| Post Translational Modifications | Phosphorylated at multiple Ser/Thr residues. Phosphorylated on tyrosine by LYN.which impairs its antiproliferative activity. Phosphorylation at Tyr-262 enhances proteasomal degradation, this position is dephosphorylated by PTPN2. Polyubiquitinated. Exhibits a rapid proteasomal degradation with a half-life under 1 hour, ubiquitination depends on endoplasmic reticulum association. |
| 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. Down-regulates the TGF-beta signaling pathway by promoting dephosphorylation of TGFB1 by PP1. May promote apoptosis by inducing p53/TP53 phosphorylation on 'Ser-15'. Plays an essential role in autophagy by tuning translation during starvation, thus enabling lysosomal biogenesis and a sustained autophagic flux. Acts also a viral restriction factor by attenuating HIV-1 replication. Mechanistically, mediates the inhibition of HIV-1 TAR RNA-mediated translation. (Microbial infection) Promotes enterovirus 71 replication by mediating the internal ribosome entry site (IRES) activity of viral 5'-UTR. |
| Protein Name | Protein Phosphatase 1 Regulatory Subunit 15aGrowth Arrest And Dna Damage-Inducible Protein Gadd34Myeloid Differentiation Primary Response Protein Myd116 Homolog |
| Database Links | Reactome: R-HSA-2173788Reactome: R-HSA-9648895 |
| Cellular Localisation | Endoplasmic Reticulum MembranePeripheral Membrane ProteinCytoplasmic SideMitochondrion Outer MembraneAssociates With Membranes Via An N-Terminal Amphipathic Intramembrane Region |
| Alternative Antibody Names | Anti-Protein Phosphatase 1 Regulatory Subunit 15a antibodyAnti-Growth Arrest And Dna Damage-Inducible Protein Gadd34 antibodyAnti-Myeloid Differentiation Primary Response Protein Myd116 Homolog antibodyAnti-PPP1R15A antibodyAnti-GADD34 antibody |
Information sourced from Uniprot.org
