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Q99LX0

- PARK7_MOUSE

UniProt

Q99LX0 - PARK7_MOUSE

Protein

Protein DJ-1

Gene

Park7

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    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. mRNA binding Source: UniProtKB
    2. peptidase activity Source: UniProtKB
    3. peroxiredoxin activity Source: MGI
    4. protein binding Source: ParkinsonsUK-UCL
    5. protein homodimerization activity Source: UniProtKB
    6. 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 hydrogen peroxide Source: UniProtKB
    5. cellular response to oxidative stress Source: UniProtKB
    6. cellular response to reactive oxygen species Source: MGI
    7. dopamine uptake involved in synaptic transmission Source: MGI
    8. enzyme active site formation via L-cysteine sulfinic acid Source: ParkinsonsUK-UCL
    9. hydrogen peroxide metabolic process Source: MGI
    10. inflammatory response Source: UniProtKB-KW
    11. membrane depolarization Source: MGI
    12. membrane hyperpolarization Source: MGI
    13. mitochondrion organization Source: UniProtKB
    14. negative regulation of cell death Source: UniProtKB
    15. negative regulation of extrinsic apoptotic signaling pathway Source: Ensembl
    16. negative regulation of hydrogen peroxide-mediated programmed cell death Source: ParkinsonsUK-UCL
    17. negative regulation of neuron apoptotic process Source: ParkinsonsUK-UCL
    18. negative regulation of protein binding Source: UniProtKB
    19. negative regulation of protein catabolic process Source: ParkinsonsUK-UCL
    20. negative regulation of protein ubiquitination Source: ParkinsonsUK-UCL
    21. negative regulation of ubiquitin-protein transferase activity Source: ParkinsonsUK-UCL
    22. positive regulation of oxidative phosphorylation uncoupler activity Source: UniProtKB
    23. positive regulation of transcription from RNA polymerase II promoter Source: ParkinsonsUK-UCL
    24. protein stabilization Source: UniProtKB
    25. regulation of androgen receptor signaling pathway Source: Ensembl
    26. regulation of inflammatory response Source: UniProtKB
    27. regulation of neuron apoptotic process Source: UniProtKB
    28. response to hydrogen peroxide Source: MGI
    29. single fertilization Source: UniProtKB-KW
    30. synaptic transmission, dopaminergic Source: MGI

    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. membrane raft Source: UniProtKB-SubCell
    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-SubCell

    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

    ArrayExpressiQ99LX0.
    BgeeiQ99LX0.
    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. 7 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

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    MASKRALVIL AKGAEEMETV IPVDVMRRAG IKVTVAGLAG KDPVQCSRDV    50
    MICPDTSLED AKTQGPYDVV VLPGGNLGAQ NLSESPMVKE ILKEQESRKG 100
    LIAAICAGPT ALLAHEVGFG CKVTTHPLAK DKMMNGSHYS YSESRVEKDG 150
    LILTSRGPGT SFEFALAIVE ALVGKDMANQ VKAPLVLKD 189
    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. 7 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

    ArrayExpressi Q99LX0.
    Bgeei Q99LX0.
    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

    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 1, 2014
    This is version 106 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