CPLM-019718

Genbank Nucleotide ID

Protein Synonyms/Alias

Oncogene DJ1; Parkinson disease protein 7

Homo sapiens (Human)

Position	Peptide	Type	References
41	TVAGLAGKDPVQCSR	ubiquitination	[1, 2, 3, 4]
63	ASLEDAKKEGPYDVV	ubiquitination	[3]
89	LSESAAVKEILKEQE	ubiquitination	[5]
130	VTTHPLAKDKMMNGG	sumoylation	[6, 7]
148	YSENRVEKDGLILTS	acetylation	[8]
148	YSENRVEKDGLILTS	ubiquitination	[1, 4]
182	KEVAAQVKAPLVLKD	ubiquitination	[3]
188	VKAPLVLKD******	ubiquitination	[3]

[1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[2] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
[3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
[5] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[6] Crystal structure of human DJ-1, a protein associated with early onset Parkinson's disease.
Tao X, Tong L.
J Biol Chem. 2003 Aug 15;278(33):31372-9. [PMID: 12761214]
[7] Proper SUMO-1 conjugation is essential to DJ-1 to exert its full activities.
Shinbo Y, Niki T, Taira T, Ooe H, Takahashi-Niki K, Maita C, Seino C, Iguchi-Ariga SM, Ariga H.
Cell Death Differ. 2006 Jan;13(1):96-108. [PMID: 15976810]
[8] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]

Functional Description

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.

ACT_SITE 106 106 Probable.
ACT_SITE 126 126 Probable.
MOD_RES 67 67 Phosphotyrosine.
MOD_RES 106 106 Cysteine sulfinic acid (-SO2H).
CROSSLNK 130 130 Glycyl lysine isopeptide (Lys-Gly)

3D-structure; Autophagy; Chaperone; Complete proteome; Cytoplasm; Direct protein sequencing; Disease mutation; Fertilization; Hydrolase; Inflammatory response; Isopeptide bond; Mitochondrion; Neurodegeneration; Nucleus; Oxidation; Parkinson disease; Parkinsonism; Phosphoprotein; Polymorphism; Protease; Reference proteome; RNA-binding; Stress response; Tumor suppressor; Ubl conjugation; Zymogen.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO:0005634; C:nucleus; IDA:UniProtKB.
GO:0003729; F:mRNA binding; IDA:UniProtKB.
GO:0008233; F:peptidase activity; IDA:UniProtKB.
GO:0004601; F:peroxidase activity; ISS:UniProtKB.
GO:0051920; F:peroxiredoxin activity; IEA:Compara.
GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO:0008344; P:adult locomotory behavior; IEA:Compara.
GO:0006914; P:autophagy; IEA:UniProtKB-KW.
GO:0008219; P:cell death; IEA:UniProtKB-KW.
GO:0070301; P:cellular response to hydrogen peroxide; IDA:UniProtKB.
GO:0051583; P:dopamine uptake involved in synaptic transmission; IEA:Compara.
GO:0042743; P:hydrogen peroxide metabolic process; IEA:Compara.
GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO:0051899; P:membrane depolarization; IEA:Compara.
GO:0060081; P:membrane hyperpolarization; IEA:Compara.
GO:0007005; P:mitochondrion organization; ISS:UniProtKB.
GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IMP:UniProtKB.
GO:0043524; P:negative regulation of neuron apoptotic process; IDA:BHF-UCL.
GO:0032091; P:negative regulation of protein binding; IDA:UniProtKB.
GO:2000277; P:positive regulation of oxidative phosphorylation uncoupler activity; IEA:Compara.
GO:0050821; P:protein stabilization; IMP:UniProtKB.
GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
GO:0060765; P:regulation of androgen receptor signaling pathway; IDA:UniProtKB.
GO:0050727; P:regulation of inflammatory response; ISS:UniProtKB.
GO:0007338; P:single fertilization; IEA:UniProtKB-KW.

IPR006287; DJ1.
IPR002818; ThiJ/PfpI.