Q6Q0C0 · TRAF7_HUMAN
- ProteinE3 ubiquitin-protein ligase TRAF7
- GeneTRAF7
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids670 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
E3 ubiquitin and SUMO-protein ligase that plays a role in different biological processes such as innate immunity, inflammation or apoptosis (PubMed:15001576, PubMed:37086853).
Potentiates MAP3K3-mediated activation of JUN/AP1 and DDIT3 transcriptional regulators (PubMed:14743216).
Negatively regulates MYB transcriptional activity by sequestering it to the cytosol via SUMOylation (By similarity).
Plays a role in the phosphorylation of MAPK1 and/or MAPK3, probably via its interaction with MAP3K3. Negatively regulates RLR-mediated innate immunity by promoting 'Lys-48'-linked ubiquitination of TBK1 through its RING domain to inhibit the cellular antiviral response (PubMed:37086853).
Promotes 'Lys-29'-linked polyubiquitination of NEMO/IKBKG and RELA leading to targeting these two proteins to lysosomal degradative pathways, reducing the transcriptional activity of NF-kappa-B (PubMed:21518757).
Potentiates MAP3K3-mediated activation of JUN/AP1 and DDIT3 transcriptional regulators (PubMed:14743216).
Negatively regulates MYB transcriptional activity by sequestering it to the cytosol via SUMOylation (By similarity).
Plays a role in the phosphorylation of MAPK1 and/or MAPK3, probably via its interaction with MAP3K3. Negatively regulates RLR-mediated innate immunity by promoting 'Lys-48'-linked ubiquitination of TBK1 through its RING domain to inhibit the cellular antiviral response (PubMed:37086853).
Promotes 'Lys-29'-linked polyubiquitination of NEMO/IKBKG and RELA leading to targeting these two proteins to lysosomal degradative pathways, reducing the transcriptional activity of NF-kappa-B (PubMed:21518757).
Catalytic activity
Pathway
Protein modification; protein ubiquitination.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasmic vesicle | |
Cellular Component | intracellular membrane-bounded organelle | |
Cellular Component | nucleolus | |
Cellular Component | plasma membrane | |
Cellular Component | ubiquitin ligase complex | |
Molecular Function | ubiquitin protein ligase activity | |
Molecular Function | ubiquitin-protein transferase activity | |
Molecular Function | zinc ion binding | |
Biological Process | apoptotic process | |
Biological Process | Notch signaling pathway | |
Biological Process | positive regulation of apoptotic signaling pathway | |
Biological Process | positive regulation of MAPK cascade | |
Biological Process | positive regulation of neuron apoptotic process | |
Biological Process | positive regulation of ubiquitin-dependent protein catabolic process | |
Biological Process | protein K29-linked ubiquitination | |
Biological Process | protein ubiquitination | |
Biological Process | regulation of ERK1 and ERK2 cascade | |
Biological Process | ribosomal large subunit assembly |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameE3 ubiquitin-protein ligase TRAF7
- 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 accessionQ6Q0C0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Colocalizes with MAP3K3 to vesicle-like structures throughout the cytoplasm.
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Cardiac, facial, and digital anomalies with developmental delay (CAFDADD)
- Note
- DescriptionAn autosomal dominant disorder characterized by delayed motor and speech development, developmental regression, congenital heart defects, limb and digital anomalies, and dysmorphic features. Cardiac features include pulmonary stenosis, patent ductus arteriosus, aortic coarctation, valvular defects, hypoplastic left heart, double outlet right ventricle, and conduction abnormalities. Dysmorphic facial features include multiple hair whorls or hairline abnormalities, ptosis, epicanthal folds, and low-set or dysplastic ears.
- See alsoMIM:618164
Natural variants in CAFDADD
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_081685 | 346 | K>E | in CAFDADD; no significant effect on phosphorylation of MAPK1 and/or MAPK3; dbSNP:rs1567252467 | |
VAR_081686 | 371 | R>G | in CAFDADD; decreased phosphorylation of MAPK1 and/or MAPK3; dbSNP:rs1567252659 | |
VAR_081687 | 601 | T>A | in CAFDADD; decreased phosphorylation of MAPK1 and/or MAPK3; dbSNP:rs1567254067 | |
VAR_081688 | 655 | R>Q | in CAFDADD; decreased phosphorylation of MAPK1 and/or MAPK3; dbSNP:rs1331463984 |
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 131 | Complete loss of IFN-beta promoter inhibition after viral infection. | ||||
Sequence: C → S | ||||||
Natural variant | VAR_081685 | 346 | in CAFDADD; no significant effect on phosphorylation of MAPK1 and/or MAPK3; dbSNP:rs1567252467 | |||
Sequence: K → E | ||||||
Natural variant | VAR_081686 | 371 | in CAFDADD; decreased phosphorylation of MAPK1 and/or MAPK3; dbSNP:rs1567252659 | |||
Sequence: R → G | ||||||
Natural variant | VAR_081687 | 601 | in CAFDADD; decreased phosphorylation of MAPK1 and/or MAPK3; dbSNP:rs1567254067 | |||
Sequence: T → A | ||||||
Natural variant | VAR_081688 | 655 | in CAFDADD; decreased phosphorylation of MAPK1 and/or MAPK3; dbSNP:rs1331463984 | |||
Sequence: R → Q |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 944 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
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_0000051296 | 1-670 | UniProt | E3 ubiquitin-protein ligase TRAF7 | |||
Sequence: MSSGKSARYNRFSGGPSNLPTPDVTTGTRMETTFGPAFSAVTTITKADGTSTYKQHCRTPSSSSTLAYSPRDEEDSMPPISTPRRSDSAISVRSLHSESSMSLRSTFSLPEEEEEPEPLVFAEQPSVKLCCQLCCSVFKDPVITTCGHTFCRRCALKSEKCPVDNVKLTVVVNNIAVAEQIGELFIHCRHGCRVAGSGKPPIFEVDPRGCPFTIKLSARKDHEGSCDYRPVRCPNNPSCPPLLRMNLEAHLKECEHIKCPHSKYGCTFIGNQDTYETHLETCRFEGLKEFLQQTDDRFHEMHVALAQKDQEIAFLRSMLGKLSEKIDQLEKSLELKFDVLDENQSKLSEDLMEFRRDASMLNDELSHINARLNMGILGSYDPQQIFKCKGTFVGHQGPVWCLCVYSMGDLLFSGSSDKTIKVWDTCTTYKCQKTLEGHDGIVLALCIQGCKLYSGSADCTIIVWDIQNLQKVNTIRAHDNPVCTLVSSHNVLFSGSLKAIKVWDIVGTELKLKKELTGLNHWVRALVAAQSYLYSGSYQTIKIWDIRTLDCIHVLQTSGGSVYSIAVTNHHIVCGTYENLIHVWDIESKEQVRTLTGHVGTVYALAVISTPDQTKVFSASYDRSLRVWSMDNMICTQTLLRHQGSVTALAVSRGRLFSGAVDSTVKVWTC | |||||||
Modified residue (large scale data) | 13 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 21 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 59 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 61 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 61 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 63 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 64 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 69 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 76 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 86 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 88 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 88 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 91 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 94 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 97 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 99 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 108 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 317 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 658 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated by MAP3K3.
Ubiquitinates itself upon phosphorylation.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Ubiquitously expressed with high levels in skeletal muscle, heart, colon, spleen, kidney, liver and placenta.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Homodimer. Interacts with MAP3K3 and promotes the kinase activity of this enzyme.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q6Q0C0 | CYTH4 Q9UIA0 | 2 | EBI-307556, EBI-11521003 | |
BINARY | Q6Q0C0 | LIME1 Q9H400 | 2 | EBI-307556, EBI-2830566 | |
BINARY | Q6Q0C0 | MAP3K3 Q99759 | 3 | EBI-307556, EBI-307281 | |
XENO | Q6Q0C0 | Ripk4 Q9ERK0 | 2 | EBI-307556, EBI-6116422 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, zinc finger, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-37 | Disordered | ||||
Sequence: MSSGKSARYNRFSGGPSNLPTPDVTTGTRMETTFGPA | ||||||
Compositional bias | 49-70 | Polar residues | ||||
Sequence: GTSTYKQHCRTPSSSSTLAYSP | ||||||
Region | 49-97 | Disordered | ||||
Sequence: GTSTYKQHCRTPSSSSTLAYSPRDEEDSMPPISTPRRSDSAISVRSLHS | ||||||
Compositional bias | 81-97 | Polar residues | ||||
Sequence: STPRRSDSAISVRSLHS | ||||||
Zinc finger | 131-165 | RING-type | ||||
Sequence: CQLCCSVFKDPVITTCGHTFCRRCALKSEKCPVDN | ||||||
Zinc finger | 222-276 | TRAF-type | ||||
Sequence: HEGSCDYRPVRCPNNPSCPPLLRMNLEAHLKECEHIKCPHSKYGCTFIGNQDTYE | ||||||
Repeat | 394-433 | WD 1 | ||||
Sequence: GHQGPVWCLCVYSMGDLLFSGSSDKTIKVWDTCTTYKCQK | ||||||
Repeat | 437-474 | WD 2 | ||||
Sequence: GHDGIVLALCIQGCKLYSGSADCTIIVWDIQNLQKVNT | ||||||
Repeat | 477-513 | WD 3 | ||||
Sequence: AHDNPVCTLVSSHNVLFSGSLKAIKVWDIVGTELKLK | ||||||
Repeat | 515-554 | WD 4 | ||||
Sequence: ELTGLNHWVRALVAAQSYLYSGSYQTIKIWDIRTLDCIHV | ||||||
Repeat | 557-594 | WD 5 | ||||
Sequence: TSGGSVYSIAVTNHHIVCGTYENLIHVWDIESKEQVRT | ||||||
Repeat | 597-638 | WD 6 | ||||
Sequence: GHVGTVYALAVISTPDQTKVFSASYDRSLRVWSMDNMICTQT | ||||||
Repeat | 641-669 | WD 7 | ||||
Sequence: RHQGSVTALAVSRGRLFSGAVDSTVKVWT |
Sequence similarities
Belongs to the WD repeat TRAF7 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q6Q0C0-1
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
- Length670
- Mass (Da)74,609
- Last updated2004-07-05 v1
- Checksum5624045D674849C6
Q6Q0C0-2
- Name2
- Differences from canonical
- 1-76: Missing
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H3BUP4 | H3BUP4_HUMAN | TRAF7 | 54 | ||
H3BR17 | H3BR17_HUMAN | TRAF7 | 147 | ||
A0A087WUB0 | A0A087WUB0_HUMAN | TRAF7 | 86 | ||
A0A994J4N1 | A0A994J4N1_HUMAN | TRAF7 | 589 |
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_051607 | 1-76 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 49-70 | Polar residues | ||||
Sequence: GTSTYKQHCRTPSSSSTLAYSP | ||||||
Compositional bias | 81-97 | Polar residues | ||||
Sequence: STPRRSDSAISVRSLHS |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY569455 EMBL· GenBank· DDBJ | AAS68363.1 EMBL· GenBank· DDBJ | mRNA | ||
AL136921 EMBL· GenBank· DDBJ | CAB66855.1 EMBL· GenBank· DDBJ | mRNA |