Ttc5
entrez
305837
canonical
uniprot
Q5BK48
canonical
ensembl
ENSRNOG00000008850
resolver
ensembl
ENSRNOG00055026252
resolver
ensembl
ENSRNOG00060027657
resolver
ensembl
ENSRNOG00065031049
resolver
ensp
ENSRNOP00000011741
resolver
ensp
ENSRNOP00055037159
resolver
ensp
ENSRNOP00060040005
resolver
ensp
ENSRNOP00065044008
resolver
enst
ENSRNOT00000011741
resolver
enst
ENSRNOT00055045339
resolver
enst
ENSRNOT00060048071
resolver
enst
ENSRNOT00065053548
resolver
genesymbol
Ttc5
resolver
uniprot_entry
TTC5_RAT
resolver
amino_acid_sequence
MMADEEEEAKQVLQKLQELVDQLYCFRDSYFETHSVEDAGQKQQDVQEEMEKTLRQMEEVLGSVQVEAQALMLKGKALNVTPDYSPEAEVLLSKAVKLEPELVEAWNQLGEVYWKKGDVAAAHTCFSGALTHCKNKVSLQNLSMVLRQLQTDSGDEHSRHVMDSVRQAKLAVQMDVLDGRSWYILGNAYLSLYFNTGQNPKISQQALSAYAQAEKVDRKASSNPDLHLNRATLHKYEESYGEALEGFSQAATLDPAWPEPQQREQQLLEFLSRLTNLLASKGKTKPKKLQSMLGNLRPAHLGPCGDGRYQSATGQKVTLQLKPLSTLQPGVNSGTVVLGKVVFSLTTEEKVPFTFGLVDSDGPCYAVMVYNVVQSWGVLIGDSVAIPEPNLRHHQIQHKGKDYSFSSVRVETPLLLVVNGKPQNSSSQASATVASRPQCE
uniprot
proteins
function
FUNCTION: Cofactor involved in the regulation of various cellular mechanisms such as actin regulation, autophagy, chromatin regulation and DNA repair. In physiological conditions, interacts with cofactor JMY in the cytoplasm which prevents JMY's actin nucleation activity and ability to activate the Arp2/3 complex. Acts as a negative regulator of nutrient stress-induced autophagy by inhibiting JMY's interaction with MAP1LC3B, thereby preventing autophagosome formation (By similarity). Involves in tubulin autoregulation by promoting its degradation in response to excess soluble tubulin. To do so, associates with the active ribosome near the ribosome exit tunnel and with nascent tubulin polypeptides early during their translation, triggering tubulin mRNA-targeted degradation (By similarity). Following DNA damage, phosphorylated by DNA damage responsive protein kinases ATM and CHEK2, leading to its nuclear accumulation and stability. Nuclear TTC5/STRAP promotes the assembly of a stress-responsive p53/TP53 coactivator complex, which includes the coactivators JMY and p300, thereby increasing p53/TP53-dependent transcription and apoptosis. Also recruits arginine methyltransferase PRMT5 to p53/TP53 when DNA is damaged, allowing PRMT5 to methylate p53/TP53. In DNA stress conditions, also prevents p53/TP53 degradation by E3 ubiquitin ligase MDM2. Upon heat-shock stress, forms a chromatin-associated complex with heat-shock factor 1 HSF1 and p300/EP300 to stimulate heat-shock-responsive transcription, thereby increasing cell survival. Mitochondrial TTC5/STRAP interacts with ATP synthase subunit beta ATP5F1B which decreased ATP synthase activity and lowers mitochondrial ATP production, thereby regulating cellular respiration and mitochondrial-dependent apoptosis. Mitochondrial TTC5/STRAP also regulates p53/TP53-mediated apoptosis (By similarity). {ECO:0000250|UniProtKB:Q8N0Z6, ECO:0000250|UniProtKB:Q99LG4}.
uniprot
proteins
mass_dalton
48793
uniprot
proteins
post_translational_modification
PTM: Phosphorylation by ATM kinase induces nuclear accumulation while interfering with nuclear export, and phosphorylation by CHEK2 kinase enhances nuclear stability. {ECO:0000250|UniProtKB:Q99LG4}.
uniprot
proteins
pubmed
15489334
uniprot
proteins
sequence_length
440
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q99LG4}. Cytoplasm {ECO:0000250|UniProtKB:Q99LG4}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q99LG4}. Mitochondrion matrix {ECO:0000250|UniProtKB:Q99LG4}. Note=Phosphorylation at Ser-203 results in nuclear localization, while unphosphorylated protein localizes to the cytoplasm. Nuclear localization may be necessary for DNA damage-dependent stabilization of the protein. {ECO:0000250|UniProtKB:Q99LG4}.
uniprot
proteins