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Protein DJ-1 (DJ-1) (Oncogene DJ1) (Parkinson disease protein 7) (Parkinsonism-associated deglycase) (Protein deglycase DJ-1) (EC 3.1.2.-) (EC 3.5.1.124)

 PARK7_HUMAN             Reviewed;         189 AA.
Q99497; B2R4Z1; O14805; Q6DR95; Q7LFU2;
07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 2.
25-OCT-2017, entry version 182.
RecName: Full=Protein/nucleic acid deglycase DJ-1 {ECO:0000305|PubMed:25416785, ECO:0000305|PubMed:28596309};
EC=3.1.2.- {ECO:0000269|PubMed:25416785};
EC=3.5.1.- {ECO:0000269|PubMed:28596309};
EC=3.5.1.124 {ECO:0000269|PubMed:25416785};
AltName: Full=Maillard deglycase {ECO:0000303|PubMed:28596309};
AltName: Full=Oncogene DJ1 {ECO:0000305};
AltName: Full=Parkinson disease protein 7 {ECO:0000305};
AltName: Full=Parkinsonism-associated deglycase {ECO:0000312|HGNC:HGNC:16369};
AltName: Full=Protein DJ-1 {ECO:0000305};
Short=DJ-1;
Flags: Precursor;
Name=PARK7 {ECO:0000312|HGNC:HGNC:16369};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
TISSUE=Cervix carcinoma;
PubMed=9070310; DOI=10.1006/bbrc.1997.6132;
Nagakubo D., Taita T., Kitaura H., Ikeda M., Tamai K.,
Iguchi-Ariga S.M.M., Ariga H.;
"DJ-1, a novel oncogene which transforms mouse NIH3T3 cells in
cooperation with ras.";
Biochem. Biophys. Res. Commun. 231:509-513(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lung;
Beaudoin R., Hod Y.;
"Homo sapiens RNA-binding protein regulatory subunit mRNA.";
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Ariga H., Niki T.;
"Human DJ-1 cDNA from PC3 cells.";
Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Thalamus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Cervix;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
TISSUE=Kidney;
PubMed=11223268; DOI=10.1016/S0378-1119(00)00590-4;
Taira T., Takahashi K., Kitagawa R., Iguchi-Ariga S.M.M., Ariga H.;
"Molecular cloning of human and mouse DJ-1 genes and identification of
Sp1-dependent activation of the human DJ-1 promoter.";
Gene 263:285-292(2001).
[9]
PROTEIN SEQUENCE OF 6-27; 33-89; 99-122 AND 149-175, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 138-189, AND VARIANT SER-150.
Zou H.Q., Chan P.;
"DJ-1 gene G150S mutation.";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[11]
INTERACTION WITH PIAS2, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=11477070; DOI=10.1074/jbc.M101730200;
Takahashi K., Taira T., Niki T., Seino C., Iguchi-Ariga S.M.M.,
Ariga H.;
"DJ-1 positively regulates the androgen receptor by impairing the
binding of PIASx alpha to the receptor.";
J. Biol. Chem. 276:37556-37563(2001).
[12]
DEGRADATION BY THE PROTEASOME, SUBCELLULAR LOCATION, INTERACTION WITH
PIAS2, HOMODIMERIZATION, MUTAGENESIS OF LYS-130, AND CHARACTERIZATION
OF VARIANT PARK7 PRO-166.
PubMed=12851414; DOI=10.1074/jbc.M304272200;
Miller D.W., Ahmad R., Hague S., Baptista M.J., Canet-Aviles R.,
McLendon C., Carter D.M., Zhu P.-P., Stadler J., Chandran J.,
Klinefelter G.R., Blackstone C., Cookson M.R.;
"L166P mutant DJ-1, causative for recessive Parkinson's disease, is
degraded through the ubiquitin-proteasome system.";
J. Biol. Chem. 278:36588-36595(2003).
[13]
DEGRADATION BY THE PROTEASOME, AND CHARACTERIZATION OF VARIANTS PARK7
ILE-26 AND PRO-166.
PubMed=14713311;
Moore D.J., Zhang L., Dawson T.M., Dawson V.L.;
"A missense mutation (L166P) in DJ-1, linked to familial Parkinson's
disease, confers reduced protein stability and impairs homo-
oligomerization.";
J. Neurochem. 87:1558-1567(2003).
[14]
FUNCTION, INTERACTION WITH EFCAB6, AND COMPONENT OF A COMPLEX COMPOSED
OF AR; EFCAB6 AND PARK7.
PubMed=12612053;
Niki T., Takahashi-Niki K., Taira T., Iguchi-Ariga S.M.M., Ariga H.;
"DJBP: a novel DJ-1-binding protein, negatively regulates the androgen
receptor by recruiting histone deacetylase complex, and DJ-1
antagonizes this inhibition by abrogation of this complex.";
Mol. Cancer Res. 1:247-261(2003).
[15]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=14579415; DOI=10.1002/mrd.10360;
Yoshida K., Sato Y., Yoshiike M., Nozawa S., Ariga H., Iwamoto T.;
"Immunocytochemical localization of DJ-1 in human male reproductive
tissue.";
Mol. Reprod. Dev. 66:391-397(2003).
[16]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=14705119; DOI=10.1002/ana.10782;
Rizzu P., Hinkle D.A., Zhukareva V., Bonifati V., Severijnen L.-A.,
Martinez D., Ravid R., Kamphorst W., Eberwine J.H., Lee V.M.-Y.,
Trojanowski J.Q., Heutink P.;
"DJ-1 colocalizes with tau inclusions: a link between parkinsonism and
dementia.";
Ann. Neurol. 55:113-118(2004).
[17]
TISSUE SPECIFICITY.
PubMed=14662519; DOI=10.1093/brain/awh054;
Bandopadhyay R., Kingsbury A.E., Cookson M.R., Reid A.R., Evans I.M.,
Hope A.D., Pittman A.M., Lashley T., Canet-Aviles R., Miller D.W.,
McLendon C., Strand C., Leonard A.J., Abou-Sleiman P.M., Healy D.G.,
Ariga H., Wood N.W., de Silva R., Revesz T., Hardy J.A., Lees A.J.;
"The expression of DJ-1 (PARK7) in normal human CNS and idiopathic
Parkinson's disease.";
Brain 127:420-430(2004).
[18]
FUNCTION, INDUCTION, AND MUTAGENESIS OF VAL-51 AND CYS-53.
PubMed=14749723; DOI=10.1038/sj.embor.7400074;
Taira T., Saito Y., Niki T., Iguchi-Ariga S.M., Takahashi K.,
Ariga H.;
"DJ-1 has a role in antioxidative stress to prevent cell death.";
EMBO Rep. 5:213-218(2004).
[19]
FUNCTION, AND MUTAGENESIS OF CYS-46; CYS-53 AND CYS-106.
PubMed=15502874; DOI=10.1371/journal.pbio.0020362;
Shendelman S., Jonason A., Martinat C., Leete T., Abeliovich A.;
"DJ-1 is a redox-dependent molecular chaperone that inhibits alpha-
synuclein aggregate formation.";
PLoS Biol. 2:1-10(2004).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-67, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[21]
SUMOYLATION AT LYS-130, OXIDATION, SUBCELLULAR LOCATION, INDUCTION,
AND FUNCTION.
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
activities.";
Cell Death Differ. 13:96-108(2006).
[22]
FUNCTION, INTERACTION WITH HIPK1, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF CYS-106.
PubMed=16390825; DOI=10.1080/10715760500456847;
Sekito A., Koide-Yoshida S., Niki T., Taira T., Iguchi-Ariga S.M.M.,
Ariga H.;
"DJ-1 interacts with HIPK1 and affects H2O2-induced cell death.";
Free Radic. Res. 40:155-165(2006).
[23]
FUNCTION.
PubMed=17015834; DOI=10.1073/pnas.0607260103;
Clements C.M., McNally R.S., Conti B.J., Mak T.W., Ting J.P.;
"DJ-1, a cancer- and Parkinson's disease-associated protein,
stabilizes the antioxidant transcriptional master regulator Nrf2.";
Proc. Natl. Acad. Sci. U.S.A. 103:15091-15096(2006).
[24]
FUNCTION.
PubMed=18626009; DOI=10.1073/pnas.0708518105;
van der Brug M.P., Blackinton J., Chandran J., Hao L.Y., Lal A.,
Mazan-Mamczarz K., Martindale J., Xie C., Ahmad R., Thomas K.J.,
Beilina A., Gibbs J.R., Ding J., Myers A.J., Zhan M., Cai H.,
Bonini N.M., Gorospe M., Cookson M.R.;
"RNA binding activity of the recessive parkinsonism protein DJ-1
supports involvement in multiple cellular pathways.";
Proc. Natl. Acad. Sci. U.S.A. 105:10244-10249(2008).
[25]
FUNCTION, COMPONENT OF A COMPLEX COMPOSED OF PRKN; PARK7 AND PINK1,
SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANT PARK7 PRO-166.
PubMed=19229105; DOI=10.1172/JCI37617;
Xiong H., Wang D., Chen L., Choo Y.S., Ma H., Tang C., Xia K.,
Jiang W., Ronai Z., Zhuang X., Zhang Z.;
"Parkin, PINK1, and DJ-1 form a ubiquitin E3 ligase complex promoting
unfolded protein degradation.";
J. Clin. Invest. 119:650-660(2009).
[26]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-46; CYS-53 AND
CYS-106.
PubMed=18711745; DOI=10.1002/jnr.21831;
Junn E., Jang W.H., Zhao X., Jeong B.S., Mouradian M.M.;
"Mitochondrial localization of DJ-1 leads to enhanced
neuroprotection.";
J. Neurosci. Res. 87:123-129(2009).
[27]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITES, AND MUTAGENESIS
OF CYS-106 AND HIS-126.
PubMed=20304780; DOI=10.1093/hmg/ddq113;
Chen J., Li L., Chin L.S.;
"Parkinson disease protein DJ-1 converts from a zymogen to a protease
by carboxyl-terminal cleavage.";
Hum. Mol. Genet. 19:2395-2408(2010).
[28]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[29]
FUNCTION, INTERACTION WITH BBS1; CLCF1; MTERF AND OTUD7B, AND
MUTAGENESIS OF CYS-106.
PubMed=21097510; DOI=10.1074/jbc.M110.147371;
McNally R.S., Davis B.K., Clements C.M., Accavitti-Loper M.A.,
Mak T.W., Ting J.P.;
"DJ-1 enhances cell survival through the binding of cezanne, a
negative regulator of NF-{kappa}B.";
J. Biol. Chem. 286:4098-4106(2011).
[30]
FUNCTION, CAUTION, MUTAGENESIS OF GLU-18; CYS-106 AND HIS-126, AND
CHARACTERIZATION OF VARIANT PARK7 PRO-166.
PubMed=22523093; DOI=10.1093/hmg/dds155;
Lee J.Y., Song J., Kwon K., Jang S., Kim C., Baek K., Kim J., Park C.;
"Human DJ-1 and its homologs are novel glyoxalases.";
Hum. Mol. Genet. 21:3215-3225(2012).
[31]
FUNCTION, DEVELOPMENTAL STAGE, INDUCTION BY HYPERGLYCEMIC CONDITIONS,
TISSUE SPECIFICITY, AND INVOLVEMENT IN DISEASE.
PubMed=22611253; DOI=10.1093/jmcb/mjs025;
Jain D., Jain R., Eberhard D., Eglinger J., Bugliani M., Piemonti L.,
Marchetti P., Lammert E.;
"Age- and diet-dependent requirement of DJ-1 for glucose homeostasis
in mice with implications for human type 2 diabetes.";
J. Mol. Cell Biol. 4:221-230(2012).
[32]
FUNCTION, PALMITOYLATION AT CYS-46; CYS-53 AND CYS-106, SUBCELLULAR
LOCATION, MUTAGENESIS OF CYS-46 AND CYS-106, AND CHARACTERIZATION OF
VARIANT PARK7 PRO-166.
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).
[33]
FUNCTION, COPPER-BINDING, CHARACTERIZATION OF VARIANTS PARK7 THR-104
AND ALA-149, AND MUTAGENESIS OF CYS-106.
PubMed=23792957; DOI=10.1074/jbc.M113.482091;
Bjorkblom B., Adilbayeva A., Maple-Grodem J., Piston D., Okvist M.,
Xu X.M., Brede C., Larsen J.P., Moller S.G.;
"Parkinson disease protein DJ-1 binds metals and protects against
metal-induced cytotoxicity.";
J. Biol. Chem. 288:22809-22820(2013).
[34]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[35]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, CAUTION,
MUTAGENESIS OF CYS-46; CYS-53 AND CYS-106, AND COFACTOR.
PubMed=25416785; DOI=10.1074/jbc.M114.597815;
Richarme G., Mihoub M., Dairou J., Bui L.C., Leger T., Lamouri A.;
"Parkinsonism-associated protein DJ-1/Park7 is a major protein
deglycase that repairs methylglyoxal- and glyoxal-glycated cysteine,
arginine and lysine residues.";
J. Biol. Chem. 290:1885-1897(2015).
[36]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[37]
CAUTION.
PubMed=27903648; DOI=10.1074/jbc.M116.743823;
Pfaff D.H., Fleming T., Nawroth P., Teleman A.A.;
"Evidence against a role for the Parkinsonism-associated protein DJ-1
in methylglyoxal detoxification.";
J. Biol. Chem. 292:685-690(2017).
[38]
FUNCTION, AND CAUTION.
PubMed=28013050; DOI=10.1016/j.bbrc.2016.12.134;
Richarme G., Dairou J.;
"Parkinsonism-associated protein DJ-1 is a bona fide deglycase.";
Biochem. Biophys. Res. Commun. 483:387-391(2017).
[39]
FUNCTION, AND INDUCTION BY SULFORAPHANE.
PubMed=26995087; DOI=10.1016/j.bbrc.2016.03.056;
Advedissian T., Deshayes F., Poirier F., Viguier M., Richarme G.;
"The Parkinsonism-associated protein DJ-1/Park7 prevents glycation
damage in human keratinocyte.";
Biochem. Biophys. Res. Commun. 473:87-91(2016).
[40]
FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-106, SUBCELLULAR
LOCATION, AND CAUTION.
PubMed=28596309; DOI=10.1126/science.aag1095;
Richarme G., Liu C., Mihoub M., Abdallah J., Leger T., Joly N.,
Liebart J.C., Jurkunas U.V., Nadal M., Bouloc P., Dairou J.,
Lamouri A.;
"Guanine glycation repair by DJ-1/Park7 and its bacterial homologs.";
Science 357:208-211(2017).
[41]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), AND HOMODIMERIZATION.
PubMed=12914946; DOI=10.1016/S0014-5793(03)00764-6;
Huai Q., Sun Y., Wang H., Chin L.-S., Li L., Robinson H., Ke H.;
"Crystal structure of DJ-1/RS and implication on familial Parkinson's
disease.";
FEBS Lett. 549:171-175(2003).
[42]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF WILD-TYPE AND MUTANT ARG-130,
AND HOMODIMERIZATION.
PubMed=12761214; DOI=10.1074/jbc.M304221200;
Tao X., Tong L.;
"Crystal structure of human DJ-1, a protein associated with early
onset Parkinson's disease.";
J. Biol. Chem. 278:31372-31379(2003).
[43]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS), AND HOMODIMERIZATION.
PubMed=12796482; DOI=10.1074/jbc.M305878200;
Honbou K., Suzuki N.N., Horiuchi M., Niki T., Taira T., Ariga H.,
Inagaki F.;
"The crystal structure of DJ-1, a protein related to male fertility
and Parkinson's disease.";
J. Biol. Chem. 278:31380-31384(2003).
[44]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, OXIDATION AT CYS-106,
AND HOMODIMERIZATION.
PubMed=12939276; DOI=10.1074/jbc.M304517200;
Lee S.-J., Kim S.J., Kim I.-K., Ko J., Jeong C.-S., Kim G.-H.,
Park C., Kang S.-O., Suh P.-G., Lee H.-S., Cha S.-S.;
"Crystal structures of human DJ-1 and Escherichia coli Hsp31, which
share an evolutionarily conserved domain.";
J. Biol. Chem. 278:44552-44559(2003).
[45]
X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS), HOMODIMERIZATION, OXIDATION,
AND LACK OF PROTEOLYTIC ACTIVITY.
PubMed=12855764; DOI=10.1073/pnas.1133288100;
Wilson M.A., Collins J.L., Hod Y., Ringe D., Petsko G.A.;
"The 1.1-A resolution crystal structure of DJ-1, the protein mutated
in autosomal recessive early onset Parkinson's disease.";
Proc. Natl. Acad. Sci. U.S.A. 100:9256-9261(2003).
[46]
X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS), MUTAGENESIS OF CYS-46; CYS-53
AND CYS-106, OXIDATION, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15181200; DOI=10.1073/pnas.0402959101;
Canet-Aviles R.M., Wilson M.A., Miller D.W., Ahmad R., McLendon C.,
Bandyopadhyay S., Baptista M.J., Ringe D., Petsko G.A., Cookson M.R.;
"The Parkinson's disease protein DJ-1 is neuroprotective due to
cysteine-sulfinic acid-driven mitochondrial localization.";
Proc. Natl. Acad. Sci. U.S.A. 101:9103-9108(2004).
[47]
VARIANTS PARK7 ILE-26 AND ALA-149, AND VARIANT GLN-98.
PubMed=12953260; DOI=10.1002/ana.10675;
Abou-Sleiman P.M., Healy D.G., Quinn N., Lees A.J., Wood N.W.;
"The role of pathogenic DJ-1 mutations in Parkinson's disease.";
Ann. Neurol. 54:283-286(2003).
[48]
VARIANT PARK7 PRO-166, AND SUBCELLULAR LOCATION.
PubMed=12446870; DOI=10.1126/science.1077209;
Bonifati V., Rizzu P., van Baren M.J., Schaap O., Breedveld G.J.,
Krieger E., Dekker M.C.J., Squitieri F., Ibanez P., Joosse M.,
van Dongen J.W., Vanacore N., van Swieten J.C., Brice A., Meco G.,
van Duijn C.M., Oostra B.A., Heutink P.;
"Mutations in the DJ-1 gene associated with autosomal recessive early-
onset Parkinsonism.";
Science 299:256-259(2003).
[49]
VARIANT GLN-98.
PubMed=14705128; DOI=10.1002/ana.10816;
Hedrich K., Schaefer N., Hering R., Hagenah J., Lanthaler A.J.,
Schwinger E., Kramer P.L., Ozelius L.J., Bressman S.B., Abbruzzese G.,
Martinelli P., Kostic V., Pramstaller P.P., Vieregge P., Riess O.,
Klein C.;
"The R98Q variation in DJ-1 represents a rare polymorphism.";
Ann. Neurol. 55:145-146(2004).
[50]
VARIANT PARK7 ASP-64, AND X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
PubMed=15365989; DOI=10.1002/humu.20089;
Hering R., Strauss K.M., Tao X., Bauer A., Woitalla D., Mietz E.M.,
Petrovic S., Bauer P., Schaible W., Mueller T., Schoels L., Klein C.,
Berg D., Meyer P.T., Schulz J.B., Wollnik B., Tong L., Krueger R.,
Riess O.;
"Novel homozygous p.E64D mutation in DJ1 in early onset Parkinson
disease (PARK7).";
Hum. Mutat. 24:321-329(2004).
[51]
CHARACTERIZATION OF VARIANTS PARK7 ASP-64 AND PRO-166.
PubMed=14607841; DOI=10.1074/jbc.M309204200;
Goerner K., Holtorf E., Odoy S., Nuscher B., Yamamoto A., Regula J.T.,
Beyer K., Haass C., Kahle P.J.;
"Differential effects of Parkinson's disease-associated mutations on
stability and folding of DJ-1.";
J. Biol. Chem. 279:6943-6951(2004).
[52]
VARIANT PARK7 THR-104, AND VARIANTS GLN-98 AND SER-171.
PubMed=15254937; DOI=10.1002/mds.20131;
Clark L.N., Afridi S., Mejia-Santana H., Harris J., Louis E.D.,
Cote L.J., Andrews H., Singleton A., Wavrant De-Vrieze F., Hardy J.,
Mayeux R., Fahn S., Waters C., Ford B., Frucht S., Ottman R.,
Marder K.;
"Analysis of an early-onset Parkinson's disease cohort for DJ-1
mutations.";
Mov. Disord. 19:796-800(2004).
[53]
VARIANT GLN-98.
PubMed=14872018; DOI=10.1212/01.WNL.0000113022.51739.88;
Hedrich K., Djarmati A., Schafer N., Hering R., Wellenbrock C.,
Weiss P.H., Hilker R., Vieregge P., Ozelius L.J., Heutink P.,
Bonifati V., Schwinger E., Lang A.E., Noth J., Bressman S.B.,
Pramstaller P.P., Riess O., Klein C.;
"DJ-1 (PARK7) mutations are less frequent than Parkin (PARK2)
mutations in early-onset Parkinson disease.";
Neurology 62:389-394(2004).
[54]
VARIANT LYS-163.
PubMed=16240358; DOI=10.1002/ana.20666;
Annesi G., Savettieri G., Pugliese P., D'Amelio M., Tarantino P.,
Ragonese P., La Bella V., Piccoli T., Civitelli D., Annesi F.,
Fierro B., Piccoli F., Arabia G., Caracciolo M., Ciro Candiano I.C.,
Quattrone A.;
"DJ-1 mutations and parkinsonism-dementia-amyotrophic lateral
sclerosis complex.";
Ann. Neurol. 58:803-807(2005).
[55]
VARIANT SER-39.
PubMed=16632486; DOI=10.1093/hmg/ddl104;
Tang B., Xiong H., Sun P., Zhang Y., Wang D., Hu Z., Zhu Z., Ma H.,
Pan Q., Xia J.-H., Xia K., Zhang Z.;
"Association of PINK1 and DJ-1 confers digenic inheritance of early-
onset Parkinson's disease.";
Hum. Mol. Genet. 15:1816-1825(2006).
[56]
CHARACTERIZATION OF VARIANT PARK7 PRO-166.
PubMed=17846173; DOI=10.1083/jcb.200611128;
Olzmann J.A., Li L., Chudaev M.V., Chen J., Perez F.A., Palmiter R.D.,
Chin L.S.;
"Parkin-mediated K63-linked polyubiquitination targets misfolded DJ-1
to aggresomes via binding to HDAC6.";
J. Cell Biol. 178:1025-1038(2007).
[57]
VARIANT ASP-64, AND FUNCTION.
PubMed=20186336; DOI=10.1371/journal.pone.0009367;
Krebiehl G., Ruckerbauer S., Burbulla L.F., Kieper N., Maurer B.,
Waak J., Wolburg H., Gizatullina Z., Gellerich F.N., Woitalla D.,
Riess O., Kahle P.J., Proikas-Cezanne T., Kruger R.;
"Reduced basal autophagy and impaired mitochondrial dynamics due to
loss of Parkinson's disease-associated protein DJ-1.";
PLoS ONE 5:E9367-E9367(2010).
-!- 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
(PubMed:25416785, PubMed:28596309). 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 (PubMed:25416785, PubMed:28013050, PubMed:26995087). 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 (PubMed:28596309). Also displays an
apparent glyoxalase activity that in fact reflects its deglycase
activity (PubMed:22523093). 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,
PubMed:26995087). 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). 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). 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 (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). 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: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:26995087,
ECO:0000269|PubMed:28013050, ECO:0000269|PubMed:28596309,
ECO:0000269|PubMed:9070310}.
-!- CATALYTIC ACTIVITY: An N(omega)-(1-hydroxy-2-oxopropyl)-[protein]-
L-arginine + H(2)O = a [protein]-L-arginine + (R)-lactate.
{ECO:0000269|PubMed:25416785}.
-!- CATALYTIC ACTIVITY: An N(6)-(1-hydroxy-2-oxopropyl)-[protein]-L-
lysine + H(2)O = a [protein]-L-lysine + (R)-lactate.
{ECO:0000269|PubMed:25416785}.
-!- CATALYTIC ACTIVITY: An S-(1-hydroxy-2-oxopropyl)-[protein]-L-
cysteine + H(2)O = a [protein]-L-cysteine + (R)-lactate.
{ECO:0000269|PubMed:25416785}.
-!- COFACTOR:
Note=Deglycase activity does not require glutathione as a
cofactor, however, glycated glutathione constitutes a PARK7
substrate. {ECO:0000269|PubMed:25416785};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=173.4 uM for casein {ECO:0000269|PubMed:20304780};
KM=0.44 mM for glycated N-acetylarginine (at pH 7.0 and 22
degrees Celsius) {ECO:0000269|PubMed:25416785};
KM=0.35 mM for glycated N-acetyllysine (at pH 7.0 and 22 degrees
Celsius) {ECO:0000269|PubMed:25416785};
KM=0.32 mM for glycated N-acetylcysteine (at pH 7.0 and 22
degrees Celsius) {ECO:0000269|PubMed:25416785};
Note=kcat is 0.27 sec(-1) for the deglycation of glycated N-
acetylarginine. kcat is 0.28 sec(-1) for the deglycation of
glycated N-acetyllysine. kcat is 0.42 sec(-1) for the
deglycation of glycated N-acetylcysteine.
{ECO:0000269|PubMed:25416785};
-!- SUBUNIT: Homodimer (PubMed:12851414, PubMed:12796482,
PubMed:12855764). Binds EFCAB6/DJBP and PIAS2 (PubMed:11477070,
PubMed:12851414, PubMed:12612053). Part of a ternary complex
containing PARK7, EFCAB6/DJBP and AR (PubMed:12612053). Interacts
(via N-terminus) with OTUD7B (PubMed:21097510). Interacts with
BBS1, HIPK1, CLCF1 and MTERF (PubMed:16390825, PubMed:21097510).
Forms a complex with PINK1 and PRKN (PubMed:19229105). Interacts
(via C-terminus) with NCF1; the interaction is enhanced by LPS and
modulates NCF1 phosphorylation and membrane translocation (By
similarity). {ECO:0000250|UniProtKB:Q99LX0,
ECO:0000269|PubMed:11477070, ECO:0000269|PubMed:12612053,
ECO:0000269|PubMed:12796482, ECO:0000269|PubMed:12851414,
ECO:0000269|PubMed:12855764, ECO:0000269|PubMed:16390825,
ECO:0000269|PubMed:21097510}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-1164361, EBI-1164361;
P10275:AR; NbExp=6; IntAct=EBI-1164361, EBI-608057;
Q9UER7:DAXX; NbExp=3; IntAct=EBI-1164361, EBI-77321;
Q13158:FADD; NbExp=9; IntAct=EBI-1164361, EBI-494804;
Q9HD26:GOPC; NbExp=3; IntAct=EBI-1164361, EBI-349832;
O94776:MTA2; NbExp=3; IntAct=EBI-1164361, EBI-1783035;
Q6GQQ9:OTUD7B; NbExp=3; IntAct=EBI-1164361, EBI-527784;
P32322:PYCR1; NbExp=5; IntAct=EBI-1164361, EBI-848624;
P63244:RACK1; NbExp=4; IntAct=EBI-1164361, EBI-296739;
-!- SUBCELLULAR LOCATION: Cell 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,
ECO:0000269|PubMed:28596309}. Nucleus
{ECO:0000269|PubMed:12851414, ECO:0000269|PubMed:14579415,
ECO:0000269|PubMed:15976810, ECO:0000269|PubMed:16390825,
ECO:0000269|PubMed:28596309}. 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}.
-!- TISSUE SPECIFICITY: 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). {ECO:0000269|PubMed:14579415,
ECO:0000269|PubMed:14662519, ECO:0000269|PubMed:14705119,
ECO:0000269|PubMed:22611253, ECO:0000269|PubMed:9070310}.
-!- DEVELOPMENTAL STAGE: In pancreatic islets, expression increases
during aging. {ECO:0000269|PubMed:22611253}.
-!- INDUCTION: By hydrogen peroxide and UV irradiation
(PubMed:14749723, PubMed:15976810). In pancreatic islets,
expression increases under hyperglycemic conditions
(PubMed:22611253). Expression is also induced by sulforaphane, an
isothiocyanate obtained from cruciferous vegetables
(PubMed:26995087). {ECO:0000269|PubMed:14749723,
ECO:0000269|PubMed:15976810, ECO:0000269|PubMed:22611253,
ECO:0000269|PubMed:26995087}.
-!- PTM: Sumoylated on Lys-130 by PIAS2 or PIAS4; which is enhanced
after ultraviolet irradiation and essential for cell-growth
promoting activity and transforming activity.
{ECO:0000269|PubMed:15976810}.
-!- PTM: Cys-106 is easily oxidized to sulfinic acid.
{ECO:0000269|PubMed:12939276, ECO:0000269|PubMed:15976810}.
-!- PTM: Undergoes cleavage of a C-terminal peptide and subsequent
activation of protease activity in response to oxidative stress.
{ECO:0000269|PubMed:20304780}.
-!- DISEASE: Parkinson disease 7 (PARK7) [MIM:606324]: A
neurodegenerative disorder characterized by resting tremor,
postural tremor, bradykinesia, muscular rigidity, anxiety and
psychotic episodes. PARK7 has onset before 40 years, slow
progression and initial good response to levodopa. Some patients
may show traits reminiscent of amyotrophic lateral sclerosis-
parkinsonism/dementia complex (Guam disease).
{ECO:0000269|PubMed:12446870, ECO:0000269|PubMed:12851414,
ECO:0000269|PubMed:12953260, ECO:0000269|PubMed:14607841,
ECO:0000269|PubMed:14713311, ECO:0000269|PubMed:15254937,
ECO:0000269|PubMed:15365989, ECO:0000269|PubMed:17846173,
ECO:0000269|PubMed:19229105, ECO:0000269|PubMed:22523093,
ECO:0000269|PubMed:23792957, ECO:0000269|PubMed:23847046}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the peptidase C56 family. {ECO:0000305}.
-!- CAUTION: Glyoxalase activity was previously reported
(PubMed:22523093). It may however reflect its deglycase activity
(PubMed:25416785). {ECO:0000269|PubMed:22523093,
ECO:0000269|PubMed:25416785}.
-!- CAUTION: The protein deglycation activity has been ascribed to a
TRIS buffer artifact by a publication (PubMed:27903648). However,
clear biochemical experiments showing that PARK7 is a bona fide
deglycase have been performed (PubMed:25416785, PubMed:28013050).
Deglycase activity is even strengthened by a an article that
reports nucleotide deglycation activity (PubMed:28596309).
{ECO:0000269|PubMed:25416785, ECO:0000269|PubMed:27903648,
ECO:0000269|PubMed:28013050, ECO:0000269|PubMed:28596309}.
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=P&genename=PARK7+%40+DJ-1";
-----------------------------------------------------------------------
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EMBL; D61380; BAA09603.2; -; mRNA.
EMBL; AF021819; AAC12806.1; -; mRNA.
EMBL; AB073864; BAB71782.1; -; mRNA.
EMBL; AK312000; BAG34938.1; -; mRNA.
EMBL; AL034417; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471130; EAW71591.1; -; Genomic_DNA.
EMBL; BC008188; AAH08188.1; -; mRNA.
EMBL; AB045294; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AY648999; AAT68961.1; -; Genomic_DNA.
CCDS; CCDS93.1; -.
PIR; JC5394; JC5394.
RefSeq; NP_001116849.1; NM_001123377.1.
RefSeq; NP_009193.2; NM_007262.4.
RefSeq; XP_005263481.1; XM_005263424.3.
UniGene; Hs.419640; -.
PDB; 1J42; X-ray; 2.50 A; A=1-189.
PDB; 1P5F; X-ray; 1.10 A; A=1-189.
PDB; 1PDV; X-ray; 1.80 A; A=1-189.
PDB; 1PDW; X-ray; 2.20 A; A/B/C/D/E/F/G/H=1-189.
PDB; 1PE0; X-ray; 1.70 A; A/B=1-189.
PDB; 1Q2U; X-ray; 1.60 A; A=1-189.
PDB; 1SOA; X-ray; 1.20 A; A=1-189.
PDB; 1UCF; X-ray; 1.95 A; A/B=1-189.
PDB; 2OR3; X-ray; 1.20 A; A/B=1-189.
PDB; 2R1T; X-ray; 1.70 A; A/B=2-188.
PDB; 2R1U; X-ray; 1.50 A; A/B=2-188.
PDB; 2R1V; X-ray; 1.70 A; A/B=2-188.
PDB; 2RK3; X-ray; 1.05 A; A=1-189.
PDB; 2RK4; X-ray; 1.15 A; A=1-189.
PDB; 2RK6; X-ray; 1.15 A; A=1-189.
PDB; 3B36; X-ray; 1.50 A; A=1-189.
PDB; 3B38; X-ray; 1.85 A; A=1-189.
PDB; 3B3A; X-ray; 1.50 A; A=1-189.
PDB; 3BWE; X-ray; 2.40 A; A/B/C/D/E/F/G=1-189.
PDB; 3CY6; X-ray; 1.35 A; A=1-189.
PDB; 3CYF; X-ray; 1.60 A; A=1-189.
PDB; 3CZ9; X-ray; 1.15 A; A=1-189.
PDB; 3CZA; X-ray; 1.20 A; A=1-189.
PDB; 3EZG; X-ray; 1.15 A; A=1-189.
PDB; 3F71; X-ray; 1.20 A; A=1-189.
PDB; 3SF8; X-ray; 1.56 A; A/B=1-189.
PDB; 4BTE; X-ray; 1.38 A; A=1-189.
PDB; 4MNT; X-ray; 1.58 A; A=1-189.
PDB; 4MTC; X-ray; 1.47 A; A=1-189.
PDB; 4N0M; X-ray; 1.95 A; A=1-189.
PDB; 4N12; X-ray; 1.48 A; A=1-189.
PDB; 4OGF; X-ray; 1.60 A; A=2-188.
PDB; 4OQ4; X-ray; 1.49 A; A=1-189.
PDB; 4P2G; X-ray; 1.35 A; A=1-189.
PDB; 4P34; X-ray; 1.55 A; A=1-189.
PDB; 4P35; X-ray; 1.75 A; A=1-189.
PDB; 4P36; X-ray; 1.18 A; A=1-189.
PDB; 4RKW; X-ray; 1.50 A; A=1-189.
PDB; 4RKY; X-ray; 1.50 A; A=1-189.
PDB; 4S0Z; X-ray; 1.45 A; A=1-189.
PDB; 4ZGG; X-ray; 1.23 A; A=1-189.
PDB; 5IP5; X-ray; 1.66 A; A=1-189.
PDB; 5SY6; X-ray; 1.15 A; A=1-189.
PDB; 5SY9; X-ray; 1.10 A; A=1-189.
PDB; 5SYA; X-ray; 1.10 A; A=1-189.
PDBsum; 1J42; -.
PDBsum; 1P5F; -.
PDBsum; 1PDV; -.
PDBsum; 1PDW; -.
PDBsum; 1PE0; -.
PDBsum; 1Q2U; -.
PDBsum; 1SOA; -.
PDBsum; 1UCF; -.
PDBsum; 2OR3; -.
PDBsum; 2R1T; -.
PDBsum; 2R1U; -.
PDBsum; 2R1V; -.
PDBsum; 2RK3; -.
PDBsum; 2RK4; -.
PDBsum; 2RK6; -.
PDBsum; 3B36; -.
PDBsum; 3B38; -.
PDBsum; 3B3A; -.
PDBsum; 3BWE; -.
PDBsum; 3CY6; -.
PDBsum; 3CYF; -.
PDBsum; 3CZ9; -.
PDBsum; 3CZA; -.
PDBsum; 3EZG; -.
PDBsum; 3F71; -.
PDBsum; 3SF8; -.
PDBsum; 4BTE; -.
PDBsum; 4MNT; -.
PDBsum; 4MTC; -.
PDBsum; 4N0M; -.
PDBsum; 4N12; -.
PDBsum; 4OGF; -.
PDBsum; 4OQ4; -.
PDBsum; 4P2G; -.
PDBsum; 4P34; -.
PDBsum; 4P35; -.
PDBsum; 4P36; -.
PDBsum; 4RKW; -.
PDBsum; 4RKY; -.
PDBsum; 4S0Z; -.
PDBsum; 4ZGG; -.
PDBsum; 5IP5; -.
PDBsum; 5SY6; -.
PDBsum; 5SY9; -.
PDBsum; 5SYA; -.
ProteinModelPortal; Q99497; -.
SMR; Q99497; -.
BioGrid; 116446; 88.
CORUM; Q99497; -.
DIP; DIP-35515N; -.
IntAct; Q99497; 46.
MINT; MINT-5003468; -.
STRING; 9606.ENSP00000340278; -.
MEROPS; C56.002; -.
iPTMnet; Q99497; -.
PhosphoSitePlus; Q99497; -.
SwissPalm; Q99497; -.
BioMuta; PARK7; -.
DMDM; 56404943; -.
OGP; Q99497; -.
REPRODUCTION-2DPAGE; IPI00298547; -.
UCD-2DPAGE; Q99497; -.
EPD; Q99497; -.
PaxDb; Q99497; -.
PeptideAtlas; Q99497; -.
PRIDE; Q99497; -.
TopDownProteomics; Q99497; -.
DNASU; 11315; -.
Ensembl; ENST00000338639; ENSP00000340278; ENSG00000116288.
Ensembl; ENST00000377488; ENSP00000366708; ENSG00000116288.
Ensembl; ENST00000377491; ENSP00000366711; ENSG00000116288.
Ensembl; ENST00000493373; ENSP00000465404; ENSG00000116288.
Ensembl; ENST00000493678; ENSP00000418770; ENSG00000116288.
GeneID; 11315; -.
KEGG; hsa:11315; -.
CTD; 11315; -.
DisGeNET; 11315; -.
EuPathDB; HostDB:ENSG00000116288.12; -.
GeneCards; PARK7; -.
GeneReviews; PARK7; -.
HGNC; HGNC:16369; PARK7.
HPA; CAB005870; -.
HPA; HPA004190; -.
MalaCards; PARK7; -.
MIM; 168600; phenotype.
MIM; 602533; gene.
MIM; 606324; phenotype.
neXtProt; NX_Q99497; -.
OpenTargets; ENSG00000116288; -.
Orphanet; 90020; Amyotrophic lateral sclerosis-parkinsonism-dementia complex.
Orphanet; 2828; Young adult-onset Parkinsonism.
PharmGKB; PA32946; -.
eggNOG; KOG2764; Eukaryota.
eggNOG; COG0693; LUCA.
GeneTree; ENSGT00390000001231; -.
HOGENOM; HOG000063194; -.
HOVERGEN; HBG053511; -.
InParanoid; Q99497; -.
KO; K05687; -.
OMA; TCYPGFE; -.
OrthoDB; EOG091G12NS; -.
PhylomeDB; Q99497; -.
TreeFam; TF300119; -.
SABIO-RK; Q99497; -.
SignaLink; Q99497; -.
SIGNOR; Q99497; -.
ChiTaRS; PARK7; human.
EvolutionaryTrace; Q99497; -.
GeneWiki; PARK7; -.
GenomeRNAi; 11315; -.
PMAP-CutDB; Q99497; -.
PRO; PR:Q99497; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000116288; -.
CleanEx; HS_PARK7; -.
ExpressionAtlas; Q99497; baseline and differential.
Genevisible; Q99497; HS.
GO; GO:0030424; C:axon; ISS:ParkinsonsUK-UCL.
GO; GO:0044297; C:cell body; IEA:Ensembl.
GO; GO:0005913; C:cell-cell adherens junction; IDA:BHF-UCL.
GO; GO:0000785; C:chromatin; IDA:ParkinsonsUK-UCL.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
GO; GO:0005758; C:mitochondrial intermembrane space; IEA:Ensembl.
GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016605; C:PML body; IDA:ParkinsonsUK-UCL.
GO; GO:0098793; C:presynapse; IEA:GOC.
GO; GO:0050681; F:androgen receptor binding; IPI:ParkinsonsUK-UCL.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
GO; GO:1903135; F:cupric ion binding; IDA:ParkinsonsUK-UCL.
GO; GO:1903136; F:cuprous ion binding; IDA:ParkinsonsUK-UCL.
GO; GO:0019955; F:cytokine binding; IPI:ParkinsonsUK-UCL.
GO; GO:0019899; F:enzyme binding; IPI:ParkinsonsUK-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
GO; GO:0036478; F:L-dopa decarboxylase activator activity; IDA:ParkinsonsUK-UCL.
GO; GO:0045340; F:mercury ion binding; IDA:UniProtKB.
GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
GO; GO:0016684; F:oxidoreductase activity, acting on peroxide as acceptor; IDA:ParkinsonsUK-UCL.
GO; GO:0008233; F:peptidase activity; IDA:UniProtKB.
GO; GO:0051920; F:peroxiredoxin activity; IEA:Ensembl.
GO; GO:0036524; F:protein deglycase activity; IDA:ParkinsonsUK-UCL.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0005102; F:receptor binding; IPI:UniProtKB.
GO; GO:0070491; F:repressing transcription factor binding; IPI:ParkinsonsUK-UCL.
GO; GO:0097110; F:scaffold protein binding; IPI:ParkinsonsUK-UCL.
GO; GO:0044388; F:small protein activating enzyme binding; IPI:ParkinsonsUK-UCL.
GO; GO:0016532; F:superoxide dismutase copper chaperone activity; IDA:ParkinsonsUK-UCL.
GO; GO:0003713; F:transcription coactivator activity; IGI:ParkinsonsUK-UCL.
GO; GO:0008134; F:transcription factor binding; IPI:ParkinsonsUK-UCL.
GO; GO:0036470; F:tyrosine 3-monooxygenase activator activity; IDA:ParkinsonsUK-UCL.
GO; GO:0044390; F:ubiquitin-like protein conjugating enzyme binding; IPI:ParkinsonsUK-UCL.
GO; GO:1990381; F:ubiquitin-specific protease binding; IPI:ParkinsonsUK-UCL.
GO; GO:0032148; P:activation of protein kinase B activity; IC:ParkinsonsUK-UCL.
GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
GO; GO:0036471; P:cellular response to glyoxal; IDA:ParkinsonsUK-UCL.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:UniProtKB.
GO; GO:0034599; P:cellular response to oxidative stress; IDA:ParkinsonsUK-UCL.
GO; GO:0010273; P:detoxification of copper ion; IMP:UniProtKB.
GO; GO:0050787; P:detoxification of mercury ion; IMP:UniProtKB.
GO; GO:0006281; P:DNA repair; IDA:UniProtKB.
GO; GO:0051583; P:dopamine uptake involved in synaptic transmission; IEA:Ensembl.
GO; GO:0018323; P:enzyme active site formation via L-cysteine sulfinic acid; IEA:Ensembl.
GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
GO; GO:0036531; P:glutathione deglycation; IDA:ParkinsonsUK-UCL.
GO; GO:0046295; P:glycolate biosynthetic process; IDA:ParkinsonsUK-UCL.
GO; GO:1903189; P:glyoxal metabolic process; IDA:ParkinsonsUK-UCL.
GO; GO:0106044; P:guanine deglycation; IDA:UniProtKB.
GO; GO:0106046; P:guanine deglycation, glyoxal removal; IDA:UniProtKB.
GO; GO:0106045; P:guanine deglycation, methylglyoxal removal; IDA:UniProtKB.
GO; GO:0042743; P:hydrogen peroxide metabolic process; IDA:ParkinsonsUK-UCL.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0030073; P:insulin secretion; ISS:UniProtKB.
GO; GO:0019249; P:lactate biosynthetic process; IDA:ParkinsonsUK-UCL.
GO; GO:0051899; P:membrane depolarization; IEA:Ensembl.
GO; GO:0060081; P:membrane hyperpolarization; IEA:Ensembl.
GO; GO:0009438; P:methylglyoxal metabolic process; IDA:ParkinsonsUK-UCL.
GO; GO:0007005; P:mitochondrion organization; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:ParkinsonsUK-UCL.
GO; GO:0060548; P:negative regulation of cell death; IDA:UniProtKB.
GO; GO:2001268; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IMP:ParkinsonsUK-UCL.
GO; GO:1903073; P:negative regulation of death-inducing signaling complex assembly; IC:ParkinsonsUK-UCL.
GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IGI:ParkinsonsUK-UCL.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:0010629; P:negative regulation of gene expression; IDA:ParkinsonsUK-UCL.
GO; GO:1903206; P:negative regulation of hydrogen peroxide-induced cell death; IMP:ParkinsonsUK-UCL.
GO; GO:1903208; P:negative regulation of hydrogen peroxide-induced neuron death; IDA:ParkinsonsUK-UCL.
GO; GO:1903384; P:negative regulation of hydrogen peroxide-induced neuron intrinsic apoptotic signaling pathway; IGI:ParkinsonsUK-UCL.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:BHF-UCL.
GO; GO:1901215; P:negative regulation of neuron death; IDA:ParkinsonsUK-UCL.
GO; GO:1905259; P:negative regulation of nitrosative stress-induced intrinsic apoptotic signaling pathway; IDA:ParkinsonsUK-UCL.
GO; GO:1903202; P:negative regulation of oxidative stress-induced cell death; IDA:ParkinsonsUK-UCL.
GO; GO:1903377; P:negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; IDA:ParkinsonsUK-UCL.
GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:ParkinsonsUK-UCL.
GO; GO:1901984; P:negative regulation of protein acetylation; IDA:ParkinsonsUK-UCL.
GO; GO:0032091; P:negative regulation of protein binding; IDA:UniProtKB.
GO; GO:0046826; P:negative regulation of protein export from nucleus; IGI:ParkinsonsUK-UCL.
GO; GO:1903094; P:negative regulation of protein K48-linked deubiquitination; IDA:ParkinsonsUK-UCL.
GO; GO:0006469; P:negative regulation of protein kinase activity; IGI:ParkinsonsUK-UCL.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IGI:ParkinsonsUK-UCL.
GO; GO:0033234; P:negative regulation of protein sumoylation; IDA:ParkinsonsUK-UCL.
GO; GO:0031397; P:negative regulation of protein ubiquitination; IDA: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; IMP:ParkinsonsUK-UCL.
GO; GO:0051444; P:negative regulation of ubiquitin-protein transferase activity; IDA:ParkinsonsUK-UCL.
GO; GO:2000157; P:negative regulation of ubiquitin-specific protease activity; IDA:ParkinsonsUK-UCL.
GO; GO:0036527; P:peptidyl-arginine deglycation; IDA:ParkinsonsUK-UCL.
GO; GO:0036526; P:peptidyl-cysteine deglycation; IDA:ParkinsonsUK-UCL.
GO; GO:0036528; P:peptidyl-lysine deglycation; IDA: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; IMP:ParkinsonsUK-UCL.
GO; GO:1903599; P:positive regulation of autophagy of mitochondrion; NAS:ParkinsonsUK-UCL.
GO; GO:1903181; P:positive regulation of dopamine biosynthetic process; IDA:ParkinsonsUK-UCL.
GO; GO:0010628; P:positive regulation of gene expression; TAS:ParkinsonsUK-UCL.
GO; GO:0032757; P:positive regulation of interleukin-8 production; IDA:ParkinsonsUK-UCL.
GO; GO:1903197; P:positive regulation of L-dopa biosynthetic process; IMP:ParkinsonsUK-UCL.
GO; GO:1903200; P:positive regulation of L-dopa decarboxylase activity; IDA:ParkinsonsUK-UCL.
GO; GO:1902958; P:positive regulation of mitochondrial electron transport, NADH to ubiquinone; IMP: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; IEA:Ensembl.
GO; GO:1902177; P:positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:ParkinsonsUK-UCL.
GO; GO:0090073; P:positive regulation of protein homodimerization activity; IDA:ParkinsonsUK-UCL.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IC:ParkinsonsUK-UCL.
GO; GO:1900182; P:positive regulation of protein localization to nucleus; IDA:ParkinsonsUK-UCL.
GO; GO:1903168; P:positive regulation of pyrroline-5-carboxylate reductase activity; IDA:ParkinsonsUK-UCL.
GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; IEA:Ensembl.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IMP:ParkinsonsUK-UCL.
GO; GO:1901671; P:positive regulation of superoxide dismutase activity; IDA:ParkinsonsUK-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:ParkinsonsUK-UCL.
GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; IMP:ParkinsonsUK-UCL.
GO; GO:1903178; P:positive regulation of tyrosine 3-monooxygenase activity; IDA:ParkinsonsUK-UCL.
GO; GO:0036529; P:protein deglycation, glyoxal removal; IDA:ParkinsonsUK-UCL.
GO; GO:0036530; P:protein deglycation, methylglyoxal removal; IDA:ParkinsonsUK-UCL.
GO; GO:0006517; P:protein deglycosylation; IDA:UniProtKB.
GO; GO:0050821; P:protein stabilization; IDA:ParkinsonsUK-UCL.
GO; GO:0007265; P:Ras protein signal transduction; TAS:ParkinsonsUK-UCL.
GO; GO:0060765; P:regulation of androgen receptor signaling pathway; IDA:UniProtKB.
GO; GO:0050727; P:regulation of inflammatory response; ISS:UniProtKB.
GO; GO:0051881; P:regulation of mitochondrial membrane potential; IMP:ParkinsonsUK-UCL.
GO; GO:0043523; P:regulation of neuron apoptotic process; IDA:UniProtKB.
GO; GO:1902903; P:regulation of supramolecular fiber organization; TAS:ParkinsonsUK-UCL.
GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
Gene3D; 3.40.50.880; -; 1.
InterPro; IPR029062; Class_I_gatase-like.
InterPro; IPR002818; DJ-1/PfpI.
InterPro; IPR006287; DJ1.
Pfam; PF01965; DJ-1_PfpI; 1.
SUPFAM; SSF52317; SSF52317; 1.
TIGRFAMs; TIGR01383; not_thiJ; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Autophagy; Cell membrane; Chaperone;
Complete proteome; Copper; Cytoplasm; Direct protein sequencing;
Disease mutation; DNA damage; DNA repair; Fertilization; Hydrolase;
Inflammatory response; Isopeptide bond; Lipoprotein; Membrane;
Mitochondrion; Neurodegeneration; Nucleus; Oxidation; Palmitate;
Parkinson disease; Parkinsonism; Phosphoprotein; Polymorphism;
Protease; Reference proteome; RNA-binding; Stress response;
Tumor suppressor; Ubl conjugation; Zymogen.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:25944712}.
CHAIN 2 ? Protein/nucleic acid deglycase DJ-1.
/FTId=PRO_0000157849.
PROPEP ? 189 Removed in mature form.
/FTId=PRO_0000405558.
ACT_SITE 106 106 Nucleophile.
{ECO:0000305|PubMed:20304780,
ECO:0000305|PubMed:25416785}.
ACT_SITE 126 126 {ECO:0000305|PubMed:20304780}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:25944712}.
MOD_RES 67 67 Phosphotyrosine.
{ECO:0000244|PubMed:15592455}.
MOD_RES 106 106 Cysteine sulfinic acid (-SO2H);
alternate. {ECO:0000269|PubMed:12939276}.
MOD_RES 148 148 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q99LX0}.
MOD_RES 182 182 N6-succinyllysine.
{ECO:0000250|UniProtKB:Q99LX0}.
LIPID 46 46 S-palmitoyl cysteine.
{ECO:0000269|PubMed:23847046}.
LIPID 53 53 S-palmitoyl cysteine.
{ECO:0000269|PubMed:23847046}.
LIPID 106 106 S-palmitoyl cysteine; alternate.
{ECO:0000269|PubMed:23847046}.
CROSSLNK 130 130 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:15976810}.
VARIANT 26 26 M -> I (in PARK7; does not affect protein
stability and degradation; does not
interfere with homodimerization;
dbSNP:rs74315351).
{ECO:0000269|PubMed:12953260,
ECO:0000269|PubMed:14713311}.
/FTId=VAR_020492.
VARIANT 39 39 A -> S (probable disease-associated
mutation found in early-onset Parkinson
disease with digenic inheritance; the
patient also carries PINK1 mutation L-
399; dbSNP:rs137853051).
{ECO:0000269|PubMed:16632486}.
/FTId=VAR_072589.
VARIANT 64 64 E -> D (in PARK7; no apparent effect on
protein stability; impaired mitochondrial
morphology; dbSNP:rs74315353).
{ECO:0000269|PubMed:14607841,
ECO:0000269|PubMed:15365989,
ECO:0000269|PubMed:20186336}.
/FTId=VAR_020493.
VARIANT 98 98 R -> Q (in dbSNP:rs71653619).
{ECO:0000269|PubMed:12953260,
ECO:0000269|PubMed:14705128,
ECO:0000269|PubMed:14872018,
ECO:0000269|PubMed:15254937}.
/FTId=VAR_020494.
VARIANT 104 104 A -> T (in PARK7; loss of protection
against metal cytotoxicity;
dbSNP:rs774005786).
{ECO:0000269|PubMed:15254937,
ECO:0000269|PubMed:23792957}.
/FTId=VAR_020495.
VARIANT 149 149 D -> A (in PARK7; loss of protection
against metal cytotoxicity;
dbSNP:rs74315352).
{ECO:0000269|PubMed:12953260,
ECO:0000269|PubMed:23792957}.
/FTId=VAR_020496.
VARIANT 150 150 G -> S (in dbSNP:rs368420490).
{ECO:0000269|Ref.10}.
/FTId=VAR_020497.
VARIANT 163 163 E -> K (in dbSNP:rs74315354).
{ECO:0000269|PubMed:16240358}.
/FTId=VAR_034801.
VARIANT 166 166 L -> P (in PARK7; strongly decreases
enzymatic activity; reduces protein
stability and leads to increased
degradation; ubiquitinated by PRKN
leading to its recognition by HDAC6 and
targeting to aggresome where is degraded;
interferes with homodimerization;
abolishes interaction with PIAS2; reduced
localization in lipid rafts;
dbSNP:rs28938172).
{ECO:0000269|PubMed:12446870,
ECO:0000269|PubMed:12851414,
ECO:0000269|PubMed:14607841,
ECO:0000269|PubMed:14713311,
ECO:0000269|PubMed:17846173,
ECO:0000269|PubMed:19229105,
ECO:0000269|PubMed:22523093,
ECO:0000269|PubMed:23847046}.
/FTId=VAR_020498.
VARIANT 171 171 A -> S (in dbSNP:rs777026628).
{ECO:0000269|PubMed:15254937}.
/FTId=VAR_020499.
MUTAGEN 18 18 E->A: Strongly decreases enzymatic
activity. {ECO:0000269|PubMed:22523093}.
MUTAGEN 18 18 E->D: Strongly decreases enzymatic
activity. {ECO:0000269|PubMed:22523093}.
MUTAGEN 18 18 E->N: Strongly decreases enzymatic
activity. {ECO:0000269|PubMed:22523093}.
MUTAGEN 18 18 E->Q: Strongly decreases enzymatic
activity. {ECO:0000269|PubMed:22523093}.
MUTAGEN 46 46 C->A: Reduced localization in lipid
rafts; when associated with A-106.
{ECO:0000269|PubMed:15181200,
ECO:0000269|PubMed:15502874,
ECO:0000269|PubMed:18711745,
ECO:0000269|PubMed:23847046}.
MUTAGEN 46 46 C->A: Reduces protein stability. No
effect on oxidation.
{ECO:0000269|PubMed:15181200,
ECO:0000269|PubMed:15502874,
ECO:0000269|PubMed:18711745,
ECO:0000269|PubMed:23847046}.
MUTAGEN 46 46 C->S: No effect on mitochondrial
translocation neither on deglycase
activity. {ECO:0000269|PubMed:15181200,
ECO:0000269|PubMed:15502874,
ECO:0000269|PubMed:18711745,
ECO:0000269|PubMed:23847046,
ECO:0000269|PubMed:25416785}.
MUTAGEN 51 51 V->A: Disrupts dimer formation and
strongly reduces ability to eliminate
hydrogen peroxide.
{ECO:0000269|PubMed:14749723}.
MUTAGEN 53 53 C->A: Strongly reduces chaperone activity
and ability to eliminate hydrogen
peroxide. {ECO:0000269|PubMed:14749723,
ECO:0000269|PubMed:15181200,
ECO:0000269|PubMed:15502874,
ECO:0000269|PubMed:18711745}.
MUTAGEN 53 53 C->S: No effect on mitochondrial
translocation neither on deglycase
activity. {ECO:0000269|PubMed:14749723,
ECO:0000269|PubMed:15181200,
ECO:0000269|PubMed:15502874,
ECO:0000269|PubMed:18711745,
ECO:0000269|PubMed:25416785}.
MUTAGEN 106 106 C->A: Abolishes enzymatic activity.
Abolishes oxidation, association with
mitochondria and protease activity. No
effect on chaperone activity. Reduces
binding to OTUD7B.
{ECO:0000269|PubMed:15181200,
ECO:0000269|PubMed:15502874,
ECO:0000269|PubMed:16390825,
ECO:0000269|PubMed:18711745,
ECO:0000269|PubMed:20304780,
ECO:0000269|PubMed:21097510,
ECO:0000269|PubMed:22523093,
ECO:0000269|PubMed:23847046}.
MUTAGEN 106 106 C->A: Reduced localization in lipid
rafts; when associated with A-46.
{ECO:0000269|PubMed:15181200,
ECO:0000269|PubMed:15502874,
ECO:0000269|PubMed:16390825,
ECO:0000269|PubMed:18711745,
ECO:0000269|PubMed:20304780,
ECO:0000269|PubMed:21097510,
ECO:0000269|PubMed:23847046}.
MUTAGEN 106 106 C->D: Abolishes oxidation and association
with mitochondria. No effect on chaperone
activity. {ECO:0000269|PubMed:15181200,
ECO:0000269|PubMed:15502874,
ECO:0000269|PubMed:16390825,
ECO:0000269|PubMed:18711745,
ECO:0000269|PubMed:20304780,
ECO:0000269|PubMed:21097510,
ECO:0000269|PubMed:23847046}.
MUTAGEN 106 106 C->S: Loss of protein and nucleic acid
deglycase activity. No effect on
mitochondrial translocation. Reduced
protease activity. No effect on
protection against metal cytotoxicity.
{ECO:0000269|PubMed:15181200,
ECO:0000269|PubMed:15502874,
ECO:0000269|PubMed:16390825,
ECO:0000269|PubMed:18711745,
ECO:0000269|PubMed:20304780,
ECO:0000269|PubMed:21097510,
ECO:0000269|PubMed:23847046,
ECO:0000269|PubMed:25416785,
ECO:0000269|PubMed:28596309}.
MUTAGEN 126 126 H->A: Strongly decreases enzymatic
activity. {ECO:0000269|PubMed:20304780,
ECO:0000269|PubMed:22523093}.
MUTAGEN 130 130 K->R: Partially compensates for loss of
stability; when associated with P-166.
{ECO:0000269|PubMed:12851414}.
CONFLICT 119 119 F -> C (in Ref. 3; BAB71782).
{ECO:0000305}.
STRAND 5 10 {ECO:0000244|PDB:2RK3}.
HELIX 16 28 {ECO:0000244|PDB:2RK3}.
STRAND 32 37 {ECO:0000244|PDB:2RK3}.
TURN 38 41 {ECO:0000244|PDB:1PDW}.
STRAND 47 49 {ECO:0000244|PDB:4N0M}.
STRAND 51 53 {ECO:0000244|PDB:2OR3}.
STRAND 55 57 {ECO:0000244|PDB:2RK3}.
HELIX 58 62 {ECO:0000244|PDB:2RK3}.
STRAND 68 72 {ECO:0000244|PDB:2RK3}.
HELIX 76 84 {ECO:0000244|PDB:2RK3}.
HELIX 86 97 {ECO:0000244|PDB:2RK3}.
STRAND 101 105 {ECO:0000244|PDB:2RK3}.
TURN 106 108 {ECO:0000244|PDB:2RK3}.
HELIX 109 114 {ECO:0000244|PDB:2RK3}.
HELIX 127 129 {ECO:0000244|PDB:2RK3}.
HELIX 130 133 {ECO:0000244|PDB:2RK3}.
TURN 134 136 {ECO:0000244|PDB:2RK3}.
STRAND 139 141 {ECO:0000244|PDB:2RK3}.
STRAND 145 149 {ECO:0000244|PDB:2RK3}.
STRAND 152 155 {ECO:0000244|PDB:2RK3}.
HELIX 158 160 {ECO:0000244|PDB:2RK3}.
HELIX 161 173 {ECO:0000244|PDB:2RK3}.
HELIX 175 182 {ECO:0000244|PDB:2RK3}.
HELIX 183 185 {ECO:0000244|PDB:2RK3}.
SEQUENCE 189 AA; 19891 MW; 4B21661B3A76BC67 CRC64;
MASKRALVIL AKGAEEMETV IPVDVMRRAG IKVTVAGLAG KDPVQCSRDV VICPDASLED
AKKEGPYDVV VLPGGNLGAQ NLSESAAVKE ILKEQENRKG LIAAICAGPT ALLAHEIGFG
SKVTTHPLAK DKMMNGGHYT YSENRVEKDG LILTSRGPGT SFEFALAIVE ALNGKEVAAQ
VKAPLVLKD


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