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Protein Page:
DJ-1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
DJ-1 associated with autosomal recessive early onset parkinsonism. Involved in the oxidative stress response. Three cysteines in DJ-1 may be oxidized to cysteine sulphonic acid in the cellular response to H2O2. Loss of DJ-1 function may lead to neurodegeneration. Note: This description may include information from UniProtKB.
Protein type: Tumor suppressor; Nuclear receptor co-regulator; EC 3.4.-.-; Transcription regulation
Chromosomal Location of Human Ortholog: 1p36.23
Cellular Component: axon; chromatin; cytoplasm; cytosol; mitochondrial respiratory chain complex I; mitochondrion; nucleus; PML body
Molecular Function: androgen receptor binding; copper ion binding; cytokine binding; double-stranded DNA binding; enzyme binding; glyoxalase III activity; identical protein binding; kinase binding; mercury ion binding; mRNA binding; oxidoreductase activity, acting on peroxide as acceptor; peptidase activity; protein binding; protein homodimerization activity; receptor binding; single-stranded DNA binding; superoxide dismutase copper chaperone activity; transcription coactivator activity; transcription factor binding
Biological Process: activation of protein kinase B; detoxification of copper ion; detoxification of mercury ion; glycolate biosynthetic process; hydrogen peroxide metabolic process; methylglyoxal catabolic process to D-lactate; mitochondrion organization and biogenesis; negative regulation of apoptosis; negative regulation of neuron apoptosis; negative regulation of proteasomal ubiquitin-dependent protein catabolic process; negative regulation of protein amino acid phosphorylation; negative regulation of protein binding; negative regulation of protein export from nucleus; negative regulation of protein kinase activity; negative regulation of protein sumoylation; negative regulation of protein ubiquitination; negative regulation of ubiquitin-protein ligase activity; positive regulation of interleukin-8 production; positive regulation of peptidyl-serine phosphorylation; positive regulation of protein kinase B signaling cascade; positive regulation of transcription factor activity; positive regulation of transcription from RNA polymerase II promoter; protein deglycosylation; protein stabilization; Ras protein signal transduction; regulation of inflammatory response; regulation of mitochondrial membrane potential; regulation of neuron apoptosis; regulation of TRAIL receptor biosynthetic process
Disease: Parkinson Disease 7, Autosomal Recessive Early-onset
Reference #:  Q99497 (UniProtKB)
Alt. Names/Synonyms: DJ-1; DJ1; FLJ27376; FLJ34360; FLJ92274; Oncogene DJ1; PARK7; Parkinson disease (autosomal recessive, early onset) 7; Parkinson disease protein 7; Protein DJ-1
Gene Symbols: PARK7
Molecular weight: 19,891 Da
Basal Isoelectric point: 6.33  Predict pI for various phosphorylation states
CST Pathways:  Parkinson's Disease
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

DJ-1

Protein Structure Not Found.
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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



 LTP 

LTP: 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.


 HTP 

HTP: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 T19‑p KGAEEMEtVIPVDVM
0 1 K32 VMRRAGIKVTVAGLA
0 1 K41‑ac TVAGLAGkDPVQCsR
0 4 K41‑ub TVAGLAGkDPVQCsR
0 2 S47‑p GkDPVQCsRDVVICP
0 12 K62‑ac DASLEDAkkEGPyDV
0 1 K62‑sc DASLEDAkkEGPyDV
0 1 K63‑ac ASLEDAkkEGPyDVV
0 19 Y67‑p DAkkEGPyDVVVLPG
0 1 K89‑sc LSESAAVkEILkEQE
0 2 K93 AAVkEILKEQENRkG
0 1 K93‑sc AAVkEILkEQENRkG
0 1 K99‑ub LkEQENRkGLIAAIC
0 3 K130‑ac VTTHPLAkDkMMNGG
4 0 K130‑sm VTTHPLAkDkMMNGG
0 1 K130‑sc VTTHPLAkDkMMNGG
0 3 K132‑ac THPLAkDkMMNGGHy
0 1 K132 THPLAkDKMMNGGHy
0 2 Y139‑p kMMNGGHyTySENRV
0 3 T140 MMNGGHyTySENRVE
0 2 Y141‑p MNGGHyTySENRVEk
0 1 S142 NGGHyTySENRVEkD
0 5 K148‑ac ySENRVEkDGLILtS
0 2 K148‑ub ySENRVEkDGLILtS
1 2 T154‑p EkDGLILtSRGPGTS
1 1 S155 kDGLILtSRGPGTSF
0 1 K175‑ub IVEALNGkEVAAQVk
0 1 K182 kEVAAQVKAPLVLkD
0 1 K182‑sc kEVAAQVkAPLVLkD
0 1 K188 VkAPLVLKD______
0 2 K188‑ub VkAPLVLkD______
  mouse

 
T19 KGAEEMETVIPVDVM
K32‑ub VMRRAGIkVTVAGLA
K41 TVAGLAGKDPVQCsR
K41‑ub TVAGLAGkDPVQCsR
S47‑p GkDPVQCsRDVMICP
K62 DTSLEDAKTQGPYDV
K62 DTSLEDAKTQGPYDV
T63 TSLEDAKTQGPYDVV
Y67 DAKTQGPYDVVVLPG
K89 LSESPMVKEILkEQE
K93‑ac PMVKEILkEQESRKG
K93 PMVKEILKEQESRKG
K99 LkEQESRKGLIAAIC
K130‑ac VTTHPLAkDkMMNGS
K130 VTTHPLAKDkMMNGS
K130 VTTHPLAKDkMMNGS
K132 THPLAkDKMMNGSHY
K132‑ub THPLAkDkMMNGSHY
Y139 kMMNGSHYsYsESRV
S140‑p MMNGSHYsYsESRVE
Y141 MNGSHYsYsESRVEk
S142‑p NGSHYsYsESRVEkD
K148‑ac YsESRVEkDGLILTS
K148‑ub YsESRVEkDGLILTS
T154 EkDGLILTSRGPGTS
S155 kDGLILTSRGPGTSF
K175 IVEALVGKDMANQVk
K182‑ub KDMANQVkAPLVLKD
K182 KDMANQVKAPLVLKD
K188 VkAPLVLKD______
K188 VkAPLVLKD______
  rat

 
T19 KGAEEMETVIPVDIM
K32 IMRRAGIKVTVAGLA
K41 TVAGLAGKDPVQCSR
K41 TVAGLAGKDPVQCSR
S47 GKDPVQCSRDVVICP
K62 DTSLEEAKTQGPYDV
K62 DTSLEEAKTQGPYDV
T63 TSLEEAKTQGPYDVV
Y67 EAKTQGPYDVVVLPG
K89 LSESALVKEILkEQE
K93‑ac ALVKEILkEQENRKG
K93 ALVKEILKEQENRKG
K99 LkEQENRKGLIAAIC
K130‑ac VTSHPLAkDkMMNGS
K130 VTSHPLAKDkMMNGS
K130 VTSHPLAKDkMMNGS
K132‑ac SHPLAkDkMMNGSHY
K132 SHPLAkDKMMNGSHY
Y139 kMMNGSHYSYSESRV
S140 MMNGSHYSYSESRVE
Y141 MNGSHYSYSESRVEk
S142 NGSHYSYSESRVEkD
K148‑ac YSESRVEkDGLILts
K148 YSESRVEKDGLILts
T154‑p EkDGLILtsRGPGTS
S155‑p kDGLILtsRGPGTSF
K175 IVEALSGKDMANQVK
K182 KDMANQVKAPLVLkD
K182 KDMANQVKAPLVLkD
K188‑ac VKAPLVLkD______
K188 VKAPLVLKD______
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