D4A7V9
uniprot
D4A7V9
canonical
amino_acid_sequence
MAGGRGAAGRGPAEPQESYSQRQDHELQALEAIYGSDFQDLRPDARGRVREPPEINLVLYPQGLAGEEVYVQVELRVKCPPTYPDVVPEIELKNTKGLSNESVNLLKSHLEELAKKQCGEVMIFELAHHVQSFLSEHNKPPPKSFHEEMLERQAQEKQQRLLEARQKEEQEQREILHEIQKRKEEIKEEKKRKEMAKQERLEITSLTNQDHASKRDPAGHRAAAFLHGGSPDFVGNGKARAHSSGRSRRERQYSVCSGEASPGSCDILYFCVGSADQLMVHKGKCVGSDEQLGKVVYNALETATGSFVLLYEWVLQWQKKMGPCLTSQEKEKIDKCKKQIQGAETEFSSLVKLSHPNIVRYFAMNSREEKDSIVVDILAEHISGISLAAHLSHSGPVPMHQLRKYTAQLLAGLDYLHRNSVVHKVLSTASVLVDAEGTVKITDYSISKRLADICKEDVFEQTRVRFSDSALPYKTGKKGDVWRLGLLLLSLSQGQECEEYPVTIPSDLPADFQDFLKKCVCLDDKERWSPQQLLKHSFINPQPKMPLVEQSPEDSGGQDYIETIIPSNQLPSAAFFTETQRQFSRYFIEFEELQLLGKGAFGAVIKVQNKLDGCCYAVKRIPINPASRQFRRIKGEVTLLSRLHHENIVRYYNAWIERHERPAVPGTPPPDYIPQAQNSSATGGKASGDTEELGSVEAAAPPPILSSSVEWSTSAERSNSARFPVTGQDSSSDEEDEDERDGVFSQSFLPASDSDSDIIFDNEDENSKSQNQDEDCNEKDSRHEIEPSVTTEAVHYLYIQMEYCEKSTLRDTIDQGLFRDTSRLWRLFREILDGLAYIHEKGMIHRDLKPVNIFLDSDDHVKIGDFGLATDHLAFNAEGKQDDQAGDHVIKSDPSGHLTGMVGTALYVSPEVQGSTKSAYNQKVDLFSLGIILFEMSYHPMVTASERIFVLNQLRDPTSPKFPDDFEDGEHTKQKSVISWLLNHDPAKRPTAMELLKSELLPPPQMEESELHEVLHHTLANTDGKAYRTMMSQLFCQHSSPAIDYTYDSDILKGNFLIRTAKIQQLVCETIVRVFKRHGAVQLCTPLLLPRNRQIYEHNEAALFMDHSGMLVMLPFDLRVPFARYVARNNILNLKRYCIERVFRPRKLDRFHPKELLECAFDIVTSTANSSLPTAETIYTIYEVIQEFPALQERNYSIYLNHTMLLKAILLHCGIPEDKLSQVYVILYDAVTEKLTRREVEAKFCNLSLSSNSLCRLYKFIEQKGDLQDLTPTINSLIKQKTGIAQLVKYSLKDLEEVVGLLKKLGVKLQVSINLGLVYKVQQHNGIIFQFLAFSKRRQRVVPEILAAGGRYDLLIPKFRGPQALGPVPTAVGVSIAIDKIFAAVLNMGEPVTVSSCDLLVVSAGQMSMSRAINLTQKLWTAGITAEIMYDWSQSQEELQEYCRHHEITYVALVSDKEGSHVKVKSFEKERQTEKRVLESDLVDHVMQKLRTKVGDERNFRDASDNLAVQTLKGSFSNASGLFEIHGTTVVPTVSVISPEKLSASTRRRHEIQVQTRLQTTLANLHQKSSEIEILAVDLPKETILQFLSLEWDADEQAFNTTVKQLLSRLPKQRYLKLVCDEIYNIKVEKKVSVLFLYSYRDDYYRILF
uniprot
proteins
ec_number
2.7.11.1
uniprot
proteins
function
FUNCTION: Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) in response to low amino acid availability (By similarity). Plays a role as an activator of the integrated stress response (ISR) required for adaptation to amino acid starvation (By similarity). EIF2S1/eIF-2-alpha phosphorylation in response to stress converts EIF2S1/eIF-2-alpha into a global protein synthesis inhibitor, leading to a global attenuation of cap-dependent translation, and thus to a reduced overall utilization of amino acids, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activator ATF4, and hence allowing ATF4-mediated reprogramming of amino acid biosynthetic gene expression to alleviate nutrient depletion (By similarity). Required for the translational induction of protein kinase PRKCH following amino acid starvation (By similarity). Binds uncharged tRNAs (By similarity). Involved in cell cycle arrest by promoting cyclin D1 mRNA translation repression after the unfolded protein response pathway (UPR) activation or cell cycle inhibitor CDKN1A/p21 mRNA translation activation in response to amino acid deprivation (By similarity). Plays a role in the consolidation of synaptic plasticity, learning as well as formation of long-term memory (By similarity). Plays a role in neurite outgrowth inhibition (By similarity). Plays a role in feeding behavior to maintain amino acid homeostasis; contributes to the innate aversion toward diets of imbalanced amino acid composition (PubMed:15051816, PubMed:15774759). Plays a proapoptotic role in response to glucose deprivation (By similarity). Promotes global cellular protein synthesis repression in response to UV irradiation independently of the stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK) and p38 MAPK signaling pathways (By similarity). Plays a role in the antiviral response against alphavirus infection; impairs early viral mRNA translation of the incoming genomic virus RNA, thus preventing alphavirus replication (By similarity). {ECO:0000250|UniProtKB:P15442, ECO:0000250|UniProtKB:Q9P2K8, ECO:0000250|UniProtKB:Q9QZ05, ECO:0000269|PubMed:15051816, ECO:0000269|PubMed:15774759}.
uniprot
proteins
mass_dalton
186724
uniprot
proteins
post_translational_modification
PTM: Autophosphorylated; autophosphorylation on Thr-899 is increased upon amino acid starvation and in UV irradiation cells and inhibited in presence of IMPACT. {ECO:0000250|UniProtKB:Q9QZ05}.
uniprot
proteins
protein_family
GCN2 subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
Ser/Thr protein kinase family
uniprot
proteins
pubmed
15051816
uniprot
proteins
pubmed
15057822
uniprot
proteins
pubmed
15774759
uniprot
proteins
sequence_length
1649
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9QZ05}.
uniprot
proteins