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Protein

eIF-2-alpha kinase GCN2

Gene

Eif2ak4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (eIF-2-alpha/EIF2S1) on 'Ser-52' in response to low amino acid availability (PubMed:10504407, PubMed:10655230, PubMed:12176355, PubMed:12215525, PubMed:15213227, PubMed:16054071, PubMed:16176978, PubMed:16121183, PubMed:15774759, PubMed:16601681, PubMed:26102367). Plays a role as an activator of the integrated stress response (ISR) required for adapatation to amino acid starvation. Converts phosphorylated eIF-2-alpha/EIF2S1 either to a competitive inhibitor of the translation initiation factor eIF-2B, leading to a global protein synthesis repression, and thus to a reduced overall utilization of amino acids, or to a translational initiation activation of 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). 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:16054071, PubMed:15774759). 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).By similarity14 Publications
(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 (PubMed:16601681). 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 (PubMed:24310610).2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.3 Publications

Enzyme regulationi

(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).2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei618 – 6181ATPPROSITE-ProRule annotation
Active sitei846 – 8461Proton acceptorPROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi595 – 6039ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • eukaryotic initiation factor eIF2 binding Source: ParkinsonsUK-UCL
  • eukaryotic translation initiation factor 2alpha kinase activity Source: UniProtKB
  • protein serine/threonine kinase activity Source: UniProtKB
  • tRNA binding Source: UniProtKB

GO - Biological processi

  • adaptive immune response Source: UniProtKB-KW
  • cell cycle arrest Source: UniProtKB-KW
  • cellular response to amino acid starvation Source: UniProtKB
  • cellular response to cold Source: UniProtKB
  • cellular response to leucine starvation Source: UniProtKB
  • cellular response to starvation Source: MGI
  • cellular response to UV Source: UniProtKB
  • defense response to virus Source: UniProtKB-KW
  • eiF2alpha phosphorylation in response to endoplasmic reticulum stress Source: UniProtKB
  • endoplasmic reticulum unfolded protein response Source: MGI
  • induction by virus of host autophagy Source: UniProtKB
  • learning Source: UniProtKB
  • long-term memory Source: UniProtKB
  • negative regulation by host of viral genome replication Source: UniProtKB
  • negative regulation of CREB transcription factor activity Source: UniProtKB
  • negative regulation of neuron differentiation Source: UniProtKB
  • negative regulation of translation Source: MGI
  • negative regulation of translational initiation Source: UniProtKB
  • negative regulation of translational initiation in response to stress Source: UniProtKB
  • neuron projection extension Source: UniProtKB
  • positive regulation of adaptive immune response Source: UniProtKB
  • positive regulation of defense response to virus by host Source: UniProtKB
  • positive regulation of gene expression Source: ParkinsonsUK-UCL
  • positive regulation of long-term synaptic potentiation Source: UniProtKB
  • positive regulation of translational initiation in response to starvation Source: UniProtKB
  • protein autophosphorylation Source: UniProtKB
  • protein phosphorylation Source: UniProtKB
  • regulation of eIF2 alpha phosphorylation by amino acid starvation Source: UniProtKB
  • regulation of feeding behavior Source: UniProtKB
  • regulation of translational initiation Source: UniProtKB
  • regulation of translational initiation by eIF2 alpha phosphorylation Source: UniProtKB
  • regulation of translational initiation in response to stress Source: MGI
  • response to endoplasmic reticulum stress Source: ParkinsonsUK-UCL
  • T cell activation involved in immune response Source: UniProtKB
  • viral translation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Activator, Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Biological processi

Activation of host autophagy by virus, Adaptive immunity, Antiviral defense, Cell cycle, Differentiation, Growth arrest, Host-virus interaction, Immunity, Neurogenesis, Stress response, Translation regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding, tRNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
eIF-2-alpha kinase GCN2Curated
Alternative name(s):
Eukaryotic translation initiation factor 2-alpha kinase 4Imported (EC:2.7.11.13 Publications)
GCN2-like protein
Short name:
mGCN2
Gene namesi
Name:Eif2ak4Imported
Synonyms:Gcn2, Kiaa1338
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1353427. Eif2ak4.

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

  • cytosolic ribosome Source: UniProtKB
  • intracellular Source: MGI
  • polysome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Mice are viable, fertile, and exhibit no phenotypic abnormalities under standard growth conditions (PubMed:12215525). Show an increase in prenatal and neonatal mortalities when essential amino acids are absent in the maternal diet during gestation (PubMed:12215525, PubMed:15213227). In response to nutrient deprivation, display reduced abilities to chronically down-regulate hepatic protein synthesis, resulting in preservation of liver mass relative to body size and enhanced skeletal muscle loss (PubMed:15213227). Mice exhibit a lowered threshold for the induction of strong and robust long-term potentiation (LTP) in the CA1 neurons of the hippocampus and the consolidation of long-term memory (PubMed:16121183). Knockout and conditional knockout in the brain result in a diminution of the rate of food consumption and an impairment in the food aversion response in mice fed an imbalanced amino acid diet (PubMed:16054071). Mice are more susceptible to intranasal Sindbis virus infection, with high virus titers in the brain compared to similarly infected control animals (PubMed:16601681). Mice infected with yellow fever virus show a decrease in dendritic cell autophagy and an impairment in their capacity to present antigens to T-cells under amino acid starvation (PubMed:24310610).6 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi618 – 6181K → R: Inhibits autophosphorylation, eIF-2-alpha phosphorylation and antiviral activity against Sindbis virus. 1 Publication
Mutagenesisi1142 – 11421F → 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. 1 Publication
Mutagenesisi1143 – 11431R → 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. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 16481648eIF-2-alpha kinase GCN2PRO_0000085948Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei230 – 2301PhosphoserineBy similarity
Modified residuei666 – 6661PhosphothreonineBy similarity
Modified residuei898 – 8981Phosphothreonine; by autocatalysis2 Publications
Modified residuei903 – 9031Phosphothreonine; by autocatalysisBy similarity
Modified residuei1258 – 12581N6-acetyllysineBy similarity

Post-translational modificationi

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).6 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9QZ05.
MaxQBiQ9QZ05.
PaxDbiQ9QZ05.
PRIDEiQ9QZ05.

PTM databases

iPTMnetiQ9QZ05.
PhosphoSiteiQ9QZ05.

Expressioni

Tissue specificityi

Expressed in liver (PubMed:10504407). Expressed predominantly in the hippocampal CA1 region and the dentate gyrus, and to a lesser degree in CA3 (at protein level) (PubMed:16121183). Expressed in liver, lung, brain, kidney, skeletal muscle and testis (PubMed:10504407, PubMed:10655230). Expressed weakly in heart and spleen (PubMed:10655230). Expressed in the hippocampal CA1 and CA3 regions, the dentate gyrus and cerebellum (PubMed:16121183). Isoform 1 is widely expressed (PubMed:12215525). Isoform 1 is expressed in brain, liver, skeletal muscle and testis (PubMed:10655230). Isoform 3 is expressed in lung, brain, testis, prostate and choroid plexus (PubMed:12215525). Isoform 4 is expressed in muscle, lung, kidney, brain, testis and prostate (PubMed:10655230, PubMed:12215525).4 Publications

Gene expression databases

BgeeiQ9QZ05.
ExpressionAtlasiQ9QZ05. baseline and differential.
GenevisibleiQ9QZ05. MM.

Interactioni

Subunit structurei

Homodimer; homodimerization is important for kinase activation by uncharged tRNAs (By similarity). Interacts with GCN1; this interaction stimulates EIF2AK4/GCN2 kinase activity and is impaired by IMPACT upon a variety of stress conditions, such as amino acid depletion, UV-C irradiation, proteasome inhibitor treatment and glucose deprivation (PubMed:24333428). Interacts with DNAJC3; this interaction inhibits EIF2AK4/GCN2 kinase activity during endoplasmic reticulum (ER), hypothermic and amino acid-starving stress conditions (PubMed:25329545).By similarity2 Publications

GO - Molecular functioni

  • eukaryotic initiation factor eIF2 binding Source: ParkinsonsUK-UCL

Protein-protein interaction databases

BioGridi205123. 2 interactions.
STRINGi10090.ENSMUSP00000005233.

Structurei

Secondary structure

1
1648
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi19 – 3315Combined sources
Beta strandi35 – 406Combined sources
Beta strandi46 – 483Combined sources
Beta strandi55 – 595Combined sources
Beta strandi66 – 683Combined sources
Beta strandi72 – 776Combined sources
Turni81 – 844Combined sources
Beta strandi91 – 10111Combined sources
Helixi102 – 11716Combined sources
Helixi123 – 13715Combined sources
Beta strandi1532 – 15365Combined sources
Helixi1543 – 155614Combined sources
Helixi1558 – 15625Combined sources
Helixi1563 – 15653Combined sources
Beta strandi1566 – 157712Combined sources
Helixi1580 – 15867Combined sources
Helixi1595 – 160713Combined sources
Helixi1613 – 162614Combined sources
Beta strandi1631 – 16388Combined sources
Turni1639 – 16424Combined sources
Beta strandi1643 – 16475Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UKXNMR-A17-139[»]
4OTNX-ray1.90A/B1514-1648[»]
ProteinModelPortaliQ9QZ05.
SMRiQ9QZ05. Positions 21-144, 290-577, 584-657, 753-1016, 1058-1488, 1526-1648.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9QZ05.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 137113RWDPROSITE-ProRule annotationAdd
BLAST
Domaini286 – 538253Protein kinase 1PROSITE-ProRule annotationAdd
BLAST
Domaini589 – 1000412Protein kinase 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1021 – 1492472Histidyl-tRNA synthetase-likeAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili146 – 20560Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi483 – 4908Poly-Leu

Domaini

The histidyl-tRNA synthetase-like region and protein kinase domains are necessary for eIF-2-alpha kinase activity and eIF-2-alpha-mediated translational control (PubMed:10655230). The histidyl-tRNA synthetase-like domain is necessary for binding to uncharged tRNAs (PubMed:16601681). Kinase domain 1 is a degenerate kinase domain (PubMed:10504407).2 Publications

Sequence similaritiesi

Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. GCN2 subfamily.PROSITE-ProRule annotation
Contains 2 protein kinase domains.PROSITE-ProRule annotation
Contains 1 RWD domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiKOG1035. Eukaryota.
COG0124. LUCA.
GeneTreeiENSGT00530000062984.
HOVERGENiHBG051432.
InParanoidiQ9QZ05.
KOiK16196.
PhylomeDBiQ9QZ05.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
3.40.50.800. 1 hit.
InterProiIPR004154. Anticodon-bd.
IPR024435. HisRS-related_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR006575. RWD-domain.
IPR008271. Ser/Thr_kinase_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF12745. HGTP_anticodon2. 1 hit.
PF00069. Pkinase. 3 hits.
PF05773. RWD. 1 hit.
[Graphical view]
SMARTiSM00591. RWD. 1 hit.
SM00220. S_TKc. 2 hits.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
SSF56112. SSF56112. 3 hits.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 2 hits.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50908. RWD. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9QZ05-1) [UniParc]FASTAAdd to basket

Also known as: GCN2beta

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAGGRGASGR GRAEPQESYS QRQDHELQAL EAIYGSDFQD LRPDARGRVR
60 70 80 90 100
EPPEINLVLY PQGLAGEEVY VQVELQVKCP PTYPDVVPEI ELKNAKGLSN
110 120 130 140 150
ESVNLLKSHL EELAKKQCGE VMIFELAHHV QSFLSEHNKP PPKSFHEEML
160 170 180 190 200
ERQAQEKQQR LLEARRKEEQ EQREILHEIQ RRKEEIKEEK KRKEMAKQER
210 220 230 240 250
LEITSLTNQD YASKRDPAGH RAAAILHGGS PDFVGNGKAR TYSSGRSRRE
260 270 280 290 300
RQYSVCSGEP SPGSCDILHF SVGSPDQLMV HKGRCVGSDE QLGKVVYNAL
310 320 330 340 350
ETATGSFVLL HEWVLQWQKM GPCLTSQEKE KIDKCKRQIQ GAETEFSSLV
360 370 380 390 400
KLSHPNIVRY FAMNSREEED SIVIDILAEH VSGISLATHL SHSGPVPAHQ
410 420 430 440 450
LRKYTAQLLA GLDYLHSNSV VHKVLSASSV LVDAEGTVKI TDYSISKRLA
460 470 480 490 500
DICKEDVFEQ ARVRFSDSAL PYKTGKKGDV WRLGLLLLSL SQGQECGEYP
510 520 530 540 550
VTIPSDLPAD FQDFLKKCVC LDDKERWSPQ QLLKHSFINP QPKLPLVEQS
560 570 580 590 600
PEDSGGQDYI ETVIPSNQLP SAAFFSETQK QFSRYFIEFE ELQLLGKGAF
610 620 630 640 650
GAVIKVQNKL DGCCYAVKRI PINPASRHFR RIKGEVTLLS RLHHENIVRY
660 670 680 690 700
YNAWIERHER PAVPGTPPPD CTPQAQDSPA TCGKTSGDTE ELGSVEAAAP
710 720 730 740 750
PPILSSSVEW STSAERSTST RFPVTGQDSS SDEEDEDERD GVFSQSFLPA
760 770 780 790 800
SDSDSDIIFD NEDENSKSQN QDEDCNQKDG SHEIEPSVTA EAVHYLYIQM
810 820 830 840 850
EYCEKSTLRD TIDQGLFRDT SRLWRLFREI LDGLAYIHEK GMIHRDLKPV
860 870 880 890 900
NIFLDSDDHV KIGDFGLATD HLAFTAEGKQ DDQAGDGVIK SDPSGHLTGM
910 920 930 940 950
VGTALYVSPE VQGSTKSAYN QKVDLFSLGI IFFEMSYHPM VTASERIFVL
960 970 980 990 1000
NQLRDPTSPK FPDDFDDGEH TKQKSVISWL LNHDPAKRPT AMELLKSELL
1010 1020 1030 1040 1050
PPPQMEESEL HEVLHHTLAN IDGKAYRTMM SQIFCQHISP AIDYTYDSDI
1060 1070 1080 1090 1100
LKGNFLIRTA KIQQLVCETI VRVFKRHGAV QLCTPLLLPR NRQIYEHNEA
1110 1120 1130 1140 1150
ALFMDHSGML VMLPFDLRVP FARYVARNNI LNLKRYCIER VFRPRKLDRF
1160 1170 1180 1190 1200
HPKELLECAF DIVTSTTNSS LPTAETIYTI YEIIQEFPAL QERNYSIYLN
1210 1220 1230 1240 1250
HTMLLKAILL HCGIPEDKLS QVYVILYDAV TEKLTRREVE AKFCNLSLSS
1260 1270 1280 1290 1300
NSLCRLYKFI EQKGDLQDLT PTINSLIKQK TGVAQLVKYS LKDLEDVVGL
1310 1320 1330 1340 1350
LKKLGVKLQV SINLGLVYKV QQHTGIIFQF LAFSKRRQRV VPEILAAGGR
1360 1370 1380 1390 1400
YDLLIPKFRG PQTVGPVPTA VGVSIAIDKI FAAVLNMEEP VTVSSCDLLV
1410 1420 1430 1440 1450
VSVGQMSMSR AINLTQKLWT AGITAEIMYD WSQSQEELQE YCRHHEITYV
1460 1470 1480 1490 1500
ALVSDKEGSH VKVKSFEKER QTEKRVLESD LVDHVMQKLR TKVGDERNFR
1510 1520 1530 1540 1550
DASDNLAVQT LKGSFSNASG LFEIHGTTVV PNVIVLAPEK LSASTRRRHE
1560 1570 1580 1590 1600
IQVQTRLQTT LANLHQKSSE IEILAVDLPK ETILQFLSLE WDADEQAFNT
1610 1620 1630 1640
TVKQLLSRLP KQRYLKLVCD EIYNIKVEKK VSVLFLYSYR DDYYRILF
Length:1,648
Mass (Da):186,487
Last modified:March 15, 2005 - v2
Checksum:iF27841DDB317EFCB
GO
Isoform 2 (identifier: Q9QZ05-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-112: Missing.
     113-120: LAKKQCGE → MPTYIPRC

Note: No experimental confirmation available.
Show »
Length:1,536
Mass (Da):174,179
Checksum:i71FE1EBAFBAB53A9
GO
Isoform 3 (identifier: Q9QZ05-3) [UniParc]FASTAAdd to basket

Also known as: GCN2gamma

The sequence of this isoform differs from the canonical sequence as follows:
     1-78: Missing.
     79-86: CPPTYPDV → MRTQRALL

Show »
Length:1,570
Mass (Da):177,919
Checksum:i673582EE560E4421
GO
Isoform 4 (identifier: Q9QZ05-4) [UniParc]FASTAAdd to basket

Also known as: GCN2alpha

The sequence of this isoform differs from the canonical sequence as follows:
     1-278: Missing.

Show »
Length:1,370
Mass (Da):154,948
Checksum:iCD2E9DFB9920FD0F
GO
Isoform 5 (identifier: Q9QZ05-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-801: Missing.
     802-840: YCEKSTLRDT...LDGLAYIHEK → MGEDSSSGHH...VDGLFIVFQQ
     1120-1148: PFARYVARNNILNLKRYCIERVFRPRKLD → SWDAAPLKTRPSQTPPLQPYPGEPHVGNT
     1149-1648: Missing.

Show »
Length:347
Mass (Da):38,820
Checksum:i46136A7A0F53C392
GO
Isoform 6 (identifier: Q9QZ05-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-121: Missing.
     607-653: QNKLDGCCYA...HENIVRYYNA → RQGCPQSLLS...EAGSTFTSRS
     654-1648: Missing.

Note: No experimental confirmation available.
Show »
Length:532
Mass (Da):59,991
Checksum:iB0E034754953EB1B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti76 – 761Q → R in BAB28984 (PubMed:16141072).Curated
Sequence conflicti91 – 911E → D in BAB28984 (PubMed:16141072).Curated
Sequence conflicti262 – 2621P → L (PubMed:16141072).Curated
Sequence conflicti262 – 2621P → L in AAH23958 (PubMed:15489334).Curated
Sequence conflicti517 – 53923KCVCL…HSFIN → NPRRPKRRPQETSQEVWFC in BAC98144 (PubMed:14621295).CuratedAdd
BLAST
Sequence conflicti682 – 6821C → Y in AAG22589 (PubMed:10655230).Curated
Sequence conflicti682 – 6821C → Y in AAG22590 (PubMed:10655230).Curated
Sequence conflicti682 – 6821C → Y in AAG22591 (PubMed:10655230).Curated
Sequence conflicti682 – 6821C → Y in BAC98144 (PubMed:14621295).Curated
Sequence conflicti725 – 7273TGQ → MGE (PubMed:16141072).Curated
Sequence conflicti784 – 7841I → V in AAG22589 (PubMed:10655230).Curated
Sequence conflicti784 – 7841I → V in AAG22590 (PubMed:10655230).Curated
Sequence conflicti784 – 7841I → V in AAG22591 (PubMed:10655230).Curated
Sequence conflicti784 – 7841I → V in BAC98144 (PubMed:14621295).Curated
Sequence conflicti853 – 8531F → I in AAH72637 (PubMed:15489334).Curated
Sequence conflicti882 – 8821D → G in AAG22589 (PubMed:10655230).Curated
Sequence conflicti882 – 8821D → G in AAG22590 (PubMed:10655230).Curated
Sequence conflicti882 – 8821D → G in AAG22591 (PubMed:10655230).Curated
Sequence conflicti887 – 8871G → R in AAG22589 (PubMed:10655230).Curated
Sequence conflicti887 – 8871G → R in AAG22590 (PubMed:10655230).Curated
Sequence conflicti887 – 8871G → R in AAG22591 (PubMed:10655230).Curated
Sequence conflicti887 – 8871G → R in BAC98144 (PubMed:14621295).Curated
Sequence conflicti895 – 8951G → C in BAC98144 (PubMed:14621295).Curated
Sequence conflicti1021 – 10211I → T in AAG22589 (PubMed:10655230).Curated
Sequence conflicti1021 – 10211I → T in AAG22590 (PubMed:10655230).Curated
Sequence conflicti1021 – 10211I → T in AAG22591 (PubMed:10655230).Curated
Sequence conflicti1033 – 10331I → L in AAG22589 (PubMed:10655230).Curated
Sequence conflicti1033 – 10331I → L in AAG22590 (PubMed:10655230).Curated
Sequence conflicti1033 – 10331I → L in AAG22591 (PubMed:10655230).Curated
Sequence conflicti1038 – 10381I → S in AAG22589 (PubMed:10655230).Curated
Sequence conflicti1038 – 10381I → S in AAG22590 (PubMed:10655230).Curated
Sequence conflicti1038 – 10381I → S in AAG22591 (PubMed:10655230).Curated
Sequence conflicti1167 – 11671T → A in AAG22589 (PubMed:10655230).Curated
Sequence conflicti1167 – 11671T → A in AAG22590 (PubMed:10655230).Curated
Sequence conflicti1167 – 11671T → A in AAG22591 (PubMed:10655230).Curated
Sequence conflicti1183 – 11831I → V in AAG22589 (PubMed:10655230).Curated
Sequence conflicti1183 – 11831I → V in AAG22590 (PubMed:10655230).Curated
Sequence conflicti1183 – 11831I → V in AAG22591 (PubMed:10655230).Curated
Sequence conflicti1275 – 12751S → A in BAB27580 (PubMed:16141072).Curated
Sequence conflicti1283 – 12831V → I in AAG22589 (PubMed:10655230).Curated
Sequence conflicti1283 – 12831V → I in AAG22590 (PubMed:10655230).Curated
Sequence conflicti1283 – 12831V → I in AAG22591 (PubMed:10655230).Curated
Sequence conflicti1296 – 12961D → E in AAG22589 (PubMed:10655230).Curated
Sequence conflicti1296 – 12961D → E in AAG22590 (PubMed:10655230).Curated
Sequence conflicti1296 – 12961D → E in AAG22591 (PubMed:10655230).Curated
Sequence conflicti1324 – 13241T → N in AAG22589 (PubMed:10655230).Curated
Sequence conflicti1324 – 13241T → N in AAG22590 (PubMed:10655230).Curated
Sequence conflicti1324 – 13241T → N in AAG22591 (PubMed:10655230).Curated
Sequence conflicti1363 – 13642TV → AL in AAG22589 (PubMed:10655230).Curated
Sequence conflicti1363 – 13642TV → AL in AAG22590 (PubMed:10655230).Curated
Sequence conflicti1383 – 13831A → V in CAB58363 (PubMed:10504407).Curated
Sequence conflicti1383 – 13831A → V in BAC98144 (PubMed:14621295).Curated
Sequence conflicti1388 – 13881E → G in AAG22589 (PubMed:10655230).Curated
Sequence conflicti1388 – 13881E → G in AAG22590 (PubMed:10655230).Curated
Sequence conflicti1388 – 13881E → G in AAG22591 (PubMed:10655230).Curated
Sequence conflicti1403 – 14031V → A in AAG22589 (PubMed:10655230).Curated
Sequence conflicti1403 – 14031V → A in AAG22590 (PubMed:10655230).Curated
Sequence conflicti1403 – 14031V → A in AAG22591 (PubMed:10655230).Curated
Sequence conflicti1467 – 14671E → G in BAB27580 (PubMed:16141072).Curated
Sequence conflicti1532 – 15376NVIVLA → TVSVIS in AAG22589 (PubMed:10655230).Curated
Sequence conflicti1532 – 15376NVIVLA → TVSVIS in AAG22590 (PubMed:10655230).Curated
Sequence conflicti1540 – 15401K → M in BAB27580 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 801801Missing in isoform 5. 1 PublicationVSP_013039Add
BLAST
Alternative sequencei1 – 278278Missing in isoform 4. 1 PublicationVSP_013040Add
BLAST
Alternative sequencei1 – 121121Missing in isoform 6. 1 PublicationVSP_013041Add
BLAST
Alternative sequencei1 – 112112Missing in isoform 2. 1 PublicationVSP_013042Add
BLAST
Alternative sequencei1 – 7878Missing in isoform 3. 1 PublicationVSP_013043Add
BLAST
Alternative sequencei79 – 868CPPTYPDV → MRTQRALL in isoform 3. 1 PublicationVSP_013044
Alternative sequencei113 – 1208LAKKQCGE → MPTYIPRC in isoform 2. 1 PublicationVSP_013045
Alternative sequencei607 – 65347QNKLD…RYYNA → RQGCPQSLLSFLFPFHGLTG LVSILGVEREVNKIRLFEAG STFTSRS in isoform 6. 1 PublicationVSP_013046Add
BLAST
Alternative sequencei654 – 1648995Missing in isoform 6. 1 PublicationVSP_013047Add
BLAST
Alternative sequencei802 – 84039YCEKS…YIHEK → MGEDSSSGHHNPLPLKSGNR VLSSVWEEAVDGLFIVFQQ in isoform 5. 1 PublicationVSP_013048Add
BLAST
Alternative sequencei1120 – 114829PFARY…PRKLD → SWDAAPLKTRPSQTPPLQPY PGEPHVGNT in isoform 5. 1 PublicationVSP_013049Add
BLAST
Alternative sequencei1149 – 1648500Missing in isoform 5. 1 PublicationVSP_013050Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ243533 mRNA. Translation: CAB58363.1.
AF193342 mRNA. Translation: AAG22589.1.
AF193343 mRNA. Translation: AAG22590.1.
AF193344 mRNA. Translation: AAG22591.1.
AK011380 mRNA. Translation: BAB27580.1.
AK013758 mRNA. Translation: BAB28984.1.
AK077199 mRNA. Translation: BAC36677.1.
AL929163 Genomic DNA. Translation: CAM24689.1.
AL929163 Genomic DNA. Translation: CAM24690.1.
BC023958 mRNA. Translation: AAH23958.1.
BC072637 mRNA. Translation: AAH72637.1.
AK129334 Transcribed RNA. Translation: BAC98144.2.
CCDSiCCDS16576.1. [Q9QZ05-1]
CCDS50669.1. [Q9QZ05-2]
RefSeqiNP_001171277.1. NM_001177806.1. [Q9QZ05-2]
NP_038747.2. NM_013719.3.
XP_006499688.1. XM_006499625.2. [Q9QZ05-2]
UniGeneiMm.217616.

Genome annotation databases

EnsembliENSMUST00000102527; ENSMUSP00000099586; ENSMUSG00000005102. [Q9QZ05-2]
ENSMUST00000110869; ENSMUSP00000106493; ENSMUSG00000005102. [Q9QZ05-5]
ENSMUST00000110870; ENSMUSP00000106494; ENSMUSG00000005102. [Q9QZ05-4]
GeneIDi27103.
KEGGimmu:27103.
UCSCiuc008lrx.2. mouse. [Q9QZ05-2]
uc008lry.1. mouse. [Q9QZ05-1]
uc008lrz.1. mouse. [Q9QZ05-5]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ243533 mRNA. Translation: CAB58363.1.
AF193342 mRNA. Translation: AAG22589.1.
AF193343 mRNA. Translation: AAG22590.1.
AF193344 mRNA. Translation: AAG22591.1.
AK011380 mRNA. Translation: BAB27580.1.
AK013758 mRNA. Translation: BAB28984.1.
AK077199 mRNA. Translation: BAC36677.1.
AL929163 Genomic DNA. Translation: CAM24689.1.
AL929163 Genomic DNA. Translation: CAM24690.1.
BC023958 mRNA. Translation: AAH23958.1.
BC072637 mRNA. Translation: AAH72637.1.
AK129334 Transcribed RNA. Translation: BAC98144.2.
CCDSiCCDS16576.1. [Q9QZ05-1]
CCDS50669.1. [Q9QZ05-2]
RefSeqiNP_001171277.1. NM_001177806.1. [Q9QZ05-2]
NP_038747.2. NM_013719.3.
XP_006499688.1. XM_006499625.2. [Q9QZ05-2]
UniGeneiMm.217616.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UKXNMR-A17-139[»]
4OTNX-ray1.90A/B1514-1648[»]
ProteinModelPortaliQ9QZ05.
SMRiQ9QZ05. Positions 21-144, 290-577, 584-657, 753-1016, 1058-1488, 1526-1648.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi205123. 2 interactions.
STRINGi10090.ENSMUSP00000005233.

PTM databases

iPTMnetiQ9QZ05.
PhosphoSiteiQ9QZ05.

Proteomic databases

EPDiQ9QZ05.
MaxQBiQ9QZ05.
PaxDbiQ9QZ05.
PRIDEiQ9QZ05.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000102527; ENSMUSP00000099586; ENSMUSG00000005102. [Q9QZ05-2]
ENSMUST00000110869; ENSMUSP00000106493; ENSMUSG00000005102. [Q9QZ05-5]
ENSMUST00000110870; ENSMUSP00000106494; ENSMUSG00000005102. [Q9QZ05-4]
GeneIDi27103.
KEGGimmu:27103.
UCSCiuc008lrx.2. mouse. [Q9QZ05-2]
uc008lry.1. mouse. [Q9QZ05-1]
uc008lrz.1. mouse. [Q9QZ05-5]

Organism-specific databases

CTDi440275.
MGIiMGI:1353427. Eif2ak4.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG1035. Eukaryota.
COG0124. LUCA.
GeneTreeiENSGT00530000062984.
HOVERGENiHBG051432.
InParanoidiQ9QZ05.
KOiK16196.
PhylomeDBiQ9QZ05.

Miscellaneous databases

ChiTaRSiEif2ak4. mouse.
EvolutionaryTraceiQ9QZ05.
PROiQ9QZ05.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QZ05.
ExpressionAtlasiQ9QZ05. baseline and differential.
GenevisibleiQ9QZ05. MM.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
3.40.50.800. 1 hit.
InterProiIPR004154. Anticodon-bd.
IPR024435. HisRS-related_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR006575. RWD-domain.
IPR008271. Ser/Thr_kinase_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF12745. HGTP_anticodon2. 1 hit.
PF00069. Pkinase. 3 hits.
PF05773. RWD. 1 hit.
[Graphical view]
SMARTiSM00591. RWD. 1 hit.
SM00220. S_TKc. 2 hits.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
SSF56112. SSF56112. 3 hits.
PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 2 hits.
PS00108. PROTEIN_KINASE_ST. 1 hit.
PS50908. RWD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of a mammalian homolog of the GCN2 eukaryotic initiation factor 2alpha kinase."
    Berlanga J.J., Santoyo J., de Haro C.
    Eur. J. Biochem. 265:754-762(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, AUTOPHOSPHORYLATION, DOMAIN, TISSUE SPECIFICITY.
    Strain: BALB/cJ.
  2. "A mammalian homologue of GCN2 protein kinase important for translational control by phosphorylation of eukaryotic initiation factor-2alpha."
    Sood R., Porter A.C., Olsen D.A., Cavener D.R., Wek R.C.
    Genetics 154:787-801(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4), FUNCTION, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, DOMAIN, TISSUE SPECIFICITY.
    Strain: BALB/cJ.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
    Strain: C57BL/6J.
    Tissue: Testis.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 6).
    Strain: C57BL/6J and FVB/N.
    Tissue: Brain and Mammary gland.
  6. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
    DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 248-1648.
    Tissue: Embryonic tail.
  7. Okazaki N., Kikuno R., Nagase T., Ohara O., Koga H.
    Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  8. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1053-1061, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  9. "Regulated translation initiation controls stress-induced gene expression in mammalian cells."
    Harding H.P., Novoa I., Zhang Y., Zeng H., Wek R., Schapira M., Ron D.
    Mol. Cell 6:1099-1108(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, AUTOPHOSPHORYLATION.
  10. Cited for: FUNCTION, AUTOPHOSPHORYLATION AT THR-898.
  11. "The GCN2 eIF2alpha kinase is required for adaptation to amino acid deprivation in mice."
    Zhang P., McGrath B.C., Reinert J., Olsen D.S., Lei L., Gill S., Wek S.A., Vattem K.M., Wek R.C., Kimball S.R., Jefferson L.S., Cavener D.R.
    Mol. Cell. Biol. 22:6681-6688(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
  12. "Preservation of liver protein synthesis during dietary leucine deprivation occurs at the expense of skeletal muscle mass in mice deleted for eIF2 kinase GCN2."
    Anthony T.G., McDaniel B.J., Byerley R.L., McGrath B.C., Cavener D.R., McNurlan M.A., Wek R.C.
    J. Biol. Chem. 279:36553-36561(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  13. "The GCN2 kinase biases feeding behavior to maintain amino acid homeostasis in omnivores."
    Maurin A.C., Jousse C., Averous J., Parry L., Bruhat A., Cherasse Y., Zeng H., Zhang Y., Harding H.P., Ron D., Fafournoux P.
    Cell Metab. 1:273-277(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, CONDITIONAL KNOCKOUT IN BRAIN.
  14. "PERK and GCN2 contribute to eIF2alpha phosphorylation and cell cycle arrest after activation of the unfolded protein response pathway."
    Hamanaka R.B., Bennett B.S., Cullinan S.B., Diehl J.A.
    Mol. Biol. Cell 16:5493-5501(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
  16. Cited for: FUNCTION.
  17. "Antiviral effect of the mammalian translation initiation factor 2alpha kinase GCN2 against RNA viruses."
    Berlanga J.J., Ventoso I., Harding H.P., Deng J., Ron D., Sonenberg N., Carrasco L., de Haro C.
    EMBO J. 25:1730-1740(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (MICROBIAL INFECTION), CATALYTIC ACTIVITY, ENZYME REGULATION (MICROBIAL INFECTION), AUTOPHOSPHORYLATION, DISRUPTION PHENOTYPE, MUTAGENESIS OF LYS-618; PHE-1142 AND ARG-1143.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Lung, Pancreas, Spleen and Testis.
  19. "Phosphorylation of eIF2alpha at serine 51 is an important determinant of cell survival and adaptation to glucose deficiency."
    Muaddi H., Majumder M., Peidis P., Papadakis A.I., Holcik M., Scheuner D., Kaufman R.J., Hatzoglou M., Koromilas A.E.
    Mol. Biol. Cell 21:3220-3231(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  20. "IMPACT is a developmentally regulated protein in neurons that opposes the eukaryotic initiation factor 2alpha kinase GCN2 in the modulation of neurite outgrowth."
    Roffe M., Hajj G.N., Azevedo H.F., Alves V.S., Castilho B.A.
    J. Biol. Chem. 288:10860-10869(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  21. "Evolutionarily conserved IMPACT impairs various stress responses that require GCN1 for activating the eIF2 kinase GCN2."
    Cambiaghi T.D., Pereira C.M., Shanmugam R., Bolech M., Wek R.C., Sattlegger E., Castilho B.A.
    Biochem. Biophys. Res. Commun. 443:592-597(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GCN1, AUTOPHOSPHORYLATION AT THR-898.
  22. "Vaccine activation of the nutrient sensor GCN2 in dendritic cells enhances antigen presentation."
    Ravindran R., Khan N., Nakaya H.I., Li S., Loebbermann J., Maddur M.S., Park Y., Jones D.P., Chappert P., Davoust J., Weiss D.S., Virgin H.W., Ron D., Pulendran B.
    Science 343:313-317(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (MICROBIAL INFECTION), DISRUPTION PHENOTYPE.
  23. "p58IPK is an inhibitor of the eIF2alpha kinase GCN2 and its localization and expression underpin protein synthesis and ER processing capacity."
    Roobol A., Roobol J., Bastide A., Knight J.R., Willis A.E., Smales C.M.
    Biochem. J. 465:213-225(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DNAJC3.
  24. "Translational Upregulation of an Individual p21Cip1 Transcript Variant by GCN2 Regulates Cell Proliferation and Survival under Nutrient Stress."
    Lehman S.L., Cerniglia G.J., Johannes G.J., Ye J., Ryeom S., Koumenis C.
    PLoS Genet. 11:E1005212-E1005212(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  25. Cited for: STRUCTURE BY NMR OF 17-107.

Entry informationi

Entry nameiE2AK4_MOUSE
AccessioniPrimary (citable) accession number: Q9QZ05
Secondary accession number(s): A2AUM3
, A2AUM4, Q6GQT4, Q6ZPT5, Q8C5S0, Q8CIF5, Q9CT30, Q9CUV9, Q9ESB6, Q9ESB7, Q9ESB8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: March 15, 2005
Last modified: June 8, 2016
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.