Ttc5
entrez
219022
canonical
uniprot
Q99LG4
canonical
ensembl
ENSMUSG00000006288
resolver
ensp
ENSMUSP00000006451
resolver
ensp
ENSMUSP00000154412
resolver
enst
ENSMUST00000006451
resolver
enst
ENSMUST00000226768
resolver
genesymbol
Ttc5
resolver
genesymbol_syn
Strap
resolver
uniprot
A0A2I3BR21
resolver
uniprot
Q3TTN5
resolver
uniprot
Q3TZL6
resolver
uniprot
Q8BNN3
resolver
uniprot
Q8C8M9
resolver
uniprot_entry
A0A2I3BR21_MOUSE
resolver
uniprot_entry
Q8BNN3_MOUSE
resolver
uniprot_entry
Q8C8M9_MOUSE
resolver
uniprot_entry
TTC5_MOUSE
resolver
uniprot_sec
Q3TTN5
resolver
uniprot_sec
Q3TZL6
resolver
amino_acid_sequence
MMADEEEEAKHVLQKLQGLVDRLYCFRDSYFETHSVEDAGRKQQDVQEEMEKTLQQMEEVLGSAQVEAQALMLKGKALNVTPDYSPEAEVLLSKAVKLEPELVEAWNQLGEVYWKKGDVASAHTCFSGALTHCKNKVSLQNLSMVLRQLQTDSGDEHSRHVMDSVRQAKLAVQMDVLDGRSWYILGNAYLSLYFNTGQNPKISQQALSAYAQAEKVDRKASSNPDLHLNRATLHKYEESYGEALEGFSQAAALDPVWPEPQQREQQLLEFLSRLTSLLESKGKTKPKKLQSMLGSLRPAHLGPCGDGRYQSASGQKMTLELKPLSTLQPGVNSGTVVLGKVVFSLTTEEKVPFTFGLVDSDGPCYAVMVYNVVQSWGVLIGDSVAIPEPNLRHHQIRHKGKDYSFSSVRVETPLLLVVNGKPQNSSSQASATVASRPQCE
uniprot
proteins
function
FUNCTION: Cofactor involved in the regulation of various cellular mechanisms such as actin regulation, autophagy, chromatin regulation and DNA repair (PubMed:11511361, PubMed:15448695, PubMed:18451878, PubMed:30420355). 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 (PubMed:30420355). Acts as a negative regulator of nutrient stress-induced autophagy by inhibiting JMY's interaction with MAP1LC3B, thereby preventing autophagosome formation (PubMed:30420355). Involves in tubulin autoregulation by promoting its degradation in response to excess soluble tubulin (By similarity). 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 (PubMed:15448695, PubMed:18833288). 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 (PubMed:11511361). Also recruits arginine methyltransferase PRMT5 to p53/TP53 when DNA is damaged, allowing PRMT5 to methylate p53/TP53 (PubMed:19011621). In DNA stress conditions, also prevents p53/TP53 degradation by E3 ubiquitin ligase MDM2 (PubMed:11511361). 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 (PubMed:18451878). 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 (PubMed:25168243). Mitochondrial TTC5/STRAP also regulates p53/TP53-mediated apoptosis (PubMed:25168243). {ECO:0000250|UniProtKB:Q8N0Z6, ECO:0000269|PubMed:11511361, ECO:0000269|PubMed:15448695, ECO:0000269|PubMed:18451878, ECO:0000269|PubMed:18833288, ECO:0000269|PubMed:19011621, ECO:0000269|PubMed:25168243, ECO:0000269|PubMed:30420355}.
uniprot
proteins
mass_dalton
48795
uniprot
proteins
mutagenesis
MUTAGEN 13..24; /note="Missing: Increased nuclear localization in non-stress conditions. No change in protein accumulation and stability in response to DNA damage. No change in subcellular localization in non-stress conditions; when associated with 13-L--Y-24. No change in protein accumulation and stability in response to DNA damage; when associated with 13-L--Y-24."; /evidence="ECO:0000269|PubMed:18833288"; MUTAGEN 203; /note="S->A: Loss of phosphorylation at S-203; decreased nuclear localization in non-stress conditions; loss of nuclear accumulation and stability in response to DNA damage. No change in subcellular localization in non-stress conditions; when associated with 13-L--Y-24. No change in protein accumulation and stability in response to DNA damage; when associated with 13-L--Y-24."; /evidence="ECO:0000269|PubMed:15448695, ECO:0000269|PubMed:18833288"; MUTAGEN 203; /note="S->D: No change in subcellular localization in non-stress conditions. No change in protein accumulation and stability in response to DNA damage."; /evidence="ECO:0000269|PubMed:18833288"; MUTAGEN 221; /note="S->A: Decreased phosphorylation. No change in subcellular localization in non-stress conditions. No change in nuclear accumulation in response to DNA damage. Impaired stability in response to DNA damage."; /evidence="ECO:0000269|PubMed:18833288
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:0000269|PubMed:15448695, ECO:0000269|PubMed:18833288}.
uniprot
proteins
pubmed
11511361
uniprot
proteins
pubmed
15448695
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
18451878
uniprot
proteins
pubmed
18833288
uniprot
proteins
pubmed
19011621
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
22362889
uniprot
proteins
pubmed
25168243
uniprot
proteins
pubmed
30420355
uniprot
proteins
sequence_length
440
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15448695, ECO:0000269|PubMed:18833288}. Cytoplasm {ECO:0000269|PubMed:15448695, ECO:0000269|PubMed:18833288, ECO:0000269|PubMed:25168243, ECO:0000269|PubMed:30420355}. Cytoplasmic vesicle {ECO:0000269|PubMed:30420355}. Mitochondrion matrix {ECO:0000269|PubMed:25168243}. Note=Phosphorylation at Ser-203 results in nuclear localization, while unphosphorylated protein localizes to the cytoplasm (PubMed:15448695). Nuclear localization may be necessary for DNA damage-dependent stabilization of the protein (PubMed:15448695, PubMed:18833288). {ECO:0000269|PubMed:15448695, ECO:0000269|PubMed:18833288}.
uniprot
proteins