HUMAN:E2AK2

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	EIF2AK2 (synonyms: PKR, PRKR)
Protein Name(s)	Interferon-induced, double-stranded RNA-activated protein kinase Eukaryotic translation initiation factor 2-alpha kinase 2 eIF-2A protein kinase 2 Interferon-inducible RNA-dependent protein kinase P1/eIF-2A protein kinase Protein kinase RNA-activated PKR Protein kinase R (ECO:0000303 with PMID:11438532^[1]) Tyrosine-protein kinase EIF2AK2 p68 kinase
External Links
UniProt	P19525
EMBL	M35663 M85294 U50648 U50634 U50635 U50636 U50637 U50638 U50639 U50640 U50641 U50642 U50643 U50644 U50645 U50646 U50647 AF167472 AF167460 AF167462 AF167463 AF167464 AF167465 AF167466 AF167468 AF167470 AY302136 AK290655 AK313818 AY228338 AC007899 CH471053 CH471053 CH471053 BC093676 BC101475
CCDS	CCDS1786.1 CCDS46259.1
PIR	JC5225
RefSeq	NP_001129123.1 NP_001129124.1 NP_002750.1
UniGene	Hs.131431
PDB	1QU6 2A19 2A1A 3UIU
PDBsum	1QU6 2A19 2A1A 3UIU
ProteinModelPortal	P19525
SMR	P19525
BioGrid	111596
DIP	DIP-2657N
IntAct	P19525
MINT	MINT-92415
STRING	9606.ENSP00000233057
BindingDB	P19525
ChEMBL	CHEMBL5785
GuidetoPHARMACOLOGY	2016
PhosphoSite	P19525
DMDM	125527
MaxQB	P19525
PaxDb	P19525
PRIDE	P19525
DNASU	5610
Ensembl	ENST00000233057 ENST00000395127 ENST00000405334
GeneID	5610
KEGG	hsa:5610
UCSC	uc010fac.3
CTD	5610
GeneCards	GC02M037326
HGNC	HGNC:9437
HPA	CAB003845 HPA019795
MIM	176871
neXtProt	NX_P19525
PharmGKB	PA33779
eggNOG	COG0515
GeneTree	ENSGT00530000062984
HOGENOM	HOG000234351
HOVERGEN	HBG051430
InParanoid	P19525
KO	K16195
OMA	RFTFQVI
OrthoDB	EOG71VSSK
PhylomeDB	P19525
TreeFam	TF317576
Reactome	REACT_115831 REACT_6350
SignaLink	P19525
ChiTaRS	EIF2AK2
EvolutionaryTrace	P19525
GeneWiki	Protein_kinase_R
GenomeRNAi	5610
NextBio	13635839
PMAP-CutDB	P19525
PRO	PR:P19525
Proteomes	UP000005640
Bgee	P19525
CleanEx	HS_EIF2AK2
ExpressionAtlas	P19525
Genevestigator	P19525
GO	GO:0005737 GO:0005829 GO:0016020 GO:0005634 GO:0048471 GO:0005524 GO:0003725 GO:0004694 GO:0004715 GO:0044822 GO:0004672 GO:0008601 GO:0004674 GO:0000186 GO:0051607 GO:0030968 GO:0030683 GO:0045087 GO:0019048 GO:0019054 GO:0043066 GO:0008285 GO:0033689 GO:0017148 GO:0045071 GO:0032722 GO:0001819 GO:0051092 GO:1901224 GO:0032874 GO:0046777 GO:0006468 GO:1901532 GO:1902036 GO:1902033 GO:1900225 GO:0035455 GO:0009615 GO:0006351 GO:0006412 GO:0019058
Gene3D	3.30.160.20
InterPro	IPR014720 IPR011009 IPR000719 IPR017441 IPR008271
Pfam	PF00035 PF00069
SMART	SM00358
SUPFAM	SSF56112
PROSITE	PS50137 PS00107 PS50011 PS00108

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
	GO:2000145	regulation of cell motility	PMID:23112838^[2]	ECO:0000316		UniProtKB:P41374	P	Figure 8	complete CACAO 5869
involved_in	GO:0034198	cellular response to amino acid starvation	PMID:25329545^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0004694	eukaryotic translation initiation factor 2alpha kinase activity	PMID:25329545^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0017148	negative regulation of translation	PMID:12610133^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:19946888^[5]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:1902036	regulation of hematopoietic stem cell differentiation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q03963	P	Seeded From UniProt	complete
involved_in	GO:1902033	regulation of hematopoietic stem cell proliferation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q03963	P	Seeded From UniProt	complete
involved_in	GO:1901532	regulation of hematopoietic progenitor cell differentiation	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q03963	P	Seeded From UniProt	complete
involved_in	GO:1901224	positive regulation of NIK/NF-kappaB signaling	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q03963	P	Seeded From UniProt	complete
involved_in	GO:1900225	regulation of NLRP3 inflammasome complex assembly	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q03963	P	Seeded From UniProt	complete
involved_in	GO:0051092	positive regulation of NF-kappaB transcription factor activity	PMID:15121867^[6]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	PMID:15121867^[6]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0046777	protein autophosphorylation	PMID:16216244^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0046777	protein autophosphorylation	PMID:22801494^[8]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0045071	negative regulation of viral genome replication	PMID:19189853^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0045071	negative regulation of viral genome replication	PMID:19840259^[10]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0003723	RNA binding	PMID:22681889^[11]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0035455	response to interferon-alpha	PMID:19840259^[10]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0033689	negative regulation of osteoblast proliferation	PMID:16216244^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0032874	positive regulation of stress-activated MAPK cascade	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q03963	P	Seeded From UniProt	complete
involved_in	GO:0032722	positive regulation of chemokine production	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q03963	P	Seeded From UniProt	complete
involved_in	GO:0017148	negative regulation of translation	PMID:19189853^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0017148	negative regulation of translation	PMID:12882984^[12]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0009615	response to virus	PMID:19189853^[9]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	PMID:19189853^[9]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:15121867^[6]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	PMID:21123651^[13]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	PMID:15229216^[14]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	PMID:12882984^[12]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	PMID:18835251^[15]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0001819	positive regulation of cytokine production	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q03963	P	Seeded From UniProt	complete
involved_in	GO:0000186	activation of MAPKK activity	PMID:15229216^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0022626	cytosolic ribosome	PMID:21873635^[16]	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^[16]	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^[16]	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
enables	GO:0003725	double-stranded RNA binding	PMID:21266579^[17]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:16373505^[18]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P19525	F	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000052	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0018108	peptidyl-tyrosine phosphorylation	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0004713	P	Seeded From UniProt	complete
involved_in	GO:0018108	peptidyl-tyrosine phosphorylation	GO_REF:0000108	ECO:0000366	evidence based on logical inference from automatic annotation used in automatic assertion	GO:0004715	P	Seeded From UniProt	complete
involved_in	GO:0043666	regulation of phosphoprotein phosphatase activity	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0019888	P	Seeded From UniProt	complete
involved_in	GO:1902036	regulation of hematopoietic stem cell differentiation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q03963 ensembl:ENSMUSP00000024884	P	Seeded From UniProt	complete
involved_in	GO:1902033	regulation of hematopoietic stem cell proliferation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q03963 ensembl:ENSMUSP00000024884	P	Seeded From UniProt	complete
involved_in	GO:1901532	regulation of hematopoietic progenitor cell differentiation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q03963 ensembl:ENSMUSP00000024884	P	Seeded From UniProt	complete
involved_in	GO:1901224	positive regulation of NIK/NF-kappaB signaling	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q03963 ensembl:ENSMUSP00000024884	P	Seeded From UniProt	complete
involved_in	GO:1900225	regulation of NLRP3 inflammasome complex assembly	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q03963 ensembl:ENSMUSP00000024884	P	Seeded From UniProt	complete
involved_in	GO:0046777	protein autophosphorylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q03963 ensembl:ENSMUSP00000024884	P	Seeded From UniProt	complete
involved_in	GO:0045071	negative regulation of viral genome replication	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q03963 ensembl:ENSMUSP00000024884	P	Seeded From UniProt	complete
involved_in	GO:0043066	negative regulation of apoptotic process	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q03963 ensembl:ENSMUSP00000024884	P	Seeded From UniProt	complete
involved_in	GO:0032874	positive regulation of stress-activated MAPK cascade	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q03963 ensembl:ENSMUSP00000024884	P	Seeded From UniProt	complete
involved_in	GO:0032722	positive regulation of chemokine production	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q03963 ensembl:ENSMUSP00000024884	P	Seeded From UniProt	complete
involved_in	GO:0030968	endoplasmic reticulum unfolded protein response	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q03963 ensembl:ENSMUSP00000024884	P	Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q03963 ensembl:ENSMUSP00000024884	P	Seeded From UniProt	complete
involved_in	GO:0006412	translation	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q03963 ensembl:ENSMUSP00000024884	P	Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q03963 ensembl:ENSMUSP00000024884	F	Seeded From UniProt	complete
enables	GO:0003725	double-stranded RNA binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q03963 ensembl:ENSMUSP00000024884	F	Seeded From UniProt	complete
involved_in	GO:0001819	positive regulation of cytokine production	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q03963 ensembl:ENSMUSP00000024884	P	Seeded From UniProt	complete
enables	GO:0003725	double-stranded RNA binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR033366	F	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:0004674	protein serine/threonine kinase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR033366	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	P	Seeded From UniProt	complete
involved_in	GO:0008285	negative regulation of cell population proliferation	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR033366	P	Seeded From UniProt	complete
involved_in	GO:0009615	response to virus	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR033366	P	Seeded From UniProt	complete
involved_in	GO:0009636	response to toxic substance	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR033366	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:IPR033366	P	Seeded From UniProt	complete
involved_in	GO:0042981	regulation of apoptotic process	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR033366	P	Seeded From UniProt	complete
involved_in	GO:0045071	negative regulation of viral genome replication	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR033366	P	Seeded From UniProt	complete
enables	GO:0004715	non-membrane spanning protein tyrosine kinase activity	GO_REF:0000003	ECO:0000501	evidence used in automatic assertion	EC:2.7.10.2	F	Seeded From UniProt	complete
part_of	GO:0005840	ribosome	PMID:10390359^[19]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	Seeded From UniProt	complete
enables	GO:0019888	protein phosphatase regulator activity	PMID:10866685^[20]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0008285	negative regulation of cell population proliferation	PMID:1351683^[21]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	PMID:1695551^[22]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0004694	eukaryotic translation initiation factor 2alpha kinase activity	PMID:10866685^[20]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:1695551^[22]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003725	double-stranded RNA binding	PMID:1351683^[21]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0030683	evasion or tolerance by virus of host immune response	Reactome:R-HSA-168896	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-168896	ECO:0000304	author statement supported by traceable reference used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C	Seeded From UniProt	complete
enables	GO:0004713	protein tyrosine kinase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0829	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:0045087	innate immune response	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0399	P	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: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
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: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
involved_in	GO:0051607	defense response to virus	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0051	P	Seeded From UniProt	complete
involved_in	GO:0002376	immune system process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0391	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
involved_in	GO:0016032	viral process	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0945	P	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:0016310	phosphorylation	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0418	P	Seeded From UniProt	complete
part_of	GO:0048471	perinuclear region of cytoplasm	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0198	C	Seeded From UniProt	complete
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Notes

References

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

↑ Daher, A et al. (2001) Two dimerization domains in the trans-activation response RNA-binding protein (TRBP) individually reverse the protein kinase R inhibition of HIV-1 long terminal repeat expression. J. Biol. Chem. 276 33899-905 PubMed GONUTS page
↑ Xu, M et al. (2012) Double-stranded RNA-dependent protein kinase regulates the motility of breast cancer cells. PLoS ONE 7 e47721 PubMed GONUTS page
↑ ^3.0 ^3.1 Roobol, A et al. (2015) p58IPK is an inhibitor of the eIF2α kinase GCN2 and its localization and expression underpin protein synthesis and ER processing capacity. Biochem. J. 465 213-25 PubMed GONUTS page
↑ Pavio, N et al. (2003) Protein synthesis and endoplasmic reticulum stress can be modulated by the hepatitis C virus envelope protein E2 through the eukaryotic initiation factor 2alpha kinase PERK. J. Virol. 77 3578-85 PubMed GONUTS page
↑ Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 Gil, J et al. (2004) TRAF family proteins link PKR with NF-kappa B activation. Mol. Cell. Biol. 24 4502-12 PubMed GONUTS page
↑ ^7.0 ^7.1 Yoshida, K et al. (2005) Double-stranded RNA-dependent protein kinase is required for bone calcification in MC3T3-E1 cells in vitro. Exp. Cell Res. 311 117-25 PubMed GONUTS page
↑ Lu, B et al. (2012) Novel role of PKR in inflammasome activation and HMGB1 release. Nature 488 670-4 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 ^9.3 Kang, JI et al. (2009) PKR protein kinase is activated by hepatitis C virus and inhibits viral replication through translational control. Virus Res. 142 51-6 PubMed GONUTS page
↑ ^10.0 ^10.1 Chang, JH et al. (2010) Double-stranded RNA-activated protein kinase inhibits hepatitis C virus replication but may be not essential in interferon treatment. Liver Int. 30 311-8 PubMed GONUTS page
↑ Baltz, AG et al. (2012) The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Mol. Cell 46 674-90 PubMed GONUTS page
↑ ^12.0 ^12.1 Pang, Q et al. (2003) Nucleophosmin interacts with and inhibits the catalytic function of eukaryotic initiation factor 2 kinase PKR. J. Biol. Chem. 278 41709-17 PubMed GONUTS page
↑ Harashima, A et al. (2010) Phosphorylation of the NFAR proteins by the dsRNA-dependent protein kinase PKR constitutes a novel mechanism of translational regulation and cellular defense. Genes Dev. 24 2640-53 PubMed GONUTS page
↑ ^14.0 ^14.1 Silva, AM et al. (2004) Protein kinase R (PKR) interacts with and activates mitogen-activated protein kinase kinase 6 (MKK6) in response to double-stranded RNA stimulation. J. Biol. Chem. 279 37670-6 PubMed GONUTS page
↑ Cardin, E & Larose, L (2008) Nck-1 interacts with PKR and modulates its activation by dsRNA. Biochem. Biophys. Res. Commun. 377 231-5 PubMed GONUTS page
↑ ^16.0 ^16.1 ^16.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Watanabe, A et al. (2011) Raftlin is involved in the nucleocapture complex to induce poly(I:C)-mediated TLR3 activation. J. Biol. Chem. 286 10702-11 PubMed GONUTS page
↑ Su, Q et al. (2006) Tyrosine phosphorylation acts as a molecular switch to full-scale activation of the eIF2alpha RNA-dependent protein kinase. Proc. Natl. Acad. Sci. U.S.A. 103 63-8 PubMed GONUTS page
↑ Taylor, DR et al. (1999) Inhibition of the interferon-inducible protein kinase PKR by HCV E2 protein. Science 285 107-10 PubMed GONUTS page
↑ ^20.0 ^20.1 Xu, Z & Williams, BR (2000) The B56alpha regulatory subunit of protein phosphatase 2A is a target for regulation by double-stranded RNA-dependent protein kinase PKR. Mol. Cell. Biol. 20 5285-99 PubMed GONUTS page
↑ ^21.0 ^21.1 Feng, GS et al. (1992) Identification of double-stranded RNA-binding domains in the interferon-induced double-stranded RNA-activated p68 kinase. Proc. Natl. Acad. Sci. U.S.A. 89 5447-51 PubMed GONUTS page
↑ ^22.0 ^22.1 Meurs, E et al. (1990) Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon. Cell 62 379-90 PubMed GONUTS page

[PMID:11438532-1] Daher, A et al. (2001) Two dimerization domains in the trans-activation response RNA-binding protein (TRBP) individually reverse the protein kinase R inhibition of HIV-1 long terminal repeat expression. J. Biol. Chem. 276 33899-905 PubMed GONUTS page

[PMID:23112838-2] Xu, M et al. (2012) Double-stranded RNA-dependent protein kinase regulates the motility of breast cancer cells. PLoS ONE 7 e47721 PubMed GONUTS page

[PMID:25329545-3] 3.0 ^3.1 Roobol, A et al. (2015) p58IPK is an inhibitor of the eIF2α kinase GCN2 and its localization and expression underpin protein synthesis and ER processing capacity. Biochem. J. 465 213-25 PubMed GONUTS page

[PMID:12610133-4] Pavio, N et al. (2003) Protein synthesis and endoplasmic reticulum stress can be modulated by the hepatitis C virus envelope protein E2 through the eukaryotic initiation factor 2alpha kinase PERK. J. Virol. 77 3578-85 PubMed GONUTS page

[PMID:19946888-5] Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page

[PMID:15121867-6] 6.0 ^6.1 ^6.2 Gil, J et al. (2004) TRAF family proteins link PKR with NF-kappa B activation. Mol. Cell. Biol. 24 4502-12 PubMed GONUTS page

[PMID:16216244-7] 7.0 ^7.1 Yoshida, K et al. (2005) Double-stranded RNA-dependent protein kinase is required for bone calcification in MC3T3-E1 cells in vitro. Exp. Cell Res. 311 117-25 PubMed GONUTS page

[PMID:22801494-8] Lu, B et al. (2012) Novel role of PKR in inflammasome activation and HMGB1 release. Nature 488 670-4 PubMed GONUTS page

[PMID:19189853-9] 9.0 ^9.1 ^9.2 ^9.3 Kang, JI et al. (2009) PKR protein kinase is activated by hepatitis C virus and inhibits viral replication through translational control. Virus Res. 142 51-6 PubMed GONUTS page

[PMID:19840259-10] 10.0 ^10.1 Chang, JH et al. (2010) Double-stranded RNA-activated protein kinase inhibits hepatitis C virus replication but may be not essential in interferon treatment. Liver Int. 30 311-8 PubMed GONUTS page

[PMID:22681889-11] Baltz, AG et al. (2012) The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Mol. Cell 46 674-90 PubMed GONUTS page

[PMID:12882984-12] 12.0 ^12.1 Pang, Q et al. (2003) Nucleophosmin interacts with and inhibits the catalytic function of eukaryotic initiation factor 2 kinase PKR. J. Biol. Chem. 278 41709-17 PubMed GONUTS page

[PMID:21123651-13] Harashima, A et al. (2010) Phosphorylation of the NFAR proteins by the dsRNA-dependent protein kinase PKR constitutes a novel mechanism of translational regulation and cellular defense. Genes Dev. 24 2640-53 PubMed GONUTS page

[PMID:15229216-14] 14.0 ^14.1 Silva, AM et al. (2004) Protein kinase R (PKR) interacts with and activates mitogen-activated protein kinase kinase 6 (MKK6) in response to double-stranded RNA stimulation. J. Biol. Chem. 279 37670-6 PubMed GONUTS page

[PMID:18835251-15] Cardin, E & Larose, L (2008) Nck-1 interacts with PKR and modulates its activation by dsRNA. Biochem. Biophys. Res. Commun. 377 231-5 PubMed GONUTS page

[PMID:21873635-16] 16.0 ^16.1 ^16.2 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:21266579-17] Watanabe, A et al. (2011) Raftlin is involved in the nucleocapture complex to induce poly(I:C)-mediated TLR3 activation. J. Biol. Chem. 286 10702-11 PubMed GONUTS page

[PMID:16373505-18] Su, Q et al. (2006) Tyrosine phosphorylation acts as a molecular switch to full-scale activation of the eIF2alpha RNA-dependent protein kinase. Proc. Natl. Acad. Sci. U.S.A. 103 63-8 PubMed GONUTS page

[PMID:10390359-19] Taylor, DR et al. (1999) Inhibition of the interferon-inducible protein kinase PKR by HCV E2 protein. Science 285 107-10 PubMed GONUTS page

[PMID:10866685-20] 20.0 ^20.1 Xu, Z & Williams, BR (2000) The B56alpha regulatory subunit of protein phosphatase 2A is a target for regulation by double-stranded RNA-dependent protein kinase PKR. Mol. Cell. Biol. 20 5285-99 PubMed GONUTS page

[PMID:1351683-21] 21.0 ^21.1 Feng, GS et al. (1992) Identification of double-stranded RNA-binding domains in the interferon-induced double-stranded RNA-activated p68 kinase. Proc. Natl. Acad. Sci. U.S.A. 89 5447-51 PubMed GONUTS page

[PMID:1695551-22] 22.0 ^22.1 Meurs, E et al. (1990) Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon. Cell 62 379-90 PubMed GONUTS page

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HUMAN:E2AK2

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