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:
DNAJC3 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
DNAJC3 Involved in the unfolded protein response (UPR) during ER stress. Co-chaperone of HSPA8/HSC70, it stimulates its ATPase activity. May inhibit both the autophosphorylation of EIF2AK2/PKR and the ability of EIF2AK2 to catalyze phosphorylation of the EIF2A. May inhibit EIF2AK3/PERK activity. Interacts with EIF2AK3 and EIF2AK2. Forms a trimeric complex with DNAJB1 and HSPA8. Interacts with PRKRIR/P52RIPK. Up-regulated during an endoplasmic reticulum stress via ATF6. Activated in response to infection by influenza virus through the dissociation of DNAJB1. Down-regulated by DNAJB1 and PRKRIR/P52RIPK. Widely expressed with high level in the pancreas and testis. Also expressed in cell lines with different levels. Note: This description may include information from UniProtKB.
Protein type: Endoplasmic reticulum; Chaperone; Protein kinase, regulatory subunit; Inhibitor protein
Chromosomal Location of Human Ortholog: 13q32.1
Cellular Component: membrane; endoplasmic reticulum lumen; cytoplasm
Molecular Function: protein kinase inhibitor activity; chaperone binding; misfolded protein binding
Biological Process: cellular protein metabolic process; unfolded protein response, activation of signaling protein activity; proteolysis involved in cellular protein catabolic process; unfolded protein response; negative regulation of protein kinase activity; defense response to virus
Reference #:  Q13217 (UniProtKB)
Alt. Names/Synonyms: DnaJ (Hsp40) homolog, subfamily C, member 3; DnaJ homolog subfamily C member 3; DNAJC3; DNJC3; FLJ21288; HP58; Interferon-induced, double-stranded RNA-activated protein kinase inhibitor; P58; P58IPK; PRKRI; Protein kinase inhibitor of 58 kDa; Protein kinase inhibitor p58; protein-kinase, interferon-inducible double stranded RNA dependent inhibitor
Gene Symbols: DNAJC3
Molecular weight: 57,580 Da
Basal Isoelectric point: 5.83  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

DNAJC3

Protein Structure Not Found.


STRING  |  Wikipedia  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Scansite  |  Pfam  |  RCSB PDB  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


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

 
0 1 S6-p __MVAPGsVtsRLGS
0 1 T8-p MVAPGsVtsRLGSVF
0 1 S9-p VAPGsVtsRLGSVFP
0 2 K46-m2 KHLELGKkLLAAGQL
0 1 T95-p KAALPDLtKVIQLKM
0 1 K96 AALPDLtKVIQLKMD
0 1 K129 DEAEDDFKKVLkSNP
0 1 K133-ub DDFKKVLkSNPSENE
0 1 K150-ub EAQSQLIkSDEMQRL
0 2 K206 IKEGEPRKAISDLKA
0 1 K212 RKAISDLKAASKLKN
0 1 S215 ISDLKAASKLKNDNT
0 1 K270 KQVKKLNKLIESAEE
0 2 K290-ub RYTDATSkYESVMKT
0 1 K296 SkYESVMKTEPSIAE
0 1 K344 PDNVNALKDRAEAYL
0 1 K407-m1 GVKRNAKkQEIIKAY
0 6 K446-ub FIDIAAAkEVLSDPE
  mouse

 
S6 __MVAPGSVGSRLGA
G8 MVAPGSVGSRLGAVF
S9 VAPGSVGSRLGAVFP
K46 KHLELGKKLLAAGQL
T95 KAALPDLTkVIALKM
K96-ub AALPDLTkVIALKMD
K129-sc DEAEDDFkKVLKSNP
K133 DDFkKVLKSNPSEQE
K150 EAESQLVKADEMQRL
K206-ac IKEGEPRkAISDLkA
K212-ac RkAISDLkAAsKLKS
S215-p ISDLkAAsKLKSDNT
K270-ub KQVKKLNkLIESAEE
K290-ub RYTDATSkYESVMkT
K296-ub SkYESVMkTEPSVAE
K344-ub PDNVNALkDRAEAYL
K407 GVKRNAKKQEIIKAY
K446-ub FIDIAAAkEVLSDPE
  rat

 
S6 __MVAPGSVRSRLGA
R8 MVAPGSVRSRLGAVF
S9 VAPGSVRSRLGAVFP
K46 KHLELGKKLLAAGQL
T95 KAALPDLTRVIELKM
R96 AALPDLTRVIELKMD
K129 AEAEDDFKKVLKSNP
K133 DDFKKVLKSNPSENE
K150 EAQSQLVKADEMQRL
K206 IKEGEPRKAISDLKA
K212 RKAISDLKAASKLKN
S215 ISDLKAASKLKNDNT
K270 KQVKKLNKLIGsAEE
K290 RYTDATSKYESVMKA
K296 SKYESVMKAEPSVAE
K344 PDNVNALKDRAEAYL
K407 GVKRNAKKQEIIKAY
K446 FIDIAAAKEVLSDPE
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.