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Protein

Protein deglycase DJ-1

Gene

Park7

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Protein deglycase that repairs methylglyoxal- and glyoxal-glycated amino acids and proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteines, arginines and lysines residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of advanced glycation endproducts (AGE) (By similarity). Plays an important role in cell protection against oxidative stress and cell death acting as oxidative stress sensor and redox-sensitive chaperone and protease; functions probably related to its primary function (PubMed:15784737, PubMed:17015834, PubMed:20800516, PubMed:21068725). It is involved in neuroprotective mechanisms like the stabilization of NFE2L2 and PINK1 proteins, male fertility as a positive regulator of androgen signaling pathway and cell growth and transformation through, for instance, the modulation of NF-kappa-B signaling pathway (PubMed:17015834, PubMed:21097510). Its involvement in protein repair could explain other unrelated functions. Eliminates hydrogen peroxide and protects cells against hydrogen peroxide-induced cell death (PubMed:17766438). Required for correct mitochondrial morphology and function as well as for autophagy of dysfunctional mitochondria (PubMed:20186336). Plays a role in regulating expression or stability of the mitochondrial uncoupling proteins SLC25A14 and SLC25A27 in dopaminergic neurons of the substantia nigra pars compacta and attenuates the oxidative stress induced by calcium entry into the neurons via L-type channels during pacemaking (PubMed:21068725). Regulates astrocyte inflammatory responses, may modulate lipid rafts-dependent endocytosis in astrocytes and neuronal cells (PubMed:23847046, PubMed:19276172). Binds to a number of mRNAs containing multiple copies of GG or CC motifs and partially inhibits their translation but dissociates following oxidative stress (By similarity). Metal-binding protein able to bind copper as well as toxic mercury ions, enhances the cell protection mechanism against induced metal toxicity (PubMed:23792957).By similarity10 Publications

Cofactori

Note: Does not require glutathione as a cofactor, however, glycated glutathione constitutes a PARK7 substrate.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei106 – 1061NucleophileBy similarity
Active sitei126 – 1261By similarity

GO - Molecular functioni

  1. copper ion binding Source: UniProtKB
  2. cupric ion binding Source: Ensembl
  3. cuprous ion binding Source: Ensembl
  4. glyoxalase (glycolic acid-forming) activity Source: ParkinsonsUK-UCL
  5. glyoxalase III activity Source: ParkinsonsUK-UCL
  6. L-dopa decarboxylase activator activity Source: Ensembl
  7. mercury ion binding Source: UniProtKB
  8. mRNA binding Source: UniProtKB
  9. peptidase activity Source: UniProtKB
  10. peroxiredoxin activity Source: MGI
  11. protein homodimerization activity Source: UniProtKB
  12. RNA binding Source: MGI
  13. superoxide dismutase copper chaperone activity Source: Ensembl
  14. transcription coactivator activity Source: Ensembl
  15. tyrosine 3-monooxygenase activator activity Source: Ensembl

GO - Biological processi

  1. adult locomotory behavior Source: MGI
  2. autophagy Source: UniProtKB-KW
  3. cell proliferation Source: MGI
  4. cellular response to glyoxal Source: ParkinsonsUK-UCL
  5. cellular response to hydrogen peroxide Source: UniProtKB
  6. cellular response to oxidative stress Source: UniProtKB
  7. cellular response to reactive oxygen species Source: MGI
  8. detoxification of copper ion Source: UniProtKB
  9. detoxification of mercury ion Source: UniProtKB
  10. dopamine uptake involved in synaptic transmission Source: MGI
  11. enzyme active site formation via L-cysteine sulfinic acid Source: ParkinsonsUK-UCL
  12. glycolate biosynthetic process Source: ParkinsonsUK-UCL
  13. glyoxal catabolic process Source: ParkinsonsUK-UCL
  14. hydrogen peroxide metabolic process Source: MGI
  15. inflammatory response Source: UniProtKB-KW
  16. membrane depolarization Source: MGI
  17. membrane hyperpolarization Source: MGI
  18. methylglyoxal catabolic process to D-lactate Source: ParkinsonsUK-UCL
  19. mitochondrion organization Source: UniProtKB
  20. negative regulation of apoptotic process Source: ParkinsonsUK-UCL
  21. negative regulation of cell death Source: UniProtKB
  22. negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway Source: Ensembl
  23. negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway Source: ParkinsonsUK-UCL
  24. negative regulation of gene expression Source: Ensembl
  25. negative regulation of hydrogen peroxide-induced neuron death Source: ParkinsonsUK-UCL
  26. negative regulation of hydrogen peroxide-induced neuron intrinsic apoptotic signaling pathway Source: ParkinsonsUK-UCL
  27. negative regulation of oxidative stress-induced neuron death Source: ParkinsonsUK-UCL
  28. negative regulation of proteasomal ubiquitin-dependent protein catabolic process Source: Ensembl
  29. negative regulation of protein acetylation Source: Ensembl
  30. negative regulation of protein binding Source: UniProtKB
  31. negative regulation of protein catabolic process Source: ParkinsonsUK-UCL
  32. negative regulation of protein export from nucleus Source: Ensembl
  33. negative regulation of protein K48-linked deubiquitination Source: Ensembl
  34. negative regulation of protein kinase activity Source: Ensembl
  35. negative regulation of protein sumoylation Source: Ensembl
  36. negative regulation of protein ubiquitination Source: ParkinsonsUK-UCL
  37. negative regulation of TRAIL-activated apoptotic signaling pathway Source: Ensembl
  38. negative regulation of ubiquitin-protein transferase activity Source: ParkinsonsUK-UCL
  39. negative regulation of ubiquitin-specific protease activity Source: Ensembl
  40. positive regulation of androgen receptor activity Source: Ensembl
  41. positive regulation of gene expression Source: ParkinsonsUK-UCL
  42. positive regulation of interleukin-8 production Source: Ensembl
  43. positive regulation of L-dopa biosynthetic process Source: Ensembl
  44. positive regulation of mitochondrial electron transport, NADH to ubiquinone Source: ParkinsonsUK-UCL
  45. positive regulation of oxidative phosphorylation uncoupler activity Source: UniProtKB
  46. positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: MGI
  47. positive regulation of peptidyl-serine phosphorylation Source: Ensembl
  48. positive regulation of protein homodimerization activity Source: Ensembl
  49. positive regulation of protein localization to nucleus Source: Ensembl
  50. positive regulation of pyrroline-5-carboxylate reductase activity Source: Ensembl
  51. positive regulation of reactive oxygen species biosynthetic process Source: MGI
  52. positive regulation of superoxide dismutase activity Source: Ensembl
  53. positive regulation of transcription from RNA polymerase II promoter Source: ParkinsonsUK-UCL
  54. positive regulation of transcription regulatory region DNA binding Source: Ensembl
  55. protein deglycosylation Source: UniProtKB
  56. protein stabilization Source: UniProtKB
  57. regulation of inflammatory response Source: UniProtKB
  58. regulation of mitochondrial membrane potential Source: Ensembl
  59. regulation of neuron apoptotic process Source: UniProtKB
  60. response to hydrogen peroxide Source: MGI
  61. single fertilization Source: UniProtKB-KW
  62. synaptic transmission, dopaminergic Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Hydrolase, Protease

Keywords - Biological processi

Autophagy, Fertilization, Inflammatory response, Stress response

Keywords - Ligandi

Copper, RNA-binding

Protein family/group databases

MEROPSiC56.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein deglycase DJ-1By similarity (EC:3.1.2.-By similarity, EC:3.5.1.-By similarity)
Alternative name(s):
Parkinson disease protein 7 homolog
Gene namesi
Name:Park7Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:2135637. Park7.

Subcellular locationi

Cell membrane 1 Publication; Lipid-anchor 1 Publication. Cytoplasm By similarity. Membrane raft 1 Publication. Nucleus By similarity. Mitochondrion By similarity
Note: Under normal conditions, located predominantly in the cytoplasm and, to a lesser extent, in the nucleus and mitochondrion. Translocates to the mitochondrion and subsequently to the nucleus in response to oxidative stress and exerts an increased cytoprotective effect against oxidative damage (By similarity). Membrane raft localization in astrocytes and neuronal cells requires palmitoylation (PubMed:23847046).By similarity1 Publication

GO - Cellular componenti

  1. cell body Source: ParkinsonsUK-UCL
  2. chromatin Source: Ensembl
  3. cytoplasm Source: UniProtKB
  4. cytosol Source: ParkinsonsUK-UCL
  5. endoplasmic reticulum Source: MGI
  6. extracellular vesicular exosome Source: Ensembl
  7. membrane raft Source: UniProtKB-SubCell
  8. mitochondrial intermembrane space Source: ParkinsonsUK-UCL
  9. mitochondrial matrix Source: ParkinsonsUK-UCL
  10. mitochondrial respiratory chain complex I Source: Ensembl
  11. mitochondrion Source: ParkinsonsUK-UCL
  12. neuron projection Source: ParkinsonsUK-UCL
  13. nucleus Source: UniProtKB
  14. plasma membrane Source: UniProtKB-SubCell
  15. PML body Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Mitochondrion, Nucleus

Pathology & Biotechi

Disruption phenotypei

Increased sensitivity of embryonic cortical neurons to oxidative stress. Age-dependent increase in mitochondrial hydrogen peroxide production and reduced mitochondrial aconitase activity. Down-regulation of Slc25a14 and Slc25a27, compromised calcium-induced uncoupling and increased oxidation of mitochondrial matrix proteins specifically in the dopaminergic neurons of the substantia nigra pars compacta. Reduced N2el2 protein expression. Impaired mitochondrial function and morphology with reduced autophagy leading to accumulation of defective mitochondria. Targeted knockouts in astrocytes exhibit augmented LPS-induced CRK/p38 phosphorylation and signaling, they don't stimulate TLR4 endocytosis upon LPS stimulation.6 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi46 – 461C → A: Sulfinic acid detected following treatment with hydrogen peroxide. 1 Publication
Mutagenesisi53 – 531C → A: Sulfinic acid detected following treatment with hydrogen peroxide. 1 Publication
Mutagenesisi106 – 1061C → A: No sulfinic acid detected following treatment with hydrogen peroxide. 1 Publication

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei? – 189Removed in mature formPRO_0000405560
Chaini1 – ?Protein deglycase DJ-1PRO_0000157850

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi46 – 461S-palmitoyl cysteineBy similarity
Lipidationi53 – 531S-palmitoyl cysteineBy similarity
Modified residuei67 – 671PhosphotyrosineBy similarity
Modified residuei106 – 1061Cysteine sulfinic acid (-SO2H); alternateBy similarity
Lipidationi106 – 1061S-palmitoyl cysteine; alternateBy similarity
Cross-linki130 – 130Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei148 – 1481N6-acetyllysine1 Publication
Modified residuei182 – 1821N6-succinyllysine1 Publication

Post-translational modificationi

Sumoylated on Lys-130 by PIAS2 or PIAS4; which is essential for cell-growth promoting activity and transforming activity.By similarity
Undergoes cleavage of a C-terminal peptide and subsequent activation of protease activity in response to oxidative stress.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Lipoprotein, Oxidation, Palmitate, Phosphoprotein, Ubl conjugation, Zymogen

Proteomic databases

MaxQBiQ99LX0.
PaxDbiQ99LX0.
PRIDEiQ99LX0.

2D gel databases

REPRODUCTION-2DPAGEQ99LX0.
UCD-2DPAGEQ99LX0.

PTM databases

PhosphoSiteiQ99LX0.

Expressioni

Tissue specificityi

Expressed in erythroblasts and in mature red blood cells from peripheral blood (at protein level).1 Publication

Developmental stagei

Expression increases during erythroid development (at protein level).1 Publication

Inductioni

By hydrogen peroxide.1 Publication

Gene expression databases

BgeeiQ99LX0.
ExpressionAtlasiQ99LX0. baseline and differential.
GenevestigatoriQ99LX0.

Interactioni

Subunit structurei

Homodimer. Binds EFCAB6/DJBP and PIAS2. Part of a ternary complex containing PARK7, EFCAB6/DJBP and AR. Binds to HIPK1 (By similarity). Interacts (via N-terminus) with OTUD7B (PubMed:21097510). Interacts with BBS1, CLCF1 and MTERF (PubMed:21097510).By similarity1 Publication

Protein-protein interaction databases

BioGridi208257. 13 interactions.
IntActiQ99LX0. 8 interactions.
MINTiMINT-1869265.
STRINGi10090.ENSMUSP00000101300.

Structurei

3D structure databases

ProteinModelPortaliQ99LX0.
SMRiQ99LX0. Positions 1-189.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C56 family.Curated

Phylogenomic databases

eggNOGiCOG0693.
GeneTreeiENSGT00390000001231.
HOGENOMiHOG000063194.
HOVERGENiHBG053511.
InParanoidiQ99LX0.
KOiK05687.
OMAiMAGDHYK.
OrthoDBiEOG7CVPZX.
PhylomeDBiQ99LX0.
TreeFamiTF300119.

Family and domain databases

Gene3Di3.40.50.880. 1 hit.
InterProiIPR029062. Class_I_gatase-like.
IPR006287. DJ1.
IPR002818. ThiJ/PfpI.
[Graphical view]
PfamiPF01965. DJ-1_PfpI. 1 hit.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
TIGRFAMsiTIGR01383. not_thiJ. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q99LX0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASKRALVIL AKGAEEMETV IPVDVMRRAG IKVTVAGLAG KDPVQCSRDV
60 70 80 90 100
MICPDTSLED AKTQGPYDVV VLPGGNLGAQ NLSESPMVKE ILKEQESRKG
110 120 130 140 150
LIAAICAGPT ALLAHEVGFG CKVTTHPLAK DKMMNGSHYS YSESRVEKDG
160 170 180
LILTSRGPGT SFEFALAIVE ALVGKDMANQ VKAPLVLKD
Length:189
Mass (Da):20,021
Last modified:June 1, 2001 - v1
Checksum:i877C825CCA07468F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti127 – 1271P → T in BAE40278 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB015652 mRNA. Translation: BAA29063.2.
AK146368 mRNA. Translation: BAE27118.1.
AK153948 mRNA. Translation: BAE32271.1.
AK168341 mRNA. Translation: BAE40278.1.
AL607084 Genomic DNA. Translation: CAM19230.1.
BC002187 mRNA. Translation: AAH02187.1.
CCDSiCCDS18975.1.
RefSeqiNP_065594.2. NM_020569.3.
UniGeneiMm.277349.

Genome annotation databases

EnsembliENSMUST00000030805; ENSMUSP00000030805; ENSMUSG00000028964.
ENSMUST00000105673; ENSMUSP00000101298; ENSMUSG00000028964.
ENSMUST00000105674; ENSMUSP00000101299; ENSMUSG00000028964.
ENSMUST00000105675; ENSMUSP00000101300; ENSMUSG00000028964.
GeneIDi57320.
KEGGimmu:57320.
UCSCiuc008vxz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB015652 mRNA. Translation: BAA29063.2.
AK146368 mRNA. Translation: BAE27118.1.
AK153948 mRNA. Translation: BAE32271.1.
AK168341 mRNA. Translation: BAE40278.1.
AL607084 Genomic DNA. Translation: CAM19230.1.
BC002187 mRNA. Translation: AAH02187.1.
CCDSiCCDS18975.1.
RefSeqiNP_065594.2. NM_020569.3.
UniGeneiMm.277349.

3D structure databases

ProteinModelPortaliQ99LX0.
SMRiQ99LX0. Positions 1-189.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi208257. 13 interactions.
IntActiQ99LX0. 8 interactions.
MINTiMINT-1869265.
STRINGi10090.ENSMUSP00000101300.

Protein family/group databases

MEROPSiC56.002.

PTM databases

PhosphoSiteiQ99LX0.

2D gel databases

REPRODUCTION-2DPAGEQ99LX0.
UCD-2DPAGEQ99LX0.

Proteomic databases

MaxQBiQ99LX0.
PaxDbiQ99LX0.
PRIDEiQ99LX0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030805; ENSMUSP00000030805; ENSMUSG00000028964.
ENSMUST00000105673; ENSMUSP00000101298; ENSMUSG00000028964.
ENSMUST00000105674; ENSMUSP00000101299; ENSMUSG00000028964.
ENSMUST00000105675; ENSMUSP00000101300; ENSMUSG00000028964.
GeneIDi57320.
KEGGimmu:57320.
UCSCiuc008vxz.2. mouse.

Organism-specific databases

CTDi11315.
MGIiMGI:2135637. Park7.

Phylogenomic databases

eggNOGiCOG0693.
GeneTreeiENSGT00390000001231.
HOGENOMiHOG000063194.
HOVERGENiHBG053511.
InParanoidiQ99LX0.
KOiK05687.
OMAiMAGDHYK.
OrthoDBiEOG7CVPZX.
PhylomeDBiQ99LX0.
TreeFamiTF300119.

Miscellaneous databases

NextBioi313682.
PROiQ99LX0.
SOURCEiSearch...

Gene expression databases

BgeeiQ99LX0.
ExpressionAtlasiQ99LX0. baseline and differential.
GenevestigatoriQ99LX0.

Family and domain databases

Gene3Di3.40.50.880. 1 hit.
InterProiIPR029062. Class_I_gatase-like.
IPR006287. DJ1.
IPR002818. ThiJ/PfpI.
[Graphical view]
PfamiPF01965. DJ-1_PfpI. 1 hit.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
TIGRFAMsiTIGR01383. not_thiJ. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of human and mouse DJ-1 genes and identification of Sp1-dependent activation of the human DJ-1 promoter."
    Taira T., Takahashi K., Kitagawa R., Iguchi-Ariga S.M.M., Ariga H.
    Gene 263:285-292(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Kidney.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: BALB/c and NOD.
    Tissue: Thymus.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  5. Lubec G., Klug S.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 13-27; 63-89 AND 99-122, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hippocampus.
  6. "DJ-1 has a role in antioxidative stress to prevent cell death."
    Taira T., Saito Y., Niki T., Iguchi-Ariga S.M., Takahashi K., Ariga H.
    EMBO Rep. 5:213-218(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  7. "Hypersensitivity of DJ-1-deficient mice to 1-methyl-4-phenyl-1,2,3,6-tetrahydropyrindine (MPTP) and oxidative stress."
    Kim R.H., Smith P.D., Aleyasin H., Hayley S., Mount M.P., Pownall S., Wakeham A., You-Ten A.J., Kalia S.K., Horne P., Westaway D., Lozano A.M., Anisman H., Park D.S., Mak T.W.
    Proc. Natl. Acad. Sci. U.S.A. 102:5215-5220(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  8. "DJ-1, a cancer- and Parkinson's disease-associated protein, stabilizes the antioxidant transcriptional master regulator Nrf2."
    Clements C.M., McNally R.S., Conti B.J., Mak T.W., Ting J.P.
    Proc. Natl. Acad. Sci. U.S.A. 103:15091-15096(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  9. Cited for: FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF CYS-46; CYS-53 AND CYS-106.
  10. "Regulation of astrocyte inflammatory responses by the Parkinson's disease-associated gene DJ-1."
    Waak J., Weber S.S., Waldenmaier A., Gorner K., Alunni-Fabbroni M., Schell H., Vogt-Weisenhorn D., Pham T.T., Reumers V., Baekelandt V., Wurst W., Kahle P.J.
    FASEB J. 23:2478-2489(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "The familial Parkinson's disease gene DJ-1 (PARK7) is expressed in red cells and plays a role in protection against oxidative damage."
    Xu X., Martin F., Friedman J.S.
    Blood Cells Mol. Dis. 45:227-232(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  12. "DJ-1 enhances cell survival through the binding of cezanne, a negative regulator of NF-{kappa}B."
    McNally R.S., Davis B.K., Clements C.M., Accavitti-Loper M.A., Mak T.W., Ting J.P.
    J. Biol. Chem. 286:4098-4106(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BBS1; CLCF1; MTERF AND OTUD7B.
  13. "Oxidant stress evoked by pacemaking in dopaminergic neurons is attenuated by DJ-1."
    Guzman J.N., Sanchez-Padilla J., Wokosin D., Kondapalli J., Ilijic E., Schumacker P.T., Surmeier D.J.
    Nature 468:696-700(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  14. "Reduced basal autophagy and impaired mitochondrial dynamics due to loss of Parkinson's disease-associated protein DJ-1."
    Krebiehl G., Ruckerbauer S., Burbulla L.F., Kieper N., Maurer B., Waak J., Wolburg H., Gizatullina Z., Gellerich F.N., Woitalla D., Riess O., Kahle P.J., Proikas-Cezanne T., Kruger R.
    PLoS ONE 5:E9367-E9367(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  15. Cited for: FUNCTION, CAUTION.
  16. "DJ-1 associates with lipid rafts by palmitoylation and regulates lipid rafts-dependent endocytosis in astrocytes."
    Kim K.S., Kim J.S., Park J.Y., Suh Y.H., Jou I., Joe E.H., Park S.M.
    Hum. Mol. Genet. 22:4805-4817(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
  17. "Parkinson disease protein DJ-1 binds metals and protects against metal-induced cytotoxicity."
    Bjorkblom B., Adilbayeva A., Maple-Grodem J., Piston D., Okvist M., Xu X.M., Brede C., Larsen J.P., Moller S.G.
    J. Biol. Chem. 288:22809-22820(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-148, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-182, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiPARK7_MOUSE
AccessioniPrimary (citable) accession number: Q99LX0
Secondary accession number(s): O88306, Q3THB9, Q3U509
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 7, 2004
Last sequence update: June 1, 2001
Last modified: March 4, 2015
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Glyoxylase activity previously reported reflects in fact its deglycase activity (PubMed:22523093).By similarity1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.