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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. May act as an atypical peroxiredoxin-like peroxidase that scavenges hydrogen peroxide. 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 – 1061 By similarity
Active sitei126 – 1261 By similarity

GO - Molecular functioni

  1. RNA binding Source: MGI
  2. mRNA binding Source: UniProtKB
  3. peptidase activity Source: UniProtKB
  4. peroxidase activity Source: UniProtKB
  5. peroxiredoxin activity Source: MGI
  6. protein homodimerization activity Source: UniProtKB

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. hydrogen peroxide metabolic process Source: MGI
  9. inflammatory response Source: UniProtKB-KW
  10. membrane depolarization Source: MGI
  11. membrane hyperpolarization Source: MGI
  12. mitochondrion organization Source: UniProtKB
  13. negative regulation of cell death Source: UniProtKB
  14. negative regulation of extrinsic apoptotic signaling pathway Source: Ensembl
  15. negative regulation of neuron apoptotic process Source: Ensembl
  16. negative regulation of protein binding Source: UniProtKB
  17. oxidation-reduction process Source: GOC
  18. positive regulation of oxidative phosphorylation uncoupler activity Source: UniProtKB
  19. positive regulation of transcription from RNA polymerase II promoter Source: ParkinsonsUK-UCL
  20. protein stabilization Source: UniProtKB
  21. regulation of androgen receptor signaling pathway Source: Ensembl
  22. regulation of inflammatory response Source: UniProtKB
  23. regulation of neuron apoptotic process Source: UniProtKB
  24. response to hydrogen peroxide Source: MGI
  25. single fertilization Source: UniProtKB-KW
  26. 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; Lipid-anchor. Cytoplasm By similarity. Membrane raft. 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.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Ensembl
  3. membrane raft Source: UniProtKB-SubCell
  4. mitochondrion Source: MGI
  5. nucleus Source: UniProtKB
  6. plasma membrane Source: UniProtKB-SubCell
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 form By similarityPRO_0000405560
Chaini1 – ?Protein DJ-1PRO_0000157850

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi46 – 461S-palmitoyl cysteine By similarity
Lipidationi53 – 531S-palmitoyl cysteine By similarity
Modified residuei67 – 671Phosphotyrosine By similarity
Modified residuei106 – 1061Cysteine sulfinic acid (-SO2H); alternate By similarity
Lipidationi106 – 1061S-palmitoyl cysteine; alternate By 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.1 Publication

Protein-protein interaction databases

BioGridi208257. 12 interactions.
IntActiQ99LX0. 7 interactions.
MINTiMINT-1869265.
STRINGi10090.ENSMUSP00000101300.

Structurei

3D structure databases

ProteinModelPortaliQ99LX0.
SMRiQ99LX0. Positions 1-189.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase C56 family.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti127 – 1271P → T in BAE40278. 1 Publication

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

« 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: September 3, 2014
This is version 105 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

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