YEAST:GCN2

Species (Taxon ID)	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s)	GCN2 (ECO:0000312 with SGD:S000002691) (synonyms: AAS1)
Protein Name(s)	eIF-2-alpha kinase GCN2 (ECO:0000250 with UniProtKB:Q9HGN1) General control non-derepressible protein 2 (ECO:0000312 with SGD:S000002691) Serine/threonine-protein kinase GCN2 (ECO:0000305)
External Links
UniProt	P15442
EMBL	M27082 U51030 M20487 BK006938
PIR	S70139
RefSeq	NP_010569.3
PDB	1ZXE 1ZY4 1ZY5 1ZYC 1ZYD 2YZ0 4OTM
PDBsum	1ZXE 1ZY4 1ZY5 1ZYC 1ZYD 2YZ0 4OTM
ProteinModelPortal	P15442
SMR	P15442
BioGrid	32336
DIP	DIP-2346N
IntAct	P15442
MINT	MINT-625588
STRING	4932.YDR283C
iPTMnet	P15442
MaxQB	P15442
PRIDE	P15442
EnsemblFungi	YDR283C
GeneID	851877
KEGG	sce:YDR283C
EuPathDB	FungiDB:YDR283C
SGD	S000002691
GeneTree	ENSGT00530000062984
HOGENOM	HOG000172724
InParanoid	P15442
KO	K16196
OMA	KCVCLDD
OrthoDB	EOG092C0AG1
BioCyc	YEAST:G3O-29848-MONOMER
Reactome	[www.reactome.org/content/detail/R-SCE-381042 R-SCE-381042]
EvolutionaryTrace	P15442
PRO	PR:P15442
Proteomes	UP000002311
GO	GO:0022626 GO:0015934 GO:0042788 GO:0015935 GO:0005524 GO:0003725 GO:0004694 GO:0042803 GO:0004672 GO:0043621 GO:0043023 GO:0043022 GO:0031369 GO:0000049 GO:0034198 GO:0072755 GO:0071232 GO:0070301 GO:1990451 GO:0001300 GO:0000077 GO:1903833 GO:0071264 GO:0046777 GO:0006468 GO:0060733 GO:0006446 GO:0006412
Gene3D	3.10.110.10
InterPro	IPR016255 IPR024435 IPR011009 IPR000719 IPR017441 IPR006575 IPR008271 IPR016135
Pfam	PF12745 PF00069 PF05773
PIRSF	PIRSF000660
SMART	SM00591 SM00220
SUPFAM	SSF54495 SSF56112
PROSITE	PS00107 PS50011 PS00108 PS50908

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:0004860	protein kinase inhibitor activity	PMID:28057755^[1]	ECO:0000315			F		S. Cerevisiae, GCN2 Figure 3 shows that GCN2 inhibits TORC activity. Figure 5 shows the down-regulation of Kinase activity by GCN2.	complete CACAO 12945
involved_in	GO:1904262	negative regulation of TORC1 signaling	PMID:28057755^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	happens_during:(GO:1990928)	Seeded From UniProt	complete
involved_in	GO:0100002	negative regulation of protein kinase activity by protein phosphorylation	PMID:28057755^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	happens_during:(GO:1990928) has_input:(GO:0031931)	Seeded From UniProt	complete
involved_in	GO:0016239	positive regulation of macroautophagy	PMID:28057755^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	part_of:(GO:1990928)	Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	PMID:28057755^[1]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:P38873)	Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	PMID:28057755^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	has_direct_input:(UniProtKB:P38873)	Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	PMID:28057755^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_direct_input:(UniProtKB:P38873)	Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	PMID:28057755^[1]	ECO:0000314	direct assay evidence used in manual assertion		P	has_direct_input:(UniProtKB:P38873)	Seeded From UniProt	complete
involved_in	GO:0060733	regulation of eIF2 alpha phosphorylation by amino acid starvation	PMID:8798780^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0004694	eukaryotic translation initiation factor 2alpha kinase activity	PMID:8798780^[2]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0043022	ribosome binding	PMID:21849502^[3]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0060733	regulation of eIF2 alpha phosphorylation by amino acid starvation	PMID:21849502^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0031369	translation initiation factor binding	PMID:21849502^[3]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P38912	F		Seeded From UniProt	complete
enables	GO:0003725	double-stranded RNA binding	PMID:9430731^[4]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:1903833	positive regulation of cellular response to amino acid starvation	PMID:9430731^[4]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0043022	ribosome binding	PMID:9430731^[4]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0060733	regulation of eIF2 alpha phosphorylation by amino acid starvation	PMID:10983975^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0071264	positive regulation of translational initiation in response to starvation	PMID:1739968^[6]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0042788	polysomal ribosome	PMID:22888004^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:10983975^[5]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0043621	protein self-association	PMID:10983975^[5]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0043022	ribosome binding	PMID:10983975^[5]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	PMID:10983975^[5]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	PMID:10983975^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0046777	protein autophosphorylation	PMID:10983975^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0000049	tRNA binding	PMID:10983975^[5]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	PMID:2188100^[8]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0046777	protein autophosphorylation	PMID:2188100^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034198	cellular response to amino acid starvation	PMID:2188100^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034198	cellular response to amino acid starvation	PMID:3290651^[9]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0015935	small ribosomal subunit	PMID:2038314^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0015934	large ribosomal subunit	PMID:2038314^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0042788	polysomal ribosome	PMID:2038314^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0043023	ribosomal large subunit binding	PMID:2038314^[10]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0070301	cellular response to hydrogen peroxide	PMID:24333428^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0072755	cellular response to benomyl	PMID:24333428^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1990451	cellular stress response to acidic pH	PMID:24333428^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034198	cellular response to amino acid starvation	PMID:24333428^[11]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0071264	positive regulation of translational initiation in response to starvation	PMID:7623840^[12]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0042803	protein homodimerization activity	PMID:9566889^[13]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0060733	regulation of eIF2 alpha phosphorylation by amino acid starvation	PMID:7621831^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0071264	positive regulation of translational initiation in response to starvation	PMID:7621831^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0071232	cellular response to histidine	PMID:7621831^[14]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0000049	tRNA binding	PMID:7623840^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0000049	tRNA binding	PMID:7623840^[12]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	PMID:7623840^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	part_of:(GO:0034198) has_input:(UniProtKB:P20459)	Seeded From UniProt	complete
involved_in	GO:1903833	positive regulation of cellular response to amino acid starvation	PMID:7623840^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1903833	positive regulation of cellular response to amino acid starvation	PMID:6351059^[15]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P09032	P		Seeded From UniProt	complete
involved_in	GO:0046777	protein autophosphorylation	PMID:8798780^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1903833	positive regulation of cellular response to amino acid starvation	PMID:6351059^[15]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0046777	protein autophosphorylation	PMID:8798780^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0022626	cytosolic ribosome	PMID:2038314^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	PMID:2188100^[8]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006446	regulation of translational initiation	PMID:7934812^[16]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0004694	eukaryotic translation initiation factor 2alpha kinase activity	PMID:8798780^[2]	ECO:0000314	direct assay evidence used in manual assertion		F	has_direct_input:(UniProtKB:P20459)	Seeded From UniProt	complete
involved_in	GO:0001300	chronological cell aging	PMID:24244480^[17]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0000077	DNA damage checkpoint	PMID:17890903^[18]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	PMID:1739968^[6]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006446	regulation of translational initiation	PMID:1739968^[6]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0004694	eukaryotic translation initiation factor 2alpha kinase activity	PMID:1739968^[6]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0022626	cytosolic ribosome	PMID:21873635^[19]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000867953 SGD:S000002691	C		Seeded From UniProt	complete
enables	GO:0004694	eukaryotic translation initiation factor 2alpha kinase activity	PMID:21873635^[19]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1341830 MGI:MGI:1353427 PANTHER:PTN000867953 PomBase:SPBC36B7.09 RGD:70884 SGD:S000002691 UniProtKB:A0A0B4KHX7 UniProtKB:A0A1D8PQT9 UniProtKB:P19525 UniProtKB:Q9NZJ5 UniProtKB:Q9P2K8 dictyBase:DDB_G0272837	F		Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	PMID:21873635^[19]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:103075 MGI:MGI:1341830 MGI:MGI:1353448 MGI:MGI:1353449 PANTHER:PTN000113601 PomBase:SPBC36B7.09 SGD:S000002691 TAIR:locus:2024780 UniProtKB:P19525 UniProtKB:Q8IL26 WB:WBGene00006988 ZFIN:ZDB-GENE-050301-2 ZFIN:ZDB-GENE-080422-1	F		Seeded From UniProt	complete
involved_in	GO:0000077	DNA damage checkpoint	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR016255	P		Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000719 InterPro:IPR008271	F		Seeded From UniProt	complete
enables	GO:0004694	eukaryotic translation initiation factor 2alpha kinase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR016255	F		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000719 InterPro:IPR017441	F		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000719 InterPro:IPR008271 InterPro:IPR016255	P		Seeded From UniProt	complete
involved_in	GO:0010998	regulation of translational initiation by eIF2 alpha phosphorylation	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR016255	P		Seeded From UniProt	complete
enables	GO:0016301	kinase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0418	F		Seeded From UniProt	complete
enables	GO:0003723	RNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0694	F		Seeded From UniProt	complete
involved_in	GO:0006417	regulation of translation	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0810	P		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
enables	GO:0000049	tRNA binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0820	F		Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F		Seeded From UniProt	complete
involved_in	GO:0006412	translation	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0648	P		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0723	F		Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F		Seeded From UniProt	complete
involved_in	GO:0016310	phosphorylation	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0418	P		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 ^1.6 ^1.7 Yuan, W et al. (2017) General Control Nonderepressible 2 (GCN2) Kinase Inhibits Target of Rapamycin Complex 1 in Response to Amino Acid Starvation in Saccharomyces cerevisiae. J. Biol. Chem. 292 2660-2669 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 ^2.4 Zhu, S et al. (1996) Histidyl-tRNA synthetase-related sequences in GCN2 protein kinase regulate in vitro phosphorylation of eIF-2. J. Biol. Chem. 271 24989-94 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 Visweswaraiah, J et al. (2011) Evidence that eukaryotic translation elongation factor 1A (eEF1A) binds the Gcn2 protein C terminus and inhibits Gcn2 activity. J. Biol. Chem. 286 36568-79 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 Zhu, S & Wek, RC (1998) Ribosome-binding domain of eukaryotic initiation factor-2 kinase GCN2 facilitates translation control. J. Biol. Chem. 273 1808-14 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 ^5.3 ^5.4 ^5.5 ^5.6 ^5.7 Dong, J et al. (2000) Uncharged tRNA activates GCN2 by displacing the protein kinase moiety from a bipartite tRNA-binding domain. Mol. Cell 6 269-79 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 ^6.3 Dever, TE et al. (1992) Phosphorylation of initiation factor 2 alpha by protein kinase GCN2 mediates gene-specific translational control of GCN4 in yeast. Cell 68 585-96 PubMed GONUTS page
↑ Visweswaraiah, J et al. (2012) Overexpression of eukaryotic translation elongation factor 3 impairs Gcn2 protein activation. J. Biol. Chem. 287 37757-68 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 ^8.3 Wek, RC et al. (1990) Identification of positive-acting domains in GCN2 protein kinase required for translational activation of GCN4 expression. Mol. Cell. Biol. 10 2820-31 PubMed GONUTS page
↑ Roussou, I et al. (1988) Transcriptional-translational regulatory circuit in Saccharomyces cerevisiae which involves the GCN4 transcriptional activator and the GCN2 protein kinase. Mol. Cell. Biol. 8 2132-9 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 ^10.3 ^10.4 Ramirez, M et al. (1991) Ribosome association of GCN2 protein kinase, a translational activator of the GCN4 gene of Saccharomyces cerevisiae. Mol. Cell. Biol. 11 3027-36 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 ^11.3 Cambiaghi, TD et al. (2014) Evolutionarily conserved IMPACT impairs various stress responses that require GCN1 for activating the eIF2 kinase GCN2. Biochem. Biophys. Res. Commun. 443 592-7 PubMed GONUTS page
↑ ^12.0 ^12.1 ^12.2 ^12.3 ^12.4 Wek, SA et al. (1995) The histidyl-tRNA synthetase-related sequence in the eIF-2 alpha protein kinase GCN2 interacts with tRNA and is required for activation in response to starvation for different amino acids. Mol. Cell. Biol. 15 4497-506 PubMed GONUTS page
↑ Qiu, H et al. (1998) Dimerization by translation initiation factor 2 kinase GCN2 is mediated by interactions in the C-terminal ribosome-binding region and the protein kinase domain. Mol. Cell. Biol. 18 2697-711 PubMed GONUTS page
↑ ^14.0 ^14.1 ^14.2 Vazquez de Aldana, CR et al. (1995) GCN20, a novel ATP binding cassette protein, and GCN1 reside in a complex that mediates activation of the eIF-2 alpha kinase GCN2 in amino acid-starved cells. EMBO J. 14 3184-99 PubMed GONUTS page
↑ ^15.0 ^15.1 Hinnebusch, AG & Fink, GR (1983) Positive regulation in the general amino acid control of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U.S.A. 80 5374-8 PubMed GONUTS page
↑ Hinnebusch, AG (1993) Gene-specific translational control of the yeast GCN4 gene by phosphorylation of eukaryotic initiation factor 2. Mol. Microbiol. 10 215-23 PubMed GONUTS page
↑ Wu, Z et al. (2013) Independent and additive effects of glutamic acid and methionine on yeast longevity. PLoS ONE 8 e79319 PubMed GONUTS page
↑ Menacho-Marquez, M et al. (2007) Gcn2p regulates a G1/S cell cycle checkpoint in response to DNA damage. Cell Cycle 6 2302-5 PubMed GONUTS page
↑ ^19.0 ^19.1 ^19.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:28057755-1] 1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 ^1.6 ^1.7 Yuan, W et al. (2017) General Control Nonderepressible 2 (GCN2) Kinase Inhibits Target of Rapamycin Complex 1 in Response to Amino Acid Starvation in Saccharomyces cerevisiae. J. Biol. Chem. 292 2660-2669 PubMed GONUTS page

[PMID:8798780-2] 2.0 ^2.1 ^2.2 ^2.3 ^2.4 Zhu, S et al. (1996) Histidyl-tRNA synthetase-related sequences in GCN2 protein kinase regulate in vitro phosphorylation of eIF-2. J. Biol. Chem. 271 24989-94 PubMed GONUTS page

[PMID:21849502-3] 3.0 ^3.1 ^3.2 Visweswaraiah, J et al. (2011) Evidence that eukaryotic translation elongation factor 1A (eEF1A) binds the Gcn2 protein C terminus and inhibits Gcn2 activity. J. Biol. Chem. 286 36568-79 PubMed GONUTS page

[PMID:9430731-4] 4.0 ^4.1 ^4.2 Zhu, S & Wek, RC (1998) Ribosome-binding domain of eukaryotic initiation factor-2 kinase GCN2 facilitates translation control. J. Biol. Chem. 273 1808-14 PubMed GONUTS page

[PMID:10983975-5] 5.0 ^5.1 ^5.2 ^5.3 ^5.4 ^5.5 ^5.6 ^5.7 Dong, J et al. (2000) Uncharged tRNA activates GCN2 by displacing the protein kinase moiety from a bipartite tRNA-binding domain. Mol. Cell 6 269-79 PubMed GONUTS page

[PMID:1739968-6] 6.0 ^6.1 ^6.2 ^6.3 Dever, TE et al. (1992) Phosphorylation of initiation factor 2 alpha by protein kinase GCN2 mediates gene-specific translational control of GCN4 in yeast. Cell 68 585-96 PubMed GONUTS page

[PMID:22888004-7] Visweswaraiah, J et al. (2012) Overexpression of eukaryotic translation elongation factor 3 impairs Gcn2 protein activation. J. Biol. Chem. 287 37757-68 PubMed GONUTS page

[PMID:2188100-8] 8.0 ^8.1 ^8.2 ^8.3 Wek, RC et al. (1990) Identification of positive-acting domains in GCN2 protein kinase required for translational activation of GCN4 expression. Mol. Cell. Biol. 10 2820-31 PubMed GONUTS page

[PMID:3290651-9] Roussou, I et al. (1988) Transcriptional-translational regulatory circuit in Saccharomyces cerevisiae which involves the GCN4 transcriptional activator and the GCN2 protein kinase. Mol. Cell. Biol. 8 2132-9 PubMed GONUTS page

[PMID:2038314-10] 10.0 ^10.1 ^10.2 ^10.3 ^10.4 Ramirez, M et al. (1991) Ribosome association of GCN2 protein kinase, a translational activator of the GCN4 gene of Saccharomyces cerevisiae. Mol. Cell. Biol. 11 3027-36 PubMed GONUTS page

[PMID:24333428-11] 11.0 ^11.1 ^11.2 ^11.3 Cambiaghi, TD et al. (2014) Evolutionarily conserved IMPACT impairs various stress responses that require GCN1 for activating the eIF2 kinase GCN2. Biochem. Biophys. Res. Commun. 443 592-7 PubMed GONUTS page

[PMID:7623840-12] 12.0 ^12.1 ^12.2 ^12.3 ^12.4 Wek, SA et al. (1995) The histidyl-tRNA synthetase-related sequence in the eIF-2 alpha protein kinase GCN2 interacts with tRNA and is required for activation in response to starvation for different amino acids. Mol. Cell. Biol. 15 4497-506 PubMed GONUTS page

[PMID:9566889-13] Qiu, H et al. (1998) Dimerization by translation initiation factor 2 kinase GCN2 is mediated by interactions in the C-terminal ribosome-binding region and the protein kinase domain. Mol. Cell. Biol. 18 2697-711 PubMed GONUTS page

[PMID:7621831-14] 14.0 ^14.1 ^14.2 Vazquez de Aldana, CR et al. (1995) GCN20, a novel ATP binding cassette protein, and GCN1 reside in a complex that mediates activation of the eIF-2 alpha kinase GCN2 in amino acid-starved cells. EMBO J. 14 3184-99 PubMed GONUTS page

[PMID:6351059-15] 15.0 ^15.1 Hinnebusch, AG & Fink, GR (1983) Positive regulation in the general amino acid control of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U.S.A. 80 5374-8 PubMed GONUTS page

[PMID:7934812-16] Hinnebusch, AG (1993) Gene-specific translational control of the yeast GCN4 gene by phosphorylation of eukaryotic initiation factor 2. Mol. Microbiol. 10 215-23 PubMed GONUTS page

[PMID:24244480-17] Wu, Z et al. (2013) Independent and additive effects of glutamic acid and methionine on yeast longevity. PLoS ONE 8 e79319 PubMed GONUTS page

[PMID:17890903-18] Menacho-Marquez, M et al. (2007) Gcn2p regulates a G1/S cell cycle checkpoint in response to DNA damage. Cell Cycle 6 2302-5 PubMed GONUTS page

[PMID:21873635-19] 19.0 ^19.1 ^19.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

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YEAST:GCN2

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