PARK7_HUMAN
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 03-AUG-2022, entry version 214.
DE RecName: Full=Parkinson disease protein 7 {ECO:0000305};
DE AltName: Full=Maillard deglycase {ECO:0000303|PubMed:28596309};
DE AltName: Full=Oncogene DJ1 {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 AltName: 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 Flags: Precursor;
GN Name=PARK7 {ECO:0000312|HGNC:HGNC:16369};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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., Iguchi-Ariga S.M.M.,
RA Ariga H.;
RT "DJ-1, a novel oncogene which transforms mouse NIH3T3 cells in cooperation
RT 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., 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., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., 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., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT 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 Sp1-
RT 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 IDENTIFICATION BY
RP 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., Ariga H.;
RT "DJ-1 positively regulates the androgen receptor by impairing the binding
RT 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 OF
RP 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; DOI=10.1111/j.1471-4159.2003.02265.x;
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 OF
RP 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 antagonizes
RT 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., 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 BY
RP 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 cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [21]
RP SUMOYLATION AT LYS-130, OXIDATION, SUBCELLULAR LOCATION, INDUCTION, AND
RP 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 MUTAGENESIS OF
RP 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, stabilizes the
RT 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., Bonini N.M.,
RA Gorospe M., Cookson M.R.;
RT "RNA binding activity of the recessive parkinsonism protein DJ-1 supports
RT 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., Jiang W.,
RA 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 neuroprotection.";
RL J. Neurosci. Res. 87:123-129(2009).
RN [27]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITES, AND MUTAGENESIS OF
RP 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 by
RT 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., Buerckstuemmer T.,
RA 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 MUTAGENESIS
RP 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., Mak T.W.,
RA Ting J.P.;
RT "DJ-1 enhances cell survival through the binding of cezanne, a negative
RT 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 in
RT 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 lipid
RT 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 AND
RP 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 metal-
RT 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., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT 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 deglycase
RT that repairs methylglyoxal- and glyoxal-glycated cysteine, arginine and
RT 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 SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA 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 in
RT 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 damage
RT in human keratinocyte.";
RL Biochem. Biophys. Res. Commun. 473:87-91(2016).
RN [40]
RP FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-106, SUBCELLULAR LOCATION,
RP 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., Lamouri A.;
RT "Guanine glycation repair by DJ-1/Park7 and its bacterial homologs.";
RL Science 357:208-211(2017).
RN [41]
RP FUNCTION, MUTAGENESIS OF LEU-10; GLU-18; CYS-106 AND ALA-179,
RP CHARACTERIZATION OF VARIANTS PARK7 ILE-26; ASP-64; THR-104; ALA-149 AND
RP PRO-166, AND CHARACTERIZATION OF VARIANTS SER-39 AND LYS-163.
RX PubMed=28993701; DOI=10.1038/s41598-017-13146-0;
RA Matsuda N., Kimura M., Queliconi B.B., Kojima W., Mishima M., Takagi K.,
RA Koyano F., Yamano K., Mizushima T., Ito Y., Tanaka K.;
RT "Parkinson's disease-related DJ-1 functions in thiol quality control
RT against aldehyde attack in vitro.";
RL Sci. Rep. 7:12816-12816(2017).
RN [42]
RP FUNCTION.
RX PubMed=30150385; DOI=10.1073/pnas.1802901115;
RA Galligan J.J., Wepy J.A., Streeter M.D., Kingsley P.J., Mitchener M.M.,
RA Wauchope O.R., Beavers W.N., Rose K.L., Wang T., Spiegel D.A.,
RA Marnett L.J.;
RT "Methylglyoxal-derived posttranslational arginine modifications are
RT abundant histone marks.";
RL Proc. Natl. Acad. Sci. U.S.A. 115:9228-9233(2018).
RN [43]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH NENF, AND SUBCELLULAR
RP LOCATION.
RX PubMed=31536960; DOI=10.1016/j.isci.2019.08.057;
RA Moutaoufik M.T., Malty R., Amin S., Zhang Q., Phanse S., Gagarinova A.,
RA Zilocchi M., Hoell L., Minic Z., Gagarinova M., Aoki H., Stockwell J.,
RA Jessulat M., Goebels F., Broderick K., Scott N.E., Vlasblom J., Musso G.,
RA Prasad B., Lamantea E., Garavaglia B., Rajput A., Murayama K., Okazaki Y.,
RA Foster L.J., Bader G.D., Cayabyab F.S., Babu M.;
RT "Rewiring of the Human Mitochondrial Interactome during Neuronal
RT Reprogramming Reveals Regulators of the Respirasome and Neurogenesis.";
RL IScience 19:1114-1132(2019).
RN [44]
RP FUNCTION, CATALYTIC ACTIVITY, CAUTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RX PubMed=31653696; DOI=10.1074/jbc.ra119.011237;
RA Andreeva A., Bekkhozhin Z., Omertassova N., Baizhumanov T., Yeltay G.,
RA Akhmetali M., Toibazar D., Utepbergenov D.;
RT "The apparent deglycase activity of DJ-1 results from the conversion of
RT free methylglyoxal present in fast equilibrium with hemithioacetals and
RT hemiaminals.";
RL J. Biol. Chem. 294:18863-18872(2019).
RN [45]
RP FUNCTION, AND MUTAGENESIS OF CYS-106.
RX PubMed=30894531; DOI=10.1038/s41467-019-09192-z;
RA Zheng Q., Omans N.D., Leicher R., Osunsade A., Agustinus A.S.,
RA Finkin-Groner E., D'Ambrosio H., Liu B., Chandarlapaty S., Liu S.,
RA David Y.;
RT "Reversible histone glycation is associated with disease-related changes in
RT chromatin architecture.";
RL Nat. Commun. 10:1289-1289(2019).
RN [46]
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 [47]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF WILD-TYPE AND MUTANT ARG-130, AND
RP 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 onset
RT Parkinson's disease.";
RL J. Biol. Chem. 278:31372-31379(2003).
RN [48]
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 and
RT Parkinson's disease.";
RL J. Biol. Chem. 278:31380-31384(2003).
RN [49]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), FUNCTION, OXIDATION AT CYS-106, AND
RP 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., Park C.,
RA Kang S.-O., Suh P.-G., Lee H.-S., Cha S.-S.;
RT "Crystal structures of human DJ-1 and Escherichia coli Hsp31, which share
RT an evolutionarily conserved domain.";
RL J. Biol. Chem. 278:44552-44559(2003).
RN [50]
RP X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS), HOMODIMERIZATION, OXIDATION, AND
RP 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 in
RT autosomal recessive early onset Parkinson's disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:9256-9261(2003).
RN [51]
RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS), MUTAGENESIS OF CYS-46; CYS-53 AND
RP 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 cysteine-
RT sulfinic acid-driven mitochondrial localization.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9103-9108(2004).
RN [52]
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 [53]
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-onset
RT Parkinsonism.";
RL Science 299:256-259(2003).
RN [54]
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 [55]
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 disease
RT (PARK7).";
RL Hum. Mutat. 24:321-329(2004).
RN [56]
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 [57]
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., Cote L.J.,
RA Andrews H., Singleton A., Wavrant De-Vrieze F., Hardy J., Mayeux R.,
RA Fahn S., Waters C., Ford B., Frucht S., Ottman R., 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 [58]
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., Weiss P.H.,
RA Hilker R., Vieregge P., Ozelius L.J., Heutink P., Bonifati V.,
RA Schwinger E., Lang A.E., Noth J., Bressman S.B., Pramstaller P.P.,
RA Riess O., Klein C.;
RT "DJ-1 (PARK7) mutations are less frequent than Parkin (PARK2) mutations in
RT early-onset Parkinson disease.";
RL Neurology 62:389-394(2004).
RN [59]
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., Fierro B.,
RA Piccoli F., Arabia G., Caracciolo M., Ciro Candiano I.C., Quattrone A.;
RT "DJ-1 mutations and parkinsonism-dementia-amyotrophic lateral sclerosis
RT complex.";
RL Ann. Neurol. 58:803-807(2005).
RN [60]
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., Pan Q.,
RA Xia J.-H., Xia K., Zhang Z.;
RT "Association of PINK1 and DJ-1 confers digenic inheritance of early-onset
RT Parkinson's disease.";
RL Hum. Mol. Genet. 15:1816-1825(2006).
RN [61]
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 to
RT aggresomes via binding to HDAC6.";
RL J. Cell Biol. 178:1025-1038(2007).
RN [62]
RP VARIANT PARK7 PRO-10.
RX PubMed=18785233; DOI=10.1002/mds.22156;
RA Guo J.F., Xiao B., Liao B., Zhang X.W., Nie L.L., Zhang Y.H., Shen L.,
RA Jiang H., Xia K., Pan Q., Yan X.X., Tang B.S.;
RT "Mutation analysis of Parkin, PINK1, DJ-1 and ATP13A2 genes in Chinese
RT patients with autosomal recessive early-onset Parkinsonism.";
RL Mov. Disord. 23:2074-2079(2008).
RN [63]
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., Waak J.,
RA Wolburg H., Gizatullina Z., Gellerich F.N., Woitalla D., Riess O.,
RA Kahle P.J., Proikas-Cezanne T., Kruger R.;
RT "Reduced basal autophagy and impaired mitochondrial dynamics due to loss of
RT Parkinson's disease-associated protein DJ-1.";
RL PLoS ONE 5:E9367-E9367(2010).
RN [64]
RP VARIANT PARK7 GLN-45 DEL.
RX PubMed=26972524; DOI=10.1016/j.parkreldis.2016.03.001;
RA Hanagasi H.A., Giri A., Kartal E., Guven G., Bilgic B., Hauser A.K.,
RA Emre M., Heutink P., Basak N., Gasser T., Simon-Sanchez J., Lohmann E.;
RT "A novel homozygous DJ1 mutation causes parkinsonism and ALS in a Turkish
RT family.";
RL Parkinsonism Relat. Disord. 29:117-120(2016).
RN [65]
RP INVOLVEMENT IN PARK7.
RX PubMed=30928208; DOI=10.1016/j.parkreldis.2019.03.013;
RA Stephenson S.E., Djaldetti R., Rafehi H., Wilson G.R., Gillies G.,
RA Bahlo M., Lockhart P.J.;
RT "Familial early onset Parkinson's disease caused by a homozygous frameshift
RT variant in PARK7: Clinical features and literature update.";
RL Parkinsonism Relat. Disord. 64:308-311(2019).
CC -!- FUNCTION: Multifunctional protein with controversial molecular function
CC which plays an important role in cell protection against oxidative
CC stress and cell death acting as oxidative stress sensor and redox-
CC sensitive chaperone and protease (PubMed:17015834, PubMed:20304780,
CC PubMed:18711745, PubMed:12796482, PubMed:19229105, PubMed:25416785,
CC PubMed:26995087, PubMed:28993701). It is involved in neuroprotective
CC mechanisms like the stabilization of NFE2L2 and PINK1 proteins, male
CC fertility as a positive regulator of androgen signaling pathway as well
CC as cell growth and transformation through, for instance, the modulation
CC of NF-kappa-B signaling pathway (PubMed:12612053, PubMed:15502874,
CC PubMed:14749723, PubMed:17015834, PubMed:21097510, PubMed:18711745).
CC Has been described as a protein and nucleotide deglycase that catalyzes
CC the 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). But this function is rebuted by
CC other works (PubMed:27903648, PubMed:31653696). As a protein deglycase,
CC repairs methylglyoxal- and glyoxal-glycated proteins, and releases
CC repaired proteins and lactate or glycolate, respectively. Deglycates
CC cysteine, arginine and lysine residues in proteins, and thus
CC reactivates these proteins by reversing glycation by glyoxals. Acts on
CC early glycation intermediates (hemithioacetals and aminocarbinols),
CC preventing the formation of advanced glycation endproducts (AGE) that
CC cause irreversible damage (PubMed:25416785, PubMed:28013050,
CC PubMed:26995087). Also functions as a nucleotide deglycase able to
CC repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP,
CC dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair
CC system named guanine glycation repair (GG repair), dedicated to
CC reversing methylglyoxal and glyoxal damage via nucleotide sanitization
CC and direct nucleic acid repair (PubMed:28596309). Protects histones
CC from adduction by methylglyoxal, controls the levels of methylglyoxal-
CC derived argininine modifications on chromatin (PubMed:30150385). Able
CC to remove the glycations and restore histone 3, histone glycation
CC disrupts both local and global chromatin architecture by altering
CC histone-DNA interactions as well as histone acetylation and
CC ubiquitination levels (PubMed:30150385, PubMed:30894531). Displays a
CC very low glyoxalase activity that may reflect its deglycase activity
CC (PubMed:22523093, PubMed:31653696, PubMed:28993701). Eliminates
CC hydrogen peroxide and protects cells against hydrogen peroxide-induced
CC cell death (PubMed:16390825). Required for correct mitochondrial
CC morphology 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 during
CC pacemaking (PubMed:18711745). Regulates astrocyte inflammatory
CC responses, may modulate lipid rafts-dependent endocytosis in astrocytes
CC and neuronal cells (PubMed:23847046). In pancreatic islets, involved in
CC the maintenance of mitochondrial reactive oxygen species (ROS) levels
CC and glucose homeostasis in an age- and diet dependent manner. Protects
CC pancreatic beta cells from cell death induced by inflammatory and
CC cytotoxic setting (By similarity). Binds to a number of mRNAs
CC containing multiple copies of GG or CC motifs and partially inhibits
CC their translation but dissociates following oxidative stress
CC (PubMed:18626009). Metal-binding protein able to bind copper as well as
CC toxic mercury ions, enhances the cell protection mechanism against
CC induced metal toxicity (PubMed:23792957). In macrophages, interacts
CC with the NADPH oxidase subunit NCF1 to direct NADPH oxidase-dependent
CC ROS 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:28993701, ECO:0000269|PubMed:30150385,
CC ECO:0000269|PubMed:30894531, ECO:0000269|PubMed:9070310}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(omega)-(1-hydroxy-2-oxopropyl)-L-arginyl-[protein] =
CC H(+) + L-arginyl-[protein] + lactate; Xref=Rhea:RHEA:49548,
CC Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:12428, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29965,
CC ChEBI:CHEBI:131708; EC=3.5.1.124;
CC Evidence={ECO:0000269|PubMed:25416785};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-(1-hydroxy-2-oxopropyl)-L-lysyl-[protein] = H(+) +
CC L-lysyl-[protein] + lactate; Xref=Rhea:RHEA:49552, Rhea:RHEA-
CC COMP:9752, Rhea:RHEA-COMP:12429, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:131709; EC=3.5.1.124;
CC Evidence={ECO:0000269|PubMed:25416785};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-(1-hydroxy-2-oxopropyl)-L-cysteinyl-[protein] = H(+) +
CC L-cysteinyl-[protein] + lactate; Xref=Rhea:RHEA:49556, Rhea:RHEA-
CC COMP:10131, Rhea:RHEA-COMP:12430, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:131710; EC=3.5.1.124;
CC Evidence={ECO:0000269|PubMed:25416785};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(omega)-(1-hydroxy-2-oxoethyl)-L-arginyl-[protein] =
CC glycolate + H(+) + L-arginyl-[protein]; Xref=Rhea:RHEA:57188,
CC Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:14844, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29965,
CC ChEBI:CHEBI:141553; EC=3.5.1.124;
CC Evidence={ECO:0000269|PubMed:25416785};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-(1-hydroxy-2-oxoethyl)-L-lysyl-[protein] =
CC glycolate + H(+) + L-lysyl-[protein]; Xref=Rhea:RHEA:57192,
CC Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:14845, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:141554; EC=3.5.1.124;
CC Evidence={ECO:0000269|PubMed:25416785};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-(1-hydroxy-2-oxoethyl)-L-cysteinyl-[protein] =
CC glycolate + H(+) + L-cysteinyl-[protein]; Xref=Rhea:RHEA:57196,
CC Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:14846, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:141555; EC=3.5.1.124;
CC Evidence={ECO:0000269|PubMed:25416785};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-dGTP = dGTP + H(+) +
CC lactate; Xref=Rhea:RHEA:57244, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:24996, ChEBI:CHEBI:61429, ChEBI:CHEBI:141569;
CC Evidence={ECO:0000269|PubMed:28596309};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GTP = GTP + H(+) + lactate;
CC Xref=Rhea:RHEA:57256, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:24996, ChEBI:CHEBI:37565, ChEBI:CHEBI:141570;
CC Evidence={ECO:0000269|PubMed:28596309};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GDP = GDP + H(+) + lactate;
CC Xref=Rhea:RHEA:57260, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:24996, ChEBI:CHEBI:58189, ChEBI:CHEBI:141573;
CC Evidence={ECO:0000269|PubMed:28596309};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(2)-(1-hydroxy-2-oxopropyl)-GMP = GMP + H(+) + lactate;
CC Xref=Rhea:RHEA:57268, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:24996, ChEBI:CHEBI:58115, ChEBI:CHEBI:141575;
CC Evidence={ECO:0000269|PubMed:28596309};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-dGTP = dGTP + glycolate +
CC H(+); Xref=Rhea:RHEA:57248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29805, ChEBI:CHEBI:61429, ChEBI:CHEBI:141572;
CC Evidence={ECO:0000305|PubMed:28596309};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GTP = glycolate + GTP +
CC H(+); Xref=Rhea:RHEA:57252, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29805, ChEBI:CHEBI:37565, ChEBI:CHEBI:141571;
CC Evidence={ECO:0000269|PubMed:28596309};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GDP = GDP + glycolate +
CC H(+); Xref=Rhea:RHEA:57264, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29805, ChEBI:CHEBI:58189, ChEBI:CHEBI:141574;
CC Evidence={ECO:0000305|PubMed:28596309};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(2)-(1-hydroxy-2-oxoethyl)-GMP = glycolate + GMP +
CC H(+); Xref=Rhea:RHEA:57304, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29805, ChEBI:CHEBI:58115, ChEBI:CHEBI:141576;
CC Evidence={ECO:0000305|PubMed:28596309};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-guanosine in RNA + H2O = a
CC guanosine in RNA + H(+) + lactate; Xref=Rhea:RHEA:57288, Rhea:RHEA-
CC COMP:14855, Rhea:RHEA-COMP:14858, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:74269,
CC ChEBI:CHEBI:141580; Evidence={ECO:0000269|PubMed:28596309};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N(2)-(1-hydroxy-2-oxopropyl)-2'-deoxyguanosine in DNA + H2O
CC = a 2'-deoxyguanosine in DNA + H(+) + lactate; Xref=Rhea:RHEA:57300,
CC Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14856, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:24996, ChEBI:CHEBI:85445,
CC ChEBI:CHEBI:141578; Evidence={ECO:0000269|PubMed:28596309};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-guanosine in RNA + H2O = a
CC guanosine in RNA + glycolate + H(+); Xref=Rhea:RHEA:57292, Rhea:RHEA-
CC COMP:14855, Rhea:RHEA-COMP:14859, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29805, ChEBI:CHEBI:74269,
CC ChEBI:CHEBI:141581; Evidence={ECO:0000305|PubMed:28596309};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N(2)-(1-hydroxy-2-oxoethyl)-2'-deoxyguanosine in DNA + H2O
CC = a 2'-deoxyguanosine in DNA + glycolate + H(+);
CC Xref=Rhea:RHEA:57296, Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:14857,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805,
CC ChEBI:CHEBI:85445, ChEBI:CHEBI:141579;
CC Evidence={ECO:0000305|PubMed:28596309};
CC -!- COFACTOR:
CC Note=Deglycase activity does not require glutathione as a cofactor,
CC however, glycated glutathione constitutes a PARK7 substrate.
CC {ECO:0000269|PubMed:25416785, ECO:0000269|PubMed:28993701};
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 degrees
CC 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 degrees
CC 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 glycated
CC N-acetyllysine. kcat is 0.42 sec(-1) for the deglycation of glycated
CC N-acetylcysteine. kcat is 0.02 sec(-1) for glyoxalase activity
CC (PubMed:31653696). {ECO:0000269|PubMed:25416785,
CC ECO:0000269|PubMed:31653696};
CC -!- SUBUNIT: Homodimer (PubMed:12851414, PubMed:12796482, PubMed:12855764,
CC PubMed:31653696). Binds EFCAB6/DJBP and PIAS2 (PubMed:11477070,
CC PubMed:12851414, PubMed:12612053). Part of a ternary complex containing
CC PARK7, EFCAB6/DJBP and AR (PubMed:12612053). Interacts (via N-terminus)
CC with OTUD7B (PubMed:21097510). Interacts with BBS1, HIPK1, CLCF1 and
CC MTERF (PubMed:16390825, PubMed:21097510). Forms a complex with PINK1
CC and PRKN (PubMed:19229105). Interacts (via C-terminus) with NCF1; the
CC interaction is enhanced by LPS and modulates NCF1 phosphorylation and
CC membrane translocation (By similarity). Interacts with NENF
CC (PubMed:31536960). {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, ECO:0000269|PubMed:31536960,
CC ECO:0000269|PubMed:31653696}.
CC -!- INTERACTION:
CC Q99497; P01023: A2M; NbExp=3; IntAct=EBI-1164361, EBI-640741;
CC Q99497; P63010-2: AP2B1; NbExp=3; IntAct=EBI-1164361, EBI-11529439;
CC Q99497; P05067: APP; NbExp=3; IntAct=EBI-1164361, EBI-77613;
CC Q99497; P10275: AR; NbExp=6; IntAct=EBI-1164361, EBI-608057;
CC Q99497; Q8NFJ9: BBS1; NbExp=4; IntAct=EBI-1164361, EBI-1805484;
CC Q99497; Q8N5S9-2: CAMKK1; NbExp=3; IntAct=EBI-1164361, EBI-25850646;
CC Q99497; Q9UER7: DAXX; NbExp=6; IntAct=EBI-1164361, EBI-77321;
CC Q99497; P50570-2: DNM2; NbExp=3; IntAct=EBI-1164361, EBI-10968534;
CC Q99497; Q13158: FADD; NbExp=9; IntAct=EBI-1164361, EBI-494804;
CC Q99497; P06241-3: FYN; NbExp=3; IntAct=EBI-1164361, EBI-10691738;
CC Q99497; Q9HD26: GOPC; NbExp=3; IntAct=EBI-1164361, EBI-349832;
CC Q99497; P42858: HTT; NbExp=6; IntAct=EBI-1164361, EBI-466029;
CC Q99497; Q6DN90-2: IQSEC1; NbExp=3; IntAct=EBI-1164361, EBI-21911304;
CC Q99497; Q9BYQ4: KRTAP9-2; NbExp=3; IntAct=EBI-1164361, EBI-1044640;
CC Q99497; Q9BYZ2: LDHAL6B; NbExp=3; IntAct=EBI-1164361, EBI-1108377;
CC Q99497; O94776: MTA2; NbExp=3; IntAct=EBI-1164361, EBI-1783035;
CC Q99497; Q8NFH3: NUP43; NbExp=3; IntAct=EBI-1164361, EBI-1059321;
CC Q99497; Q96FW1: OTUB1; NbExp=4; IntAct=EBI-1164361, EBI-1058491;
CC Q99497; Q6GQQ9: OTUD7B; NbExp=3; IntAct=EBI-1164361, EBI-527784;
CC Q99497; Q99497: PARK7; NbExp=3; IntAct=EBI-1164361, EBI-1164361;
CC Q99497; P32322: PYCR1; NbExp=5; IntAct=EBI-1164361, EBI-848624;
CC Q99497; P63244: RACK1; NbExp=4; IntAct=EBI-1164361, EBI-296739;
CC Q99497; Q6ZNA4-2: RNF111; NbExp=3; IntAct=EBI-1164361, EBI-21535400;
CC Q99497; Q9ULX5: RNF112; NbExp=3; IntAct=EBI-1164361, EBI-25829984;
CC Q99497; Q8IUW3: SPATA2L; NbExp=3; IntAct=EBI-1164361, EBI-2510414;
CC Q99497; O14656-2: TOR1A; NbExp=3; IntAct=EBI-1164361, EBI-25847109;
CC Q99497; Q9UBQ0-2: VPS29; NbExp=3; IntAct=EBI-1164361, EBI-11141397;
CC Q99497; Q9GZS3: WDR61; NbExp=3; IntAct=EBI-1164361, EBI-358545;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q99LX0};
CC Lipid-anchor {ECO:0000250|UniProtKB:Q99LX0}. 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 {ECO:0000269|PubMed:12851414,
CC ECO:0000269|PubMed:14579415, ECO:0000269|PubMed:15976810,
CC ECO:0000269|PubMed:16390825, ECO:0000269|PubMed:28596309}. Membrane
CC raft {ECO:0000250|UniProtKB:O88767}. Mitochondrion
CC {ECO:0000269|PubMed:15181200, ECO:0000269|PubMed:18711745,
CC ECO:0000269|PubMed:19229105, ECO:0000269|PubMed:31536960}. Endoplasmic
CC reticulum {ECO:0000269|PubMed:31536960}. Note=Under normal conditions,
CC located predominantly in the cytoplasm and, to a lesser extent, in the
CC nucleus and mitochondrion. Translocates to the mitochondrion and
CC subsequently to the nucleus in response to oxidative stress and exerts
CC an increased cytoprotective effect against oxidative damage
CC (PubMed:18711745). Detected in tau inclusions in brains from
CC neurodegenerative disease patients (PubMed:14705119). Membrane raft
CC localization in astrocytes and neuronal cells requires palmitoylation.
CC {ECO:0000269|PubMed:14705119, ECO:0000269|PubMed:18711745}.
CC -!- TISSUE SPECIFICITY: Highly expressed in pancreas, kidney, skeletal
CC muscle, liver, testis and heart. Detected at slightly lower levels in
CC placenta and brain (at protein level). Detected in astrocytes, Sertoli
CC cells, spermatogonia, spermatids and spermatozoa. Expressed by
CC pancreatic islets at higher levels than surrounding exocrine tissues
CC (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 during
CC aging. {ECO:0000269|PubMed:22611253}.
CC -!- INDUCTION: By hydrogen peroxide and UV irradiation (PubMed:14749723,
CC PubMed:15976810). In pancreatic islets, expression increases under
CC hyperglycemic conditions (PubMed:22611253). Expression is also induced
CC by sulforaphane, an 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 after
CC ultraviolet irradiation and essential for cell-growth promoting
CC activity and transforming activity. {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 neurodegenerative
CC disorder characterized by resting tremor, postural tremor,
CC bradykinesia, muscular rigidity, anxiety and psychotic episodes. PARK7
CC has onset before 40 years, slow progression and initial good response
CC to levodopa. Some patients may show traits reminiscent of amyotrophic
CC lateral sclerosis-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:18785233, ECO:0000269|PubMed:19229105,
CC ECO:0000269|PubMed:22523093, ECO:0000269|PubMed:23792957,
CC ECO:0000269|PubMed:23847046, ECO:0000269|PubMed:26972524,
CC ECO:0000269|PubMed:28993701, ECO:0000269|PubMed:30928208}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the peptidase C56 family. {ECO:0000305}.
CC -!- CAUTION: Glyoxalase activity has been reported (PubMed:22523093,
CC PubMed:31653696). It may however reflect its deglycase activity
CC (PubMed:25416785). {ECO:0000269|PubMed:22523093,
CC ECO:0000269|PubMed:25416785, ECO:0000269|PubMed:31653696}.
CC -!- CAUTION: The protein deglycation activity is controversial. It has been
CC ascribed to a TRIS buffer artifact by a publication (PubMed:27903648)
CC and as a result of the removal of methylglyoxal by glyoxalase activity
CC that leads to a subsequent decomposition of hemithioacetals and
CC hemianimals due to the shift in equilibrium position by another one
CC (PubMed:31653696). However, biochemical experiments showing that PARK7
CC is a bona fide deglycase have been performed (PubMed:25416785,
CC PubMed:28013050, PubMed:28596309). {ECO:0000269|PubMed:25416785,
CC ECO:0000269|PubMed:27903648, ECO:0000269|PubMed:28013050,
CC ECO:0000269|PubMed:28596309, ECO:0000269|PubMed:31653696}.
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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 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 PDB; 6AF5; X-ray; 1.65 A; A=1-189.
DR PDB; 6AF7; X-ray; 1.30 A; A=1-189.
DR PDB; 6AF9; X-ray; 1.39 A; A=1-189.
DR PDB; 6AFA; X-ray; 1.65 A; A=1-189.
DR PDB; 6AFB; X-ray; 1.60 A; A=1-189.
DR PDB; 6AFC; X-ray; 1.45 A; A=1-189.
DR PDB; 6AFD; X-ray; 1.48 A; A=1-189.
DR PDB; 6AFE; X-ray; 1.50 A; A=1-189.
DR PDB; 6AFF; X-ray; 1.60 A; A=1-189.
DR PDB; 6AFG; X-ray; 1.50 A; A=1-189.
DR PDB; 6AFH; X-ray; 1.65 A; A=1-189.
DR PDB; 6AFI; X-ray; 1.65 A; A=1-189.
DR PDB; 6AFJ; X-ray; 1.48 A; A=1-189.
DR PDB; 6AFL; X-ray; 1.60 A; A=1-189.
DR PDB; 6E5Z; X-ray; 1.35 A; A=1-189.
DR PDB; 6M8Z; X-ray; 1.83 A; A=1-189.
DR PDB; 7C62; X-ray; 2.03 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 PDBsum; 6AF5; -.
DR PDBsum; 6AF7; -.
DR PDBsum; 6AF9; -.
DR PDBsum; 6AFA; -.
DR PDBsum; 6AFB; -.
DR PDBsum; 6AFC; -.
DR PDBsum; 6AFD; -.
DR PDBsum; 6AFE; -.
DR PDBsum; 6AFF; -.
DR PDBsum; 6AFG; -.
DR PDBsum; 6AFH; -.
DR PDBsum; 6AFI; -.
DR PDBsum; 6AFJ; -.
DR PDBsum; 6AFL; -.
DR PDBsum; 6E5Z; -.
DR PDBsum; 6M8Z; -.
DR PDBsum; 7C62; -.
DR AlphaFoldDB; Q99497; -.
DR BMRB; Q99497; -.
DR SMR; Q99497; -.
DR BioGRID; 116446; 300.
DR CORUM; Q99497; -.
DR DIP; DIP-35515N; -.
DR IntAct; Q99497; 150.
DR MINT; Q99497; -.
DR STRING; 9606.ENSP00000418770; -.
DR DrugBank; DB09130; Copper.
DR MEROPS; C56.002; -.
DR GlyGen; Q99497; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q99497; -.
DR MetOSite; 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 jPOST; Q99497; -.
DR MassIVE; Q99497; -.
DR PaxDb; Q99497; -.
DR PeptideAtlas; Q99497; -.
DR PRIDE; Q99497; -.
DR ProteomicsDB; 78298; -.
DR TopDownProteomics; Q99497; -.
DR Antibodypedia; 1372; 895 antibodies from 51 providers.
DR DNASU; 11315; -.
DR Ensembl; ENST00000338639.10; ENSP00000340278.5; ENSG00000116288.13.
DR Ensembl; ENST00000377488.5; ENSP00000366708.1; ENSG00000116288.13.
DR Ensembl; ENST00000377491.5; ENSP00000366711.1; ENSG00000116288.13.
DR Ensembl; ENST00000493373.5; ENSP00000465404.1; ENSG00000116288.13.
DR Ensembl; ENST00000493678.5; ENSP00000418770.1; ENSG00000116288.13.
DR GeneID; 11315; -.
DR KEGG; hsa:11315; -.
DR MANE-Select; ENST00000338639.10; ENSP00000340278.5; NM_007262.5; NP_009193.2.
DR CTD; 11315; -.
DR DisGeNET; 11315; -.
DR GeneCards; PARK7; -.
DR GeneReviews; PARK7; -.
DR HGNC; HGNC:16369; PARK7.
DR HPA; ENSG00000116288; Low tissue specificity.
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; Parkinson-dementia complex of Guam.
DR Orphanet; 2828; Young-onset Parkinson disease.
DR PharmGKB; PA32946; -.
DR VEuPathDB; HostDB:ENSG00000116288; -.
DR eggNOG; KOG2764; Eukaryota.
DR GeneTree; ENSGT00390000001231; -.
DR HOGENOM; CLU_000445_44_2_1; -.
DR InParanoid; Q99497; -.
DR OMA; TSYPAMK; -.
DR OrthoDB; 1165707at2759; -.
DR PhylomeDB; Q99497; -.
DR TreeFam; TF300119; -.
DR BioCyc; MetaCyc:ENSG00000116288-MON; -.
DR BRENDA; 3.5.1.124; 2681.
DR BRENDA; 4.2.1.130; 2681.
DR PathwayCommons; Q99497; -.
DR Reactome; R-HSA-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-HSA-9613829; Chaperone Mediated Autophagy.
DR Reactome; R-HSA-9615710; Late endosomal microautophagy.
DR Reactome; R-HSA-9646399; Aggrephagy.
DR SABIO-RK; Q99497; -.
DR SignaLink; Q99497; -.
DR SIGNOR; Q99497; -.
DR BioGRID-ORCS; 11315; 20 hits in 1087 CRISPR screens.
DR ChiTaRS; PARK7; human.
DR EvolutionaryTrace; Q99497; -.
DR GeneWiki; PARK7; -.
DR GenomeRNAi; 11315; -.
DR Pharos; Q99497; Tbio.
DR PRO; PR:Q99497; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q99497; protein.
DR Bgee; ENSG00000116288; Expressed in adult organism and 207 other tissues.
DR ExpressionAtlas; Q99497; baseline and differential.
DR Genevisible; Q99497; HS.
DR GO; GO:0005912; C:adherens junction; HDA:BHF-UCL.
DR GO; GO:0030424; C:axon; ISS:ParkinsonsUK-UCL.
DR GO; GO:0044297; C:cell body; IEA:Ensembl.
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; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA: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:0005654; C:nucleoplasm; IDA:HPA.
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:0045296; F:cadherin binding; HDA: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:0140297; F:DNA-binding transcription factor binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0019899; F:enzyme binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:1990422; F:glyoxalase (glycolic acid-forming) activity; IDA:UniProtKB.
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:0050681; F:nuclear androgen receptor binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0016684; F:oxidoreductase activity, acting on peroxide as acceptor; IDA:ParkinsonsUK-UCL.
DR GO; GO:0019826; F:oxygen sensor activity; IEA:Ensembl.
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:0044877; F:protein-containing complex binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0097110; F:scaffold protein binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0005102; F:signaling receptor binding; IPI:UniProtKB.
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: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:0110095; P:cellular detoxification of aldehyde; IDA:UniProtKB.
DR GO; GO:0140041; P:cellular detoxification of methylglyoxal; IDA:UniProtKB.
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:0070994; P:detection of oxidative stress; IEA:Ensembl.
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: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:0016570; P:histone modification; IMP: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:0061727; P:methylglyoxal catabolic process to lactate; IDA:UniProtKB.
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:0051091; P:positive regulation of DNA-binding transcription factor activity; IMP: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: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:0031334; P:positive regulation of protein-containing complex assembly; 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:1901671; P:positive regulation of superoxide dismutase activity; IDA:ParkinsonsUK-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; 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:0006508; P:proteolysis; IEA:UniProtKB-KW.
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:0035065; P:regulation of histone acetylation; IMP:UniProtKB.
DR GO; GO:0033182; P:regulation of histone ubiquitination; IMP: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:0006979; P:response to oxidative stress; IBA:GO_Central.
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; Copper;
KW Cytoplasm; Direct protein sequencing; Disease variant; DNA damage;
KW DNA repair; Endoplasmic reticulum; Fertilization; Hydrolase;
KW Inflammatory response; Isopeptide bond; Lipoprotein; Membrane;
KW Mitochondrion; Neurodegeneration; Nucleus; Oxidation; Palmitate;
KW Parkinson disease; Parkinsonism; Phosphoprotein; Protease;
KW Reference proteome; RNA-binding; Stress response; Tumor suppressor;
KW Ubl conjugation; Zymogen.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:25944712"
FT CHAIN 2..?
FT /note="Parkinson disease protein 7"
FT /id="PRO_0000157849"
FT PROPEP ?..189
FT /note="Removed in mature form"
FT /id="PRO_0000405558"
FT ACT_SITE 106
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:20304780,
FT ECO:0000305|PubMed:25416785"
FT ACT_SITE 126
FT /evidence="ECO:0000305|PubMed:20304780"
FT SITE 149..150
FT /note="Cleavage; by CASP6"
FT /evidence="ECO:0000250|UniProtKB:Q99LX0"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:25944712"
FT MOD_RES 67
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15592455"
FT MOD_RES 106
FT /note="Cysteine sulfinic acid (-SO2H); alternate"
FT /evidence="ECO:0000269|PubMed:12939276"
FT MOD_RES 148
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99LX0"
FT MOD_RES 182
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99LX0"
FT LIPID 46
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:23847046"
FT LIPID 53
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:23847046"
FT LIPID 106
FT /note="S-palmitoyl cysteine; alternate"
FT /evidence="ECO:0000269|PubMed:23847046"
FT CROSSLNK 130
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:15976810"
FT VARIANT 10
FT /note="L -> P (in PARK7; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:18785233"
FT /id="VAR_084339"
FT VARIANT 26
FT /note="M -> I (in PARK7; does not affect protein stability
FT and degradation; does not interfere with homodimerization;
FT decreased detoxification acivity on methylglyocal-adducted
FT CoA; dbSNP:rs74315351)"
FT /evidence="ECO:0000269|PubMed:12953260,
FT ECO:0000269|PubMed:14713311, ECO:0000269|PubMed:28993701"
FT /id="VAR_020492"
FT VARIANT 39
FT /note="A -> S (probable disease-associated variant found in
FT early-onset Parkinson disease with digenic inheritance; no
FT effect on detoxification acivity on methylglyocal-adducted
FT CoA; the patient also carries PINK1 mutation L-399;
FT dbSNP:rs137853051)"
FT /evidence="ECO:0000269|PubMed:16632486,
FT ECO:0000269|PubMed:28993701"
FT /id="VAR_072589"
FT VARIANT 45
FT /note="Missing (in PARK7)"
FT /evidence="ECO:0000269|PubMed:26972524"
FT /id="VAR_083277"
FT VARIANT 64
FT /note="E -> D (in PARK7; no apparent effect on protein
FT stability; impaired mitochondrial morphology; no effect on
FT detoxification acivity on methylglyocal-adducted CoA;
FT dbSNP:rs74315353)"
FT /evidence="ECO:0000269|PubMed:14607841,
FT ECO:0000269|PubMed:15365989, ECO:0000269|PubMed:20186336,
FT ECO:0000269|PubMed:28993701"
FT /id="VAR_020493"
FT VARIANT 98
FT /note="R -> Q (in dbSNP:rs71653619)"
FT /evidence="ECO:0000269|PubMed:12953260,
FT ECO:0000269|PubMed:14705128, ECO:0000269|PubMed:14872018,
FT ECO:0000269|PubMed:15254937"
FT /id="VAR_020494"
FT VARIANT 104
FT /note="A -> T (in PARK7; loss of protection against metal
FT cytotoxicity; decreased detoxification acivity on
FT methylglyocal-adducted CoA; dbSNP:rs774005786)"
FT /evidence="ECO:0000269|PubMed:15254937,
FT ECO:0000269|PubMed:23792957, ECO:0000269|PubMed:28993701"
FT /id="VAR_020495"
FT VARIANT 149
FT /note="D -> A (in PARK7; loss of protection against metal
FT cytotoxicity; decreased detoxification acivity on
FT methylglyocal-adducted CoA; dbSNP:rs74315352)"
FT /evidence="ECO:0000269|PubMed:12953260,
FT ECO:0000269|PubMed:23792957, ECO:0000269|PubMed:28993701"
FT /id="VAR_020496"
FT VARIANT 150
FT /note="G -> S (in dbSNP:rs368420490)"
FT /evidence="ECO:0000269|Ref.10"
FT /id="VAR_020497"
FT VARIANT 163
FT /note="E -> K (unknown pathological significance; no effect
FT on detoxification acivity on methylglyocal-adducted CoA;
FT dbSNP:rs74315354)"
FT /evidence="ECO:0000269|PubMed:16240358,
FT ECO:0000269|PubMed:28993701"
FT /id="VAR_034801"
FT VARIANT 166
FT /note="L -> P (in PARK7; strongly decreases enzymatic
FT activity; reduces protein stability and leads to increased
FT degradation; ubiquitinated by PRKN leading to its
FT recognition by HDAC6 and targeting to aggresome where is
FT degraded; interferes with homodimerization; abolishes
FT interaction with PIAS2; reduced localization in lipid
FT rafts; almost abolished detoxification acivity on
FT methylglyocal-adducted CoA; dbSNP:rs28938172)"
FT /evidence="ECO:0000269|PubMed:12446870,
FT ECO:0000269|PubMed:12851414, ECO:0000269|PubMed:14607841,
FT ECO:0000269|PubMed:14713311, ECO:0000269|PubMed:17846173,
FT ECO:0000269|PubMed:19229105, ECO:0000269|PubMed:22523093,
FT ECO:0000269|PubMed:23847046, ECO:0000269|PubMed:28993701"
FT /id="VAR_020498"
FT VARIANT 171
FT /note="A -> S (in dbSNP:rs777026628)"
FT /evidence="ECO:0000269|PubMed:15254937"
FT /id="VAR_020499"
FT MUTAGEN 10
FT /note="L->P: Abolishes detoxification acivity on
FT methylglyocal-adducted CoA."
FT /evidence="ECO:0000269|PubMed:28993701"
FT MUTAGEN 18
FT /note="E->A: Strongly decreases enzymatic activity. Almost
FT abolishes detoxification acivity on methylglyocal-adducted
FT CoA."
FT /evidence="ECO:0000269|PubMed:22523093,
FT ECO:0000269|PubMed:28993701"
FT MUTAGEN 18
FT /note="E->D: Strongly decreases enzymatic activity."
FT /evidence="ECO:0000269|PubMed:22523093"
FT MUTAGEN 18
FT /note="E->N: Strongly decreases enzymatic activity."
FT /evidence="ECO:0000269|PubMed:22523093"
FT MUTAGEN 18
FT /note="E->Q: Strongly decreases enzymatic activity."
FT /evidence="ECO:0000269|PubMed:22523093"
FT MUTAGEN 46
FT /note="C->A: Reduces protein stability. No effect on
FT oxidation."
FT /evidence="ECO:0000269|PubMed:15181200,
FT ECO:0000269|PubMed:15502874, ECO:0000269|PubMed:18711745,
FT ECO:0000269|PubMed:23847046"
FT MUTAGEN 46
FT /note="C->A: Reduces protein stability. No effect on
FT oxidation. Reduced localization in lipid rafts; when
FT associated with A-106."
FT /evidence="ECO:0000269|PubMed:15181200,
FT ECO:0000269|PubMed:15502874, ECO:0000269|PubMed:18711745,
FT ECO:0000269|PubMed:23847046"
FT MUTAGEN 46
FT /note="C->S: No effect on mitochondrial translocation
FT neither on deglycase activity."
FT /evidence="ECO:0000269|PubMed:15181200,
FT ECO:0000269|PubMed:15502874, ECO:0000269|PubMed:18711745,
FT ECO:0000269|PubMed:23847046, ECO:0000269|PubMed:25416785"
FT MUTAGEN 51
FT /note="V->A: Disrupts dimer formation and strongly reduces
FT ability to eliminate hydrogen peroxide."
FT /evidence="ECO:0000269|PubMed:14749723"
FT MUTAGEN 53
FT /note="C->A: Strongly reduces chaperone activity and
FT ability to eliminate hydrogen peroxide."
FT /evidence="ECO:0000269|PubMed:14749723,
FT ECO:0000269|PubMed:15181200, ECO:0000269|PubMed:15502874,
FT ECO:0000269|PubMed:18711745"
FT MUTAGEN 53
FT /note="C->S: No effect on mitochondrial translocation
FT neither on deglycase activity."
FT /evidence="ECO:0000269|PubMed:14749723,
FT ECO:0000269|PubMed:15181200, ECO:0000269|PubMed:15502874,
FT ECO:0000269|PubMed:18711745, ECO:0000269|PubMed:25416785"
FT MUTAGEN 106
FT /note="C->A: Abolishes enzymatic activity. Abolishes
FT oxidation, association with mitochondria and protease
FT activity. No effect on chaperone activity. Reduces binding
FT to OTUD7B."
FT /evidence="ECO:0000269|PubMed:15181200,
FT ECO:0000269|PubMed:15502874, ECO:0000269|PubMed:16390825,
FT ECO:0000269|PubMed:18711745, ECO:0000269|PubMed:20304780,
FT ECO:0000269|PubMed:21097510, ECO:0000269|PubMed:22523093,
FT ECO:0000269|PubMed:23847046"
FT MUTAGEN 106
FT /note="C->A: Abolishes enzymatic activity. Abolishes
FT oxidation, association with mitochondria and protease
FT activity. No effect on chaperone activity. Reduces binding
FT to OTUD7B. Removes the glycations and restores histone 3.
FT Reduced localization in lipid rafts; when associated with
FT A-46."
FT /evidence="ECO:0000269|PubMed:15181200,
FT ECO:0000269|PubMed:15502874, ECO:0000269|PubMed:16390825,
FT ECO:0000269|PubMed:18711745, ECO:0000269|PubMed:20304780,
FT ECO:0000269|PubMed:21097510, ECO:0000269|PubMed:22523093,
FT ECO:0000269|PubMed:23847046, ECO:0000269|PubMed:30894531"
FT MUTAGEN 106
FT /note="C->D: Abolishes oxidation and association with
FT mitochondria. No effect on chaperone activity."
FT /evidence="ECO:0000269|PubMed:15181200,
FT ECO:0000269|PubMed:15502874, ECO:0000269|PubMed:16390825,
FT ECO:0000269|PubMed:18711745, ECO:0000269|PubMed:20304780,
FT ECO:0000269|PubMed:21097510, ECO:0000269|PubMed:23847046"
FT MUTAGEN 106
FT /note="C->S: Loss of protein and nucleic acid deglycase
FT activity. No effect on mitochondrial translocation. Reduced
FT protease activity. No effect on protection against metal
FT cytotoxicity. No effect on methylglyoxal-adducted
FT glutathione or CoA."
FT /evidence="ECO:0000269|PubMed:15181200,
FT ECO:0000269|PubMed:15502874, ECO:0000269|PubMed:16390825,
FT ECO:0000269|PubMed:18711745, ECO:0000269|PubMed:20304780,
FT ECO:0000269|PubMed:21097510, ECO:0000269|PubMed:23847046,
FT ECO:0000269|PubMed:25416785, ECO:0000269|PubMed:28596309,
FT ECO:0000269|PubMed:28993701"
FT MUTAGEN 126
FT /note="H->A: Strongly decreases enzymatic activity."
FT /evidence="ECO:0000269|PubMed:20304780,
FT ECO:0000269|PubMed:22523093"
FT MUTAGEN 130
FT /note="K->R: Partially compensates for loss of stability;
FT when associated with P-166."
FT /evidence="ECO:0000269|PubMed:12851414"
FT MUTAGEN 179
FT /note="A->T: No effect on detoxification acivity on
FT methylglyocal-adducted CoA."
FT /evidence="ECO:0000269|PubMed:28993701"
FT CONFLICT 119
FT /note="F -> C (in Ref. 3; BAB71782)"
FT /evidence="ECO:0000305"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:2RK3"
FT HELIX 16..28
FT /evidence="ECO:0007829|PDB:2RK3"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:2RK3"
FT TURN 38..41
FT /evidence="ECO:0007829|PDB:1PDW"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:4N0M"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:2OR3"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:2RK3"
FT HELIX 58..62
FT /evidence="ECO:0007829|PDB:2RK3"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:2RK3"
FT HELIX 76..84
FT /evidence="ECO:0007829|PDB:2RK3"
FT HELIX 86..97
FT /evidence="ECO:0007829|PDB:2RK3"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:2RK3"
FT TURN 106..108
FT /evidence="ECO:0007829|PDB:2RK3"
FT HELIX 109..114
FT /evidence="ECO:0007829|PDB:2RK3"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:2RK3"
FT HELIX 130..133
FT /evidence="ECO:0007829|PDB:2RK3"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:2RK3"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:2RK3"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:2RK3"
FT STRAND 152..155
FT /evidence="ECO:0007829|PDB:2RK3"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:2RK3"
FT HELIX 161..173
FT /evidence="ECO:0007829|PDB:2RK3"
FT HELIX 175..182
FT /evidence="ECO:0007829|PDB:2RK3"
FT HELIX 183..185
FT /evidence="ECO:0007829|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
