Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

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

 PARK7_CHICK             Reviewed;         189 AA.
17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
10-OCT-2018, entry version 89.
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=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:0000250|UniProtKB:Q99497};
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
PubMed=15976810; DOI=10.1038/sj.cdd.4401704;
Shinbo Y., Niki T., Taira T., Ooe H., Takahashi-Niki K., Maita C.,
Seino C., Iguchi-Ariga S.M.M., Ariga H.;
"Proper SUMO-1 conjugation is essential to DJ-1 to exert its full
Cell Death Differ. 13:96-108(2006).
-!- 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. It is involved in neuroprotective
mechanisms as well as cell growth and transformation. Its
involvement in protein repair could also explain other unrelated
functions. 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. Regulates astrocyte inflammatory
responses, may modulate lipid rafts-dependent endocytosis in
astrocytes and neuronal cells. 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).
{ECO:0000250|UniProtKB:Q99497, ECO:0000250|UniProtKB:Q99LX0}.
-!- 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. {ECO:0000250|UniProtKB:Q99497}.
{ECO:0000250|UniProtKB:O88767}; Lipid-anchor
{ECO:0000250|UniProtKB:O88767}. Cytoplasm
{ECO:0000250|UniProtKB:Q99497}. Nucleus
{ECO:0000250|UniProtKB:Q99497}. Membrane raft
{ECO:0000250|UniProtKB:O88767}. Mitochondrion
-!- PTM: Sumoylated on Lys-130; 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; AB076264; BAB79527.1; -; mRNA.
RefSeq; NP_989916.1; NM_204585.1.
UniGene; Gga.3836; -.
ProteinModelPortal; Q8UW59; -.
SMR; Q8UW59; -.
BioGrid; 675570; 1.
STRING; 9031.ENSGALP00000000741; -.
MEROPS; C56.971; -.
PaxDb; Q8UW59; -.
PRIDE; Q8UW59; -.
GeneID; 395277; -.
KEGG; gga:395277; -.
CTD; 11315; -.
eggNOG; KOG2764; Eukaryota.
eggNOG; COG0693; LUCA.
HOGENOM; HOG000063194; -.
HOVERGEN; HBG053511; -.
InParanoid; Q8UW59; -.
KO; K05687; -.
PhylomeDB; Q8UW59; -.
PRO; PR:Q8UW59; -.
Proteomes; UP000000539; Unplaced.
GO; GO:0005737; C:cytoplasm; ISS:AgBase.
GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:AgBase.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0098793; C:presynapse; IEA:GOC.
GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
GO; GO:0008233; F:peptidase activity; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0008344; P:adult locomotory behavior; ISS:AgBase.
GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
GO; GO:0070301; P:cellular response to hydrogen peroxide; ISS:UniProtKB.
GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
GO; GO:0006281; P:DNA repair; ISS:UniProtKB.
GO; GO:0051583; P:dopamine uptake involved in synaptic transmission; ISS:AgBase.
GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
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:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0030073; P:insulin secretion; ISS:UniProtKB.
GO; GO:0060548; P:negative regulation of cell death; ISS:UniProtKB.
GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; ISS:UniProtKB.
GO; GO:0002866; P:positive regulation of acute inflammatory response to antigenic stimulus; ISS:UniProtKB.
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:0006517; P:protein deglycosylation; ISS:UniProtKB.
GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
GO; GO:0043523; P:regulation of neuron apoptotic process; ISS:UniProtKB.
GO; GO:0042542; P:response to hydrogen peroxide; ISS:AgBase.
GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
GO; GO:0001963; P:synaptic transmission, dopaminergic; ISS:AgBase.
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.
2: Evidence at transcript level;
Acetylation; Autophagy; Cell membrane; Chaperone; Complete proteome;
Copper; Cytoplasm; Fertilization; Hydrolase; Inflammatory response;
Isopeptide bond; Lipoprotein; Membrane; Mitochondrion; Nucleus;
Oxidation; Palmitate; Phosphoprotein; Protease; Reference proteome;
RNA-binding; Stress response; Tumor suppressor; Ubl conjugation;
CHAIN 1 ? 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 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; 19943 MW; A39FE229D97DB942 CRC64;

Related products :

Catalog number Product name Quantity
EIAAB32390 E3 ubiquitin-protein ligase parkin,Homo sapiens,Human,PARK2,Parkinson disease protein 2,Parkinson juvenile disease protein 2,PRKN
EIAAB29908 Cap1,Contraception-associated protein 1,Fertility protein SP22,Park7,Parkinson disease protein 7 homolog,Protein CAP1,Protein DJ-1,Rat,Rattus norvegicus
EIAAB29910 Mouse,Mus musculus,Park7,Parkinson disease protein 7 homolog,Protein DJ-1
EIAAB29909 Bos taurus,Bovine,PARK7,Parkinson disease protein 7 homolog,Protein DJ-1
EIAAB29911 Chicken,Gallus gallus,PARK7,Parkinson disease protein 7 homolog,Protein DJ-1
EIAAB29912 Homo sapiens,Human,Oncogene DJ1,PARK7,Parkinson disease protein 7,Protein DJ-1
orb81255 Human Parkinson Disease Protein 7 protein Proteins 5
E2138m ELISA kit 14 kDa submandibular gland protein,GCDFP-15,Gross cystic disease fluid protein 15,Mouse,Mus musculus,Pip,Prolactin-induced protein,Prolactin-inducible protein homolog,SMGP 96T
U2138m CLIA kit 14 kDa submandibular gland protein,GCDFP-15,Gross cystic disease fluid protein 15,Mouse,Mus musculus,Pip,Prolactin-induced protein,Prolactin-inducible protein homolog,SMGP 96T
U2138m CLIA 14 kDa submandibular gland protein,GCDFP-15,Gross cystic disease fluid protein 15,Mouse,Mus musculus,Pip,Prolactin-induced protein,Prolactin-inducible protein homolog,SMGP 96T
E2138m ELISA 14 kDa submandibular gland protein,GCDFP-15,Gross cystic disease fluid protein 15,Mouse,Mus musculus,Pip,Prolactin-induced protein,Prolactin-inducible protein homolog,SMGP 96T
RPR-575 Recombinant Human Parkinson Disease Protein 7 5
PRO-575 Recombinant Human Parkinson Disease Protein 7 5µg
PRO-575 Recombinant Human Parkinson Disease Protein 7 1mg
PRO-575 Recombinant Human Parkinson Disease Protein 7 20µg
pro-575 Recombinant Human Parkinson Disease Protein 7 20
pro-575 Recombinant Human Parkinson Disease Protein 7 1mg
pro-575 Recombinant Human Parkinson Disease Protein 7 5
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
7-05801 Recombinant Human Parkinson Disease Protein 7 20
228-11203-3 Recombinant Human Parkinson Disease Protein 7 1 mg
ant-317 Mouse Anti Human Parkinson Disease Protein 7 5
P1236035Par Total Protein _ Parkinson's Disease Brain 1 mg
228-11203-2 Recombinant Human Parkinson Disease Protein 7 20
CF59 Parkinson Juvenile Disease Protein 2 PARK2 500


GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur

Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur



9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017


france@gentaur.com | Gentaur

Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123

GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U

spain@gentaur.com | Gentaur

ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636

GENTAUR Poland Sp. z o.o.

ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556


Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur