Ppp1r15a
entrez
17872
canonical
uniprot
P17564
canonical
ensembl
ENSMUSG00000040435
resolver
ensp
ENSMUSP00000049488
resolver
genesymbol
Ppp1r15a
resolver
genesymbol_syn
Gadd34
resolver
genesymbol_syn
Myd116
resolver
uniprot
B2RRL7
resolver
uniprot
Q3TJS6
resolver
uniprot
Q3U3L5
resolver
uniprot
Q8C579
resolver
uniprot_entry
B2RRL7_MOUSE
resolver
uniprot_entry
PR15A_MOUSE
resolver
uniprot_sec
Q3TJS6
resolver
uniprot_sec
Q3U3L5
resolver
uniprot_sec
Q8C579
resolver
amino_acid_sequence
MAPSPRPQHVLHWRDAHNFYLLSPLMGLLSRAWSRLRGPEVPEAWLAKTVTGADQIEAAALLTPTPVSGNLLPHGETEESGSPEQSQAAQRLCLVEAESSPPETWGLSNVDEYNAKPGQDDLREKEMERTAGKATLQPAGLQGADKRLGEVVAREEGVAEPAYPTSQLEGGPAENEEDGETVKTYQASAASIAPGYKPSTPVPFLGEAEHQATEEKGTENKADPSNSPSSGSHSRAWEYYSREKPKQEGEAKVEAHRAGQGHPCRNAEAEEGGPETTFVCTGNAFLKAWVYRPGEDTEEEDNSDSDSAEEDTAQTGATPHTSAFLKAWVYRPGEDTEEEDSDSDSAEEDTAQTGATPHTSAFLKAWVYRPGEDTEEENSDLDSAEEDTAQTGATPHTSAFLKAWVYRPGEDTEEENSDLDSAEEDTAQTGATPHTSPFLKAWVYRPGEDTEDDTEEEEDSENVAPGDSETADSSQSPCLQPQRCLPGEKTKGRGEEPPLFQVAFYLPGEKPESPWAAPKLPLRLQRRLRLFKAPTRDQDPEIPLKARKVHFAEKVTVHFLAVWAGPAQAARRGPWEQFARDRSRFARRIAQAEEKLGPYLTPDSRARAWARLRNPSLPQSEPRSSSEATPLTQDVTTPSPLPSETPSPSLYLGGRRG
uniprot
proteins
function
FUNCTION: Recruits the serine/threonine-protein phosphatase PPP1CA to prevents excessive phosphorylation of the translation initiation factor eIF-2A/EIF2S1, thereby reversing the shut-off of protein synthesis initiated by stress-inducible kinases and facilitating recovery of cells from stress (PubMed:11381086, PubMed:12824288). Down-regulates the TGF-beta signaling pathway by promoting dephosphorylation of TGFB1 by PP1 (By similarity). May promote apoptosis by inducing TP53 phosphorylation on 'Ser-15' (By similarity). Plays an essential role in autophagy by tuning translation during starvation, thus enabling lysosomal biogenesis and a sustained autophagic flux (By similarity). Also acts a viral restriction factor by attenuating vesicular stomatitis virus (VSV) replication (PubMed:17670836). {ECO:0000250|UniProtKB:O75807, ECO:0000269|PubMed:11381086, ECO:0000269|PubMed:12606582, ECO:0000269|PubMed:12824288, ECO:0000269|PubMed:16478986, ECO:0000269|PubMed:17670836}.
uniprot
proteins
mass_dalton
71840
uniprot
proteins
mutagenesis
MUTAGEN 549; /note="V->E: Abolishes interaction with PP1."; /evidence="ECO:0000269|PubMed:11381086
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at multiple Ser/Thr residues. Phosphorylated on tyrosine by LYN; which impairs its antiproliferative activity. Phosphorylation at Tyr-239 enhances proteasomal degradation, this position is dephosphorylated by PTPN2. {ECO:0000250|UniProtKB:O75807}.; PTM: Polyubiquitinated. Exhibits a rapid proteasomal degradation with a half-life under 1 hour, ubiquitination depends on endoplasmic reticulum association. {ECO:0000250|UniProtKB:O75807}.
uniprot
proteins
protein_family
PPP1R15 family
uniprot
proteins
pubmed
11381086
uniprot
proteins
pubmed
11517336
uniprot
proteins
pubmed
12606582
uniprot
proteins
pubmed
12824288
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16478986
uniprot
proteins
pubmed
17670836
uniprot
proteins
pubmed
19131336
uniprot
proteins
pubmed
2339071
uniprot
proteins
pubmed
8139541
uniprot
proteins
pubmed
9023344
uniprot
proteins
pubmed
9371605
uniprot
proteins
sequence_length
657
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side {ECO:0000250|UniProtKB:O75807}. Mitochondrion outer membrane; Peripheral membrane protein; Cytoplasmic side {ECO:0000250|UniProtKB:O75807}. Note=Associates with membranes via an N-terminal amphipathic intramembrane region. {ECO:0000250|UniProtKB:O75807}.
uniprot
proteins