-76 | Acidic residues | ||||
Sequence: EDEEDRDELDREEEEEDGEEEEVEAV | ||||||
Compositional bias | 143-166 | Acidic residues | ||||
Sequence: EDLRGEDEEDEEEVLEEVEEEDLD | ||||||
Sequence conflict | 276 | in Ref. 1; BAD07472/BAD07473 and 5; BAB70617 | ||||
Sequence: G → E | ||||||
Alternative sequence | VSP_012516 | 381 | in isoform 4 | |||
Sequence: D → V | ||||||
Alternative sequence | VSP_012517 | 382-630 | in isoform 4 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_010395 | 490-518 | in isoform 2 | |||
Sequence: VEVGGRRGWAVGAARESTHHKEKVGPGGS → EPKEPSWPPAQPSLTYYVCPTDRPEFSFT | ||||||
Alternative sequence | VSP_010396 | 519-630 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB100366 EMBL· GenBank· DDBJ | BAD07472.1 EMBL· GenBank· DDBJ | mRNA | ||
AB100367 EMBL· GenBank· DDBJ | BAD07473.1 EMBL· GenBank· DDBJ | mRNA | ||
AF258579 EMBL· GenBank· DDBJ | AAG23782.1 EMBL· GenBank· DDBJ | mRNA | ||
CR457349 EMBL· GenBank· DDBJ | CAG33630.1 EMBL· GenBank· DDBJ | mRNA | ||
AK027601 EMBL· GenBank· DDBJ | BAG51358.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471165 EMBL· GenBank· DDBJ | EAW53712.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471165 EMBL· GenBank· DDBJ | EAW53708.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471165 EMBL· GenBank· DDBJ | EAW53709.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC004956 EMBL· GenBank· DDBJ | AAH04956.1 EMBL· GenBank· DDBJ | mRNA | ||
BC009762 EMBL· GenBank· DDBJ | AAH09762.2 EMBL· GenBank· DDBJ | mRNA | ||
BC018765 EMBL· GenBank· DDBJ | AAH18765.2 EMBL· GenBank· DDBJ | mRNA | ||
BC071887 EMBL· GenBank· DDBJ | AAH71887.1 EMBL· GenBank· DDBJ | mRNA | ||
BC090953 EMBL· GenBank· DDBJ | AAH90953.1 EMBL· GenBank· DDBJ | mRNA | ||
AB063180 EMBL· GenBank· DDBJ | BAB70617.1 EMBL· GenBank· DDBJ | mRNA |