Detailed entry information

Protein Information (annotations from UniProt)

Database IDHIV0002090
UniProt IDQ99497
Primary gene name(s)PARK7
Synonym gene name(s)unknown
Protein nameProtein deglycase DJ-1
Protein functionProtein deglycase that repairs methylglyoxal- and glyoxal-glycated amino acids and proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteines, arginines and lysines 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, PubMed:25416785. 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, PubMed:17015834, PubMed:20304780, PubMed:18711745, PubMed:12796482, PubMed:19229105, PubMed:25416785. 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, PubMed:12612053, PubMed:15502874, PubMed:14749723, PubMed:17015834, PubMed:21097510, PubMed:18711745. Its involvement in protein repair could also explain other unrelated functions. Eliminates hydrogen peroxide and protects cells against hydrogen peroxide-induced cell death, PubMed:16390825. Required for correct mitochondrial morphology and function as well as for autophagy of dysfunctional mitochondria, PubMed:19229105, PubMed:16632486. 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, PubMed:18711745. Regulates astrocyte inflammatory responses, may modulate lipid rafts-dependent endocytosis in astrocytes and neuronal cells, PubMed:23847046. Binds to a number of mRNAs containing multiple copies of GG or CC motifs and partially inhibits their translation but dissociates following oxidative stress, PubMed:18626009. Metal-binding protein able to bind copper as well as toxic mercury ions, enhances the cell protection mechanism against induced metal toxicity, PubMed:23792957. {ECO:0000250|UniProtKB:Q99LX0, ECO:0000269|PubMed:11477070, ECO:0000269|PubMed:12612053, ECO:0000269|PubMed:12855764, ECO:0000269|PubMed:12939276, ECO:0000269|PubMed:14749723, ECO:0000269|PubMed:15181200, ECO:0000269|PubMed:15502874, ECO:0000269|PubMed:15976810, ECO:0000269|PubMed:16390825, ECO:0000269|PubMed:17015834, ECO:0000269|PubMed:18626009, ECO:0000269|PubMed:18711745, ECO:0000269|PubMed:19229105, ECO:0000269|PubMed:20186336, ECO:0000269|PubMed:20304780, ECO:0000269|PubMed:21097510, ECO:0000269|PubMed:22523093, ECO:0000269|PubMed:23792957, ECO:0000269|PubMed:23847046, ECO:0000269|PubMed:25416785, ECO:0000269|PubMed:9070310}.
Subcellular locationCell membrane {ECO:0000250|UniProtKB:O88767};
Lipid-anchor {ECO:0000250|UniProtKB:O88767}. Cytoplasm {ECO:0000269|PubMed:12851414, ECO:0000269|PubMed:14579415, ECO:0000269|PubMed:15976810, ECO:0000269|PubMed:19229105}. Nucleus {ECO:0000269|PubMed:12851414, ECO:0000269|PubMed:14579415, ECO:0000269|PubMed:15976810}. Membrane raft {ECO:0000250|UniProtKB:O88767}. Mitochondrion {ECO:0000269|PubMed:15181200, ECO:0000269|PubMed:18711745, ECO:0000269|PubMed:19229105}. Note=Under normal conditions, located predominantly in the cytoplasm and, to a lesser extent, in the nucleus and mitochondrion. Translocates to the mitochondrion and subsequently to the nucleus in response to oxidative stress and exerts an increased cytoprotective effect against oxidative damage, PubMed:18711745. Detected in tau inclusions in brains from neurodegenerative disease patients, PubMed:14705119. Membrane raft localization in astrocytes and neuronal cells requires palmitoylation. {ECO:0000269|PubMed:14705119, ECO:0000269|PubMed:18711745}.
ECO codeClick here for more information.
Amino acid sequence
FASTA format: Q99497
Gene Ontology
(Biological Process)
Complete annatation
activation of protein kinase B activity [GO:0032148];
adult locomotory behavior [GO:0008344];
autophagy [GO:0006914];
cellular response to glyoxal [GO:0036471];
cellular response to hydrogen peroxide [GO:0070301];
cellular response to oxidative stress [GO:0034599];
detoxification of copper ion [GO:0010273];
detoxification of mercury ion [GO:0050787];
dopamine uptake involved in synaptic transmission [GO:0051583];
enzyme active site formation via L-cysteine sulfinic acid [GO:0018323];
glutathione deglycation [GO:0036531];
glycolate biosynthetic process [GO:0046295];
glyoxal metabolic process [GO:1903189];
hydrogen peroxide metabolic process [GO:0042743];
inflammatory response [GO:0006954];
lactate biosynthetic process [GO:0019249];
membrane depolarization [GO:0051899];
membrane hyperpolarization [GO:0060081];
methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione [GO:0019243];
methylglyoxal metabolic process [GO:0009438];
mitochondrion organization [GO:0007005];
negative regulation of apoptotic process [GO:0043066];
negative regulation of cell death [GO:0060548];
negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway [GO:2001268];
negative regulation of death-inducing signaling complex assembly [GO:1903073];
negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway [GO:1902236];
negative regulation of extrinsic apoptotic signaling pathway [GO:2001237];
negative regulation of gene expression [GO:0010629];
negative regulation of hydrogen peroxide-induced cell death [GO:1903206];
negative regulation of hydrogen peroxide-induced neuron death [GO:1903208];
negative regulation of hydrogen peroxide-induced neuron intrinsic apoptotic signaling pathway [GO:1903384];
negative regulation of neuron apoptotic process [GO:0043524];
negative regulation of neuron death [GO:1901215];
negative regulation of nitrosative stress-induced intrinsic apoptotic signaling pathway [GO:1905259];
negative regulation of oxidative stress-induced cell death [GO:1903202];
negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway [GO:1903377];
negative regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032435];
negative regulation of protein acetylation [GO:1901984];
negative regulation of protein binding [GO:0032091];
negative regulation of protein export from nucleus [GO:0046826];
negative regulation of protein K48-linked deubiquitination [GO:1903094];
negative regulation of protein kinase activity [GO:0006469];
negative regulation of protein phosphorylation [GO:0001933];
negative regulation of protein sumoylation [GO:0033234];
negative regulation of protein ubiquitination [GO:0031397];
negative regulation of TRAIL-activated apoptotic signaling pathway [GO:1903122];
negative regulation of ubiquitin-protein transferase activity [GO:0051444];
negative regulation of ubiquitin-specific protease activity [GO:2000157];
peptidyl-arginine deglycation [GO:0036527];
peptidyl-cysteine deglycation [GO:0036526];
peptidyl-lysine deglycation [GO:0036528];
positive regulation of androgen receptor activity [GO:2000825];
positive regulation of dopamine biosynthetic process [GO:1903181];
positive regulation of gene expression [GO:0010628];
positive regulation of interleukin-8 production [GO:0032757];
positive regulation of L-dopa biosynthetic process [GO:1903197];
positive regulation of L-dopa decarboxylase activity [GO:1903200];
positive regulation of mitochondrial electron transport, NADH to ubiquinone [GO:1902958];
positive regulation of mitophagy [GO:1903599];
positive regulation of oxidative phosphorylation uncoupler activity [GO:2000277];
positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway [GO:1902177];
positive regulation of peptidyl-serine phosphorylation [GO:0033138];
positive regulation of protein homodimerization activity [GO:0090073];
positive regulation of protein kinase B signaling [GO:0051897];
positive regulation of protein localization to nucleus [GO:1900182];
positive regulation of pyrroline-5-carboxylate reductase activity [GO:1903168];
positive regulation of reactive oxygen species biosynthetic process [GO:1903428];
positive regulation of sequence-specific DNA binding transcription factor activity [GO:0051091];
positive regulation of superoxide dismutase activity [GO:1901671];
positive regulation of transcription from RNA polymerase II promoter [GO:0045944];
positive regulation of transcription regulatory region DNA binding [GO:2000679];
positive regulation of tyrosine 3-monooxygenase activity [GO:1903178];
protein deglycation, glyoxal removal [GO:0036529];
protein deglycation, methylglyoxal removal [GO:0036530];
protein deglycosylation [GO:0006517];
protein stabilization [GO:0050821];
Ras protein signal transduction [GO:0007265];
regulation of androgen receptor signaling pathway [GO:0060765];
regulation of fibril organization [GO:1902903];
regulation of inflammatory response [GO:0050727];
regulation of mitochondrial membrane potential [GO:0051881];
regulation of neuron apoptotic process [GO:0043523];
single fertilization [GO:0007338]
Gene Ontology
(Molecular Function)
Complete annatation
androgen receptor binding [GO:0050681];
copper ion binding [GO:0005507];
cupric ion binding [GO:1903135];
cuprous ion binding [GO:1903136];
cytokine binding [GO:0019955];
enzyme binding [GO:0019899];
glyoxalase, glycolic acid-forming activity [GO:1990422];
glyoxalase III activity [GO:0019172];
identical protein binding [GO:0042802];
kinase binding [GO:0019900];
L-dopa decarboxylase activator activity [GO:0036478];
mercury ion binding [GO:0045340];
mRNA binding [GO:0003729];
oxidoreductase activity, acting on peroxide as acceptor [GO:0016684];
peptidase activity [GO:0008233];
peroxiredoxin activity [GO:0051920];
protein homodimerization activity [GO:0042803];
receptor binding [GO:0005102];
repressing transcription factor binding [GO:0070491];
scaffold protein binding [GO:0097110];
small protein activating enzyme binding [GO:0044388];
superoxide dismutase copper chaperone activity [GO:0016532];
transcription coactivator activity [GO:0003713];
transcription factor binding [GO:0008134];
tyrosine 3-monooxygenase activator activity [GO:0036470];
ubiquitin-like protein conjugating enzyme binding [GO:0044390];
ubiquitin-specific protease binding [GO:1990381]
Gene Ontology
(Cellular Component)
Complete annatation
axon [GO:0030424];
cell body [GO:0044297];
chromatin [GO:0000785];
cytoplasm [GO:0005737];
cytosol [GO:0005829];
endoplasmic reticulum [GO:0005783];
extracellular exosome [GO:0070062];
membrane raft [GO:0045121];
mitochondrial intermembrane space [GO:0005758];
mitochondrial matrix [GO:0005759];
mitochondrion [GO:0005739];
nucleus [GO:0005634];
plasma membrane [GO:0005886];
PML body [GO:0016605];
presynapse [GO:0098793]
Protein-protein interaction116446
Phylogenetic treeQ99497
HIV replication factor status Zhou et al., Cell. Host. Microbe., 2008
Brass et al., Science, 2008
Smith et al., J. Immunol, 2010
gene status
Lu et al., J. Virol., 2011
      Folds changes 8h: unknown; Folds changes 16h: unknown; Tested: unknown;
Schoggins JW and Rice CM, Curr. Opin. Virol., 2011
      Targeted viruses: unknown
      Viral life cycle: unknown
      Mechanism related to antiviral activity: unknown
Anti-viral restriction factor Liu et al., Retrovirology, 2011
      unknown (Triplicates)

Gene Expression Profile       top

            Up-regulated;            Down-regulated

For brief introduction to each study, please go to the help page.

Gene expression during HIV latency

(1). Mohammadi et al., PLoS Pathog., 2014

Differentially expressed transcripts (Pairwise) during latency and subsequent viral reactivation using several agents - Primary CD4+ T-cell based model

DMSO: Dimethyl suloxyde (negative control) - 0.0033% final
SAHA: Vorinostat (Histone deacetylase inhibitor) - 0.5 μM
CD3: TCR Stimulation by IL-2+ antiCD3/anti-CD28 antibodies
IL7: Interleukin-7 based stimulation
DISU: Disulfiram (alcohol dehydrogenase inhibitor) - 0.5 μM
AZA: 5-azacytidine (AZA; DNA methylation inhibitor) - 1 μM
Experimental Condition Log2 Fold Change P value Adjusted P value
AZA vs. CD31.709841178559583.61174810392662e-073.07723388481526e-06
AZA vs. DISU-0.2627424554734450.3000313051555470.86128089010194
AZA vs. IL70.2260451679566150.239387096186910.991191558227577
AZA vs. SAHA-0.2520196942919640.3015081626701220.673514629574603
DISU vs. CD3-1.985358745589911.35146573376765e-071.60662416962252e-06
DISU vs. IL70.479498589136180.05766593791188180.316459415370083
DISU vs. SAHA0.01259930310511270.9655322003525770.992637214624418
DMSO vs. AZA-0.01014679976674150.9516588751349511
DMSO vs. CD3-1.730826064652671.35755948482696e-071.16268525519717e-06
DMSO vs. DISU0.2508386303184950.3048847037518470.811498856723186
DMSO vs. IL70.2432966492596630.1757519070988760.68633407932787
DMSO vs. SAHA-0.2485436575566730.2916626280910830.643202731630189
HIV vs. Mock in Activation-0.1852784736984940.7657666273336160.999983755607037
HIV vs. Mock in Latency-0.08109980220673930.6235070323677560.999834320637052
IL7 vs. CD3-1.476311785595036.56226765771706e-065.31504892019179e-05
SAHA vs. CD3-1.985922958075925.74996223967617e-086.42028305206408e-07
SAHA vs. IL7-0.4807683294343880.04861365945338150.180438633132831
(2). Iglesias-Ussel et al., J. Virol., 2013

Up and Downregulated transcripts during Latency (Latently infected CD4+ T cells vs Uninfected)- Primary CD4+Tcell based model
Log2 Fold Change P Value
unknown unknown

Gene expression during HIV infection and replication

(1). Imbeault et al., PloS Pathog., 2012

Transcriptomic profiling of HIV-1 infected CD4+ T cells - Primary CD4+ T cells
Experiment type Log2 Fold Change P Value Adjusted P Value
Infected vs. Mock unknown unknown unknown
Infected vs. Bystander unknown unknown unknown
(2). Lefebvre et al., J. Virol., 2011

Transcriptome analysis of T-cell line (Sup T1)
Log2 Fold Change unknown
(3). Li et al., J. Immunol., 2013

Lymphatic tissue
Acute Fold Change Acute P Value Asymt Fold Change Asypt P Value AIDS Fold Change AIDS P Value
unknown unknown unknown unknown unknown unknown
(4). Chang et al., MBio., 2011

Transcriptome analysis of T-cell line (Sup T1)

Derived from Sherrill-Mix et al., BMC Retrovirol., 2015 cross validation
Up-regulated (True) FALSE
(5). Sherrill-Mix et al., BMC Retrovirol., 2015

Deep RNA-seq analysis of primary human T cell infected with low passage HIV isolate HIV89.6 - Primary CD4+ T cell based
Test Status Log2 Fold Change P Value
OK -0.0936191 0.563308
(6). Rotger et al., PLoS Pathog., 2010

Genome-wide mRNA expression of CD4+ T cells from HIV-infected patient
(Genes differentially expressed (at adjusted p<0.01) according to the empirical Bayes approach)
Log2 Fold Change P Value
unknown unknown

Proteomic/Transcriptomics studies indicating differentially expressed genes mediated by HIV

(1). Greenwood et al., Elife, 2016

Activated (CD3/CD28) Primary human CD4+ T cells infected with pNL4-3-dE-EGFP. The table shows the complete (unfiltered) TMT (tandem mass tag)-based proteomic time course dataset
6 h 24 h 48 h 72 h RTi
1.045 0.993 1.112 1.217 1.047
(2). Navare et al., Virology, 2012

SUP-T1 cell line
FC-4hpi P-value FC-8hpi P-value FC-20hpi P-value Category
unknown unknown unknown unknown unknown unknown unknown
(3). Hyrcza et al., J. Virolo., 2007

Primary human CD4+ and CD8+ T Cells
Affymetrix Prob ID Fold Change In CD8? Category
unknown unknown unknown unknown

Protein Overview       top

Drug-protein Interaction       (annotations from DrugBank)      top

not found

Protein Secondary Structure       (annotations from PDB)      top

PDB Accession Method Resolution Chain Structure Preview
1J42 X-ray 2.5Å A=1-189.
1P5F X-ray 1.1Å A=1-189.
1PDV X-ray 1.8Å A=1-189.
1PDW X-ray 2.2Å A/B/C/D/E/F/G/H=1-189.
1PE0 X-ray 1.7Å A/B=1-189.
1Q2U X-ray 1.6Å A=1-189.
1SOA X-ray 1.2Å A=1-189.
1UCF X-ray 1.9Å A/B=1-189.
2OR3 X-ray 1.2Å A/B=1-189.
2R1T X-ray 1.7Å A/B=2-188.
2R1U X-ray 1.5Å A/B=2-188.
2R1V X-ray 1.7Å A/B=2-188.
2RK3 X-ray 1.0Å A=1-189.
2RK4 X-ray 1.1Å A=1-189.
2RK6 X-ray 1.1Å A=1-189.
3B36 X-ray 1.5Å A=1-189.
3B38 X-ray 1.8Å A=1-189.
3B3A X-ray 1.5Å A=1-189.
3BWE X-ray 2.4Å A/B/C/D/E/F/G=1-189.
3CY6 X-ray 1.3Å A=1-189.
3CYF X-ray 1.6Å A=1-189.
3CZ9 X-ray 1.1Å A=1-189.
3CZA X-ray 1.2Å A=1-189.
3EZG X-ray 1.1Å A=1-189.
3F71 X-ray 1.2Å A=1-189.
3SF8 X-ray 1.5Å A/B=1-189.
4BTE X-ray 1.3Å A=1-189.
4MNT X-ray 1.5Å A=1-189.
4MTC X-ray 1.4Å A=1-189.
4N0M X-ray 1.9Å A=1-189.
4N12 X-ray 1.4Å A=1-189.
4OGF X-ray 1.6Å A=2-188.
4OQ4 X-ray 1.4Å A=1-189.
4P2G X-ray 1.3Å A=1-189.
4P34 X-ray 1.5Å A=1-189.
4P35 X-ray 1.7Å A=1-189.
4P36 X-ray 1.1Å A=1-189.
4RKW X-ray 1.5Å A=1-189.
4RKY X-ray 1.5Å A=1-189.
4S0Z X-ray 1.4Å A=1-189.
4ZGG X-ray 1.2Å A=1-189.

HIV-1 Interaction       (annotations from NCBI HIV-1 Interaction Database)      top

HIV Partner Interaction Type PubMed
Tat upregulates 23364796

Metabolic/Signalling Pathway       (annotations from KEGG database)      top

Pathway Accession Number Description
hsa05012 Parkinson's disease - Homo sapiens (human)