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Protein/nucleic acid deglycase DJ-1 (EC 3.1.2.-) (EC 3.5.1.-) (EC (Contraception-associated protein 1) (Protein CAP1) (Fertility protein SP22) (Maillard deglycase) (Parkinson disease protein 7 homolog) (Parkinsonism-associated deglycase) (Protein DJ-1) (DJ-1)

 PARK7_RAT               Reviewed;         189 AA.
07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
07-NOV-2018, entry version 138.
RecName: Full=Protein/nucleic acid deglycase DJ-1 {ECO:0000250|UniProtKB:Q99497};
EC=3.1.2.- {ECO:0000250|UniProtKB:Q99497};
EC=3.5.1.- {ECO:0000250|UniProtKB:Q99497};
EC= {ECO:0000250|UniProtKB:Q99497};
AltName: Full=Contraception-associated protein 1 {ECO:0000303|PubMed:9792810};
Short=Protein CAP1;
AltName: Full=Fertility protein SP22 {ECO:0000303|PubMed:9733139};
AltName: Full=Maillard deglycase {ECO:0000250|UniProtKB:Q99497};
AltName: Full=Parkinson disease protein 7 homolog {ECO:0000305};
AltName: Full=Parkinsonism-associated deglycase {ECO:0000250|UniProtKB:Q99497};
AltName: Full=Protein DJ-1 {ECO:0000250|UniProtKB:Q99497};
Flags: Precursor;
Name=Park7 {ECO:0000312|RGD:621808}; Synonyms=Cap1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
PubMed=9792810; DOI=10.1006/bbrc.1998.9512;
Wagenfeld A., Gromoll J., Cooper T.G.;
"Molecular cloning and expression of rat contraception associated
protein 1 (CAP1), a protein putatively involved in fertilization.";
Biochem. Biophys. Res. Commun. 251:545-549(1998).
STRAIN=Sprague-Dawley; TISSUE=Testis;
Welch J.E., Barbee R.R., Roberts N.L., Suarez J.D., Klinefelter G.R.;
"SP22: a novel fertility protein from a highly conserved gene
J. Androl. 19:385-393(1998).
STRAIN=Sprague-Dawley; TISSUE=Testis;
Welch J.E., Barbee R.R., Roberts N.L., Suarez J.D., Klinefelter G.R.;
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
Hod Y., Pentyala S.N., Whyard T.C., El-Maghrabi M.R.;
"Identification and characterization of a novel protein that regulates
RNA-protein interaction.";
J. Cell. Biochem. 72:435-444(1999).
PROTEIN SEQUENCE OF 33-48; 63-89; 100-122; 133-145 AND 157-175, AND
STRAIN=Sprague-Dawley; TISSUE=Brain, Hippocampus, and Spinal cord;
Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.;
Submitted (JUL-2007) to UniProtKB.
PubMed=23847046; DOI=10.1093/hmg/ddt332;
Kim K.S., Kim J.S., Park J.Y., Suh Y.H., Jou I., Joe E.H., Park S.M.;
"DJ-1 associates with lipid rafts by palmitoylation and regulates
lipid rafts-dependent endocytosis in astrocytes.";
Hum. Mol. Genet. 22:4805-4817(2013).
-!- FUNCTION: 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 (By similarity). 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 (By similarity). 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 (By similarity). In macrophages,
interacts with the NADPH oxidase subunit NCF1 to direct NADPH
oxidase-dependent ROS production, and protects against sepsis (By
similarity). {ECO:0000250|UniProtKB:Q99497,
-!- CATALYTIC ACTIVITY: An N(omega)-(1-hydroxy-2-oxopropyl)-[protein]-
L-arginine + H(2)O = a [protein]-L-arginine + lactate.
-!- CATALYTIC ACTIVITY: An N(6)-(1-hydroxy-2-oxopropyl)-[protein]-L-
lysine + H(2)O = a [protein]-L-lysine + lactate.
-!- CATALYTIC ACTIVITY: An S-(1-hydroxy-2-oxopropyl)-[protein]-L-
cysteine + H(2)O = a [protein]-L-cysteine + lactate.
-!- CATALYTIC ACTIVITY: An N(omega)-(1-hydroxy-2-oxoethyl)-[protein]-
L-arginine + H(2)O = a [protein]-L-arginine + glycolate.
-!- CATALYTIC ACTIVITY: An N(6)-(1-hydroxy-2-oxoethyl)-[protein]-L-
lysine + H(2)O = a [protein]-L-lysine + glycolate.
-!- CATALYTIC ACTIVITY: An S-(1-hydroxy-2-oxoethyl)-[protein]-L-
cysteine + H(2)O = a [protein]-L-cysteine + glycolate.
-!- CATALYTIC ACTIVITY: N(2)-(1-hydroxy-2-oxopropyl)-dGTP + H(2)O =
dGTP + lactate. {ECO:0000250|UniProtKB:Q99497}.
-!- CATALYTIC ACTIVITY: N(2)-(1-hydroxy-2-oxopropyl)-GTP + H(2)O = GTP
+ lactate. {ECO:0000250|UniProtKB:Q99497}.
-!- CATALYTIC ACTIVITY: N(2)-(1-hydroxy-2-oxopropyl)-GDP + H(2)O = GDP
+ lactate. {ECO:0000250|UniProtKB:Q99497}.
-!- CATALYTIC ACTIVITY: N(2)-(1-hydroxy-2-oxopropyl)-GMP + H(2)O = GMP
+ lactate. {ECO:0000250|UniProtKB:Q99497}.
-!- CATALYTIC ACTIVITY: N(2)-(1-hydroxy-2-oxoethyl)-dGTP + H(2)O =
dGTP + glycolate. {ECO:0000250|UniProtKB:Q99497}.
-!- CATALYTIC ACTIVITY: N(2)-(1-hydroxy-2-oxoethyl)-GTP + H(2)O = GTP
+ glycolate. {ECO:0000250|UniProtKB:Q99497}.
-!- CATALYTIC ACTIVITY: N(2)-(1-hydroxy-2-oxoethyl)-GDP + H(2)O = GDP
+ glycolate. {ECO:0000250|UniProtKB:Q99497}.
-!- CATALYTIC ACTIVITY: N(2)-(1-hydroxy-2-oxoethyl)-GMP + H(2)O = GMP
+ glycolate. {ECO:0000250|UniProtKB:Q99497}.
-!- CATALYTIC ACTIVITY: An N(2)-(1-hydroxy-2-oxopropyl)-guanosine in
RNA + H(2)O = a guanosine in RNA + lactate.
-!- CATALYTIC ACTIVITY: An N(2)-(1-hydroxy-2-oxopropyl)-2'-
deoxyguanosine in DNA + H(2)O = a 2'-deoxyguanosine in RNA +
lactate. {ECO:0000250|UniProtKB:Q99497}.
-!- CATALYTIC ACTIVITY: An N(2)-(1-hydroxy-2-oxoethyl)-guanosine in
RNA + H(2)O = a guanosine in RNA + glycolate.
-!- CATALYTIC ACTIVITY: An N(2)-(1-hydroxy-2-oxoethyl)-2'-
deoxyguanosine in DNA + H(2)O = a 2'-deoxyguanosine in RNA +
glycolate. {ECO:0000250|UniProtKB:Q99497}.
Note=Deglycase activity does not require glutathione as a
cofactor, however, glycated glutathione constitutes a PARK7
substrate. {ECO:0000250|UniProtKB:Q99497};
-!- SUBUNIT: Homodimer. Binds EFCAB6/DJBP and PIAS2. Part of a ternary
complex containing PARK7, EFCAB6/DJBP and AR. Interacts (via N-
terminus) with OTUD7B. Interacts with BBS1, HIPK1, CLCF1 and
MTERF. Forms a complex with PINK1 and PRKN (By similarity).
Interacts (via C-terminus) with NCF1; the interaction is enhanced
by LPS and modulates NCF1 phosphorylation and membrane
translocation (By similarity). {ECO:0000250|UniProtKB:Q99497,
{ECO:0000250|UniProtKB:Q99LX0}; Lipid-anchor
{ECO:0000250|UniProtKB:Q99LX0}. Cytoplasm
{ECO:0000269|PubMed:10022524}. Membrane raft
{ECO:0000269|PubMed:23847046}. Nucleus
{ECO:0000269|PubMed:10022524}. Mitochondrion
{ECO:0000250|UniProtKB:Q99497}. 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 (By similarity). Membrane raft localization in astrocytes
and neuronal cells requires palmitoylation (PubMed:23847046).
{ECO:0000250|UniProtKB:Q99497, ECO:0000269|PubMed:23847046}.
-!- TISSUE SPECIFICITY: Ubiquitous. Detected on epididymal sperm.
Highly expressed in testis and prostate. Detected at lower levels
in heart, lung, brain, liver, kidney, seminal vesicle, caput and
corpus epididymis. {ECO:0000269|PubMed:9792810}.
-!- PTM: Sumoylated on Lys-130 by PIAS2 or PIAS4; which is essential
for cell-growth promoting activity and transforming activity.
-!- PTM: Undergoes cleavage of a C-terminal peptide and subsequent
activation of protease activity in response to oxidative stress.
-!- SIMILARITY: Belongs to the peptidase C56 family. {ECO:0000305}.
-!- CAUTION: Glyoxylase activity previously reported may reflect in
fact its deglycase activity. {ECO:0000250|UniProtKB:Q99497}.
-!- CAUTION: The protein deglycation activity has been ascribed to a
TRIS buffer artifact by a publication, which has then been
rebutted by clear biochemical experiments showing that PARK7 is a
bona fide deglycase. Deglycase activity is even strengthened by a
novel article that reports nucleotide deglycation activity.
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
EMBL; AJ007291; CAA07434.1; -; mRNA.
EMBL; AF157511; AAD43956.1; -; mRNA.
EMBL; AF157512; AAD43957.1; -; mRNA.
PIR; JE0344; JE0344.
RefSeq; NP_001264179.1; NM_001277250.1.
RefSeq; NP_001264180.1; NM_001277251.1.
RefSeq; NP_001264181.1; NM_001277252.1.
RefSeq; NP_001264182.1; NM_001277253.1.
RefSeq; NP_476484.1; NM_057143.2.
UniGene; Rn.30105; -.
ProteinModelPortal; O88767; -.
SMR; O88767; -.
BioGrid; 250731; 76.
IntAct; O88767; 1.
STRING; 10116.ENSRNOP00000024711; -.
MEROPS; C56.002; -.
iPTMnet; O88767; -.
PhosphoSitePlus; O88767; -.
World-2DPAGE; 0004:O88767; -.
PaxDb; O88767; -.
PRIDE; O88767; -.
Ensembl; ENSRNOT00000024711; ENSRNOP00000024711; ENSRNOG00000018289.
Ensembl; ENSRNOT00000087402; ENSRNOP00000072068; ENSRNOG00000018289.
GeneID; 117287; -.
KEGG; rno:117287; -.
UCSC; RGD:621808; rat.
CTD; 11315; -.
RGD; 621808; Park7.
eggNOG; KOG2764; Eukaryota.
eggNOG; COG0693; LUCA.
GeneTree; ENSGT00390000001231; -.
HOGENOM; HOG000063194; -.
HOVERGEN; HBG053511; -.
InParanoid; O88767; -.
KO; K05687; -.
Reactome; R-RNO-3899300; SUMOylation of transcription cofactors.
PRO; PR:O88767; -.
Proteomes; UP000002494; Chromosome 5.
Bgee; ENSRNOG00000018289; Expressed in 10 organ(s), highest expression level in skeletal muscle tissue.
ExpressionAtlas; O88767; baseline and differential.
Genevisible; O88767; RN.
GO; GO:0030424; C:axon; IDA:RGD.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0070062; C:extracellular exosome; ISS:ParkinsonsUK-UCL.
GO; GO:0045121; C:membrane raft; IDA:RGD.
GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016605; C:PML body; ISS:ParkinsonsUK-UCL.
GO; GO:0061827; C:sperm head; IDA:RGD.
GO; GO:0050681; F:androgen receptor binding; ISS:ParkinsonsUK-UCL.
GO; GO:0005507; F:copper ion binding; ISS:UniProtKB.
GO; GO:1903135; F:cupric ion binding; ISS:ParkinsonsUK-UCL.
GO; GO:1903136; F:cuprous ion binding; ISS:ParkinsonsUK-UCL.
GO; GO:0019955; F:cytokine binding; ISS:ParkinsonsUK-UCL.
GO; GO:0036478; F:L-dopa decarboxylase activator activity; ISS:ParkinsonsUK-UCL.
GO; GO:0045340; F:mercury ion binding; ISS:UniProtKB.
GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
GO; GO:0008233; F:peptidase activity; ISS:UniProtKB.
GO; GO:0036524; F:protein deglycase activity; IBA:GO_Central.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0070491; F:repressing transcription factor binding; ISS:ParkinsonsUK-UCL.
GO; GO:0097110; F:scaffold protein binding; ISS:ParkinsonsUK-UCL.
GO; GO:0005102; F:signaling receptor binding; ISS:ParkinsonsUK-UCL.
GO; GO:0044388; F:small protein activating enzyme binding; ISS:ParkinsonsUK-UCL.
GO; GO:0016532; F:superoxide dismutase copper chaperone activity; ISS:ParkinsonsUK-UCL.
GO; GO:0003713; F:transcription coactivator activity; ISS:ParkinsonsUK-UCL.
GO; GO:0008134; F:transcription factor binding; ISS:ParkinsonsUK-UCL.
GO; GO:0036470; F:tyrosine 3-monooxygenase activator activity; ISS:ParkinsonsUK-UCL.
GO; GO:0044390; F:ubiquitin-like protein conjugating enzyme binding; ISS:ParkinsonsUK-UCL.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
GO; GO:0036471; P:cellular response to glyoxal; ISS:ParkinsonsUK-UCL.
GO; GO:0070301; P:cellular response to hydrogen peroxide; ISS:UniProtKB.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEP:RGD.
GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
GO; GO:0010273; P:detoxification of copper ion; ISS:UniProtKB.
GO; GO:0050787; P:detoxification of mercury ion; ISS:UniProtKB.
GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
GO; GO:0009566; P:fertilization; TAS:ParkinsonsUK-UCL.
GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
GO; GO:0046295; P:glycolate biosynthetic process; ISS:ParkinsonsUK-UCL.
GO; GO:0106044; P:guanine deglycation; ISS:UniProtKB.
GO; GO:0106046; P:guanine deglycation, glyoxal removal; ISS:UniProtKB.
GO; GO:0106045; P:guanine deglycation, methylglyoxal removal; ISS:UniProtKB.
GO; GO:0042743; P:hydrogen peroxide metabolic process; ISS:ParkinsonsUK-UCL.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0030073; P:insulin secretion; ISS:UniProtKB.
GO; GO:0060135; P:maternal process involved in female pregnancy; IEP:RGD.
GO; GO:0007005; P:mitochondrion organization; ISS:UniProtKB.
GO; GO:0060548; P:negative regulation of cell death; ISS:UniProtKB.
GO; GO:2001268; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; ISS:ParkinsonsUK-UCL.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISS:ParkinsonsUK-UCL.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISS:ParkinsonsUK-UCL.
GO; GO:1901215; P:negative regulation of neuron death; IMP:RGD.
GO; GO:1904782; P:negative regulation of NMDA glutamate receptor activity; IMP:RGD.
GO; GO:1903377; P:negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; ISS:ParkinsonsUK-UCL.
GO; GO:1901984; P:negative regulation of protein acetylation; ISS:ParkinsonsUK-UCL.
GO; GO:0032091; P:negative regulation of protein binding; ISS:UniProtKB.
GO; GO:0046826; P:negative regulation of protein export from nucleus; ISS:ParkinsonsUK-UCL.
GO; GO:1903094; P:negative regulation of protein K48-linked deubiquitination; ISS:ParkinsonsUK-UCL.
GO; GO:0006469; P:negative regulation of protein kinase activity; ISS:ParkinsonsUK-UCL.
GO; GO:0001933; P:negative regulation of protein phosphorylation; ISS:ParkinsonsUK-UCL.
GO; GO:0033234; P:negative regulation of protein sumoylation; ISS:ParkinsonsUK-UCL.
GO; GO:0031397; P:negative regulation of protein ubiquitination; ISS:ParkinsonsUK-UCL.
GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; ISS:UniProtKB.
GO; GO:1903122; P:negative regulation of TRAIL-activated apoptotic signaling pathway; ISS:ParkinsonsUK-UCL.
GO; GO:2000157; P:negative regulation of ubiquitin-specific protease activity; ISS:ParkinsonsUK-UCL.
GO; GO:0002866; P:positive regulation of acute inflammatory response to antigenic stimulus; ISS:UniProtKB.
GO; GO:2000825; P:positive regulation of androgen receptor activity; ISS:ParkinsonsUK-UCL.
GO; GO:1903181; P:positive regulation of dopamine biosynthetic process; ISS:ParkinsonsUK-UCL.
GO; GO:1905516; P:positive regulation of fertilization; IMP:RGD.
GO; GO:0032757; P:positive regulation of interleukin-8 production; ISS:ParkinsonsUK-UCL.
GO; GO:1903197; P:positive regulation of L-dopa biosynthetic process; ISS:ParkinsonsUK-UCL.
GO; GO:1903200; P:positive regulation of L-dopa decarboxylase activity; ISS:ParkinsonsUK-UCL.
GO; GO:1902958; P:positive regulation of mitochondrial electron transport, NADH to ubiquinone; ISS:ParkinsonsUK-UCL.
GO; GO:0033864; P:positive regulation of NAD(P)H oxidase activity; ISS:UniProtKB.
GO; GO:2000277; P:positive regulation of oxidative phosphorylation uncoupler activity; ISS:UniProtKB.
GO; GO:0090073; P:positive regulation of protein homodimerization activity; ISS:ParkinsonsUK-UCL.
GO; GO:1900182; P:positive regulation of protein localization to nucleus; ISS:ParkinsonsUK-UCL.
GO; GO:1903168; P:positive regulation of pyrroline-5-carboxylate reductase activity; ISS:ParkinsonsUK-UCL.
GO; GO:1901671; P:positive regulation of superoxide dismutase activity; ISS:ParkinsonsUK-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:ParkinsonsUK-UCL.
GO; GO:1903178; P:positive regulation of tyrosine 3-monooxygenase activity; ISS:ParkinsonsUK-UCL.
GO; GO:0036529; P:protein deglycation, glyoxal removal; IBA:GO_Central.
GO; GO:0006517; P:protein deglycosylation; ISS:UniProtKB.
GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
GO; GO:0060765; P:regulation of androgen receptor signaling pathway; ISS:ParkinsonsUK-UCL.
GO; GO:0050727; P:regulation of inflammatory response; ISS:UniProtKB.
GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISS:ParkinsonsUK-UCL.
GO; GO:0043523; P:regulation of neuron apoptotic process; ISS:UniProtKB.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0006979; P:response to oxidative stress; IMP:RGD.
GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
GO; GO:0007283; P:spermatogenesis; IEP:RGD.
Gene3D;; -; 1.
InterPro; IPR029062; Class_I_gatase-like.
InterPro; IPR006287; DJ-1.
InterPro; IPR002818; DJ-1/PfpI.
Pfam; PF01965; DJ-1_PfpI; 1.
SUPFAM; SSF52317; SSF52317; 1.
TIGRFAMs; TIGR01383; not_thiJ; 1.
1: Evidence at protein level;
Acetylation; Autophagy; Cell membrane; Chaperone; Complete proteome;
Copper; Cytoplasm; Direct protein sequencing; Fertilization;
Hydrolase; Inflammatory response; Isopeptide bond; Lipoprotein;
Membrane; Mitochondrion; Nucleus; Oxidation; Palmitate;
Phosphoprotein; Protease; Reference proteome; RNA-binding;
Stress response; Tumor suppressor; Ubl conjugation; Zymogen.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q99497}.
CHAIN 2 ? Protein/nucleic acid deglycase DJ-1.
PROPEP ? 189 Removed in mature form.
ACT_SITE 106 106 Nucleophile.
ACT_SITE 126 126 {ECO:0000250|UniProtKB:Q99497}.
MOD_RES 2 2 N-acetylalanine.
MOD_RES 67 67 Phosphotyrosine.
MOD_RES 106 106 Cysteine sulfinic acid (-SO2H);
MOD_RES 148 148 N6-acetyllysine.
MOD_RES 182 182 N6-succinyllysine.
LIPID 46 46 S-palmitoyl cysteine.
LIPID 53 53 S-palmitoyl cysteine.
LIPID 106 106 S-palmitoyl cysteine; alternate.
CROSSLNK 130 130 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
SEQUENCE 189 AA; 19974 MW; 08AC2C37D62A9455 CRC64;

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EIAAB45359 hGMH1,Homo sapiens,HSD23,HSD-23,Human,PDLs22,Periodontal ligament-specific protein 22,Protein GMH1 homolog,Protein unc-50 homolog,UNC50,UNCL,Uncoordinated-like protein
27-226 APBA3 is a member of the X11 protein family. It is an adapter protein that interacts with the Alzheimer's disease amyloid precursor protein. This protein is believed to be involved in signal transduct 0.05 mg
EIAAB39415 Fertility-related protein WMP1,Rat,Rat sperm DNA no.3,Rattus norvegicus,Rsd3,RSD-3,Spata7,Spermatogenesis-associated protein 7 homolog
EIAAB46018 C6orf55,Dopamine-responsive gene 1 protein,DRG-1,Homo sapiens,HSPC228,Human,LIP5,LYST-interacting protein 5,My012,SBP1,SKD1-binding protein 1,Vacuolar protein sorting-associated protein VTA1 homolog,V
25-230 CNBP is a nucleic-acid binding protein with seven zinc-finger domains. The protein has a preference for binding single stranded DNA and RNA. The protein functions in cap-independent translation of orn 0.05 mg
EIAAB38179 DSHP,Duncan disease SH2-protein,Homo sapiens,Human,SAP,SH2 domain-containing protein 1A,SH2D1A,Signaling lymphocytic activation molecule-associated protein,SLAM-associated protein,T-cell signal transd
EIAAB40620 ChET 9 protein,CHET9,Chromatin precipitated E2F target 9 protein,Homo sapiens,Human,JJAZ1,Joined to JAZF1 protein,KIAA0160,Polycomb protein SUZ12,Suppressor of zeste 12 protein homolog,SUZ12
EIAAB11408 Dlk2,DLK-2,Egfl9,EGF-like protein 9,Endothelial cell-specific protein S-1,Epidermal growth factor-like protein 9,Protein delta homolog 2,Rat,Rattus norvegicus
EIAAB11411 Dlk2,DLK-2,Egfl9,EGF-like protein 9,Endothelial cell-specific protein S-1,Epidermal growth factor-like protein 9,Mouse,Mus musculus,Protein delta homolog 2
EIAAB46376 C1orf139,EVI,GPR177,Homo sapiens,Human,Integral membrane protein GPR177,Protein evenness interrupted homolog,Protein wntless homolog,Putative NF-kappa-B-activating protein 373,UNQ85_PRO18667,WLS
orb81255 Human Parkinson Disease Protein 7 protein PARK7 Human Recombinant fused to N-terminal His-Tag produced in E.coli is a single, non-glycosylated polypeptide chain containing 225 amino acids and having a 5
EIAAB39347 Mouse,Mus musculus,Spata24,Spermatogenesis-associated protein 24,TATA-binding protein-like factor-interacting protein,Testis protein T6441 homolog,Tipt,Tipt2,TLF-interacting protein,TRF2-interacting p


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