Eif2ak4
entrez
27103
canonical
uniprot
Q9QZ05
canonical
ensembl
ENSMUSG00000005102
resolver
ensp
ENSMUSP00000005233
resolver
ensp
ENSMUSP00000099586
resolver
ensp
ENSMUSP00000106498
resolver
ensp
ENSMUSP00000318673
resolver
ensp
ENSMUSP00000318674
resolver
ensp
ENSMUSP00000318680
resolver
ensp
ENSMUSP00000318692
resolver
enst
ENSMUST00000005233
resolver
enst
ENSMUST00000110874
resolver
genesymbol
Eif2ak4
resolver
genesymbol_syn
Gcn2
resolver
genesymbol_syn
Kiaa1338
resolver
uniprot
A2AUM0
resolver
uniprot
A2AUM1
resolver
uniprot
A2AUM3
resolver
uniprot
A2AUM4
resolver
uniprot
Q6GQT4
resolver
uniprot
Q6ZPT5
resolver
uniprot
Q8C5S0
resolver
uniprot
Q8CIF5
resolver
uniprot
Q9CT30
resolver
uniprot
Q9CUV9
resolver
uniprot
Q9ESB6
resolver
uniprot
Q9ESB7
resolver
uniprot
Q9ESB8
resolver
uniprot_entry
A2AUM0_MOUSE
resolver
uniprot_entry
A2AUM1_MOUSE
resolver
uniprot_entry
E2AK4_MOUSE
resolver
uniprot_sec
A2AUM3
resolver
uniprot_sec
A2AUM4
resolver
uniprot_sec
Q6GQT4
resolver
uniprot_sec
Q6ZPT5
resolver
uniprot_sec
Q8C5S0
resolver
uniprot_sec
Q8CIF5
resolver
uniprot_sec
Q9CT30
resolver
uniprot_sec
Q9CUV9
resolver
uniprot_sec
Q9ESB6
resolver
uniprot_sec
Q9ESB7
resolver
uniprot_sec
Q9ESB8
resolver
activity_regulation
ACTIVITY REGULATION: (Microbial infection) Kinase activity is enhanced by alphavirus genomic RNA sequences (PubMed:16601681). Kinase activity is stimulated upon binding to uncharged tRNAs (PubMed:16601681). Activated by serum starvation (in vitro) (PubMed:10504407). {ECO:0000269|PubMed:10504407, ECO:0000269|PubMed:16601681}.
uniprot
proteins
amino_acid_sequence
MAGGRGASGRGRAEPQESYSQRQDHELQALEAIYGSDFQDLRPDARGRVREPPEINLVLYPQGLAGEEVYVQVELQVKCPPTYPDVVPEIELKNAKGLSNESVNLLKSHLEELAKKQCGEVMIFELAHHVQSFLSEHNKPPPKSFHEEMLERQAQEKQQRLLEARRKEEQEQREILHEIQRRKEEIKEEKKRKEMAKQERLEITSLTNQDYASKRDPAGHRAAAILHGGSPDFVGNGKARTYSSGRSRRERQYSVCSGEPSPGSCDILHFSVGSPDQLMVHKGRCVGSDEQLGKVVYNALETATGSFVLLHEWVLQWQKMGPCLTSQEKEKIDKCKRQIQGAETEFSSLVKLSHPNIVRYFAMNSREEEDSIVIDILAEHVSGISLATHLSHSGPVPAHQLRKYTAQLLAGLDYLHSNSVVHKVLSASSVLVDAEGTVKITDYSISKRLADICKEDVFEQARVRFSDSALPYKTGKKGDVWRLGLLLLSLSQGQECGEYPVTIPSDLPADFQDFLKKCVCLDDKERWSPQQLLKHSFINPQPKLPLVEQSPEDSGGQDYIETVIPSNQLPSAAFFSETQKQFSRYFIEFEELQLLGKGAFGAVIKVQNKLDGCCYAVKRIPINPASRHFRRIKGEVTLLSRLHHENIVRYYNAWIERHERPAVPGTPPPDCTPQAQDSPATCGKTSGDTEELGSVEAAAPPPILSSSVEWSTSAERSTSTRFPVTGQDSSSDEEDEDERDGVFSQSFLPASDSDSDIIFDNEDENSKSQNQDEDCNQKDGSHEIEPSVTAEAVHYLYIQMEYCEKSTLRDTIDQGLFRDTSRLWRLFREILDGLAYIHEKGMIHRDLKPVNIFLDSDDHVKIGDFGLATDHLAFTAEGKQDDQAGDGVIKSDPSGHLTGMVGTALYVSPEVQGSTKSAYNQKVDLFSLGIIFFEMSYHPMVTASERIFVLNQLRDPTSPKFPDDFDDGEHTKQKSVISWLLNHDPAKRPTAMELLKSELLPPPQMEESELHEVLHHTLANIDGKAYRTMMSQIFCQHISPAIDYTYDSDILKGNFLIRTAKIQQLVCETIVRVFKRHGAVQLCTPLLLPRNRQIYEHNEAALFMDHSGMLVMLPFDLRVPFARYVARNNILNLKRYCIERVFRPRKLDRFHPKELLECAFDIVTSTTNSSLPTAETIYTIYEIIQEFPALQERNYSIYLNHTMLLKAILLHCGIPEDKLSQVYVILYDAVTEKLTRREVEAKFCNLSLSSNSLCRLYKFIEQKGDLQDLTPTINSLIKQKTGVAQLVKYSLKDLEDVVGLLKKLGVKLQVSINLGLVYKVQQHTGIIFQFLAFSKRRQRVVPEILAAGGRYDLLIPKFRGPQTVGPVPTAVGVSIAIDKIFAAVLNMEEPVTVSSCDLLVVSVGQMSMSRAINLTQKLWTAGITAEIMYDWSQSQEELQEYCRHHEITYVALVSDKEGSHVKVKSFEKERQTEKRVLESDLVDHVMQKLRTKVGDERNFRDASDNLAVQTLKGSFSNASGLFEIHGTTVVPNVIVLAPEKLSASTRRRHEIQVQTRLQTTLANLHQKSSEIEILAVDLPKETILQFLSLEWDADEQAFNTTVKQLLSRLPKQRYLKLVCDEIYNIKVEKKVSVLFLYSYRDDYYRILF
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 (PubMed:10504407, PubMed:10655230, PubMed:12176355, PubMed:12215525, PubMed:15213227, PubMed:15774759, PubMed:16054071, PubMed:16121183, PubMed:16176978, PubMed:16601681, PubMed:26102367). Plays a role as an activator of the integrated stress response (ISR) required for adaptation to amino acid starvation (PubMed:10655230, PubMed:11106749, PubMed:12176355, PubMed:15213227, PubMed:16176978, PubMed:26102367). 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 (PubMed:10655230, PubMed:11106749, PubMed:12176355, PubMed:15213227, PubMed:16176978, PubMed:26102367). Required for the translational induction of protein kinase PRKCH following amino acid starvation (PubMed:19797084). 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 (PubMed:16176978, PubMed:26102367). Plays a role in the consolidation of synaptic plasticity, learning as well as formation of long-term memory (PubMed:16121183). Plays a role in neurite outgrowth inhibition (PubMed:23447528). Plays a role in feeding behavior to maintain amino acid homeostasis; contributes to the innate aversion toward diets of imbalanced amino acid composition (PubMed:15774759, PubMed:16054071). Plays a proapoptotic role in response to glucose deprivation (PubMed:20660158). 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 (PubMed:12176355). {ECO:0000250|UniProtKB:P15442, ECO:0000269|PubMed:10504407, ECO:0000269|PubMed:10655230, ECO:0000269|PubMed:11106749, ECO:0000269|PubMed:12176355, ECO:0000269|PubMed:12215525, ECO:0000269|PubMed:15213227, ECO:0000269|PubMed:15774759, ECO:0000269|PubMed:16054071, ECO:0000269|PubMed:16121183, ECO:0000269|PubMed:16176978, ECO:0000269|PubMed:16601681, ECO:0000269|PubMed:19797084, ECO:0000269|PubMed:20660158, ECO:0000269|PubMed:23447528, ECO:0000269|PubMed:26102367}.; FUNCTION: (Microbial infection) 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. {ECO:0000269|PubMed:16601681}.; FUNCTION: (Microbial infection) Plays a role in modulating the adaptive immune response to Yellow fever virus infection; promotes dendritic cells to initiate autophagy and antigene presentation to both CD4(+) and CD8(+) T-cells under amino acid starvation. {ECO:0000269|PubMed:24310610}.
uniprot
proteins
mass_dalton
186487
uniprot
proteins
mutagenesis
MUTAGEN 618; /note="K->R: Inhibits autophosphorylation, eIF-2-alpha phosphorylation and antiviral activity against Sindbis virus."; /evidence="ECO:0000269|PubMed:16601681"; MUTAGEN 1142; /note="F->L: Decreases autophosphorylation, binding to tRNA and Sindbis virus genomic RNA and eIF-2-alpha phosphorylation in amino acid-starved cells; when associated with I-1143."; /evidence="ECO:0000269|PubMed:16601681"; MUTAGEN 1143; /note="R->I: Decreases autophosphorylation, binding to tRNA and Sindbis virus genomic RNA and eIF-2-alpha phosphorylation in amino acid-starved cells; when associated with L-1142."; /evidence="ECO:0000269|PubMed:16601681
uniprot
proteins
post_translational_modification
PTM: Autophosphorylated; autophosphorylation on Thr-898 is increased upon amino acid starvation and in UV irradiation cells and inhibited in presence of IMPACT (PubMed:10504407, PubMed:10655230, PubMed:11106749, PubMed:12176355, PubMed:16601681, PubMed:24333428). {ECO:0000269|PubMed:10504407, ECO:0000269|PubMed:10655230, ECO:0000269|PubMed:11106749, ECO:0000269|PubMed:12176355, ECO:0000269|PubMed:16601681, ECO:0000269|PubMed:24333428}.
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
10504407
uniprot
proteins
pubmed
10655230
uniprot
proteins
pubmed
11106749
uniprot
proteins
pubmed
12176355
uniprot
proteins
pubmed
12215525
uniprot
proteins
pubmed
14621295
uniprot
proteins
pubmed
15213227
uniprot
proteins
pubmed
15273307
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15774759
uniprot
proteins
pubmed
16054071
uniprot
proteins
pubmed
16121183
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16176978
uniprot
proteins
pubmed
16601681
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19797084
uniprot
proteins
pubmed
20660158
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23447528
uniprot
proteins
pubmed
24310610
uniprot
proteins
pubmed
24333428
uniprot
proteins
pubmed
25329545
uniprot
proteins
pubmed
26102367
uniprot
proteins
sequence_length
1648
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:23447528}.
uniprot
proteins