Q9BRZ2 · TRI56_HUMAN
- ProteinE3 ubiquitin-protein ligase TRIM56
- GeneTRIM56
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids755 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
In response to pathogen- and host-derived double-stranded DNA (dsDNA), targets STING1 to 'Lys-63'-linked ubiquitination, thereby promoting its homodimerization, a step required for the production of type I interferon IFN-beta (By similarity).
Also mediate monoubiquitination of CGAS, thereby promoting CGAS oligomerization and subsequent activation (PubMed:29426904).
Promotes also TNFalpha-induced NF-kappa-B signaling by mediating 'Lys-63'-linked ubiquitination TAK1, leading to enhanced interaction between TAK1 and CHUK/IKKalpha (PubMed:35952808).
Independently of its E3 ubiquitin ligase activity, positive regulator of TLR3 signaling. Potentiates extracellular double stranded RNA (dsRNA)-induced expression of IFNB1 and interferon-stimulated genes ISG15, IFIT1/ISG56, CXCL10, OASL and CCL5/RANTES (PubMed:22948160).
Promotes establishment of an antiviral state by TLR3 ligand and TLR3-mediated chemokine induction following infection by hepatitis C virus (PubMed:22948160).
Acts as a restriction factor of Zika virus through direct interaction with the viral RNA via its C-terminal region (PubMed:31251739).
Catalytic activity
Pathway
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Molecular Function | RNA binding | |
Molecular Function | ubiquitin protein ligase activity | |
Molecular Function | ubiquitin-protein transferase activity | |
Molecular Function | zinc ion binding | |
Biological Process | defense response to virus | |
Biological Process | innate immune response | |
Biological Process | positive regulation of innate immune response | |
Biological Process | positive regulation of interferon-beta production | |
Biological Process | positive regulation of non-canonical NF-kappaB signal transduction | |
Biological Process | positive regulation of type I interferon-mediated signaling pathway | |
Biological Process | protein K63-linked ubiquitination | |
Biological Process | protein monoubiquitination | |
Biological Process | regulation of type I interferon production | |
Biological Process | response to type I interferon |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameE3 ubiquitin-protein ligase TRIM56
- 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 accessionQ9BRZ2
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 21 | Complete loss of autoubiquitination. Complete loss of autoubiquitination, loss of antiviral activity against yellow fever virus and human coronavirus virus OC43, but normal induction of interferon-beta following Sendai virus infection; when associated with A-24. | ||||
Sequence: C → A | ||||||
Mutagenesis | 24 | Complete loss of autoubiquitination, loss of antiviral activity against yellow fever virus and human coronavirus virus OC43, but normal induction of interferon-beta following Sendia virus infection; when associated with A-24. | ||||
Sequence: C → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 879 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 (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000056288 | 1-755 | UniProt | E3 ubiquitin-protein ligase TRIM56 | |||
Sequence: MVSHGSSPSLLEALSSDFLACKICLEQLRAPKTLPCLHTYCQDCLAQLADGGRVRCPECRETVPVPPEGVASFKTNFFVNGLLDLVKARACGDLRAGKPACALCPLVGGTSTGGPATARCLDCADDLCQACADGHRCTRQTHTHRVVDLVGYRAGWYDEEARERQAAQCPQHPGEALRFLCQPCSQLLCRECRLDPHLDHPCLPLAEAVRARRPGLEGLLAGVDNNLVELEAARRVEKEALARLREQAARVGTQVEEAAEGVLRALLAQKQEVLGQLRAHVEAAEEAARERLAELEGREQVARAAAAFARRVLSLGREAEILSLEGAIAQRLRQLQGCPWAPGPAPCLLPQLELHPGLLDKNCHLLRLSFEEQQPQKDGGKDGAGTQGGEESQSRREDEPKTERQGGVQPQAGDGAQTPKEEKAQTTREEGAQTLEEDRAQTPHEDGGPQPHRGGRPNKKKKFKGRLKSISREPSPALGPNLDGSGLLPRPIFYCSFPTRMPGDKRSPRITGLCPFGPREILVADEQNRALKRFSLNGDYKGTVPVPEGCSPCSVAALQSAVAFSASARLYLINPNGEVQWRRALSLSQASHAVAALPSGDRVAVSVAGHVEVYNMEGSLATRFIPGGKASRGLRALVFLTTSPQGHFVGSDWQQNSVVICDGLGQVVGEYKGPGLHGCQPGSVSVDKKGYIFLTLREVNKVVILDPKGSLLGDFLTAYHGLEKPRVTTMVDGRYLVVSLSNGTIHIFRVRSPDS | |||||||
Modified residue (large scale data) | 3 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 6 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 7 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 9 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 418 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 418 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 434 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 442 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 442 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 469 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 471 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 475 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 475 | 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 TICAM1 (PubMed:22948160).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9BRZ2 | TICAM1 Q8IUC6 | 2 | EBI-1048636, EBI-525995 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for zinc finger, coiled coil, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Zinc finger | 21-60 | RING-type | ||||
Sequence: CKICLEQLRAPKTLPCLHTYCQDCLAQLADGGRVRCPECR | ||||||
Zinc finger | 98-149 | B box-type 1 | ||||
Sequence: KPACALCPLVGGTSTGGPATARCLDCADDLCQACADGHRCTRQTHTHRVVDL | ||||||
Zinc finger | 164-205 | B box-type 2 | ||||
Sequence: RQAAQCPQHPGEALRFLCQPCSQLLCRECRLDPHLDHPCLPL | ||||||
Coiled coil | 216-314 | |||||
Sequence: LEGLLAGVDNNLVELEAARRVEKEALARLREQAARVGTQVEEAAEGVLRALLAQKQEVLGQLRAHVEAAEEAARERLAELEGREQVARAAAAFARRVLS | ||||||
Region | 371-484 | Disordered | ||||
Sequence: EEQQPQKDGGKDGAGTQGGEESQSRREDEPKTERQGGVQPQAGDGAQTPKEEKAQTTREEGAQTLEEDRAQTPHEDGGPQPHRGGRPNKKKKFKGRLKSISREPSPALGPNLDG | ||||||
Compositional bias | 421-453 | Basic and acidic residues | ||||
Sequence: EEKAQTTREEGAQTLEEDRAQTPHEDGGPQPHR |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q9BRZ2-1
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
- Length755
- Mass (Da)81,488
- Last updated2004-12-21 v3
- ChecksumCF72D0C8EC9F69E7
Q9BRZ2-2
- Name2
Q9BRZ2-3
- Name3
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
C9JI91 | C9JI91_HUMAN | TRIM56 | 305 | ||
A0A0D9SF19 | A0A0D9SF19_HUMAN | TRIM56 | 65 |
Sequence caution
Features
Showing features for sequence conflict, alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 230 | in Ref. 1; AK092927 | ||||
Sequence: L → P | ||||||
Alternative sequence | VSP_029109 | 259-269 | in isoform 3 | |||
Sequence: AEGVLRALLAQ → CLLRTESCKAE | ||||||
Alternative sequence | VSP_029110 | 270-755 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_029111 | 273-308 | in isoform 2 | |||
Sequence: VLGQLRAHVEAAEEAARERLAELEGREQVARAAAAF → NHLNPGGGSCSELRSHHCTPAWVTRMKLHLKKKKKK | ||||||
Alternative sequence | VSP_029112 | 309-755 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 421-453 | Basic and acidic residues | ||||
Sequence: EEKAQTTREEGAQTLEEDRAQTPHEDGGPQPHR |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK075255 EMBL· GenBank· DDBJ | BAC11500.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK092927 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
AC105446 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC005847 EMBL· GenBank· DDBJ | AAH05847.3 EMBL· GenBank· DDBJ | mRNA | ||
BC011882 EMBL· GenBank· DDBJ | AAH11882.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC048194 EMBL· GenBank· DDBJ | AAH48194.1 EMBL· GenBank· DDBJ | mRNA | ||
AL512757 EMBL· GenBank· DDBJ | CAC21676.1 EMBL· GenBank· DDBJ | mRNA |