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Database: UniProt
Entry: Q99497
LinkDB: Q99497
Original site: Q99497 
ID   PARK7_HUMAN             Reviewed;         189 AA.
AC   Q99497; B2R4Z1; O14805; Q6DR95; Q7LFU2;
DT   07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 2.
DT   22-NOV-2017, entry version 183.
DE   RecName: Full=Protein/nucleic acid deglycase DJ-1 {ECO:0000305|PubMed:25416785, ECO:0000305|PubMed:28596309};
DE            EC=3.1.2.- {ECO:0000269|PubMed:25416785};
DE            EC=3.5.1.- {ECO:0000269|PubMed:28596309};
DE            EC=3.5.1.124 {ECO:0000269|PubMed:25416785};
DE   AltName: Full=Maillard deglycase {ECO:0000303|PubMed:28596309};
DE   AltName: Full=Oncogene DJ1 {ECO:0000305};
DE   AltName: Full=Parkinson disease protein 7 {ECO:0000305};
DE   AltName: Full=Parkinsonism-associated deglycase {ECO:0000312|HGNC:HGNC:16369};
DE   AltName: Full=Protein DJ-1 {ECO:0000305};
DE            Short=DJ-1;
DE   Flags: Precursor;
GN   Name=PARK7 {ECO:0000312|HGNC:HGNC:16369};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=9070310; DOI=10.1006/bbrc.1997.6132;
RA   Nagakubo D., Taita T., Kitaura H., Ikeda M., Tamai K.,
RA   Iguchi-Ariga S.M.M., Ariga H.;
RT   "DJ-1, a novel oncogene which transforms mouse NIH3T3 cells in
RT   cooperation with ras.";
RL   Biochem. Biophys. Res. Commun. 231:509-513(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Lung;
RA   Beaudoin R., Hod Y.;
RT   "Homo sapiens RNA-binding protein regulatory subunit mRNA.";
RL   Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Ariga H., Niki T.;
RT   "Human DJ-1 cDNA from PC3 cells.";
RL   Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Thalamus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA   Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA   Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA   McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA   Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA   Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA   Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA   Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA   Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA   Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA   Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA   Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA   Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA   Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA   Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA   Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA   Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA   Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA   Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA   Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA   Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA   Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA   Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Cervix;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
RC   TISSUE=Kidney;
RX   PubMed=11223268; DOI=10.1016/S0378-1119(00)00590-4;
RA   Taira T., Takahashi K., Kitagawa R., Iguchi-Ariga S.M.M., Ariga H.;
RT   "Molecular cloning of human and mouse DJ-1 genes and identification of
RT   Sp1-dependent activation of the human DJ-1 promoter.";
RL   Gene 263:285-292(2001).
RN   [9]
RP   PROTEIN SEQUENCE OF 6-27; 33-89; 99-122 AND 149-175, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA   Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL   Submitted (DEC-2008) to UniProtKB.
RN   [10]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 138-189, AND VARIANT SER-150.
RA   Zou H.Q., Chan P.;
RT   "DJ-1 gene G150S mutation.";
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [11]
RP   INTERACTION WITH PIAS2, SUBCELLULAR LOCATION, AND FUNCTION.
RX   PubMed=11477070; DOI=10.1074/jbc.M101730200;
RA   Takahashi K., Taira T., Niki T., Seino C., Iguchi-Ariga S.M.M.,
RA   Ariga H.;
RT   "DJ-1 positively regulates the androgen receptor by impairing the
RT   binding of PIASx alpha to the receptor.";
RL   J. Biol. Chem. 276:37556-37563(2001).
RN   [12]
RP   DEGRADATION BY THE PROTEASOME, SUBCELLULAR LOCATION, INTERACTION WITH
RP   PIAS2, HOMODIMERIZATION, MUTAGENESIS OF LYS-130, AND CHARACTERIZATION
RP   OF VARIANT PARK7 PRO-166.
RX   PubMed=12851414; DOI=10.1074/jbc.M304272200;
RA   Miller D.W., Ahmad R., Hague S., Baptista M.J., Canet-Aviles R.,
RA   McLendon C., Carter D.M., Zhu P.-P., Stadler J., Chandran J.,
RA   Klinefelter G.R., Blackstone C., Cookson M.R.;
RT   "L166P mutant DJ-1, causative for recessive Parkinson's disease, is
RT   degraded through the ubiquitin-proteasome system.";
RL   J. Biol. Chem. 278:36588-36595(2003).
RN   [13]
RP   DEGRADATION BY THE PROTEASOME, AND CHARACTERIZATION OF VARIANTS PARK7
RP   ILE-26 AND PRO-166.
RX   PubMed=14713311;
RA   Moore D.J., Zhang L., Dawson T.M., Dawson V.L.;
RT   "A missense mutation (L166P) in DJ-1, linked to familial Parkinson's
RT   disease, confers reduced protein stability and impairs homo-
RT   oligomerization.";
RL   J. Neurochem. 87:1558-1567(2003).
RN   [14]
RP   FUNCTION, INTERACTION WITH EFCAB6, AND COMPONENT OF A COMPLEX COMPOSED
RP   OF AR; EFCAB6 AND PARK7.
RX   PubMed=12612053;
RA   Niki T., Takahashi-Niki K., Taira T., Iguchi-Ariga S.M.M., Ariga H.;
RT   "DJBP: a novel DJ-1-binding protein, negatively regulates the androgen
RT   receptor by recruiting histone deacetylase complex, and DJ-1
RT   antagonizes this inhibition by abrogation of this complex.";
RL   Mol. Cancer Res. 1:247-261(2003).
RN   [15]
RP   TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=14579415; DOI=10.1002/mrd.10360;
RA   Yoshida K., Sato Y., Yoshiike M., Nozawa S., Ariga H., Iwamoto T.;
RT   "Immunocytochemical localization of DJ-1 in human male reproductive
RT   tissue.";
RL   Mol. Reprod. Dev. 66:391-397(2003).
RN   [16]
RP   TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=14705119; DOI=10.1002/ana.10782;
RA   Rizzu P., Hinkle D.A., Zhukareva V., Bonifati V., Severijnen L.-A.,
RA   Martinez D., Ravid R., Kamphorst W., Eberwine J.H., Lee V.M.-Y.,
RA   Trojanowski J.Q., Heutink P.;
RT   "DJ-1 colocalizes with tau inclusions: a link between parkinsonism and
RT   dementia.";
RL   Ann. Neurol. 55:113-118(2004).
RN   [17]
RP   TISSUE SPECIFICITY.
RX   PubMed=14662519; DOI=10.1093/brain/awh054;
RA   Bandopadhyay R., Kingsbury A.E., Cookson M.R., Reid A.R., Evans I.M.,
RA   Hope A.D., Pittman A.M., Lashley T., Canet-Aviles R., Miller D.W.,
RA   McLendon C., Strand C., Leonard A.J., Abou-Sleiman P.M., Healy D.G.,
RA   Ariga H., Wood N.W., de Silva R., Revesz T., Hardy J.A., Lees A.J.;
RT   "The expression of DJ-1 (PARK7) in normal human CNS and idiopathic
RT   Parkinson's disease.";
RL   Brain 127:420-430(2004).
RN   [18]
RP   FUNCTION, INDUCTION, AND MUTAGENESIS OF VAL-51 AND CYS-53.
RX   PubMed=14749723; DOI=10.1038/sj.embor.7400074;
RA   Taira T., Saito Y., Niki T., Iguchi-Ariga S.M., Takahashi K.,
RA   Ariga H.;
RT   "DJ-1 has a role in antioxidative stress to prevent cell death.";
RL   EMBO Rep. 5:213-218(2004).
RN   [19]
RP   FUNCTION, AND MUTAGENESIS OF CYS-46; CYS-53 AND CYS-106.
RX   PubMed=15502874; DOI=10.1371/journal.pbio.0020362;
RA   Shendelman S., Jonason A., Martinat C., Leete T., Abeliovich A.;
RT   "DJ-1 is a redox-dependent molecular chaperone that inhibits alpha-
RT   synuclein aggregate formation.";
RL   PLoS Biol. 2:1-10(2004).
RN   [20]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-67, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=15592455; DOI=10.1038/nbt1046;
RA   Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA   Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT   "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT   cells.";
RL   Nat. Biotechnol. 23:94-101(2005).
RN   [21]
RP   SUMOYLATION AT LYS-130, OXIDATION, SUBCELLULAR LOCATION, INDUCTION,
RP   AND FUNCTION.
RX   PubMed=15976810; DOI=10.1038/sj.cdd.4401704;
RA   Shinbo Y., Niki T., Taira T., Ooe H., Takahashi-Niki K., Maita C.,
RA   Seino C., Iguchi-Ariga S.M.M., Ariga H.;
RT   "Proper SUMO-1 conjugation is essential to DJ-1 to exert its full
RT   activities.";
RL   Cell Death Differ. 13:96-108(2006).
RN   [22]
RP   FUNCTION, INTERACTION WITH HIPK1, SUBCELLULAR LOCATION, AND
RP   MUTAGENESIS OF CYS-106.
RX   PubMed=16390825; DOI=10.1080/10715760500456847;
RA   Sekito A., Koide-Yoshida S., Niki T., Taira T., Iguchi-Ariga S.M.M.,
RA   Ariga H.;
RT   "DJ-1 interacts with HIPK1 and affects H2O2-induced cell death.";
RL   Free Radic. Res. 40:155-165(2006).
RN   [23]
RP   FUNCTION.
RX   PubMed=17015834; DOI=10.1073/pnas.0607260103;
RA   Clements C.M., McNally R.S., Conti B.J., Mak T.W., Ting J.P.;
RT   "DJ-1, a cancer- and Parkinson's disease-associated protein,
RT   stabilizes the antioxidant transcriptional master regulator Nrf2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15091-15096(2006).
RN   [24]
RP   FUNCTION.
RX   PubMed=18626009; DOI=10.1073/pnas.0708518105;
RA   van der Brug M.P., Blackinton J., Chandran J., Hao L.Y., Lal A.,
RA   Mazan-Mamczarz K., Martindale J., Xie C., Ahmad R., Thomas K.J.,
RA   Beilina A., Gibbs J.R., Ding J., Myers A.J., Zhan M., Cai H.,
RA   Bonini N.M., Gorospe M., Cookson M.R.;
RT   "RNA binding activity of the recessive parkinsonism protein DJ-1
RT   supports involvement in multiple cellular pathways.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10244-10249(2008).
RN   [25]
RP   FUNCTION, COMPONENT OF A COMPLEX COMPOSED OF PRKN; PARK7 AND PINK1,
RP   SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANT PARK7 PRO-166.
RX   PubMed=19229105; DOI=10.1172/JCI37617;
RA   Xiong H., Wang D., Chen L., Choo Y.S., Ma H., Tang C., Xia K.,
RA   Jiang W., Ronai Z., Zhuang X., Zhang Z.;
RT   "Parkin, PINK1, and DJ-1 form a ubiquitin E3 ligase complex promoting
RT   unfolded protein degradation.";
RL   J. Clin. Invest. 119:650-660(2009).
RN   [26]
RP   FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-46; CYS-53 AND
RP   CYS-106.
RX   PubMed=18711745; DOI=10.1002/jnr.21831;
RA   Junn E., Jang W.H., Zhao X., Jeong B.S., Mouradian M.M.;
RT   "Mitochondrial localization of DJ-1 leads to enhanced
RT   neuroprotection.";
RL   J. Neurosci. Res. 87:123-129(2009).
RN   [27]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITES, AND MUTAGENESIS
RP   OF CYS-106 AND HIS-126.
RX   PubMed=20304780; DOI=10.1093/hmg/ddq113;
RA   Chen J., Li L., Chin L.S.;
RT   "Parkinson disease protein DJ-1 converts from a zymogen to a protease
RT   by carboxyl-terminal cleavage.";
RL   Hum. Mol. Genet. 19:2395-2408(2010).
RN   [28]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [29]
RP   FUNCTION, INTERACTION WITH BBS1; CLCF1; MTERF AND OTUD7B, AND
RP   MUTAGENESIS OF CYS-106.
RX   PubMed=21097510; DOI=10.1074/jbc.M110.147371;
RA   McNally R.S., Davis B.K., Clements C.M., Accavitti-Loper M.A.,
RA   Mak T.W., Ting J.P.;
RT   "DJ-1 enhances cell survival through the binding of cezanne, a
RT   negative regulator of NF-{kappa}B.";
RL   J. Biol. Chem. 286:4098-4106(2011).
RN   [30]
RP   FUNCTION, CAUTION, MUTAGENESIS OF GLU-18; CYS-106 AND HIS-126, AND
RP   CHARACTERIZATION OF VARIANT PARK7 PRO-166.
RX   PubMed=22523093; DOI=10.1093/hmg/dds155;
RA   Lee J.Y., Song J., Kwon K., Jang S., Kim C., Baek K., Kim J., Park C.;
RT   "Human DJ-1 and its homologs are novel glyoxalases.";
RL   Hum. Mol. Genet. 21:3215-3225(2012).
RN   [31]
RP   FUNCTION, DEVELOPMENTAL STAGE, INDUCTION BY HYPERGLYCEMIC CONDITIONS,
RP   TISSUE SPECIFICITY, AND INVOLVEMENT IN DISEASE.
RX   PubMed=22611253; DOI=10.1093/jmcb/mjs025;
RA   Jain D., Jain R., Eberhard D., Eglinger J., Bugliani M., Piemonti L.,
RA   Marchetti P., Lammert E.;
RT   "Age- and diet-dependent requirement of DJ-1 for glucose homeostasis
RT   in mice with implications for human type 2 diabetes.";
RL   J. Mol. Cell Biol. 4:221-230(2012).
RN   [32]
RP   FUNCTION, PALMITOYLATION AT CYS-46; CYS-53 AND CYS-106, SUBCELLULAR
RP   LOCATION, MUTAGENESIS OF CYS-46 AND CYS-106, AND CHARACTERIZATION OF
RP   VARIANT PARK7 PRO-166.
RX   PubMed=23847046; DOI=10.1093/hmg/ddt332;
RA   Kim K.S., Kim J.S., Park J.Y., Suh Y.H., Jou I., Joe E.H., Park S.M.;
RT   "DJ-1 associates with lipid rafts by palmitoylation and regulates
RT   lipid rafts-dependent endocytosis in astrocytes.";
RL   Hum. Mol. Genet. 22:4805-4817(2013).
RN   [33]
RP   FUNCTION, COPPER-BINDING, CHARACTERIZATION OF VARIANTS PARK7 THR-104
RP   AND ALA-149, AND MUTAGENESIS OF CYS-106.
RX   PubMed=23792957; DOI=10.1074/jbc.M113.482091;
RA   Bjorkblom B., Adilbayeva A., Maple-Grodem J., Piston D., Okvist M.,
RA   Xu X.M., Brede C., Larsen J.P., Moller S.G.;
RT   "Parkinson disease protein DJ-1 binds metals and protects against
RT   metal-induced cytotoxicity.";
RL   J. Biol. Chem. 288:22809-22820(2013).
RN   [34]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [35]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, CAUTION,
RP   MUTAGENESIS OF CYS-46; CYS-53 AND CYS-106, AND COFACTOR.
RX   PubMed=25416785; DOI=10.1074/jbc.M114.597815;
RA   Richarme G., Mihoub M., Dairou J., Bui L.C., Leger T., Lamouri A.;
RT   "Parkinsonism-associated protein DJ-1/Park7 is a major protein
RT   deglycase that repairs methylglyoxal- and glyoxal-glycated cysteine,
RT   arginine and lysine residues.";
RL   J. Biol. Chem. 290:1885-1897(2015).
RN   [36]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
RA   Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [37]
RP   CAUTION.
RX   PubMed=27903648; DOI=10.1074/jbc.M116.743823;
RA   Pfaff D.H., Fleming T., Nawroth P., Teleman A.A.;
RT   "Evidence against a role for the Parkinsonism-associated protein DJ-1
RT   in methylglyoxal detoxification.";
RL   J. Biol. Chem. 292:685-690(2017).
RN   [38]
RP   FUNCTION, AND CAUTION.
RX   PubMed=28013050; DOI=10.1016/j.bbrc.2016.12.134;
RA   Richarme G., Dairou J.;
RT   "Parkinsonism-associated protein DJ-1 is a bona fide deglycase.";
RL   Biochem. Biophys. Res. Commun. 483:387-391(2017).
RN   [39]
RP   FUNCTION, AND INDUCTION BY SULFORAPHANE.
RX   PubMed=26995087; DOI=10.1016/j.bbrc.2016.03.056;
RA   Advedissian T., Deshayes F., Poirier F., Viguier M., Richarme G.;
RT   "The Parkinsonism-associated protein DJ-1/Park7 prevents glycation
RT   damage in human keratinocyte.";
RL   Biochem. Biophys. Res. Commun. 473:87-91(2016).
RN   [40]
RP   FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-106, SUBCELLULAR
RP   LOCATION, AND CAUTION.
RX   PubMed=28596309; DOI=10.1126/science.aag1095;
RA   Richarme G., Liu C., Mihoub M., Abdallah J., Leger T., Joly N.,
RA   Liebart J.C., Jurkunas U.V., Nadal M., Bouloc P., Dairou J.,
RA   Lamouri A.;
RT   "Guanine glycation repair by DJ-1/Park7 and its bacterial homologs.";
RL   Science 357:208-211(2017).
RN   [41]
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), AND HOMODIMERIZATION.
RX   PubMed=12914946; DOI=10.1016/S0014-5793(03)00764-6;
RA   Huai Q., Sun Y., Wang H., Chin L.-S., Li L., Robinson H., Ke H.;
RT   "Crystal structure of DJ-1/RS and implication on familial Parkinson's
RT   disease.";
RL   FEBS Lett. 549:171-175(2003).
RN   [42]
RP   X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF WILD-TYPE AND MUTANT ARG-130,
RP   AND HOMODIMERIZATION.
RX   PubMed=12761214; DOI=10.1074/jbc.M304221200;
RA   Tao X., Tong L.;
RT   "Crystal structure of human DJ-1, a protein associated with early
RT   onset Parkinson's disease.";
RL   J. Biol. Chem. 278:31372-31379(2003).
RN   [43]
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS), AND HOMODIMERIZATION.
RX   PubMed=12796482; DOI=10.1074/jbc.M305878200;
RA   Honbou K., Suzuki N.N., Horiuchi M., Niki T., Taira T., Ariga H.,
RA   Inagaki F.;
RT   "The crystal structure of DJ-1, a protein related to male fertility
RT   and Parkinson's disease.";
RL   J. Biol. Chem. 278:31380-31384(2003).
RN   [44]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, OXIDATION AT CYS-106,
RP   AND HOMODIMERIZATION.
RX   PubMed=12939276; DOI=10.1074/jbc.M304517200;
RA   Lee S.-J., Kim S.J., Kim I.-K., Ko J., Jeong C.-S., Kim G.-H.,
RA   Park C., Kang S.-O., Suh P.-G., Lee H.-S., Cha S.-S.;
RT   "Crystal structures of human DJ-1 and Escherichia coli Hsp31, which
RT   share an evolutionarily conserved domain.";
RL   J. Biol. Chem. 278:44552-44559(2003).
RN   [45]
RP   X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS), HOMODIMERIZATION, OXIDATION,
RP   AND LACK OF PROTEOLYTIC ACTIVITY.
RX   PubMed=12855764; DOI=10.1073/pnas.1133288100;
RA   Wilson M.A., Collins J.L., Hod Y., Ringe D., Petsko G.A.;
RT   "The 1.1-A resolution crystal structure of DJ-1, the protein mutated
RT   in autosomal recessive early onset Parkinson's disease.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:9256-9261(2003).
RN   [46]
RP   X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS), MUTAGENESIS OF CYS-46; CYS-53
RP   AND CYS-106, OXIDATION, FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=15181200; DOI=10.1073/pnas.0402959101;
RA   Canet-Aviles R.M., Wilson M.A., Miller D.W., Ahmad R., McLendon C.,
RA   Bandyopadhyay S., Baptista M.J., Ringe D., Petsko G.A., Cookson M.R.;
RT   "The Parkinson's disease protein DJ-1 is neuroprotective due to
RT   cysteine-sulfinic acid-driven mitochondrial localization.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9103-9108(2004).
RN   [47]
RP   VARIANTS PARK7 ILE-26 AND ALA-149, AND VARIANT GLN-98.
RX   PubMed=12953260; DOI=10.1002/ana.10675;
RA   Abou-Sleiman P.M., Healy D.G., Quinn N., Lees A.J., Wood N.W.;
RT   "The role of pathogenic DJ-1 mutations in Parkinson's disease.";
RL   Ann. Neurol. 54:283-286(2003).
RN   [48]
RP   VARIANT PARK7 PRO-166, AND SUBCELLULAR LOCATION.
RX   PubMed=12446870; DOI=10.1126/science.1077209;
RA   Bonifati V., Rizzu P., van Baren M.J., Schaap O., Breedveld G.J.,
RA   Krieger E., Dekker M.C.J., Squitieri F., Ibanez P., Joosse M.,
RA   van Dongen J.W., Vanacore N., van Swieten J.C., Brice A., Meco G.,
RA   van Duijn C.M., Oostra B.A., Heutink P.;
RT   "Mutations in the DJ-1 gene associated with autosomal recessive early-
RT   onset Parkinsonism.";
RL   Science 299:256-259(2003).
RN   [49]
RP   VARIANT GLN-98.
RX   PubMed=14705128; DOI=10.1002/ana.10816;
RA   Hedrich K., Schaefer N., Hering R., Hagenah J., Lanthaler A.J.,
RA   Schwinger E., Kramer P.L., Ozelius L.J., Bressman S.B., Abbruzzese G.,
RA   Martinelli P., Kostic V., Pramstaller P.P., Vieregge P., Riess O.,
RA   Klein C.;
RT   "The R98Q variation in DJ-1 represents a rare polymorphism.";
RL   Ann. Neurol. 55:145-146(2004).
RN   [50]
RP   VARIANT PARK7 ASP-64, AND X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX   PubMed=15365989; DOI=10.1002/humu.20089;
RA   Hering R., Strauss K.M., Tao X., Bauer A., Woitalla D., Mietz E.M.,
RA   Petrovic S., Bauer P., Schaible W., Mueller T., Schoels L., Klein C.,
RA   Berg D., Meyer P.T., Schulz J.B., Wollnik B., Tong L., Krueger R.,
RA   Riess O.;
RT   "Novel homozygous p.E64D mutation in DJ1 in early onset Parkinson
RT   disease (PARK7).";
RL   Hum. Mutat. 24:321-329(2004).
RN   [51]
RP   CHARACTERIZATION OF VARIANTS PARK7 ASP-64 AND PRO-166.
RX   PubMed=14607841; DOI=10.1074/jbc.M309204200;
RA   Goerner K., Holtorf E., Odoy S., Nuscher B., Yamamoto A., Regula J.T.,
RA   Beyer K., Haass C., Kahle P.J.;
RT   "Differential effects of Parkinson's disease-associated mutations on
RT   stability and folding of DJ-1.";
RL   J. Biol. Chem. 279:6943-6951(2004).
RN   [52]
RP   VARIANT PARK7 THR-104, AND VARIANTS GLN-98 AND SER-171.
RX   PubMed=15254937; DOI=10.1002/mds.20131;
RA   Clark L.N., Afridi S., Mejia-Santana H., Harris J., Louis E.D.,
RA   Cote L.J., Andrews H., Singleton A., Wavrant De-Vrieze F., Hardy J.,
RA   Mayeux R., Fahn S., Waters C., Ford B., Frucht S., Ottman R.,
RA   Marder K.;
RT   "Analysis of an early-onset Parkinson's disease cohort for DJ-1
RT   mutations.";
RL   Mov. Disord. 19:796-800(2004).
RN   [53]
RP   VARIANT GLN-98.
RX   PubMed=14872018; DOI=10.1212/01.WNL.0000113022.51739.88;
RA   Hedrich K., Djarmati A., Schafer N., Hering R., Wellenbrock C.,
RA   Weiss P.H., Hilker R., Vieregge P., Ozelius L.J., Heutink P.,
RA   Bonifati V., Schwinger E., Lang A.E., Noth J., Bressman S.B.,
RA   Pramstaller P.P., Riess O., Klein C.;
RT   "DJ-1 (PARK7) mutations are less frequent than Parkin (PARK2)
RT   mutations in early-onset Parkinson disease.";
RL   Neurology 62:389-394(2004).
RN   [54]
RP   VARIANT LYS-163.
RX   PubMed=16240358; DOI=10.1002/ana.20666;
RA   Annesi G., Savettieri G., Pugliese P., D'Amelio M., Tarantino P.,
RA   Ragonese P., La Bella V., Piccoli T., Civitelli D., Annesi F.,
RA   Fierro B., Piccoli F., Arabia G., Caracciolo M., Ciro Candiano I.C.,
RA   Quattrone A.;
RT   "DJ-1 mutations and parkinsonism-dementia-amyotrophic lateral
RT   sclerosis complex.";
RL   Ann. Neurol. 58:803-807(2005).
RN   [55]
RP   VARIANT SER-39.
RX   PubMed=16632486; DOI=10.1093/hmg/ddl104;
RA   Tang B., Xiong H., Sun P., Zhang Y., Wang D., Hu Z., Zhu Z., Ma H.,
RA   Pan Q., Xia J.-H., Xia K., Zhang Z.;
RT   "Association of PINK1 and DJ-1 confers digenic inheritance of early-
RT   onset Parkinson's disease.";
RL   Hum. Mol. Genet. 15:1816-1825(2006).
RN   [56]
RP   CHARACTERIZATION OF VARIANT PARK7 PRO-166.
RX   PubMed=17846173; DOI=10.1083/jcb.200611128;
RA   Olzmann J.A., Li L., Chudaev M.V., Chen J., Perez F.A., Palmiter R.D.,
RA   Chin L.S.;
RT   "Parkin-mediated K63-linked polyubiquitination targets misfolded DJ-1
RT   to aggresomes via binding to HDAC6.";
RL   J. Cell Biol. 178:1025-1038(2007).
RN   [57]
RP   VARIANT ASP-64, AND FUNCTION.
RX   PubMed=20186336; DOI=10.1371/journal.pone.0009367;
RA   Krebiehl G., Ruckerbauer S., Burbulla L.F., Kieper N., Maurer B.,
RA   Waak J., Wolburg H., Gizatullina Z., Gellerich F.N., Woitalla D.,
RA   Riess O., Kahle P.J., Proikas-Cezanne T., Kruger R.;
RT   "Reduced basal autophagy and impaired mitochondrial dynamics due to
RT   loss of Parkinson's disease-associated protein DJ-1.";
RL   PLoS ONE 5:E9367-E9367(2010).
CC   -!- FUNCTION: Protein and nucleotide deglycase that catalyzes the
CC       deglycation of the Maillard adducts formed between amino groups of
CC       proteins or nucleotides and reactive carbonyl groups of glyoxals
CC       (PubMed:25416785, PubMed:28596309). Thus, functions as a protein
CC       deglycase that repairs methylglyoxal- and glyoxal-glycated
CC       proteins, and releases repaired proteins and lactate or glycolate,
CC       respectively. Deglycates cysteine, arginine and lysine residues in
CC       proteins, and thus reactivates these proteins by reversing
CC       glycation by glyoxals. Acts on early glycation intermediates
CC       (hemithioacetals and aminocarbinols), preventing the formation of
CC       advanced glycation endproducts (AGE) that cause irreversible
CC       damage (PubMed:25416785, PubMed:28013050, PubMed:26995087). Also
CC       functions as a nucleotide deglycase able to repair glycated
CC       guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in
CC       DNA and RNA. Is thus involved in a major nucleotide repair system
CC       named guanine glycation repair (GG repair), dedicated to reversing
CC       methylglyoxal and glyoxal damage via nucleotide sanitization and
CC       direct nucleic acid repair (PubMed:28596309). Also displays an
CC       apparent glyoxalase activity that in fact reflects its deglycase
CC       activity (PubMed:22523093). Plays an important role in cell
CC       protection against oxidative stress and cell death acting as
CC       oxidative stress sensor and redox-sensitive chaperone and
CC       protease; functions probably related to its primary function
CC       (PubMed:17015834, PubMed:20304780, PubMed:18711745,
CC       PubMed:12796482, PubMed:19229105, PubMed:25416785,
CC       PubMed:26995087). It is involved in neuroprotective mechanisms
CC       like the stabilization of NFE2L2 and PINK1 proteins, male
CC       fertility as a positive regulator of androgen signaling pathway as
CC       well as cell growth and transformation through, for instance, the
CC       modulation of NF-kappa-B signaling pathway (PubMed:12612053,
CC       PubMed:15502874, PubMed:14749723, PubMed:17015834,
CC       PubMed:21097510, PubMed:18711745). Eliminates hydrogen peroxide
CC       and protects cells against hydrogen peroxide-induced cell death
CC       (PubMed:16390825). Required for correct mitochondrial morphology
CC       and function as well as for autophagy of dysfunctional
CC       mitochondria (PubMed:19229105, PubMed:16632486). Plays a role in
CC       regulating expression or stability of the mitochondrial uncoupling
CC       proteins SLC25A14 and SLC25A27 in dopaminergic neurons of the
CC       substantia nigra pars compacta and attenuates the oxidative stress
CC       induced by calcium entry into the neurons via L-type channels
CC       during pacemaking (PubMed:18711745). Regulates astrocyte
CC       inflammatory responses, may modulate lipid rafts-dependent
CC       endocytosis in astrocytes and neuronal cells (PubMed:23847046). In
CC       pancreatic islets, involved in the maintenance of mitochondrial
CC       reactive oxygen species (ROS) levels and glucose homeostasis in an
CC       age- and diet dependent manner. Protects pancreatic beta cells
CC       from cell death induced by inflammatory and cytotoxic setting (By
CC       similarity). Binds to a number of mRNAs containing multiple copies
CC       of GG or CC motifs and partially inhibits their translation but
CC       dissociates following oxidative stress (PubMed:18626009). Metal-
CC       binding protein able to bind copper as well as toxic mercury ions,
CC       enhances the cell protection mechanism against induced metal
CC       toxicity (PubMed:23792957). In macrophages, interacts with the
CC       NADPH oxidase subunit NCF1 to direct NADPH oxidase-dependent ROS
CC       production, and protects against sepsis (By similarity).
CC       {ECO:0000250|UniProtKB:Q99LX0, ECO:0000269|PubMed:11477070,
CC       ECO:0000269|PubMed:12612053, ECO:0000269|PubMed:12855764,
CC       ECO:0000269|PubMed:12939276, ECO:0000269|PubMed:14749723,
CC       ECO:0000269|PubMed:15181200, ECO:0000269|PubMed:15502874,
CC       ECO:0000269|PubMed:15976810, ECO:0000269|PubMed:16390825,
CC       ECO:0000269|PubMed:17015834, ECO:0000269|PubMed:18626009,
CC       ECO:0000269|PubMed:18711745, ECO:0000269|PubMed:19229105,
CC       ECO:0000269|PubMed:20186336, ECO:0000269|PubMed:20304780,
CC       ECO:0000269|PubMed:21097510, ECO:0000269|PubMed:22523093,
CC       ECO:0000269|PubMed:23792957, ECO:0000269|PubMed:23847046,
CC       ECO:0000269|PubMed:25416785, ECO:0000269|PubMed:26995087,
CC       ECO:0000269|PubMed:28013050, ECO:0000269|PubMed:28596309,
CC       ECO:0000269|PubMed:9070310}.
CC   -!- CATALYTIC ACTIVITY: An N(omega)-(1-hydroxy-2-oxopropyl)-[protein]-
CC       L-arginine + H(2)O = a [protein]-L-arginine + (R)-lactate.
CC       {ECO:0000269|PubMed:25416785}.
CC   -!- CATALYTIC ACTIVITY: An N(6)-(1-hydroxy-2-oxopropyl)-[protein]-L-
CC       lysine + H(2)O = a [protein]-L-lysine + (R)-lactate.
CC       {ECO:0000269|PubMed:25416785}.
CC   -!- CATALYTIC ACTIVITY: An S-(1-hydroxy-2-oxopropyl)-[protein]-L-
CC       cysteine + H(2)O = a [protein]-L-cysteine + (R)-lactate.
CC       {ECO:0000269|PubMed:25416785}.
CC   -!- COFACTOR:
CC       Note=Deglycase activity does not require glutathione as a
CC       cofactor, however, glycated glutathione constitutes a PARK7
CC       substrate. {ECO:0000269|PubMed:25416785};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=173.4 uM for casein {ECO:0000269|PubMed:20304780};
CC         KM=0.44 mM for glycated N-acetylarginine (at pH 7.0 and 22
CC         degrees Celsius) {ECO:0000269|PubMed:25416785};
CC         KM=0.35 mM for glycated N-acetyllysine (at pH 7.0 and 22 degrees
CC         Celsius) {ECO:0000269|PubMed:25416785};
CC         KM=0.32 mM for glycated N-acetylcysteine (at pH 7.0 and 22
CC         degrees Celsius) {ECO:0000269|PubMed:25416785};
CC         Note=kcat is 0.27 sec(-1) for the deglycation of glycated N-
CC         acetylarginine. kcat is 0.28 sec(-1) for the deglycation of
CC         glycated N-acetyllysine. kcat is 0.42 sec(-1) for the
CC         deglycation of glycated N-acetylcysteine.
CC         {ECO:0000269|PubMed:25416785};
CC   -!- SUBUNIT: Homodimer (PubMed:12851414, PubMed:12796482,
CC       PubMed:12855764). Binds EFCAB6/DJBP and PIAS2 (PubMed:11477070,
CC       PubMed:12851414, PubMed:12612053). Part of a ternary complex
CC       containing PARK7, EFCAB6/DJBP and AR (PubMed:12612053). Interacts
CC       (via N-terminus) with OTUD7B (PubMed:21097510). Interacts with
CC       BBS1, HIPK1, CLCF1 and MTERF (PubMed:16390825, PubMed:21097510).
CC       Forms a complex with PINK1 and PRKN (PubMed:19229105). Interacts
CC       (via C-terminus) with NCF1; the interaction is enhanced by LPS and
CC       modulates NCF1 phosphorylation and membrane translocation (By
CC       similarity). {ECO:0000250|UniProtKB:Q99LX0,
CC       ECO:0000269|PubMed:11477070, ECO:0000269|PubMed:12612053,
CC       ECO:0000269|PubMed:12796482, ECO:0000269|PubMed:12851414,
CC       ECO:0000269|PubMed:12855764, ECO:0000269|PubMed:16390825,
CC       ECO:0000269|PubMed:21097510}.
CC   -!- INTERACTION:
CC       Self; NbExp=3; IntAct=EBI-1164361, EBI-1164361;
CC       P10275:AR; NbExp=6; IntAct=EBI-1164361, EBI-608057;
CC       Q9UER7:DAXX; NbExp=3; IntAct=EBI-1164361, EBI-77321;
CC       Q13158:FADD; NbExp=9; IntAct=EBI-1164361, EBI-494804;
CC       Q9HD26:GOPC; NbExp=3; IntAct=EBI-1164361, EBI-349832;
CC       O94776:MTA2; NbExp=3; IntAct=EBI-1164361, EBI-1783035;
CC       Q6GQQ9:OTUD7B; NbExp=3; IntAct=EBI-1164361, EBI-527784;
CC       P32322:PYCR1; NbExp=5; IntAct=EBI-1164361, EBI-848624;
CC       P63244:RACK1; NbExp=4; IntAct=EBI-1164361, EBI-296739;
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000250|UniProtKB:O88767}; Lipid-anchor
CC       {ECO:0000250|UniProtKB:O88767}. Cytoplasm
CC       {ECO:0000269|PubMed:12851414, ECO:0000269|PubMed:14579415,
CC       ECO:0000269|PubMed:15976810, ECO:0000269|PubMed:19229105,
CC       ECO:0000269|PubMed:28596309}. Nucleus
CC       {ECO:0000269|PubMed:12851414, ECO:0000269|PubMed:14579415,
CC       ECO:0000269|PubMed:15976810, ECO:0000269|PubMed:16390825,
CC       ECO:0000269|PubMed:28596309}. Membrane raft
CC       {ECO:0000250|UniProtKB:O88767}. Mitochondrion
CC       {ECO:0000269|PubMed:15181200, ECO:0000269|PubMed:18711745,
CC       ECO:0000269|PubMed:19229105}. Note=Under normal conditions,
CC       located predominantly in the cytoplasm and, to a lesser extent, in
CC       the nucleus and mitochondrion. Translocates to the mitochondrion
CC       and subsequently to the nucleus in response to oxidative stress
CC       and exerts an increased cytoprotective effect against oxidative
CC       damage (PubMed:18711745). Detected in tau inclusions in brains
CC       from neurodegenerative disease patients (PubMed:14705119).
CC       Membrane raft localization in astrocytes and neuronal cells
CC       requires palmitoylation. {ECO:0000269|PubMed:14705119,
CC       ECO:0000269|PubMed:18711745}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in pancreas, kidney, skeletal
CC       muscle, liver, testis and heart. Detected at slightly lower levels
CC       in placenta and brain (at protein level). Detected in astrocytes,
CC       Sertoli cells, spermatogonia, spermatids and spermatozoa.
CC       Expressed by pancreatic islets at higher levels than surrounding
CC       exocrine tissues (PubMed:22611253). {ECO:0000269|PubMed:14579415,
CC       ECO:0000269|PubMed:14662519, ECO:0000269|PubMed:14705119,
CC       ECO:0000269|PubMed:22611253, ECO:0000269|PubMed:9070310}.
CC   -!- DEVELOPMENTAL STAGE: In pancreatic islets, expression increases
CC       during aging. {ECO:0000269|PubMed:22611253}.
CC   -!- INDUCTION: By hydrogen peroxide and UV irradiation
CC       (PubMed:14749723, PubMed:15976810). In pancreatic islets,
CC       expression increases under hyperglycemic conditions
CC       (PubMed:22611253). Expression is also induced by sulforaphane, an
CC       isothiocyanate obtained from cruciferous vegetables
CC       (PubMed:26995087). {ECO:0000269|PubMed:14749723,
CC       ECO:0000269|PubMed:15976810, ECO:0000269|PubMed:22611253,
CC       ECO:0000269|PubMed:26995087}.
CC   -!- PTM: Sumoylated on Lys-130 by PIAS2 or PIAS4; which is enhanced
CC       after ultraviolet irradiation and essential for cell-growth
CC       promoting activity and transforming activity.
CC       {ECO:0000269|PubMed:15976810}.
CC   -!- PTM: Cys-106 is easily oxidized to sulfinic acid.
CC       {ECO:0000269|PubMed:12939276, ECO:0000269|PubMed:15976810}.
CC   -!- PTM: Undergoes cleavage of a C-terminal peptide and subsequent
CC       activation of protease activity in response to oxidative stress.
CC       {ECO:0000269|PubMed:20304780}.
CC   -!- DISEASE: Parkinson disease 7 (PARK7) [MIM:606324]: A
CC       neurodegenerative disorder characterized by resting tremor,
CC       postural tremor, bradykinesia, muscular rigidity, anxiety and
CC       psychotic episodes. PARK7 has onset before 40 years, slow
CC       progression and initial good response to levodopa. Some patients
CC       may show traits reminiscent of amyotrophic lateral sclerosis-
CC       parkinsonism/dementia complex (Guam disease).
CC       {ECO:0000269|PubMed:12446870, ECO:0000269|PubMed:12851414,
CC       ECO:0000269|PubMed:12953260, ECO:0000269|PubMed:14607841,
CC       ECO:0000269|PubMed:14713311, ECO:0000269|PubMed:15254937,
CC       ECO:0000269|PubMed:15365989, ECO:0000269|PubMed:17846173,
CC       ECO:0000269|PubMed:19229105, ECO:0000269|PubMed:22523093,
CC       ECO:0000269|PubMed:23792957, ECO:0000269|PubMed:23847046}.
CC       Note=The disease is caused by mutations affecting the gene
CC       represented in this entry.
CC   -!- SIMILARITY: Belongs to the peptidase C56 family. {ECO:0000305}.
CC   -!- CAUTION: Glyoxalase activity was previously reported
CC       (PubMed:22523093). It may however reflect its deglycase activity
CC       (PubMed:25416785). {ECO:0000269|PubMed:22523093,
CC       ECO:0000269|PubMed:25416785}.
CC   -!- CAUTION: The protein deglycation activity has been ascribed to a
CC       TRIS buffer artifact by a publication (PubMed:27903648). However,
CC       clear biochemical experiments showing that PARK7 is a bona fide
CC       deglycase have been performed (PubMed:25416785, PubMed:28013050).
CC       Deglycase activity is even strengthened by a an article that
CC       reports nucleotide deglycation activity (PubMed:28596309).
CC       {ECO:0000269|PubMed:25416785, ECO:0000269|PubMed:27903648,
CC       ECO:0000269|PubMed:28013050, ECO:0000269|PubMed:28596309}.
CC   -!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
CC       polymorphism database;
CC       URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=P&genename=PARK7+%40+DJ-1";
DR   EMBL; D61380; BAA09603.2; -; mRNA.
DR   EMBL; AF021819; AAC12806.1; -; mRNA.
DR   EMBL; AB073864; BAB71782.1; -; mRNA.
DR   EMBL; AK312000; BAG34938.1; -; mRNA.
DR   EMBL; AL034417; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471130; EAW71591.1; -; Genomic_DNA.
DR   EMBL; BC008188; AAH08188.1; -; mRNA.
DR   EMBL; AB045294; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AY648999; AAT68961.1; -; Genomic_DNA.
DR   CCDS; CCDS93.1; -.
DR   PIR; JC5394; JC5394.
DR   RefSeq; NP_001116849.1; NM_001123377.1.
DR   RefSeq; NP_009193.2; NM_007262.4.
DR   RefSeq; XP_005263481.1; XM_005263424.3.
DR   UniGene; Hs.419640; -.
DR   PDB; 1J42; X-ray; 2.50 A; A=1-189.
DR   PDB; 1P5F; X-ray; 1.10 A; A=1-189.
DR   PDB; 1PDV; X-ray; 1.80 A; A=1-189.
DR   PDB; 1PDW; X-ray; 2.20 A; A/B/C/D/E/F/G/H=1-189.
DR   PDB; 1PE0; X-ray; 1.70 A; A/B=1-189.
DR   PDB; 1Q2U; X-ray; 1.60 A; A=1-189.
DR   PDB; 1SOA; X-ray; 1.20 A; A=1-189.
DR   PDB; 1UCF; X-ray; 1.95 A; A/B=1-189.
DR   PDB; 2OR3; X-ray; 1.20 A; A/B=1-189.
DR   PDB; 2R1T; X-ray; 1.70 A; A/B=2-188.
DR   PDB; 2R1U; X-ray; 1.50 A; A/B=2-188.
DR   PDB; 2R1V; X-ray; 1.70 A; A/B=2-188.
DR   PDB; 2RK3; X-ray; 1.05 A; A=1-189.
DR   PDB; 2RK4; X-ray; 1.15 A; A=1-189.
DR   PDB; 2RK6; X-ray; 1.15 A; A=1-189.
DR   PDB; 3B36; X-ray; 1.50 A; A=1-189.
DR   PDB; 3B38; X-ray; 1.85 A; A=1-189.
DR   PDB; 3B3A; X-ray; 1.50 A; A=1-189.
DR   PDB; 3BWE; X-ray; 2.40 A; A/B/C/D/E/F/G=1-189.
DR   PDB; 3CY6; X-ray; 1.35 A; A=1-189.
DR   PDB; 3CYF; X-ray; 1.60 A; A=1-189.
DR   PDB; 3CZ9; X-ray; 1.15 A; A=1-189.
DR   PDB; 3CZA; X-ray; 1.20 A; A=1-189.
DR   PDB; 3EZG; X-ray; 1.15 A; A=1-189.
DR   PDB; 3F71; X-ray; 1.20 A; A=1-189.
DR   PDB; 3SF8; X-ray; 1.56 A; A/B=1-189.
DR   PDB; 4BTE; X-ray; 1.38 A; A=1-189.
DR   PDB; 4MNT; X-ray; 1.58 A; A=1-189.
DR   PDB; 4MTC; X-ray; 1.47 A; A=1-189.
DR   PDB; 4N0M; X-ray; 1.95 A; A=1-189.
DR   PDB; 4N12; X-ray; 1.48 A; A=1-189.
DR   PDB; 4OGF; X-ray; 1.60 A; A=2-188.
DR   PDB; 4OQ4; X-ray; 1.49 A; A=1-189.
DR   PDB; 4P2G; X-ray; 1.35 A; A=1-189.
DR   PDB; 4P34; X-ray; 1.55 A; A=1-189.
DR   PDB; 4P35; X-ray; 1.75 A; A=1-189.
DR   PDB; 4P36; X-ray; 1.18 A; A=1-189.
DR   PDB; 4RKW; X-ray; 1.50 A; A=1-189.
DR   PDB; 4RKY; X-ray; 1.50 A; A=1-189.
DR   PDB; 4S0Z; X-ray; 1.45 A; A=1-189.
DR   PDB; 4ZGG; X-ray; 1.23 A; A=1-189.
DR   PDB; 5IP5; X-ray; 1.66 A; A=1-189.
DR   PDB; 5SY6; X-ray; 1.15 A; A=1-189.
DR   PDB; 5SY9; X-ray; 1.10 A; A=1-189.
DR   PDB; 5SYA; X-ray; 1.10 A; A=1-189.
DR   PDBsum; 1J42; -.
DR   PDBsum; 1P5F; -.
DR   PDBsum; 1PDV; -.
DR   PDBsum; 1PDW; -.
DR   PDBsum; 1PE0; -.
DR   PDBsum; 1Q2U; -.
DR   PDBsum; 1SOA; -.
DR   PDBsum; 1UCF; -.
DR   PDBsum; 2OR3; -.
DR   PDBsum; 2R1T; -.
DR   PDBsum; 2R1U; -.
DR   PDBsum; 2R1V; -.
DR   PDBsum; 2RK3; -.
DR   PDBsum; 2RK4; -.
DR   PDBsum; 2RK6; -.
DR   PDBsum; 3B36; -.
DR   PDBsum; 3B38; -.
DR   PDBsum; 3B3A; -.
DR   PDBsum; 3BWE; -.
DR   PDBsum; 3CY6; -.
DR   PDBsum; 3CYF; -.
DR   PDBsum; 3CZ9; -.
DR   PDBsum; 3CZA; -.
DR   PDBsum; 3EZG; -.
DR   PDBsum; 3F71; -.
DR   PDBsum; 3SF8; -.
DR   PDBsum; 4BTE; -.
DR   PDBsum; 4MNT; -.
DR   PDBsum; 4MTC; -.
DR   PDBsum; 4N0M; -.
DR   PDBsum; 4N12; -.
DR   PDBsum; 4OGF; -.
DR   PDBsum; 4OQ4; -.
DR   PDBsum; 4P2G; -.
DR   PDBsum; 4P34; -.
DR   PDBsum; 4P35; -.
DR   PDBsum; 4P36; -.
DR   PDBsum; 4RKW; -.
DR   PDBsum; 4RKY; -.
DR   PDBsum; 4S0Z; -.
DR   PDBsum; 4ZGG; -.
DR   PDBsum; 5IP5; -.
DR   PDBsum; 5SY6; -.
DR   PDBsum; 5SY9; -.
DR   PDBsum; 5SYA; -.
DR   ProteinModelPortal; Q99497; -.
DR   SMR; Q99497; -.
DR   BioGrid; 116446; 88.
DR   CORUM; Q99497; -.
DR   DIP; DIP-35515N; -.
DR   IntAct; Q99497; 46.
DR   MINT; MINT-5003468; -.
DR   STRING; 9606.ENSP00000340278; -.
DR   MEROPS; C56.002; -.
DR   iPTMnet; Q99497; -.
DR   PhosphoSitePlus; Q99497; -.
DR   SwissPalm; Q99497; -.
DR   BioMuta; PARK7; -.
DR   DMDM; 56404943; -.
DR   OGP; Q99497; -.
DR   REPRODUCTION-2DPAGE; IPI00298547; -.
DR   UCD-2DPAGE; Q99497; -.
DR   EPD; Q99497; -.
DR   PaxDb; Q99497; -.
DR   PeptideAtlas; Q99497; -.
DR   PRIDE; Q99497; -.
DR   TopDownProteomics; Q99497; -.
DR   DNASU; 11315; -.
DR   Ensembl; ENST00000338639; ENSP00000340278; ENSG00000116288.
DR   Ensembl; ENST00000377488; ENSP00000366708; ENSG00000116288.
DR   Ensembl; ENST00000377491; ENSP00000366711; ENSG00000116288.
DR   Ensembl; ENST00000493373; ENSP00000465404; ENSG00000116288.
DR   Ensembl; ENST00000493678; ENSP00000418770; ENSG00000116288.
DR   GeneID; 11315; -.
DR   KEGG; hsa:11315; -.
DR   CTD; 11315; -.
DR   DisGeNET; 11315; -.
DR   EuPathDB; HostDB:ENSG00000116288.12; -.
DR   GeneCards; PARK7; -.
DR   GeneReviews; PARK7; -.
DR   HGNC; HGNC:16369; PARK7.
DR   HPA; CAB005870; -.
DR   HPA; HPA004190; -.
DR   MalaCards; PARK7; -.
DR   MIM; 168600; phenotype.
DR   MIM; 602533; gene.
DR   MIM; 606324; phenotype.
DR   neXtProt; NX_Q99497; -.
DR   OpenTargets; ENSG00000116288; -.
DR   Orphanet; 90020; Amyotrophic lateral sclerosis-parkinsonism-dementia complex.
DR   Orphanet; 2828; Young adult-onset Parkinsonism.
DR   PharmGKB; PA32946; -.
DR   eggNOG; KOG2764; Eukaryota.
DR   eggNOG; COG0693; LUCA.
DR   GeneTree; ENSGT00390000001231; -.
DR   HOGENOM; HOG000063194; -.
DR   HOVERGEN; HBG053511; -.
DR   InParanoid; Q99497; -.
DR   KO; K05687; -.
DR   OMA; TCYPGFE; -.
DR   OrthoDB; EOG091G12NS; -.
DR   PhylomeDB; Q99497; -.
DR   TreeFam; TF300119; -.
DR   SABIO-RK; Q99497; -.
DR   SignaLink; Q99497; -.
DR   SIGNOR; Q99497; -.
DR   ChiTaRS; PARK7; human.
DR   EvolutionaryTrace; Q99497; -.
DR   GeneWiki; PARK7; -.
DR   GenomeRNAi; 11315; -.
DR   PMAP-CutDB; Q99497; -.
DR   PRO; PR:Q99497; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   Bgee; ENSG00000116288; -.
DR   CleanEx; HS_PARK7; -.
DR   ExpressionAtlas; Q99497; baseline and differential.
DR   Genevisible; Q99497; HS.
DR   GO; GO:0030424; C:axon; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0044297; C:cell body; IEA:Ensembl.
DR   GO; GO:0005913; C:cell-cell adherens junction; IDA:BHF-UCL.
DR   GO; GO:0000785; C:chromatin; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl.
DR   GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR   GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR   GO; GO:0005758; C:mitochondrial intermembrane space; IEA:Ensembl.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016605; C:PML body; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0050681; F:androgen receptor binding; IPI:ParkinsonsUK-UCL.
DR   GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
DR   GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
DR   GO; GO:1903135; F:cupric ion binding; IDA:ParkinsonsUK-UCL.
DR   GO; GO:1903136; F:cuprous ion binding; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0019955; F:cytokine binding; IPI:ParkinsonsUK-UCL.
DR   GO; GO:0019899; F:enzyme binding; IPI:ParkinsonsUK-UCL.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR   GO; GO:0036478; F:L-dopa decarboxylase activator activity; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0045340; F:mercury ion binding; IDA:UniProtKB.
DR   GO; GO:0003729; F:mRNA binding; IDA:UniProtKB.
DR   GO; GO:0016684; F:oxidoreductase activity, acting on peroxide as acceptor; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0008233; F:peptidase activity; IDA:UniProtKB.
DR   GO; GO:0051920; F:peroxiredoxin activity; IEA:Ensembl.
DR   GO; GO:0036524; F:protein deglycase activity; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0005102; F:receptor binding; IPI:UniProtKB.
DR   GO; GO:0070491; F:repressing transcription factor binding; IPI:ParkinsonsUK-UCL.
DR   GO; GO:0097110; F:scaffold protein binding; IPI:ParkinsonsUK-UCL.
DR   GO; GO:0044388; F:small protein activating enzyme binding; IPI:ParkinsonsUK-UCL.
DR   GO; GO:0016532; F:superoxide dismutase copper chaperone activity; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0003713; F:transcription coactivator activity; IGI:ParkinsonsUK-UCL.
DR   GO; GO:0008134; F:transcription factor binding; IPI:ParkinsonsUK-UCL.
DR   GO; GO:0036470; F:tyrosine 3-monooxygenase activator activity; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0044390; F:ubiquitin-like protein conjugating enzyme binding; IPI:ParkinsonsUK-UCL.
DR   GO; GO:1990381; F:ubiquitin-specific protease binding; IPI:ParkinsonsUK-UCL.
DR   GO; GO:0032148; P:activation of protein kinase B activity; IC:ParkinsonsUK-UCL.
DR   GO; GO:0008344; P:adult locomotory behavior; IEA:Ensembl.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0036471; P:cellular response to glyoxal; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:UniProtKB.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0010273; P:detoxification of copper ion; IMP:UniProtKB.
DR   GO; GO:0050787; P:detoxification of mercury ion; IMP:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; IDA:UniProtKB.
DR   GO; GO:0051583; P:dopamine uptake involved in synaptic transmission; IEA:Ensembl.
DR   GO; GO:0018323; P:enzyme active site formation via L-cysteine sulfinic acid; IEA:Ensembl.
DR   GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR   GO; GO:0036531; P:glutathione deglycation; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0046295; P:glycolate biosynthetic process; IDA:ParkinsonsUK-UCL.
DR   GO; GO:1903189; P:glyoxal metabolic process; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0106044; P:guanine deglycation; IDA:UniProtKB.
DR   GO; GO:0106046; P:guanine deglycation, glyoxal removal; IDA:UniProtKB.
DR   GO; GO:0106045; P:guanine deglycation, methylglyoxal removal; IDA:UniProtKB.
DR   GO; GO:0042743; P:hydrogen peroxide metabolic process; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR   GO; GO:0030073; P:insulin secretion; ISS:UniProtKB.
DR   GO; GO:0019249; P:lactate biosynthetic process; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0051899; P:membrane depolarization; IEA:Ensembl.
DR   GO; GO:0060081; P:membrane hyperpolarization; IEA:Ensembl.
DR   GO; GO:0009438; P:methylglyoxal metabolic process; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0007005; P:mitochondrion organization; ISS:UniProtKB.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0060548; P:negative regulation of cell death; IDA:UniProtKB.
DR   GO; GO:2001268; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IMP:ParkinsonsUK-UCL.
DR   GO; GO:1903073; P:negative regulation of death-inducing signaling complex assembly; IC:ParkinsonsUK-UCL.
DR   GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IGI:ParkinsonsUK-UCL.
DR   GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:UniProtKB.
DR   GO; GO:0010629; P:negative regulation of gene expression; IDA:ParkinsonsUK-UCL.
DR   GO; GO:1903206; P:negative regulation of hydrogen peroxide-induced cell death; IMP:ParkinsonsUK-UCL.
DR   GO; GO:1903208; P:negative regulation of hydrogen peroxide-induced neuron death; IDA:ParkinsonsUK-UCL.
DR   GO; GO:1903384; P:negative regulation of hydrogen peroxide-induced neuron intrinsic apoptotic signaling pathway; IGI:ParkinsonsUK-UCL.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:BHF-UCL.
DR   GO; GO:1901215; P:negative regulation of neuron death; IDA:ParkinsonsUK-UCL.
DR   GO; GO:1905259; P:negative regulation of nitrosative stress-induced intrinsic apoptotic signaling pathway; IDA:ParkinsonsUK-UCL.
DR   GO; GO:1903202; P:negative regulation of oxidative stress-induced cell death; IDA:ParkinsonsUK-UCL.
DR   GO; GO:1903377; P:negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:ParkinsonsUK-UCL.
DR   GO; GO:1901984; P:negative regulation of protein acetylation; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0032091; P:negative regulation of protein binding; IDA:UniProtKB.
DR   GO; GO:0046826; P:negative regulation of protein export from nucleus; IGI:ParkinsonsUK-UCL.
DR   GO; GO:1903094; P:negative regulation of protein K48-linked deubiquitination; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0006469; P:negative regulation of protein kinase activity; IGI:ParkinsonsUK-UCL.
DR   GO; GO:0001933; P:negative regulation of protein phosphorylation; IGI:ParkinsonsUK-UCL.
DR   GO; GO:0033234; P:negative regulation of protein sumoylation; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0031397; P:negative regulation of protein ubiquitination; IDA:ParkinsonsUK-UCL.
DR   GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; ISS:UniProtKB.
DR   GO; GO:1903122; P:negative regulation of TRAIL-activated apoptotic signaling pathway; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0051444; P:negative regulation of ubiquitin-protein transferase activity; IDA:ParkinsonsUK-UCL.
DR   GO; GO:2000157; P:negative regulation of ubiquitin-specific protease activity; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0036527; P:peptidyl-arginine deglycation; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0036526; P:peptidyl-cysteine deglycation; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0036528; P:peptidyl-lysine deglycation; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0002866; P:positive regulation of acute inflammatory response to antigenic stimulus; ISS:UniProtKB.
DR   GO; GO:2000825; P:positive regulation of androgen receptor activity; IMP:ParkinsonsUK-UCL.
DR   GO; GO:1903599; P:positive regulation of autophagy of mitochondrion; NAS:ParkinsonsUK-UCL.
DR   GO; GO:1903181; P:positive regulation of dopamine biosynthetic process; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0010628; P:positive regulation of gene expression; TAS:ParkinsonsUK-UCL.
DR   GO; GO:0032757; P:positive regulation of interleukin-8 production; IDA:ParkinsonsUK-UCL.
DR   GO; GO:1903197; P:positive regulation of L-dopa biosynthetic process; IMP:ParkinsonsUK-UCL.
DR   GO; GO:1903200; P:positive regulation of L-dopa decarboxylase activity; IDA:ParkinsonsUK-UCL.
DR   GO; GO:1902958; P:positive regulation of mitochondrial electron transport, NADH to ubiquinone; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0033864; P:positive regulation of NAD(P)H oxidase activity; ISS:UniProtKB.
DR   GO; GO:2000277; P:positive regulation of oxidative phosphorylation uncoupler activity; IEA:Ensembl.
DR   GO; GO:1902177; P:positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0090073; P:positive regulation of protein homodimerization activity; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0051897; P:positive regulation of protein kinase B signaling; IC:ParkinsonsUK-UCL.
DR   GO; GO:1900182; P:positive regulation of protein localization to nucleus; IDA:ParkinsonsUK-UCL.
DR   GO; GO:1903168; P:positive regulation of pyrroline-5-carboxylate reductase activity; IDA:ParkinsonsUK-UCL.
DR   GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; IEA:Ensembl.
DR   GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IMP:ParkinsonsUK-UCL.
DR   GO; GO:1901671; P:positive regulation of superoxide dismutase activity; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:ParkinsonsUK-UCL.
DR   GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; IMP:ParkinsonsUK-UCL.
DR   GO; GO:1903178; P:positive regulation of tyrosine 3-monooxygenase activity; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0036529; P:protein deglycation, glyoxal removal; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0036530; P:protein deglycation, methylglyoxal removal; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0006517; P:protein deglycosylation; IDA:UniProtKB.
DR   GO; GO:0050821; P:protein stabilization; IDA:ParkinsonsUK-UCL.
DR   GO; GO:0007265; P:Ras protein signal transduction; TAS:ParkinsonsUK-UCL.
DR   GO; GO:0060765; P:regulation of androgen receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0050727; P:regulation of inflammatory response; ISS:UniProtKB.
DR   GO; GO:0051881; P:regulation of mitochondrial membrane potential; IMP:ParkinsonsUK-UCL.
DR   GO; GO:0043523; P:regulation of neuron apoptotic process; IDA:UniProtKB.
DR   GO; GO:1902903; P:regulation of supramolecular fiber organization; TAS:ParkinsonsUK-UCL.
DR   GO; GO:0007338; P:single fertilization; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR006287; DJ-1.
DR   InterPro; IPR002818; DJ-1/PfpI.
DR   Pfam; PF01965; DJ-1_PfpI; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   TIGRFAMs; TIGR01383; not_thiJ; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Autophagy; Cell membrane; Chaperone;
KW   Complete proteome; Copper; Cytoplasm; Direct protein sequencing;
KW   Disease mutation; DNA damage; DNA repair; Fertilization; Hydrolase;
KW   Inflammatory response; Isopeptide bond; Lipoprotein; Membrane;
KW   Mitochondrion; Neurodegeneration; Nucleus; Oxidation; Palmitate;
KW   Parkinson disease; Parkinsonism; Phosphoprotein; Polymorphism;
KW   Protease; Reference proteome; RNA-binding; Stress response;
KW   Tumor suppressor; Ubl conjugation; Zymogen.
FT   INIT_MET      1      1       Removed. {ECO:0000244|PubMed:25944712}.
FT   CHAIN         2      ?       Protein/nucleic acid deglycase DJ-1.
FT                                /FTId=PRO_0000157849.
FT   PROPEP        ?    189       Removed in mature form.
FT                                /FTId=PRO_0000405558.
FT   ACT_SITE    106    106       Nucleophile.
FT                                {ECO:0000305|PubMed:20304780,
FT                                ECO:0000305|PubMed:25416785}.
FT   ACT_SITE    126    126       {ECO:0000305|PubMed:20304780}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000244|PubMed:25944712}.
FT   MOD_RES      67     67       Phosphotyrosine.
FT                                {ECO:0000244|PubMed:15592455}.
FT   MOD_RES     106    106       Cysteine sulfinic acid (-SO2H);
FT                                alternate. {ECO:0000269|PubMed:12939276}.
FT   MOD_RES     148    148       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q99LX0}.
FT   MOD_RES     182    182       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:Q99LX0}.
FT   LIPID        46     46       S-palmitoyl cysteine.
FT                                {ECO:0000269|PubMed:23847046}.
FT   LIPID        53     53       S-palmitoyl cysteine.
FT                                {ECO:0000269|PubMed:23847046}.
FT   LIPID       106    106       S-palmitoyl cysteine; alternate.
FT                                {ECO:0000269|PubMed:23847046}.
FT   CROSSLNK    130    130       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO).
FT                                {ECO:0000269|PubMed:15976810}.
FT   VARIANT      26     26       M -> I (in PARK7; does not affect protein
FT                                stability and degradation; does not
FT                                interfere with homodimerization;
FT                                dbSNP:rs74315351).
FT                                {ECO:0000269|PubMed:12953260,
FT                                ECO:0000269|PubMed:14713311}.
FT                                /FTId=VAR_020492.
FT   VARIANT      39     39       A -> S (probable disease-associated
FT                                mutation found in early-onset Parkinson
FT                                disease with digenic inheritance; the
FT                                patient also carries PINK1 mutation L-
FT                                399; dbSNP:rs137853051).
FT                                {ECO:0000269|PubMed:16632486}.
FT                                /FTId=VAR_072589.
FT   VARIANT      64     64       E -> D (in PARK7; no apparent effect on
FT                                protein stability; impaired mitochondrial
FT                                morphology; dbSNP:rs74315353).
FT                                {ECO:0000269|PubMed:14607841,
FT                                ECO:0000269|PubMed:15365989,
FT                                ECO:0000269|PubMed:20186336}.
FT                                /FTId=VAR_020493.
FT   VARIANT      98     98       R -> Q (in dbSNP:rs71653619).
FT                                {ECO:0000269|PubMed:12953260,
FT                                ECO:0000269|PubMed:14705128,
FT                                ECO:0000269|PubMed:14872018,
FT                                ECO:0000269|PubMed:15254937}.
FT                                /FTId=VAR_020494.
FT   VARIANT     104    104       A -> T (in PARK7; loss of protection
FT                                against metal cytotoxicity;
FT                                dbSNP:rs774005786).
FT                                {ECO:0000269|PubMed:15254937,
FT                                ECO:0000269|PubMed:23792957}.
FT                                /FTId=VAR_020495.
FT   VARIANT     149    149       D -> A (in PARK7; loss of protection
FT                                against metal cytotoxicity;
FT                                dbSNP:rs74315352).
FT                                {ECO:0000269|PubMed:12953260,
FT                                ECO:0000269|PubMed:23792957}.
FT                                /FTId=VAR_020496.
FT   VARIANT     150    150       G -> S (in dbSNP:rs368420490).
FT                                {ECO:0000269|Ref.10}.
FT                                /FTId=VAR_020497.
FT   VARIANT     163    163       E -> K (in dbSNP:rs74315354).
FT                                {ECO:0000269|PubMed:16240358}.
FT                                /FTId=VAR_034801.
FT   VARIANT     166    166       L -> P (in PARK7; strongly decreases
FT                                enzymatic activity; reduces protein
FT                                stability and leads to increased
FT                                degradation; ubiquitinated by PRKN
FT                                leading to its recognition by HDAC6 and
FT                                targeting to aggresome where is degraded;
FT                                interferes with homodimerization;
FT                                abolishes interaction with PIAS2; reduced
FT                                localization in lipid rafts;
FT                                dbSNP:rs28938172).
FT                                {ECO:0000269|PubMed:12446870,
FT                                ECO:0000269|PubMed:12851414,
FT                                ECO:0000269|PubMed:14607841,
FT                                ECO:0000269|PubMed:14713311,
FT                                ECO:0000269|PubMed:17846173,
FT                                ECO:0000269|PubMed:19229105,
FT                                ECO:0000269|PubMed:22523093,
FT                                ECO:0000269|PubMed:23847046}.
FT                                /FTId=VAR_020498.
FT   VARIANT     171    171       A -> S (in dbSNP:rs777026628).
FT                                {ECO:0000269|PubMed:15254937}.
FT                                /FTId=VAR_020499.
FT   MUTAGEN      18     18       E->A: Strongly decreases enzymatic
FT                                activity. {ECO:0000269|PubMed:22523093}.
FT   MUTAGEN      18     18       E->D: Strongly decreases enzymatic
FT                                activity. {ECO:0000269|PubMed:22523093}.
FT   MUTAGEN      18     18       E->N: Strongly decreases enzymatic
FT                                activity. {ECO:0000269|PubMed:22523093}.
FT   MUTAGEN      18     18       E->Q: Strongly decreases enzymatic
FT                                activity. {ECO:0000269|PubMed:22523093}.
FT   MUTAGEN      46     46       C->A: Reduced localization in lipid
FT                                rafts; when associated with A-106.
FT                                {ECO:0000269|PubMed:15181200,
FT                                ECO:0000269|PubMed:15502874,
FT                                ECO:0000269|PubMed:18711745,
FT                                ECO:0000269|PubMed:23847046}.
FT   MUTAGEN      46     46       C->A: Reduces protein stability. No
FT                                effect on oxidation.
FT                                {ECO:0000269|PubMed:15181200,
FT                                ECO:0000269|PubMed:15502874,
FT                                ECO:0000269|PubMed:18711745,
FT                                ECO:0000269|PubMed:23847046}.
FT   MUTAGEN      46     46       C->S: No effect on mitochondrial
FT                                translocation neither on deglycase
FT                                activity. {ECO:0000269|PubMed:15181200,
FT                                ECO:0000269|PubMed:15502874,
FT                                ECO:0000269|PubMed:18711745,
FT                                ECO:0000269|PubMed:23847046,
FT                                ECO:0000269|PubMed:25416785}.
FT   MUTAGEN      51     51       V->A: Disrupts dimer formation and
FT                                strongly reduces ability to eliminate
FT                                hydrogen peroxide.
FT                                {ECO:0000269|PubMed:14749723}.
FT   MUTAGEN      53     53       C->A: Strongly reduces chaperone activity
FT                                and ability to eliminate hydrogen
FT                                peroxide. {ECO:0000269|PubMed:14749723,
FT                                ECO:0000269|PubMed:15181200,
FT                                ECO:0000269|PubMed:15502874,
FT                                ECO:0000269|PubMed:18711745}.
FT   MUTAGEN      53     53       C->S: No effect on mitochondrial
FT                                translocation neither on deglycase
FT                                activity. {ECO:0000269|PubMed:14749723,
FT                                ECO:0000269|PubMed:15181200,
FT                                ECO:0000269|PubMed:15502874,
FT                                ECO:0000269|PubMed:18711745,
FT                                ECO:0000269|PubMed:25416785}.
FT   MUTAGEN     106    106       C->A: Abolishes enzymatic activity.
FT                                Abolishes oxidation, association with
FT                                mitochondria and protease activity. No
FT                                effect on chaperone activity. Reduces
FT                                binding to OTUD7B.
FT                                {ECO:0000269|PubMed:15181200,
FT                                ECO:0000269|PubMed:15502874,
FT                                ECO:0000269|PubMed:16390825,
FT                                ECO:0000269|PubMed:18711745,
FT                                ECO:0000269|PubMed:20304780,
FT                                ECO:0000269|PubMed:21097510,
FT                                ECO:0000269|PubMed:22523093,
FT                                ECO:0000269|PubMed:23847046}.
FT   MUTAGEN     106    106       C->A: Reduced localization in lipid
FT                                rafts; when associated with A-46.
FT                                {ECO:0000269|PubMed:15181200,
FT                                ECO:0000269|PubMed:15502874,
FT                                ECO:0000269|PubMed:16390825,
FT                                ECO:0000269|PubMed:18711745,
FT                                ECO:0000269|PubMed:20304780,
FT                                ECO:0000269|PubMed:21097510,
FT                                ECO:0000269|PubMed:23847046}.
FT   MUTAGEN     106    106       C->D: Abolishes oxidation and association
FT                                with mitochondria. No effect on chaperone
FT                                activity. {ECO:0000269|PubMed:15181200,
FT                                ECO:0000269|PubMed:15502874,
FT                                ECO:0000269|PubMed:16390825,
FT                                ECO:0000269|PubMed:18711745,
FT                                ECO:0000269|PubMed:20304780,
FT                                ECO:0000269|PubMed:21097510,
FT                                ECO:0000269|PubMed:23847046}.
FT   MUTAGEN     106    106       C->S: Loss of protein and nucleic acid
FT                                deglycase activity. No effect on
FT                                mitochondrial translocation. Reduced
FT                                protease activity. No effect on
FT                                protection against metal cytotoxicity.
FT                                {ECO:0000269|PubMed:15181200,
FT                                ECO:0000269|PubMed:15502874,
FT                                ECO:0000269|PubMed:16390825,
FT                                ECO:0000269|PubMed:18711745,
FT                                ECO:0000269|PubMed:20304780,
FT                                ECO:0000269|PubMed:21097510,
FT                                ECO:0000269|PubMed:23847046,
FT                                ECO:0000269|PubMed:25416785,
FT                                ECO:0000269|PubMed:28596309}.
FT   MUTAGEN     126    126       H->A: Strongly decreases enzymatic
FT                                activity. {ECO:0000269|PubMed:20304780,
FT                                ECO:0000269|PubMed:22523093}.
FT   MUTAGEN     130    130       K->R: Partially compensates for loss of
FT                                stability; when associated with P-166.
FT                                {ECO:0000269|PubMed:12851414}.
FT   CONFLICT    119    119       F -> C (in Ref. 3; BAB71782).
FT                                {ECO:0000305}.
FT   STRAND        5     10       {ECO:0000244|PDB:2RK3}.
FT   HELIX        16     28       {ECO:0000244|PDB:2RK3}.
FT   STRAND       32     37       {ECO:0000244|PDB:2RK3}.
FT   TURN         38     41       {ECO:0000244|PDB:1PDW}.
FT   STRAND       47     49       {ECO:0000244|PDB:4N0M}.
FT   STRAND       51     53       {ECO:0000244|PDB:2OR3}.
FT   STRAND       55     57       {ECO:0000244|PDB:2RK3}.
FT   HELIX        58     62       {ECO:0000244|PDB:2RK3}.
FT   STRAND       68     72       {ECO:0000244|PDB:2RK3}.
FT   HELIX        76     84       {ECO:0000244|PDB:2RK3}.
FT   HELIX        86     97       {ECO:0000244|PDB:2RK3}.
FT   STRAND      101    105       {ECO:0000244|PDB:2RK3}.
FT   TURN        106    108       {ECO:0000244|PDB:2RK3}.
FT   HELIX       109    114       {ECO:0000244|PDB:2RK3}.
FT   HELIX       127    129       {ECO:0000244|PDB:2RK3}.
FT   HELIX       130    133       {ECO:0000244|PDB:2RK3}.
FT   TURN        134    136       {ECO:0000244|PDB:2RK3}.
FT   STRAND      139    141       {ECO:0000244|PDB:2RK3}.
FT   STRAND      145    149       {ECO:0000244|PDB:2RK3}.
FT   STRAND      152    155       {ECO:0000244|PDB:2RK3}.
FT   HELIX       158    160       {ECO:0000244|PDB:2RK3}.
FT   HELIX       161    173       {ECO:0000244|PDB:2RK3}.
FT   HELIX       175    182       {ECO:0000244|PDB:2RK3}.
FT   HELIX       183    185       {ECO:0000244|PDB:2RK3}.
SQ   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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