Q38HM4 · TRI63_MOUSE
- ProteinE3 ubiquitin-protein ligase TRIM63
- GeneTrim63
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids350 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
E3 ubiquitin ligase. Mediates the ubiquitination and subsequent proteasomal degradation of CKM, GMEB1 and HIBADH. Regulates the proteasomal degradation of muscle proteins under amino acid starvation, where muscle protein is catabolized to provide other organs with amino acids. Inhibits de novo skeletal muscle protein synthesis under amino acid starvation. Regulates proteasomal degradation of cardiac troponin I/TNNI3 and probably of other sarcomeric-associated proteins. May play a role in striated muscle atrophy and hypertrophy by regulating an anti-hypertrophic PKC-mediated signaling pathway. May regulate the organization of myofibrils through TTN in muscle cells.
Catalytic activity
Pathway
Protein modification; protein ubiquitination.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | contractile muscle fiber | |
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | M band | |
Cellular Component | nucleus | |
Cellular Component | Z disc | |
Molecular Function | ubiquitin protein ligase activity | |
Molecular Function | ubiquitin-protein transferase activity | |
Molecular Function | zinc ion binding | |
Biological Process | cellular response to dexamethasone stimulus | |
Biological Process | muscle contraction | |
Biological Process | negative regulation of cardiac muscle hypertrophy | |
Biological Process | proteasome-mediated ubiquitin-dependent protein catabolic process | |
Biological Process | protein monoubiquitination | |
Biological Process | protein ubiquitination | |
Biological Process | regulation of gene expression | |
Biological Process | response to denervation involved in regulation of muscle adaptation | |
Biological Process | response to electrical stimulus involved in regulation of muscle adaptation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameE3 ubiquitin-protein ligase TRIM63
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ38HM4
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localizes to the M- and Z-lines in skeletal muscle (By similarity).
Colocalizes with TNNI3 in myocytes
Colocalizes with TNNI3 in myocytes
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
No visible phenotype under normal conditions. Under amino acid starvation, mice continue to synthesize muscle protein and degrade less muscle protein than wild-type, leading to a decrease in the blood levels of free amino acids. Besides, mutant mice display higher creatine kinase activity under amino acid starvation.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000056291 | 1-350 | E3 ubiquitin-protein ligase TRIM63 | |||
Sequence: MDYKSGLIPDGNAMENLEKQLICPICLEMFTKPVVILPCQHNLCRKCANDIFQAANPYWTNRGGSVSMSGGRFRCPSCRHEVIMDRHGVYGLQRNLLVENIIDIYKQECSSRPLQKGSHPMCKEHEDEKINIYCLTCEVPTCSLCKVFGAHQACEVAPLQSIFQGQKTELSNCISMLVAGNDRVQTIISQLVDSCRVTKENSHQVKEELSQKFDTLYAILDEKKSELLQRITQEQEEKLGFIEALILQYREQLEKSTKLVETAIQSLDEPGGATFLSSAKQLIKSNVEASKGCQLGKTEQGFENMDYFTLDLEHIAEALRAIDFGTDEEEEEFTEEEADEEEGVTTEGHQ |
Proteomic databases
PTM databases
Expression
Induction
By hydrogen peroxide. Up-regulated in response to amino acid starvation.
Interaction
Subunit
Homodimer. Homooligomer and heterooligomer. Interacts with SUMO2, titin/TTN and GMEB1. Interacts with TRIM54 and probably with TRIM55 (By similarity).
Interacts with TNNI3. Forms a ternary complex with RACK1 and PRKCE. Interacts with CKM
Interacts with TNNI3. Forms a ternary complex with RACK1 and PRKCE. Interacts with CKM
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for zinc finger, region, coiled coil, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Zinc finger | 23-79 | RING-type | ||||
Sequence: CPICLEMFTKPVVILPCQHNLCRKCANDIFQAANPYWTNRGGSVSMSGGRFRCPSCR | ||||||
Region | 74-218 | Interaction with TTN | ||||
Sequence: RCPSCRHEVIMDRHGVYGLQRNLLVENIIDIYKQECSSRPLQKGSHPMCKEHEDEKINIYCLTCEVPTCSLCKVFGAHQACEVAPLQSIFQGQKTELSNCISMLVAGNDRVQTIISQLVDSCRVTKENSHQVKEELSQKFDTLYA | ||||||
Zinc finger | 117-159 | B box-type | ||||
Sequence: GSHPMCKEHEDEKINIYCLTCEVPTCSLCKVFGAHQACEVAPL | ||||||
Coiled coil | 207-269 | |||||
Sequence: EELSQKFDTLYAILDEKKSELLQRITQEQEEKLGFIEALILQYREQLEKSTKLVETAIQSLDE | ||||||
Domain | 267-325 | COS | ||||
Sequence: LDEPGGATFLSSAKQLIKSNVEASKGCQLGKTEQGFENMDYFTLDLEHIAEALRAIDFG | ||||||
Compositional bias | 325-343 | Acidic residues | ||||
Sequence: GTDEEEEEFTEEEADEEEG | ||||||
Region | 325-350 | Disordered | ||||
Sequence: GTDEEEEEFTEEEADEEEGVTTEGHQ |
Domain
The RING-type zinc finger mediates interaction with SUMO2 and localization to the nucleus (By similarity).
Also required for the E3 ubiquitin ligase activity
Also required for the E3 ubiquitin ligase activity
The B box-type zinc finger mediates homodimerization.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q38HM4-1
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
- Length350
- Mass (Da)39,491
- Last updated2005-11-22 v1
- Checksum1840B7BB2F77DEC1
Q38HM4-2
- Name2
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for sequence conflict, alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 6 | in Ref. 2; BAC35199 | ||||
Sequence: G → S | ||||||
Sequence conflict | 42 | in Ref. 2; BAC35199 | ||||
Sequence: N → D | ||||||
Alternative sequence | VSP_016647 | 111-151 | in isoform 2 | |||
Sequence: SRPLQKGSHPMCKEHEDEKINIYCLTCEVPTCSLCKVFGAH → RSVCSRTAPPLPQAPPTSRSLQLLSPAQRASTLYRRQNLSS | ||||||
Alternative sequence | VSP_016648 | 152-350 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 325-343 | Acidic residues | ||||
Sequence: GTDEEEEEFTEEEADEEEG |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DQ229108 EMBL· GenBank· DDBJ | ABB16283.1 EMBL· GenBank· DDBJ | mRNA | ||
AK052911 EMBL· GenBank· DDBJ | BAC35199.1 EMBL· GenBank· DDBJ | mRNA |