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Q99LX0

- PARK7_MOUSE

UniProt

Q99LX0 - PARK7_MOUSE

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Protein

Protein DJ-1

Gene

Park7

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

Functioni

Protects cells against oxidative stress and cell death. 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. Eliminates hydrogen peroxide and protects cells against hydrogen peroxide-induced cell death. Following removal of a C-terminal peptide, displays protease activity and enhanced cytoprotective action against oxidative stress-induced apoptosis. Stabilizes NFE2L2 by preventing its association with KEAP1 and its subsequent ubiquitination. Binds to OTUD7B and inhibits its deubiquitinating activity. Enhances RELA nuclear translocation. Binds to a number of mRNAs containing multiple copies of GG or CC motifs and partially inhibits their translation but dissociates following oxidative stress. Required for correct mitochondrial morphology and function and for autophagy of dysfunctional mitochondria. Regulates astrocyte inflammatory responses. Acts as a positive regulator of androgen receptor-dependent transcription. Prevents aggregation of SNCA. Plays a role in fertilization. Has no proteolytic activity. Has cell-growth promoting activity and transforming activity. May function as a redox-sensitive chaperone. May regulate lipid rafts-dependent endocytosis in astrocytes and neuronal cells.8 Publications

Sites

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

GO - Molecular functioni

  1. glyoxalase (glycolic acid-forming) activity Source: ParkinsonsUK-UCL
  2. glyoxalase III activity Source: ParkinsonsUK-UCL
  3. mRNA binding Source: UniProtKB
  4. peptidase activity Source: UniProtKB
  5. peroxiredoxin activity Source: MGI
  6. protein homodimerization activity Source: UniProtKB
  7. RNA binding Source: MGI

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. dopamine uptake involved in synaptic transmission Source: MGI
  9. enzyme active site formation via L-cysteine sulfinic acid Source: ParkinsonsUK-UCL
  10. glycolate biosynthetic process Source: ParkinsonsUK-UCL
  11. glyoxal catabolic process Source: ParkinsonsUK-UCL
  12. hydrogen peroxide metabolic process Source: MGI
  13. inflammatory response Source: UniProtKB-KW
  14. lactate biosynthetic process Source: GOC
  15. membrane depolarization Source: MGI
  16. membrane hyperpolarization Source: MGI
  17. methylglyoxal catabolic process to D-lactate Source: ParkinsonsUK-UCL
  18. mitochondrion organization Source: UniProtKB
  19. negative regulation of apoptotic process Source: ParkinsonsUK-UCL
  20. negative regulation of cell death Source: UniProtKB
  21. negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway Source: Ensembl
  22. negative regulation of extrinsic apoptotic signaling pathway Source: Ensembl
  23. negative regulation of hydrogen peroxide-induced neuron death Source: ParkinsonsUK-UCL
  24. negative regulation of neuron apoptotic process Source: Ensembl
  25. negative regulation of oxidative stress-induced neuron death Source: ParkinsonsUK-UCL
  26. negative regulation of protein binding Source: UniProtKB
  27. negative regulation of protein catabolic process Source: ParkinsonsUK-UCL
  28. negative regulation of protein export from nucleus Source: Ensembl
  29. negative regulation of protein K48-linked deubiquitination Source: Ensembl
  30. negative regulation of protein kinase activity Source: Ensembl
  31. negative regulation of protein ubiquitination Source: ParkinsonsUK-UCL
  32. negative regulation of ubiquitin-protein transferase activity Source: ParkinsonsUK-UCL
  33. negative regulation of ubiquitin-specific protease activity Source: Ensembl
  34. positive regulation of androgen receptor activity Source: Ensembl
  35. positive regulation of interleukin-8 production Source: Ensembl
  36. positive regulation of mitochondrial electron transport, NADH to ubiquinone Source: ParkinsonsUK-UCL
  37. positive regulation of oxidative phosphorylation uncoupler activity Source: UniProtKB
  38. positive regulation of protein localization to nucleus Source: Ensembl
  39. positive regulation of transcription from RNA polymerase II promoter Source: ParkinsonsUK-UCL
  40. protein stabilization Source: UniProtKB
  41. regulation of inflammatory response Source: UniProtKB
  42. regulation of neuron apoptotic process Source: UniProtKB
  43. response to hydrogen peroxide Source: MGI
  44. single fertilization Source: UniProtKB-KW
  45. 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

RNA-binding

Protein family/group databases

MEROPSiC56.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein DJ-1 (EC:3.4.-.-)
Alternative name(s):
Parkinson disease protein 7 homolog
Gene namesi
Name:Park7
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. Membrane raft localization in astrocytes and neuronal cells requires palmitoylation (By similarity).By similarity

GO - Cellular componenti

  1. cell body Source: ParkinsonsUK-UCL
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: ParkinsonsUK-UCL
  4. extracellular vesicular exosome Source: Ensembl
  5. mitochondrial intermembrane space Source: ParkinsonsUK-UCL
  6. mitochondrial matrix Source: ParkinsonsUK-UCL
  7. mitochondrion Source: ParkinsonsUK-UCL
  8. neuron projection Source: ParkinsonsUK-UCL
  9. nucleus Source: UniProtKB
  10. plasma membrane Source: UniProtKB-KW
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 formBy similarityPRO_0000405560
Chaini1 – ?Protein 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 (By similarity). Interacts (via N-terminus) with OTUD7B. Interacts with BBS1, CLCF1 and MTERF. Binds to HIPK1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi208257. 12 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.
OMAiVGREKAY.
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS18975.1.
RefSeqi NP_065594.2. NM_020569.3.
UniGenei Mm.277349.

3D structure databases

ProteinModelPortali Q99LX0.
SMRi Q99LX0. Positions 1-189.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 208257. 12 interactions.
IntActi Q99LX0. 8 interactions.
MINTi MINT-1869265.
STRINGi 10090.ENSMUSP00000101300.

Protein family/group databases

MEROPSi C56.002.

PTM databases

PhosphoSitei Q99LX0.

2D gel databases

REPRODUCTION-2DPAGE Q99LX0.
UCD-2DPAGE Q99LX0.

Proteomic databases

MaxQBi Q99LX0.
PaxDbi Q99LX0.
PRIDEi Q99LX0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000030805 ; ENSMUSP00000030805 ; ENSMUSG00000028964 .
ENSMUST00000105673 ; ENSMUSP00000101298 ; ENSMUSG00000028964 .
ENSMUST00000105674 ; ENSMUSP00000101299 ; ENSMUSG00000028964 .
ENSMUST00000105675 ; ENSMUSP00000101300 ; ENSMUSG00000028964 .
GeneIDi 57320.
KEGGi mmu:57320.
UCSCi uc008vxz.2. mouse.

Organism-specific databases

CTDi 11315.
MGIi MGI:2135637. Park7.

Phylogenomic databases

eggNOGi COG0693.
GeneTreei ENSGT00390000001231.
HOGENOMi HOG000063194.
HOVERGENi HBG053511.
InParanoidi Q99LX0.
KOi K05687.
OMAi VGREKAY.
OrthoDBi EOG7CVPZX.
PhylomeDBi Q99LX0.
TreeFami TF300119.

Miscellaneous databases

NextBioi 313682.
PROi Q99LX0.
SOURCEi Search...

Gene expression databases

Bgeei Q99LX0.
ExpressionAtlasi Q99LX0. baseline and differential.
Genevestigatori Q99LX0.

Family and domain databases

Gene3Di 3.40.50.880. 1 hit.
InterProi IPR029062. Class_I_gatase-like.
IPR006287. DJ1.
IPR002818. ThiJ/PfpI.
[Graphical view ]
Pfami PF01965. DJ-1_PfpI. 1 hit.
[Graphical view ]
SUPFAMi SSF52317. SSF52317. 1 hit.
TIGRFAMsi TIGR01383. not_thiJ. 1 hit.
ProtoNeti Search...

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. "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.
  16. "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: October 29, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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