DJ-1 Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of advanced glycation endproducts (AGE) that cause irreversible damage. Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair. Also displays an apparent glyoxalase activity that in fact reflects its deglycase activity. Plays an important role in cell protection against oxidative stress and cell death acting as oxidative stress sensor and redox-sensitive chaperone and protease; functions probably related to its primary function. It is involved in neuroprotective mechanisms like the stabilization of NFE2L2 and PINK1 proteins, male fertility as a positive regulator of androgen signaling pathway as well as cell growth and transformation through, for instance, the modulation of NF-kappa-B signaling pathway. Eliminates hydrogen peroxide and protects cells against hydrogen peroxide-induced cell death. Required for correct mitochondrial morphology and function as well as for autophagy of dysfunctional mitochondria. Plays a role in regulating expression or stability of the mitochondrial uncoupling proteins SLC25A14 and SLC25A27 in dopaminergic neurons of the substantia nigra pars compacta and attenuates the oxidative stress induced by calcium entry into the neurons via L-type channels during pacemaking. Regulates astrocyte inflammatory responses, may modulate lipid rafts-dependent endocytosis in astrocytes and neuronal cells. In pancreatic islets, involved in the maintenance of mitochondrial reactive oxygen species (ROS) levels and glucose homeostasis in an age- and diet dependent manner. Protects pancreatic beta cells from cell death induced by inflammatory and cytotoxic setting. Binds to a number of mRNAs containing multiple copies of GG or CC motifs and partially inhibits their translation but dissociates following oxidative stress. Metal-binding protein able to bind copper as well as toxic mercury ions, enhances the cell protection mechanism against induced metal toxicity. In macrophages, interacts with the NADPH oxidase subunit NCF1 to direct NADPH oxidase-dependent ROS production, and protects against sepsis. Belongs to the peptidase C56 family. Highly expressed in pancreas, kidney, skeletal muscle, liver, testis and heart. Detected at slightly lower levels in placenta and brain (at protein level). Detected in astrocytes, Sertoli cells, spermatogonia, spermatids and spermatozoa. Expressed by pancreatic islets at higher levels than surrounding exocrine tissues (PubMed:22611253). Note: This description may include information from UniProtKB.
Protein type: EC 3.4.-.-; Nuclear receptor co-regulator; Transcription regulation; Tumor suppressor
Chromosomal Location of mouse Ortholog: 4|4 E2
Cellular Component:  axon; cell body; chromatin; cytoplasm; cytosol; endoplasmic reticulum; membrane; membrane raft; mitochondrial intermembrane space; mitochondrial matrix; mitochondrion; neuron projection; nucleus; perinuclear region of cytoplasm; plasma membrane; PML body; sperm head
Molecular Function:  androgen receptor binding; copper ion binding; cupric ion binding; cuprous ion binding; cytokine binding; enzyme binding; hydrolase activity; identical protein binding; kinase binding; L-dopa decarboxylase activator activity; mercury ion binding; mRNA binding; oxidoreductase activity, acting on peroxide as acceptor; peptidase activity; peroxiredoxin activity; protein binding; protein deglycase activity; protein homodimerization activity; repressing transcription factor binding; RNA binding; scaffold protein binding; signaling receptor binding; small protein activating enzyme binding; superoxide dismutase copper chaperone activity; transcription coactivator activity; transcription factor binding; tyrosine 3-monooxygenase activator activity; ubiquitin-like protein conjugating enzyme binding; ubiquitin-specific protease binding
Biological Process:  adult locomotory behavior; autophagy; cellular response to DNA damage stimulus; cellular response to glyoxal; cellular response to hydrogen peroxide; cellular response to oxidative stress; cellular response to reactive oxygen species; detoxification of copper ion; detoxification of mercury ion; DNA repair; dopamine uptake involved in synaptic transmission; enzyme active site formation via L-cysteine sulfinic acid; glucose homeostasis; glutathione deglycation; glycolate biosynthetic process; glyoxal metabolic process; guanine deglycation; guanine deglycation, glyoxal removal; guanine deglycation, methylglyoxal removal; hydrogen peroxide metabolic process; inflammatory response; insulin secretion; lactate biosynthetic process; membrane depolarization; membrane hyperpolarization; mitochondrion organization; negative regulation of apoptotic process; negative regulation of cell death; negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; negative regulation of extrinsic apoptotic signaling pathway; negative regulation of gene expression; negative regulation of hydrogen peroxide-induced cell death; negative regulation of hydrogen peroxide-induced neuron death; negative regulation of hydrogen peroxide-induced neuron intrinsic apoptotic signaling pathway; negative regulation of neuron apoptotic process; negative regulation of neuron death; negative regulation of nitrosative stress-induced intrinsic apoptotic signaling pathway; negative regulation of NMDA glutamate receptor activity; negative regulation of oxidative stress-induced cell death; negative regulation of oxidative stress-induced neuron death; negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; negative regulation of proteasomal ubiquitin-dependent protein catabolic process; negative regulation of protein acetylation; negative regulation of protein binding; negative regulation of protein catabolic process; negative regulation of protein export from nucleus; negative regulation of protein K48-linked deubiquitination; negative regulation of protein kinase activity; negative regulation of protein phosphorylation; negative regulation of protein sumoylation; negative regulation of protein ubiquitination; negative regulation of reactive oxygen species biosynthetic process; negative regulation of TRAIL-activated apoptotic signaling pathway; negative regulation of ubiquitin-protein transferase activity; negative regulation of ubiquitin-specific protease activity; peptidyl-arginine deglycation; peptidyl-cysteine deglycation; peptidyl-lysine deglycation; positive regulation of acute inflammatory response to antigenic stimulus; positive regulation of androgen receptor activity; positive regulation of DNA-binding transcription factor activity; positive regulation of dopamine biosynthetic process; positive regulation of fertilization; positive regulation of gene expression; positive regulation of interleukin-8 production; positive regulation of L-dopa biosynthetic process; positive regulation of L-dopa decarboxylase activity; positive regulation of mitochondrial electron transport, NADH to ubiquinone; positive regulation of NAD(P)H oxidase activity; positive regulation of oxidative phosphorylation uncoupler activity; positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; positive regulation of peptidyl-serine phosphorylation; positive regulation of protein homodimerization activity; positive regulation of protein localization to nucleus; positive regulation of pyrroline-5-carboxylate reductase activity; positive regulation of reactive oxygen species biosynthetic process; positive regulation of superoxide dismutase activity; positive regulation of transcription by RNA polymerase II; positive regulation of transcription regulatory region DNA binding; positive regulation of tyrosine 3-monooxygenase activity; protein deglycation, glyoxal removal; protein stabilization; proteolysis; regulation of androgen receptor signaling pathway; regulation of inflammatory response; regulation of mitochondrial membrane potential; regulation of neuron apoptotic process; response to hydrogen peroxide; response to oxidative stress; single fertilization; synaptic transmission, dopaminergic
Reference #:  Q99LX0 (UniProtKB)
Alt. Names/Synonyms: DJ-1; Dj1; Maillard deglycase; OTTMUSP00000010787; OTTMUSP00000010788; OTTMUSP00000010789; OTTMUSP00000010895; Park7; Parkinson disease (autosomal recessive, early onset) 7; Parkinson disease protein 7 homolog; Parkinsonism-associated deglycase; protein deglycase DJ-1; Protein DJ-1; Protein/nucleic acid deglycase DJ-1; RNA-binding protein regulatory subunit
Gene Symbols: Park7
Molecular weight: 20,021 Da
Basal Isoelectric point: 6.32  Predict pI for various phosphorylation states
CST Pathways:  Parkinson's Disease
Protein-Specific Antibodies, siRNAs or Recombinant Proteins from Cell Signaling Technology® Total Proteins
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DJ-1

Protein Structure Not Found.


Cross-references to other databases:  AlphaFold  |  STRING  |  BioGPS  |  Pfam  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene  |  NURSA