Home

PKR (human)

Overview PKR a protein kinase of the PEK family. Upon binding double-stranded RNA, it becomes autophosphorylated and activated. Phosphorylates and inhibits the alpha subunit of eIF2 alpha, which leads to an inhibition of the initiation of protein synthesis. Controls the activation of several transcription factors such as NF-kappaB, p53 and Stats. Mediates apoptosis induced by many different stimuli, such as LPS, TNF-alpha, viral infection and serum starvation. Note: This description may include information from UniProtKB. Protein type: EC 2.7.10.2; Protein kinase, Ser/Thr (non-receptor); Protein kinase, Other; Kinase, protein; Translation; EC 2.7.11.1; Other group; PEK family Cellular Component: cytosol Molecular Function: protein serine/threonine kinase activity; protein binding; double-stranded RNA binding; non-membrane spanning protein tyrosine kinase activity; protein phosphatase type 2A regulator activity; eukaryotic translation initiation factor 2alpha kinase activity; ATP binding Biological Process: virus-infected cell apoptosis; negative regulation of cell proliferation; translation; modification by virus of host cellular process; unfolded protein response; virus-host interaction; protein amino acid autophosphorylation; negative regulation of osteoblast proliferation; viral infectious cycle; defense response to virus; protein amino acid phosphorylation; evasion by virus of host immune response Reference #:  P19525 (UniProtKB) Alt. Names/Synonyms: double stranded RNA activated protein kinase; E2AK2; eIF-2A protein kinase 2; EIF2AK1; EIF2AK2; Eukaryotic translation initiation factor 2-alpha kinase 2; Interferon-induced, double-stranded RNA-activated protein kinase; interferon-inducible elF2alpha kinase; Interferon-inducible RNA-dependent protein kinase; MGC126524; P1/eIF-2A protein kinase; p68 kinase; PKR; PRKR; Protein kinase RNA-activated; protein kinase, interferon-inducible double stranded RNA dependent Gene Symbols: EIF2AK2 Molecular weight: 62,094 Da Basal Isoelectric point: 8.58  Predict pI for various phosphorylation states CST Pathways:  Translation: eIF2 Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below PKR 1QU6 - A=1-170 (human) 2A19 - B/C=258-550 (human) 2A1A - B=258-550 (human) 3UIU - A/B=254-551 (human) 1X48 - A=96-171 (mouse) 1X49 - A=1-85 (mouse) Substrate Sequence Logo

STRING  |  Scansite  |  KinBase  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 1QU6 2A19 2A1A 3UIU  |  ENZYME  |  Phospho3D  |  DISEASE  |  Source  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene

	Sites Implicated In
cell cycle regulation: T446‑p cell growth, altered: Y101‑p, Y162‑p, Y293‑p, T446‑p translation, altered: Y101‑p, Y162‑p, Y293‑p enzymatic activity, induced: S83‑p, T88‑p, T89‑p, T90‑p, Y101‑p, Y162‑p, S242‑p, T255‑p, T258‑p, Y293‑p, T446‑p, T451‑p

	Modification Sites and Domains	Show Modification Legend
Click here to view phosphorylation modifications only

	Modification Sites in Parent Protein, Orthologs, and Isoforms	Show Modification Legend

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human
0	1		S6-p	__MAGDLsAGFFMEE
0	1		N32	LKYQELPNSGPPHDR
0	1		K61-m1	EGEGRSKkEAKNAAA
0	1		K69	EAKNAAAKLAVEILN
0	1		K69-m1	EAKNAAAkLAVEILN
1	6		S83-p	NKEKKAVsPLLLttt
1	0		T88-p	AVsPLLLtttNsSEG
1	0		T89-p	VsPLLLtttNsSEGL
1	0		T90-p	sPLLLtttNsSEGLS
0	1		S92-p	LLLtttNsSEGLSMG
1	0		Y101-p	EGLSMGNyIGLINRI
0	1		T115	IAQKKRLTVNYEQCA
0	1		Y142-p	CKMGQKEySIGTGST
1	0		Y162-p	QLAAKLAyLQILSEE
0	5		-	gap
0	3		S179-p	VKSDYLSsGsFATTC
0	3		S181-p	SDYLSsGsFATTCES
2	1		S242-p	NQRKAKRsLAPRFDL
0	3		-	gap
2	0		T255-p	DLPDMKEtKYtVDKR
2	0		T258-p	DMKEtKYtVDKRFGM
0	4		K268-u	KRFGMDFkEIELIGS
1	0		Y293-p	HRIDGKTyVIKRVkY
0	1		K299-u	TyVIKRVkYNNEkAE
0	4		K304-u	RVkYNNEkAEREVKA
0	1		K385-u	IEKRRGEkLDkVLAL
0	1		K388-u	RRGEkLDkVLALELF
0	8		K400-u	ELFEQITkGVDYIHS
0	4		K408-u	GVDYIHSkKLIHRDL
0	3		K416-u	KLIHRDLkPSNIFLV
0	2		K426-u	NIFLVDTkQVkIGDF
0	4		K429-u	LVDTkQVkIGDFGLV
0	2		K440-u	FGLVTSLkNDGKRtR
6	1		T446-p	LkNDGKRtRSKGtLR
4	1		T451-p	KRtRSKGtLRyMsPE
0	1		Y454-p	RSKGtLRyMsPEQIS
0	1		S456-p	KGtLRyMsPEQISSQ
0	1		K509-u	IISDIFDkKEKTLLQ
0	2		K517-u	KEKTLLQkLLSkKPE
0	2		K521-u	LLQkLLSkKPEDRPN
0	1		T535-p	NTSEILRtLTVWKKs
0	3		S542-p	tLTVWKKsPEKNERH

	mouse
T5	___MASDTPGFYMDK
T31-p	ITYKELStSGPPHDR
Q60	EAKGRSKQEARNAAA
K68-a	EARNAAAkLAVDILD
K68	EARNAAAKLAVDILD
C82	DNENKVDCHTSASEQ
H83	NENKVDCHTSASEQG
T84	ENKVDCHTSASEQGL
S85	NKVDCHTSASEQGLF
S87	VDCHTSASEQGLFVG
Y96	QGLFVGNYIGLVNSF
S110-p	FAQKKKLsVNYEQCE
Y137	CKIGQTMYGTGSGVT
Y157	QLAAKEAYQKLLKsP
S163-p	AYQKLLKsPPKTAGT
-	gap
-	gap
-	gap
S223-p	RKSGVKVsPDDVQRN
N230	sPDDVQRNKYTLDAR
T233	DVQRNKYTLDARFNS
E243	ARFNSDFEDIEEIGL
Y268	HRIDGKRYAIKRVKY
K274	RYAIKRVKYNTEKAE
K279	RVKYNTEKAEHEVQA
K347	MRNRNQSKVDKALIL
K350	RNQSKVDKALILDLY
T362	DLYEQIVTGVEYIHS
K370	GVEYIHSKGLIHRDL
K378-u	GLIHRDLkPGNIFLV
R388	NIFLVDERHIKIGDF
K391	LVDERHIKIGDFGLA
E402	FGLATALENDGKSRt
T409-p	ENDGKSRtRRTGTLQ
T414	SRtRRTGTLQYMSPE
Y417	RRTGTLQYMSPEQLF
S419	TGTLQYMSPEQLFLK
N473	FSNDIFDNKEKSLLK
K481	KEKSLLKKLLSEKPK
E485	LLKKLLSEKPKDRPE
T499	ETSEILKTLAEWRNI
S507	LAEWRNISEKKKRNT

Home  |  Curator Login With enhanced literature mining using Linguamatics I2E Produced by 3rd Millennium  |  Design by Digizyme ©2003-2013 Cell Signaling Technology, Inc.