Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
PKR (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

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: Translation; Kinase, protein; Protein kinase, Ser/Thr (non-receptor); Protein kinase, Other; EC 2.7.10.2; EC 2.7.11.1; Other group; PEK family
Cellular Component: perinuclear region of cytoplasm; cytoplasm; nucleus; 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; ATP binding; eukaryotic translation initiation factor 2alpha kinase activity; protein kinase activity
Biological Process: positive regulation of cytokine production; activation of MAPKK activity; transcription, DNA-dependent; translation; unfolded protein response; response to virus; protein amino acid autophosphorylation; viral infectious cycle; protein amino acid phosphorylation; positive regulation of chemokine production; positive regulation of stress-activated MAPK cascade; evasion by virus of host immune response; activation of NF-kappaB transcription factor; negative regulation of cell proliferation; modification by virus of host cellular process; negative regulation of viral genome replication; negative regulation of translation; virus-host interaction; innate immune response; negative regulation of osteoblast proliferation; defense response to virus
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® Total Proteins
Select Structure to View Below

PKR

Protein Structure Not Found.

Substrate Sequence Logo
Sequence Logo

STRING  |  Scansite  |  KinBase  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho3D  |  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
 

Show Multiple Sequence Alignment


 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

 
1 6 S83-p NKEKKAVsPLLLttt
1 0 T88-p AVsPLLLtttNSSEG
1 0 T89-p VsPLLLtttNSSEGL
1 0 T90-p sPLLLtttNSSEGLS
1 0 Y101-p EGLSMGNyIGLINRI
0 1 T115 IAQKKRLTVNYEQCA
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 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
7 1 T446-p LkNDGKRtRSKGtLR
4 1 T451-p KRtRSKGtLRYMsPE
0 1 S456-p KGtLRYMsPEQISSQ
0 2 K517-u KEKTLLQkLLSkKPE
0 2 K521-u LLQkLLSkKPEDRPN
0 4 S542-p TLTVWKKsPEKNERH
3071 : Phospho-PKR (Thr446/451) Antibody
3071 : Phospho-PKR (Thr446/451) Antibody
  mouse

 
C82 DNENKVDCHTSASEQ
H83 NENKVDCHTSASEQG
T84 ENKVDCHTSASEQGL
S85 NKVDCHTSASEQGLF
Y96 QGLFVGNYIGLVNSF
S110-p FAQKKKLsVNYEQCE
Y157 QLAAKEAYQKLLKsP
S163-p AYQKLLKsPPKTAGT
- gap
- gap
- gap
S223-p RKSGVKVsPDDVQRN
N230 sPDDVQRNKYTLDAR
T233 DVQRNKYTLDARFNS
E243 ARFNSDFEDIEEIGL
Y268 HRIDGKRYAIKRVKY
K274 RYAIKRVKYNTEKAE
K279 RVKYNTEKAEHEVQA
T362 DLYEQIVTGVEYIHS
K370 GVEYIHSKGLIHRDL
K378-u GLIHRDLkPGNIFLV
R388 NIFLVDERHIKIGDF
K391 LVDERHIKIGDFGLA
E402 FGLATALENDGKSRt
T409-p ENDGKSRtRRTGTLQ
T414 SRtRRTGTLQYMSPE
S419 TGTLQYMSPEQLFLK
K481 KEKSLLKKLLSEKPK
E485 LLKKLLSEKPKDRPE
S507 LAEWRNISEKKKRNT
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.