D3ZSP7 · TTC3_RAT
- ProteinE3 ubiquitin-protein ligase TTC3
- GeneTtc3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids2000 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
E3 ubiquitin-protein ligase which catalyzes the formation of 'Lys-48'-polyubiquitin chains (By similarity).
Mediates the ubiquitination and subsequent degradation of phosphorylated Akt (AKT1, AKT2 and AKT3) in the nucleus (By similarity).
Acts as a terminal regulator of Akt signaling after activation; its phosphorylation by Akt, which is a prerequisite for ubiquitin ligase activity, suggests the existence of a regulation mechanism required to control Akt levels after activation (By similarity).
Positively regulates TGFB1-induced epithelial-mesenchymal transition and myofibroblast differentiation by mediating the ubiquitination and subsequent degradation of SMURF2 (By similarity).
Regulates neuronal differentiation by regulating actin remodeling and Golgi organization via a signaling cascade involving RHOA, CIT and ROCK (PubMed:24695496).
Inhibits cell proliferation (By similarity).
Mediates the ubiquitination and subsequent degradation of phosphorylated Akt (AKT1, AKT2 and AKT3) in the nucleus (By similarity).
Acts as a terminal regulator of Akt signaling after activation; its phosphorylation by Akt, which is a prerequisite for ubiquitin ligase activity, suggests the existence of a regulation mechanism required to control Akt levels after activation (By similarity).
Positively regulates TGFB1-induced epithelial-mesenchymal transition and myofibroblast differentiation by mediating the ubiquitination and subsequent degradation of SMURF2 (By similarity).
Regulates neuronal differentiation by regulating actin remodeling and Golgi organization via a signaling cascade involving RHOA, CIT and ROCK (PubMed:24695496).
Inhibits cell proliferation (By similarity).
Catalytic activity
Pathway
Protein modification; protein ubiquitination.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | Golgi apparatus | |
Cellular Component | nucleus | |
Cellular Component | vacuole | |
Molecular Function | metal ion binding | |
Molecular Function | ubiquitin-protein transferase activity | |
Biological Process | negative regulation of axon extension | |
Biological Process | negative regulation of neuron differentiation | |
Biological Process | protein K48-linked ubiquitination | |
Biological Process | ubiquitin-dependent protein catabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameE3 ubiquitin-protein ligase TTC3
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionD3ZSP7
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Nuclear localization may be dependent on the proteolytic cleavage of full length protein in the cytoplasm (By similarity).
This cleavage may reveal an N-terminal nuclear localization signal, allowing N-terminal fragments to enter the nucleus (By similarity).
This cleavage may reveal an N-terminal nuclear localization signal, allowing N-terminal fragments to enter the nucleus (By similarity).
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000448697 | 1-2000 | E3 ubiquitin-protein ligase TTC3 | ||
Modified residue | 397 | Phosphoserine | |||
Modified residue | 1029 | Phosphoserine | |||
Modified residue | 1080 | Phosphoserine | |||
Post-translational modification
Phosphorylation on Ser-397 by Akt is required for ubiquitin ligase activity.
Proteolytically cleaved into differently sized N- and C-terminal fragments.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Interacts (when phosphorylated on Ser-397) with AKT1, AKT2 and AKT3 (when phosphorylated) (By similarity).
Interacts with CIT (By similarity).
Interacts with POLG (By similarity).
Interacts with HSP70 (By similarity).
Interacts with SMURF2 (By similarity).
Interacts with CIT (By similarity).
Interacts with POLG (By similarity).
Interacts with HSP70 (By similarity).
Interacts with SMURF2 (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, repeat, compositional bias, zinc finger.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 20-249 | Interaction with POLG | |||
Repeat | 250-283 | TPR 1 | |||
Repeat | 284-317 | TPR 2 | |||
Region | 442-478 | Disordered | |||
Repeat | 556-592 | TPR 3 | |||
Repeat | 596-629 | TPR 4 | |||
Compositional bias | 804-826 | Basic and acidic residues | |||
Region | 804-828 | Disordered | |||
Region | 1041-1087 | Disordered | |||
Region | 1233-1308 | Disordered | |||
Compositional bias | 1266-1280 | Polar residues | |||
Region | 1423-1448 | Disordered | |||
Region | 1806-1839 | Disordered | |||
Compositional bias | 1808-1839 | Polar residues | |||
Compositional bias | 1894-1913 | Basic and acidic residues | |||
Region | 1894-1947 | Disordered | |||
Zinc finger | 1952-1991 | RING-type; atypical | |||
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,000
- Mass (Da)225,783
- Last updated2015-07-22 v3
- Checksum2716C704140F51AE
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I6AR04 | A0A8I6AR04_RAT | Ttc3 | 1981 | ||
A0A8I6ABF8 | A0A8I6ABF8_RAT | Ttc3 | 1963 | ||
A0A8I5Y675 | A0A8I5Y675_RAT | Ttc3 | 1992 | ||
A0A8I5Y7R0 | A0A8I5Y7R0_RAT | Ttc3 | 311 | ||
A0A8L2QUD9 | A0A8L2QUD9_RAT | Ttc3 | 2000 | ||
A0A8I6A4G2 | A0A8I6A4G2_RAT | Ttc3 | 1626 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 804-826 | Basic and acidic residues | |||
Compositional bias | 1266-1280 | Polar residues | |||
Compositional bias | 1808-1839 | Polar residues | |||
Compositional bias | 1894-1913 | Basic and acidic residues | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AABR07033674 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AABR07033675 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AABR07033676 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |