Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00905
Entry Name
UniProt Accession
Theoretical PI
6.32
Molecular Weight
19891.05
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Protein DJ-1
Protein Synonyms/Alias
3.4.-.-; Oncogene DJ1; Parkinson disease protein 7;
Gene Name
PARK7
Gene Synonyms/Alias
Created Date
07-DEC-2004
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
46
Canonical
AGKDPVQCSRDVVIC
[1]
S-Palmitoylation
53
Canonical
CSRDVVICPDASLED
[1]
S-Palmitoylation
106
Canonical
KGLIAAICAGPTALL
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Kim KS, Kim JS, Park JY, Suh YH, Jou I, Joe EH, Park SM. DJ-1 associates with lipid rafts by palmitoylation and regulates lipid rafts-dependent endocytosis in astrocytes. Hum Mol Genet. 2013 Dec 1;22(23):4805-17. doi: 10.1093/hmg/ddt332.Epub 2013 Jul 11.[PMID:23847046]
Functional Description
Protects cells against oxidative stress and cell death. 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. Eliminates hydrogen peroxide and protects cells against hydrogen peroxide-induced cell death. Following removal of a C-terminal peptide, displays protease activity and enhanced cytoprotective action against oxidative stress-induced apoptosis. Stabilizes NFE2L2 by preventing its association with KEAP1 and its subsequent ubiquitination. Binds to OTUD7B and inhibits its deubiquitinating activity. Enhances RELA nuclear translocation. Binds to a number of mRNAs containing multiple copies of GG or CC motifs and partially inhibits their translation but dissociates following oxidative stress. Required for correct mitochondrial morphology and function and for autophagy of dysfunctional mitochondria. Regulates astrocyte inflammatory responses. Acts as a positive regulator of androgen receptor-dependent transcription. Prevents aggregation of SNCA. Plays a role in fertilization. Has no proteolytic activity. Has cell-growth promoting activity and transforming activity. May function as a redox-sensitive chaperone. May regulate lipid rafts-dependent endocytosis in astrocytes and neuronal cells.
Sequence Annotation
Active site: 106 106
Active site: 126 126
Modified residue: 67 67 Phosphotyrosine.
Modified residue: 106 106 Cysteine sulfinic acid (-SO2H);alternate.
Modified residue: 148 148 N6-acetyllysine.
Modified residue: 182 182 N6-succinyllysine.
Protein Length
189 AA.
Protein Sequence
(Canonical)
MASKRALVIL AKGAEEMETV IPVDVMRRAG IKVTVAGLAG KDPVQCSRDV VICPDASLED  60
AKKEGPYDVV VLPGGNLGAQ NLSESAAVKE ILKEQENRKG LIAAICAGPT ALLAHEIGFG  120
SKVTTHPLAK DKMMNGGHYT YSENRVEKDG LILTSRGPGT SFEFALAIVE ALNGKEVAAQ  180
VKAPLVLKD                                                          189
FASTA
(Canonical)
>LipidDB-9606-00905|Q99497
MASKRALVILAKGAEEMETVIPVDVMRRAGIKVTVAGLAGKDPVQCSRDVVICPDASLED
AKKEGPYDVVVLPGGNLGAQNLSESAAVKEILKEQENRKGLIAAICAGPTALLAHEIGFG
SKVTTHPLAKDKMMNGGHYTYSENRVEKDGLILTSRGPGTSFEFALAIVEALNGKEVAAQ
VKAPLVLKD
Gene Ontology
GO:0000785; C:chromatin; IDA:ParkinsonsUK-UCL
GO:0005737; C:cytoplasm; IDA:UniProtKB
GO:0005829; C:cytosol; IMP:UniProtKB
GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB
GO:0005739; C:mitochondrion; IDA:UniProtKB
GO:0005634; C:nucleus; IDA:UniProtKB
GO:0005886; C:plasma membrane; IEA:UniProtKB-KW
GO:0016605; C:PML body; IDA:ParkinsonsUK-UCL
GO:0050681; F:androgen receptor binding; IPI:ParkinsonsUK-UCL
GO:1903135; F:cupric ion binding; IDA:ParkinsonsUK-UCL
GO:1903136; F:cuprous ion binding; IDA:ParkinsonsUK-UCL
GO:0019955; F:cytokine binding; IPI:ParkinsonsUK-UCL
GO:0019899; F:enzyme binding; IPI:ParkinsonsUK-UCL
GO:1990422; F:glyoxalase (glycolic acid-forming) activity; IDA:ParkinsonsUK-UCL
GO:0019172; F:glyoxalase III activity; IDA:ParkinsonsUK-UCL
GO:0042802; F:identical protein binding; IPI:ParkinsonsUK-UCL
GO:0036478; F:L-dopa decarboxylase activator activity; IDA:ParkinsonsUK-UCL
GO:0003729; F:mRNA binding; IDA:UniProtKB
GO:0016684; F:oxidoreductase activity, acting on peroxide as acceptor; IDA:ParkinsonsUK-UCL
GO:0008233; F:peptidase activity; IDA:UniProtKB
GO:0004601; F:peroxidase activity; IEA:Ensembl
GO:0051920; F:peroxiredoxin activity; IEA:Ensembl
GO:0042803; F:protein homodimerization activity; IDA:UniProtKB
GO:0005102; F:receptor binding; IPI:UniProtKB
GO:0070491; F:repressing transcription factor binding; IPI:ParkinsonsUK-UCL
GO:0003723; F:RNA binding; TAS:ParkinsonsUK-UCL
GO:0097110; F:scaffold protein binding; IPI:ParkinsonsUK-UCL
GO:0044388; F:small protein activating enzyme binding; IPI:ParkinsonsUK-UCL
GO:0044390; F:small protein conjugating enzyme binding; IPI:ParkinsonsUK-UCL
GO:0016532; F:superoxide dismutase copper chaperone activity; IDA:ParkinsonsUK-UCL
GO:0003713; F:transcription coactivator activity; IGI:ParkinsonsUK-UCL
GO:0008134; F:transcription factor binding; IPI:ParkinsonsUK-UCL
GO:0036470; F:tyrosine 3-monooxygenase activator activity; IDA:ParkinsonsUK-UCL
GO:1990381; F:ubiquitin-specific protease binding; IPI:ParkinsonsUK-UCL
GO:0008344; P:adult locomotory behavior; IEA:Ensembl
GO:0006914; P:autophagy; IEA:UniProtKB-KW
GO:0036471; P:cellular response to glyoxal; IDA:ParkinsonsUK-UCL
GO:0070301; P:cellular response to hydrogen peroxide; IDA:UniProtKB
GO:0034599; P:cellular response to oxidative stress; IDA:ParkinsonsUK-UCL
GO:0051583; P:dopamine uptake involved in synaptic transmission; IEA:Ensembl
GO:0046295; P:glycolate biosynthetic process; IDA:ParkinsonsUK-UCL
GO:1903190; P:glyoxal catabolic process; IDA:ParkinsonsUK-UCL
GO:0042743; P:hydrogen peroxide metabolic process; IDA:ParkinsonsUK-UCL
GO:0006954; P:inflammatory response; IEA:UniProtKB-KW
GO:0019249; P:lactate biosynthetic process; IDA:GOC
GO:0051899; P:membrane depolarization; IEA:Ensembl
GO:0060081; P:membrane hyperpolarization; IEA:Ensembl
GO:0019243; P:methylglyoxal catabolic process to D-lactate; IDA:ParkinsonsUK-UCL
GO:0007005; P:mitochondrion organization; ISS:UniProtKB
GO:0043066; P:negative regulation of apoptotic process; IDA:ParkinsonsUK-UCL
GO:0060548; P:negative regulation of cell death; IDA:UniProtKB
GO:2001268; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IMP:ParkinsonsUK-UCL
GO:1903073; P:negative regulation of death-inducing signaling complex assembly; IC:ParkinsonsUK-UCL
GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:UniProtKB
GO:0010629; P:negative regulation of gene expression; IDA:ParkinsonsUK-UCL
GO:1903206; P:negative regulation of hydrogen peroxide-induced cell death; IMP:ParkinsonsUK-UCL
GO:1903208; P:negative regulation of hydrogen peroxide-induced neuron death; IDA:ParkinsonsUK-UCL
GO:0043524; P:negative regulation of neuron apoptotic process; IDA:BHF-UCL
GO:1901215; P:negative regulation of neuron death; IDA:ParkinsonsUK-UCL
GO:1903202; P:negative regulation of oxidative stress-induced cell death; IDA:ParkinsonsUK-UCL
GO:1903377; P:negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; IDA:ParkinsonsUK-UCL
GO:1901984; P:negative regulation of protein acetylation; IDA:ParkinsonsUK-UCL
GO:0032091; P:negative regulation of protein binding; IDA:UniProtKB
GO:0046826; P:negative regulation of protein export from nucleus; IGI:ParkinsonsUK-UCL
GO:1903094; P:negative regulation of protein K48-linked deubiquitination; IDA:ParkinsonsUK-UCL
GO:0006469; P:negative regulation of protein kinase activity; IGI:ParkinsonsUK-UCL
GO:0001933; P:negative regulation of protein phosphorylation; IGI:ParkinsonsUK-UCL
GO:0033234; P:negative regulation of protein sumoylation; IDA:ParkinsonsUK-UCL
GO:0031397; P:negative regulation of protein ubiquitination; IDA:ParkinsonsUK-UCL
GO:1903122; P:negative regulation of TRAIL-activated apoptotic signaling pathway; IMP:ParkinsonsUK-UCL
GO:0051444; P:negative regulation of ubiquitin-protein transferase activity; IDA:ParkinsonsUK-UCL
GO:2000157; P:negative regulation of ubiquitin-specific protease activity; IDA:ParkinsonsUK-UCL
GO:2000825; P:positive regulation of androgen receptor activity; IMP:ParkinsonsUK-UCL
GO:1903181; P:positive regulation of dopamine biosynthetic process; IDA:ParkinsonsUK-UCL
GO:0032757; P:positive regulation of interleukin-8 production; IDA:ParkinsonsUK-UCL
GO:1903197; P:positive regulation of L-dopa biosynthetic process; IMP:ParkinsonsUK-UCL
GO:1903200; P:positive regulation of L-dopa decarboxylase activity; IDA:ParkinsonsUK-UCL
GO:1902958; P:positive regulation of mitochondrial electron transport, NADH to ubiquinone; IMP:ParkinsonsUK-UCL
GO:2000277; P:positive regulation of oxidative phosphorylation uncoupler activity; IEA:Ensembl
GO:0090073; P:positive regulation of protein homodimerization activity; IDA:ParkinsonsUK-UCL
GO:1900182; P:positive regulation of protein localization to nucleus; IDA:ParkinsonsUK-UCL
GO:1903168; P:positive regulation of pyrroline-5-carboxylate reductase activity; IDA:ParkinsonsUK-UCL
GO:1901671; P:positive regulation of superoxide dismutase activity; IDA:ParkinsonsUK-UCL
GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:ParkinsonsUK-UCL
GO:1903178; P:positive regulation of tyrosine 3-monooxygenase activity; IDA:ParkinsonsUK-UCL
GO:0050821; P:protein stabilization; IMP:UniProtKB
GO:0060765; P:regulation of androgen receptor signaling pathway; IDA:UniProtKB
GO:1902903; P:regulation of fibril organization; TAS:ParkinsonsUK-UCL
GO:0050727; P:regulation of inflammatory response; ISS:UniProtKB
GO:0051881; P:regulation of mitochondrial membrane potential; IMP:ParkinsonsUK-UCL
GO:0043523; P:regulation of neuron apoptotic process; IDA:UniProtKB
GO:0007338; P:single fertilization; IEA:UniProtKB-KW
Interpro
InterPro; IPR029062; Class_I_gatase-like
InterPro; IPR006287; DJ1
InterPro; IPR002818; ThiJ/PfpI
Pfam
Pfam; PF01965; DJ-1_PfpI;
SMART
PROSITE
PRINTS