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PARK7 (Parkinsonism associated deglycase)

Written2016-04Valentina La Cognata, Sebastiano Cavallaro
Institute of Neurological Sciences, National Research Council, Catania (VLA, SC); Department of Biomedical and Biotechnological Sciences, Section of Human Anatomy and Histology, University of Catania (VLA) - Italy. sebastiano.cavallaro@cnr.it; v.lacognata@isn.cnr.it

Abstract PARK7 (also called DJ-1 or Parkinsonism associated deglycase) is a pleiotropic protein belonging to the peptidase C56 family. It acts as positive regulator of androgen receptor-dependent transcription, redox-sensitive chaperone, sensor for oxidative stress, and apparently protects neurons against oxidative stress and cell death. Dysfunctions in PARK7 are related to autosomal recessive early-onset Parkinson disease 7 and cancer forms. Here, we review some major data on PARK7, concerning the genetic structure, the transcription regulation, the encoded protein and functions, and its implication in human diseases.

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Identity

Other namesDJ1
DJ-1
HEL-S-67p
RS
CAP1
FLJ27376
FLJ92274
FLJ34360
HGNC (Hugo) PARK7
LocusID (NCBI) 11315
Atlas_Id 41639
Location Location Cytogenetic location: 1p36.23; Molecular location: Chromosome 1; Start 7961654; Stop 7985282based on Genome Browser Human Dec. 2013 (GRCh38/hg38) Assembly [Link to chromosome band 1p36]  [Link to chromosome band 1p36]
Location_base_pair Starts at 8021714 and ends at 8045342 bp from pter ( according to hg19-Feb_2009)  [Mapping PARK7.png]
Local_order PARK7 is flanked towards the telomeric direction by two protein-coding genes (UTS2 and TNFRSF9) and towards the centromeric direction by ERRFI1. According to NCBI MapViewer, a non-coding RNA (LOC105376694) is also present in this locus (Figure 1).
 
  Figure 1 displays the human chromosome 1 (NCBI Reference Sequence NC_000001.11) and relative localization and orientation of PARK7 and flanking genes. PARK7 is represented in red. Further genes (UTS2, TNFRSF9, ERRFI1) and a non-coding RNA (LOC105376694) map in this locus.

DNA/RNA

 
  Figure 2 displays the two full-length Reference Sequences of PARK7 gene (NCBI - Nucleotide Database). Corresponding GenBank Accession Numbers are indicated on the left. Exons are represented as boxes (blue for coding regions and white for non-coding), whereas the dashed line indicates intronic regions. The green triangle specifies the start codon, while the red one designates the stop codon.
 
  Figure 3 displays the structures of the currently known PARK7 mRNA splicing variants listed in Ensembl. Each mRNA variant is indicated with a number corresponding to that indicated in Table 1. Transcript variants are classified as coding mRNAs (black) and non-coding (gray).
Description DJ-1 maps on the distal part of the short arm of chromosome 1, cytoband 1p36.23 (Figure 1). It spans about 24 kb and includes eight exons (Figure 2). The first two exons (1A and 1B) are noncoding and alternatively spliced in the DJ-1 mRNAs (Bonifati, Rizzu, Squitieri, et al., 2003).
Transcription Currently, the NCBI RefSeq database annotates two representative transcripts as full-length PARK7 mRNAs (Figure 2). However, a total of 10 spliced variants is reported in the Ensembl database http://www.ensembl.org(Figure 3). The majority of mRNAs contain a 570 bp ORF, encoding a protein of 189 aa. Two shorter transcripts (PARK7-003 lacking exon 4, and PARK7-010 starting at an inner transcription point) produce smaller proteins (169 and 160 aa respectively) (Table 2 and Fig. 3). Other transcripts do not encode proteins and are processed via the NMD (non-sense mediated decay) mechanism.
Table 1.

#

Name

Ensembl Transcript ID

bp

Biotype

Protein

1

PARK7-004

ENST00000493373

624

Protein coding

189aa

2

PARK7-002

ENST00000338639

949

Protein coding

189aa

3

PARK7-007

ENST00000460192

567

Processed transcript

No protein

4

PARK7-001

ENST00000493678

1088

Protein coding

189aa

5

PARK7-003

ENST00000377493

795

Protein coding

169aa

6

PARK7-008

ENST00000465354

949

Processed transcript

No rotein

7

PARK7-005

ENST00000377491

977

Protein coding

189aa

8

PARK7-006

ENST00000377488

783

Protein coding

189aa

9

PARK7-009

ENST00000497113

670

Processed transcript

No protein

10

PARK7-010

ENST00000469225

711

Protein coding

160aa

Pseudogene PGOHUM00000239770: Chr. 12, Start Coordinate 49988931, Stop Coordinate 49989471 according toGenome BrowserHuman Dec. 2013 (GRCh38/hg38) Assembly
PGOHUM00000236716: Chr. 9, Start Coordinate 98680419, Stop Coordinate 98680983according to Genome BrowserHuman Dec. 2013 (GRCh38/hg38) Assembly

Protein

 
  Figure 4 shows the crystallographic structure of DJ-1 protein. This protein is a dimer composed of two portions, monomer A represented in purple and monomer B represented in green. Adapted from (Wilson et al., 2003).
Description X-ray crystallographic examination of DJ-1 protein structure indicates that it exists as a dimer (Figure 4)(Wilson et al., 2003). It contains domains found in heat shock chaperones and belongs to the ThiJ/PfpI family. This family (pfam01965) includes: ThiJ, a protein involved in thiamine biosynthesis in prokaryotes; PfpI (so-called from P. furious protease I) and other bacterial proteases; araC and other bacterial transcription factors; and the glutamine amidotransferases family (including bacteria catalases) (Bonifati, Rizzu, Squitieri, et al., 2003).
Expression DJ-1 is a ubiquitous protein, highly expressed in almost all cells and tissue (Figure 5). Distribution studies indicate that DJ-1 is preferentially expressed in testis, brain and kidney. In the brain, DJ-1 is expressed in both neurons and glial cells. The expression level of DJ-1 is increased under oxidative stress conditions both in PD and other neurodegenerative diseases(Ariga et al., 2013). DJ-1 is also frequently overexpressed in the several tumor types (Cao et al., 2015).
 
  Figure 5 (adapted from PROTEOMICS DB - www.proteomicsdb.org) shows the central and peripheral distribution of DJ-1 in human tissues. It is a ubiquitous protein, expressed in almost all human body systems.
Localisation Subcellular localization: DJ-1 is mainly localized in the nucleus, cytoplasm, and mitochondria and is secreted into culture medium or serum, cerebrospinal fluid, saliva and nipple fluid(Ariga, 2015). DJ-1 is translocated from the cytoplasm to nucleus upon addition of a mitogen to the culture medium, while it translocates to mitochondria after oxidative stress (Junn et al., 2009).
 
  Figure 6 (fromGeneCards database http://www.genecards.org/ and based on Compartments http://compartments.jensenlab.org/) shows the subcellular localizations of DJ-1 into cellular structures. Data are derived from database annotations, automatic text mining of the biomedical literature, and sequence-based predictions. The confidence of each association is indicated with numbers (the higher number corresponds to a greater confidence).
Function The product of DJ-1 is an 189 amino acidic highly conserved multifunctional protein belonging to the peptidase C56 family (Lev et al., 2006). It mainly acts as regulator of transcription, redox-sensitive chaperone, sensor for oxidative stress, cysteine protease, and seems to protect neurons from ROS-induced apoptosis (Figure 7) (Xu et al., 2005; Ariga et al., 2013).
The oxidative stress sensor activity is carried out by three cysteine residues at C46, C53 and C106: under oxidative stress conditions, C106 is firstly oxidized from SH to SOH, SO2H and to SO3H form. The other cysteine residues then follow the same process of oxidation.
The regulation of transcription is mediated by DJ-1 binding with various transcription factors without directly tie up to DNA. Transcription factors or modified proteins identified so far include TP53, the androgen receptorAR and its regulatory proteins, the polypyrimidine tract-binding protein-associated splicing factor(SFPQ), KEAP1, an inhibitor for nuclear factor erythroid-2 related factor 2 (NFE2L2), the sterol regulatory element-binding protein (SREBP), Ras-responsive element-binding protein (RREB1), and signal transducer and activator of transcription1 (STAT1) (Ariga, 2015).
DJ-1 is also involved in the activation or repression of cell growth and cell death signaling pathways. Specifically, this polypeptide modulates p53 activity, the PI3K/Akt pathway by interacting with PTEN, and intervenes in the Raf/Erk pathway together with ras (Ariga, 2015). To this regard, it should be reminded that the first identified DJ-1 function was its oncogene activity transforming mouse NIH3T3 cells in cooperation with activated ras (Nagakubo et al., 1997).
 
  Figure 7 summarizes the functions of DJ-1 and related diseases. It is though that excess of activation or loss of function of DJ-1 triggers the onset of various diseases, including cancer and oxidative stress-related diseases. Abbreviations: PD - Parkinson's Disease, FAP - familial amyloid polyneuropathy; COPD - chronic obstructive pulmonary disease. Adapted from (Ariga, 2015).
Homology The PARK7 Gene Tree shows a great evolutionary conservation across species (Figure 8). The internal nodes of the phylogenetic tree are annotated for duplication (red boxes) and speciation (blue boxes) events, which correspond to paralogs and orthologs genes respectively.
 
  Figure 8. The PARK7 Gene Tree shows the maximum likelihood phylogenetic tree representing the evolutionary history of this gene, constructed using the alignment of a representative protein for each species (green bars). This Gene tree has been generated by Ensembl (GeneTree ENSGT00390000001231).

Mutations

 
  Figure 9 shows the overall distribution of PARK7 somatic mutations in cancer listed in COSMIC Database (http://cancer.sanger.ac.uk/cosmic) (March 2016). The exact number of collected somatic mutations in different cancer types is indicated in the data labels.
Epigenetics No currently known epigenetic mechanismsregulating PARK7.
Germinal A wide spectrum of mutations in PARK7 have been identified in familial Parkinson's Disease patients from different ethnicities. Mutations include missense mutations in coding and UTR regions, frame-shifts, copy number variations, and splice sites alterations (Table 2).
Somatic

PARK7 Mutations ExonReferences
Ex1-5del(g.07561_21658del14098) EX1-5(Bonifati, Rizzu, van Baren, et al., 2003)
Ex1-5dup (breakpoints not mapped) EX1-5 (Macedo et al., 2009)
Ex2del (breakpoints not mapped) EX2 (Guo et al., 2010)
Ex5del (breakpoints not mapped) EX5 (Djarmati et al., 2004)
Ex5-7del (breakpoints not mapped) EX5-7 (Hedrich et al., 2004)
c.-122_-107del (g.10539_10554del16)5'UTR(Keyser et al., 2009)
Leu10Pro (g.11658T>C) EX2(Guo et al., 2008)
Met26Ile (g.11707G>A)EX2(Abou-Sleiman et al., 2003)
Ala39Ser (g.14192G>T)EX3(Tang et al., 2006)
Glu64Asp (g.14269G>C)EX3(Hering et al., 2004)
Gly78 (g.18230C>T) EX2(Abou-Sleiman et al., 2003)
IVS4+8_9insA (g.18256_18257insA) IVS4(Tarantino et al., 2009)
Arg98Gln (g.19778G>A) EX5(Abou-Sleiman et al., 2003)
(Lockhart et al., 2004)
(Healy et al., 2004)
(Clark et al., 2004)
(Pankratz et al., 2006)
Arg98(g.19779G>A)EX5(Abou-Sleiman et al., 2003)
Ala104Thr(g.19795G>A)EX5Clark et al., 2004)
IVS5+2_12del (g.19809_19819del11)IVS5(Hedrich et al., 2004)
Asp149Ala  (g.33774A>C)EX7(Abou-Sleiman et al., 2003)
Pro158del  (g.33799_33801delGCC)EX7Macedo et al., 2009)
Thr160 (g.33808C>A) EX7(Pankratz et al., 2006)
Glu163Lys (g.33815G>A) EX7(Annesi et al., 2005)
Leu166Pro (g.33825T>C) EX7(Bonifati, Rizzu, van Baren, et al., 2003)
Ala167 (g.33829A>G)EX7 (Abou-Sleiman et al., 2003)
Ala171Ser (g.33839G>T) EX7(Clark et al., 2004)
Lys175Glu (g.33851A>G) EX7(Nuytemans et al., 2009)
Ala179Thr (g.33863G>A)EX7(Macedo et al., 2009)
(Nuytemans et al., 2009)
Val186 (g.33886T>C)EX7(Hering et al., 2004)
c.*120insA (g.34018_34019insA)EX7(Abou-Sleiman et al., 2003)
c.*203G>A (g.34101G>A)EX7(Abou-Sleiman et al., 2003)

Table 2 displays the currently known PARK7 genetic mutations related to familial Parkinson's Disease. Details are available at the Parkinson Disease Mutation Database (http://www.molgen.vib-ua.be/PDMutDB/). Along with the germinal mutations occurring in Parkinson's Disease, genetic defects have also been observed in solid tumors. A list of the known cancer-derived mutations is available at the COSMIC Database and is summarized in Figure 9.

Implicated in

Note
Entity Parkinson's Disease
Note Mutations in PARK7 are the less common cause of autosomal recessive Parkinsonism (~ 1% of early-onset PD) (Lockhart et al., 2004; Moore et al., 2005). The first identified mutations were a large homozygous deletion and a missense mutation (L166P) identified in both Italian and Dutch consanguineous families (van Duijn et al., 2001; Bonifati, Rizzu, Squitieri, et al., 2003). The other observed familial mutations are summarized in Table 2.
  
Entity Familial amyloid polyneuropathy
Note Transthyretin (TTR), a protein causing familial amyloidotic polyneuropathy (FAP), is a substrate of DJ-1 protease (Koide-Yoshida et al., 2007). In normal conditions, both TTR and DJ-1 are secreted into the culture medium. Under oxidative stress, TTR but not DJ-1 is secreted into the culture medium, resulting in the aggregation of TTR protein. Mirror images of both the expression patterns and solubility of DJ-1 and TTR have been observed in tissues of FAP patients, and the unoxidized form of DJ-1 is secreted into the serum of FAP patients. These results suggest that oxidative stress abrogates secretion of DJ-1 and that secreted DJ-1 degrades aggregated TTR to protect against the onset of FAP (Koide-Yoshida et al., 2007).
  
Entity Chronic obstructive pulmonary disease
Disease Chronic obstructive pulmonary disease (COPD) is caused by cigarette smoking and oxidative stress. Malhotra et al. assessed the expression of NFE2L2 (NRF2) and DJ-1 in non-COPD and smoker COPD lungs and in cigarette smoke-exposed human lung epithelial cells (Beas2B) and mice (Malhotra et al., 2008). COPD patient lungs showed significantly decreased DJ-1 levels. Exposure of Bea2B cells to cigarette smoke caused oxidative modification and enhanced proteasomal degradation of DJ-1 protein. Disruption of DJ-1 in mouse lungs, mouse embryonic fibroblasts, and Beas2B cells lowered NRF2 protein stability and impaired antioxidant induction in response to cigarette smoke. Overall, DJ-1 expression was negatively associated with severity of COPD (Malhotra et al., 2008).
  
Entity Type II Diabetes
Note The expression of DJ-1 is reduced in pancreatic islets of patients with type 2 diabetes mellitus (T2DM). Under non-diabetic conditions, DJ-1 expression increases in mouse and human islets during aging. Jain et al. demonstrated that, in mouse islets, DJ-1 prevents an increase in reactive oxygen species and preserves mitochondrial integrity and physiology, prerequisites for glucose-stimulated insulin secretion(Jain et al., 2012). Accordingly, DJ-1-deficient mice developed glucose intolerance and reduced βcell area as they age or gain weight. These data suggested that DJ-1 is more generally involved in age- and lifestyle-related human diseases and show that DJ-1 plays a key role in glucose homeostasis (Jain et al., 2012).
  
Entity Stroke
Note Loss of DJ-1 increases the sensitivity to excitotoxicity and ischemia, whereas expression of DJ-1 can reverse this sensitivity and provide protection (Aleyasin et al., 2007). Importantly, DJ-1 expression decreases markers of oxidative stress after stroke insult in vivo, suggesting that DJ-1 protects through alleviation of oxidative stress (Aleyasin et al., 2007). Consistent with this finding, (Aleyasin et al., 2007) demonstrated the essential role of the oxidation-sensitive cysteine-106 residue in the neuroprotective activity of DJ-1 after stroke.
  
Entity Prostate cancer
Note he intracellular level of the DJ-1 polypeptide in prostatic benign hyperplasia BPH-1 cells is inducible and results markedly increased after exposure to stress-inducing agents (H 2 O 2 and mitomycin C). The expression of DJ-1 is relatively high in PC-3 cells at the constitutive level, and incubation with the same cytotoxic drugs does not further modulate the polypeptide expression. Both cytotoxic agents activate the apoptotic pathway in the benign prostatic cells but not in PC-3 cells, which are resistant to their action (Hod, 2004).
  
Entity Renal carcinoma
Note The expression level of DJ-1 mRNA in a series of 176 renal cell carcinomas (RCC) has been measured by (Sitaram et al., 2009). The level of DJ-1 has been demonstrated significantly elevated in clear cell RCC compared with papillary RCC and kidney cortex tissue.
  
Entity Hepatocellular carcinoma
Note DJ-1 was found significantly up-regulated in 149 hepatocellular carcinomas (HCC). DJ-1 expression correlates with preoperative alpha-fetoprotein, liver cirrhosis, vein invasion, differentiation and overall survival, thus suggesting DJ-1 as a candidate prognostic biomarker of HCC (S. Liu et al., 2010).
  
Entity Ovarian carcinoma
Note The expression and clinical role of DJ-1 and its putative association with transcriptional regulators specific proteins (SP1 and SP3) were investigated in ovarian carcinoma by (Davidson et al., 2008). RT-PCR reactions and immunohistochemistry were used to analyze the expression levels of DJ-1, Sp1 and Sp3 mRNAs and PTEN protein. DJ-1 expression resulted positively associated with Sp1 expression in effusions, and with Sp1 and Sp3 expression in solid tumors. Overall, results show DJ-1 is frequently expressed in advanced-stage ovarian carcinoma at all anatomical sites and is co-expressed with its transcriptional regulators Sp1 and Sp3. In contrast, PTEN expression is infrequent in this disease.
  
Entity Breast cancer
Note Expression of DJ-1 was examined by immunohistochemistry and in-situ hybridization in 273 breast invasive ductal carcinomas (IDCs) and 41 breast ductal carcinomas in situ (DCISs) and in cancer cell lines (MDA-MB-231). DJ-1 protein expression resulted lower than adjacent non-cancerous epithelium in 6 of the 41 DCISs and in 146 of the 273 IDCs. Patients with IDC and low DJ-1 expression had significant shorter disease-free survival and overall survival. Low expression of DJ-1 protein seems to be predictive of poor outcome in patients with IDC (Tsuchiya et al., 2012). Furthermore, RS/DJ-1 was found to be secreted in the breast cell line SUM-44 and in sera of diagnosed patients with breast cancer (Le Naour et al., 2001).
  
Entity Acute leukemia
Note DJ-1 was found overexpressed in acute leukemia (AL) patient samples and leukemia cell lines, giving the first clue that DJ-1 overexpression might be involved in leukemogenesis and/or disease progression of AL (H. Liu et al., 2008). Inactivation of DJ-1 by RNA-mediated interference (RNAi) in leukemia cell lines K562 and HL60 resulted in inhibition of the proliferation potential and enhancement of the sensitivity of leukemia cells to chemotherapeutic drug etoposide(H. Liu et al., 2008).
  
Entity Cervical cancer
Note Normal cervical epithelium and patient-matched high-grade squamous intraepithelial lesions (HSIL) with cervical carcinoma tissue were compared by using laser capture microdissection and 2-D DIGE (Arnouk et al., 2009). Significant expression changes were observed with 53 spots corresponding to 23 unique proteins, including DJ-1. Results were confirmed by immunohistochemistry using either frozen sections from the same cohort or formalin fixed paraffin embedded samples from a tissue microarray. These markers can have potential applications for increasing the predictive value of current screening methods (Arnouk et al., 2009).
  
Entity Non-small cell lung carcinoma
Note A proteomic approach using two-dimensional gels coupled with mass spectrometry was used in non-small cell lung carcinoma samples to identify proteins altered when treated with paclitaxel, a chemotherapic that activates mitogen-activated protein kinase kinase (MEK)/extracellular signal-regulated kinase and a MEK inhibitor (MacKeigan et al., 2003). This combined treatment uniquely altered the proteins RS/DJ-1 (RNA-binding regulatory subunit/DJ-1 PARK7) and RhoGDIalpha (MacKeigan et al., 2003).
  
Entity Endometrial cancer
Note RT-PCR and Western blotting were performed to determine the DJ-1 expression in 100 surgical specimens of endometrial cancer tissues, paired tumor-adjacent tissues, and 30 surgical specimens of normal endometrium tissues (Morelli et al., 2014).DJ-1 expression in endometrial cancer tissues was higher than in tumor-adjacent tissues and normal endometrial tissues. At the same time, it was associated with signs of cancer progression, including differentiation, myometrial invasion depth, and presence of lymph node metastasis. Overall, high DJ-1 expression seems to be negatively correlated with apoptosis, and it may be part of the mechanisms for the development, invasion, and metastasis in endometrial cancer (Morelli et al., 2014).
  
Entity Thyroid cancer
Note A comparative proteome analysis was performed by (Giusti et al., 2008) in order to examine the global changes of fine needle aspiration fluid protein patterns of two variants of malignant papillary thyroid cancer PTC (classical variant and tall cell variant) respect to the controls. Changes in protein expression were identified using two-dimensional electrophoresis (2DE) and peptide mass finger printing via MALDI-TOF mass spectrometry (MS), as well as Western blot analysis. A significant statistical up-regulation of 17 protein spots including DJ-1 was observed in classical PTC and/or tall cell variant PTC with respect to controls(Giusti et al., 2008).
  
Entity Pancreas adenocarcinoma
Note To identify potential novel biomarkers for pancreatic ductal adenocarcinoma (PDAC) from pancreatic juice, (Tian et al., 2008) carried out gel electrophoresis (DIGE) and tandem mass spectrometry (MS/MS) to compare the pancreatic juice profiling from 9 PDAC patients and 9 cancer-free controls. Of the differently expressed proteins, three up-regulated proteins in pancreatic cancer juice were selected for validation by Western blot and immunohistochemistry, including DJ-1. Up-regulation of DJ-1 was associated with better differentiation (Tian et al., 2008). In another study, the DJ-1 protein expression in tissue specimens from 41 patients was evaluated by immunohistochemistry and associated with a negative impact of chemotherapy with gemcitabine on patient's survival. Therefore, DJ-1 has been suggested as prognostic markers that express resistance of pancreatic cancer patients to chemotherapy with gemcitabine (Tsiaousidou et al., 2013).
  
Entity Laryngeal squamous cell carcinoma
Note A study conducted by (Shen et al., 2011)aimed to explore the correlation between DJ-1 gene and survivin gene BIRC5 in laryngeal squamous cell carcinoma. The expression levels of DJ-1 gene and survivin gene in 82 laryngeal carcinoma tissues from patients and 82 negative surgical margin tissue samples were measured by immunohistochemistry and the relationship with clinicopathologic parameters was assessed. Positive correlations were found between expression levels and patients' clinical parameters in laryngeal carcinoma tissues and tumor stages, but not with lymph node metastasis. The DJ-1 gene expression level was also related to cell differentiation. DJ-1 and survivin play a vital role in the occurrence and development of laryngeal carcinoma. DJ-1 may promote the carcinogenesis of laryngeal cells by up-regulating the survivin gene expression (Shen et al., 2011).
  
Entity Esophageal squamous cell carcinoma
Note The expression of DJ-1 in 81 esophageal squamous cell carcinoma (ESCC) tumors, 31 paired non neoplastic esophageal epithelia, and 19 paired ESCC lymph node metastases was analyzed by (Yuen et al., 2008). They found that cytoplasmic DJ-1 expression was significantly higher in ESCC and ESCC lymph node metastases than in non neoplastic esophageal epithelium. ESCC specimens with high distant metastatic potential also had a significantly higher level of nuclear DJ-1 expression. A high level of nuclear DJ-1 was significantly associated with poorer patient survival in the cohort (P = 0.028). DJ-1 expression was significantly associated with pAkt, whereas nuclear DJ-1 expression was significantly correlated with nuclear expression of DAXX. These results suggest that phosphatidylinositol 3-kinase pathway and Daxx-regulated apoptosis might be important in DJ-1-mediated ESCC progression. In conclusion, results suggest that DJ-1 plays a very important role in transformation and progression of ESCC and may be used as a prognostic marker in ESCC.
  
Entity Other malignancies
Note Increased levels of DJ-1 expression have been observed in other kinds of cancer cells and tissues, including gastric cancer (Shimwell et al., 2012; Li et al., 2013), supraglottic cancer (Zhu et al., 2012), cholangiocarcinoma (Kawase et al., 2009), glioma/glioblastomas(Hinkle et al., 2011; Wang et al., 2013), bladder carcinoma (Lee et al., 2012) and melanoma (Pardo et al., 2006). Increased levels of DJ-1 expression in cancer cells are parallel to severity of cancer with poor prognosis, including metastasis and invasion (Ariga, 2015).
  

To be noted

COMPARTMENTS (compartments.jensenlab.org) is any updated web resource that integrates evidence on protein subcellular localization from manually curated literature, high-throughput screens, automatic text mining, and sequence-based prediction methods. It can be useful to display, with a certain grade of confidence, the subcellular localization of a specific biological molecule.
PROTEOMICSDB (www.proteomicsdb.org) enables navigation of proteomes, provides biological insight and fosters the development of proteomic technology, and is a good tool to visualize the tissue distribution of mRNAs and proteins in human.

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E64D mutation in DJ1 in early onset Parkinson disease (PARK7) Hum Mutat
PMID 15365989
 
DJ-1 expression in glioblastomas shows positive correlation with p53 expression and negative correlation with epidermal growth factor receptor amplification
Hinkle DA, Mullett SJ, Gabris BE, Hamilton RL
Neuropathology 2011 Feb;31(1):29-37
PMID 20497343
 
Differential control of apoptosis by DJ-1 in prostate benign and cancer cells
Hod Y
J Cell Biochem 2004 Aug 15;92(6):1221-33
PMID 15258905
 
Age- and diet-dependent requirement of DJ-1 for glucose homeostasis in mice with implications for human type 2 diabetes
Jain D, Jain R, Eberhard D, Eglinger J, Bugliani M, Piemonti L, Marchetti P, Lammert E
J Mol Cell Biol 2012 Aug;4(4):221-30
PMID 22611253
 
Mitochondrial localization of DJ-1 leads to enhanced neuroprotection
Junn E, Jang WH, Zhao X, Jeong BS, Mouradian MM
J Neurosci Res 2009 Jan;87(1):123-9
PMID 18711745
 
Differential LC-MS-based proteomics of surgical human cholangiocarcinoma tissues
Kawase H, Fujii K, Miyamoto M, Kubota KC, Hirano S, Kondo S, Inagaki F
J Proteome Res 2009 Aug;8(8):4092-103
PMID 19569727
 
Identification of a novel functional deletion variant in the 5'-UTR of the DJ-1 gene
Keyser RJ, van der Merwe L, Venter M, Kinnear C, Warnich L, Carr J, Bardien S
BMC Med Genet 2009 Oct 13;10:105
PMID 19825160
 
DJ-1 degrades transthyretin and an inactive form of DJ-1 is secreted in familial amyloidotic polyneuropathy
Koide-Yoshida S, Niki T, Ueda M, Himeno S, Taira T, Iguchi-Ariga SM, Ando Y, Ariga H
Int J Mol Med 2007 Jun;19(6):885-93
PMID 17487420
 
Proteomics-based identification of RS/DJ-1 as a novel circulating tumor antigen in breast cancer
Le Naour F, Misek DE, Krause MC, Deneux L, Giordano TJ, Scholl S, Hanash SM
Clin Cancer Res 2001 Nov;7(11):3328-35
PMID 11705844
 
Overexpression of DJ-1 and HSP90α, and loss of PTEN associated with invasive urothelial carcinoma of urinary bladder: Possible prognostic markers
Lee H, Choi SK, Ro JY
Oncol Lett 2012 Mar;3(3):507-512
PMID 22740940
 
Role of DJ-1 in Parkinson's disease
Lev N, Roncevic D, Ickowicz D, Melamed E, Offen D
J Mol Neurosci 2006;29(3):215-25
PMID 17085780
 
High-expression of DJ-1 and loss of PTEN associated with tumor metastasis and correlated with poor prognosis of gastric carcinoma
Li Y, Cui J, Zhang CH, Yang DJ, Chen JH, Zan WH, Li B, Li Z, He YL
Int J Med Sci 2013 Sep 24;10(12):1689-97
PMID 24155657
 
Expression and role of DJ-1 in leukemia
Liu H, Wang M, Li M, Wang D, Rao Q, Wang Y, Xu Z, Wang J
Biochem Biophys Res Commun 2008 Oct 24;375(3):477-83
PMID 18722352
 
Increased DJ-1 and its prognostic significance in hepatocellular carcinoma
Liu S, Yang Z, Wei H, Shen W, Liu J, Yin Q, Li X, Yi J
Hepatogastroenterology 2010 Sep-Oct;57(102-103):1247-56
PMID 21410067
 
DJ-1 mutations are a rare cause of recessively inherited early onset parkinsonism mediated by loss of protein function
Lockhart PJ, Lincoln S, Hulihan M, Kachergus J, Wilkes K, Bisceglio G, Mash DC, Farrer MJ
J Med Genet 2004 Mar;41(3):e22
PMID 14985393
 
Proteomic profiling drug-induced apoptosis in non-small cell lung carcinoma: identification of RS/DJ-1 and RhoGDIalpha
MacKeigan JP, Clements CM, Lich JD, Pope RM, Hod Y, Ting JP
Cancer Res 2003 Oct 15;63(20):6928-34
 
Genotypic and phenotypic characteristics of Dutch patients with early onset Parkinson's disease
Macedo MG, Verbaan D, Fang Y, van Rooden SM, Visser M, Anar B, Uras A, Groen JL, Rizzu P, van Hilten JJ, Heutink P
Mov Disord 2009 Jan 30;24(2):196-203
PMID 18973254
 
Decline in NRF2-regulated antioxidants in chronic obstructive pulmonary disease lungs due to loss of its positive regulator, DJ-1
Malhotra D, Thimmulappa R, Navas-Acien A, Sandford A, Elliott M, Singh A, Chen L, Zhuang X, Hogg J, Pare P, Tuder RM, Biswal S
Am J Respir Crit Care Med 2008 Sep 15;178(6):592-604
PMID 18556627
 
Molecular pathophysiology of Parkinson's disease
Moore DJ, West AB, Dawson VL, Dawson TM
Annu Rev Neurosci 2005;28:57-87
PMID 16022590
 
DJ-1 in endometrial cancer: a possible biomarker to improve differential diagnosis between subtypes
Morelli M, Scumaci D, Di Cello A, Venturella R, Donato G, Faniello MC, Quaresima B, Cuda G, Zullo F, Costanzo F
Int J Gynecol Cancer 2014 May;24(4):649-58
PMID 24614826
 
DJ-1, a novel oncogene which transforms mouse NIH3T3 cells in cooperation with ras
Nagakubo D, Taira T, Kitaura H, Ikeda M, Tamai K, Iguchi-Ariga SM, Ariga H
Biochem Biophys Res Commun 1997 Feb 13;231(2):509-13
PMID 9070310
 
Relative contribution of simple mutations vs
Nuytemans K, Meeus B, Crosiers D, Brouwers N, Goossens D, Engelborghs S, Pals P, Pickut B, Van den Broeck M, Corsmit E, Cras P, De Deyn PP, Del-Favero J, Van Broeckhoven C, Theuns J
copy number variations in five Parkinson disease genes in the Belgian population Hum Mutat
PMID 19405094
 
Mutations in DJ-1 are rare in familial Parkinson disease
Pankratz N, Pauciulo MW, Elsaesser VE, Marek DK, Halter CA, Wojcieszek J, Rudolph A, Shults CW, Foroud T, Nichols WC; Parkinson Study Group - PROGENI Investigators
Neurosci Lett 2006 Nov 20;408(3):209-13
PMID 16997464
 
The characterization of the invasion phenotype of uveal melanoma tumour cells shows the presence of MUC18 and HMG-1 metastasis markers and leads to the identification of DJ-1 as a potential serum biomarker
Pardo M, García A, Thomas B, Piñeiro A, Akoulitchev A, Dwek RA, Zitzmann N
Int J Cancer 2006 Sep 1;119(5):1014-22
PMID 16570276
 
Significance and relationship between DJ-1 gene and surviving gene expression in laryngeal carcinoma
Shen Z, Ren Y, Ye D, Guo J, Kang C, Ding H
Eur J Histochem 2011 Mar 21;55(1):e9
PMID 21556124
 
Macrophage migration inhibitory factor and DJ-1 in gastric cancer: differences between high-incidence and low-incidence areas
Shimwell NJ, Ward DG, Mohri Y, Mohri T, Pallan L, Teng M, Miki YC, Kusunoki M, Tucker O, Wei W, Morse J, Johnson PJ
Br J Cancer 2012 Oct 23;107(9):1595-601
PMID 22968650
 
The PTEN regulator DJ-1 is associated with hTERT expression in clear cell renal cell carcinoma
Sitaram RT, Cairney CJ, Grabowski P, Keith WN, Hallberg B, Ljungberg B, Roos G
Int J Cancer 2009 Aug 15;125(4):783-90
PMID 19384955
 
Association of PINK1 and DJ-1 confers digenic inheritance of early-onset Parkinson's disease
Tang B, Xiong H, Sun P, Zhang Y, Wang D, Hu Z, Zhu Z, Ma H, Pan Q, Xia JH, Xia K, Zhang Z
Hum Mol Genet 2006 Jun 1;15(11):1816-25
PMID 16632486
 
Compound heterozygosity in DJ-1 gene non-coding portion related to parkinsonism
Tarantino P, Civitelli D, Annesi F, De Marco EV, Rocca FE, Pugliese P, Nicoletti G, Carrideo S, Provenzano G, Annesi G, Quattrone A
Parkinsonism Relat Disord 2009 May;15(4):324-6
PMID 18722801
 
Proteomic analysis identifies MMP-9, DJ-1 and A1BG as overexpressed proteins in pancreatic juice from pancreatic ductal adenocarcinoma patients
Tian M, Cui YZ, Song GH, Zong MJ, Zhou XY, Chen Y, Han JX
BMC Cancer 2008 Aug 16;8:241
PMID 18706098
 
B7H4, HSP27 and DJ-1 molecular markers as prognostic factors in pancreatic cancer
Tsiaousidou A, Lambropoulou M, Chatzitheoklitos E, Tripsianis G, Tsompanidou C, Simopoulos C, Tsaroucha AK
Pancreatology 2013 Nov-Dec;13(6):564-9
PMID 24280570
 
Clinical significance of DJ-1 as a secretory molecule: retrospective study of DJ-1 expression at mRNA and protein levels in ductal carcinoma of the breast
Tsuchiya B, Iwaya K, Kohno N, Kawate T, Akahoshi T, Matsubara O, Mukai K
Histopathology 2012 Jul;61(1):69-77
PMID 22385318
 
The positive correlation between DJ-1 and β-catenin expression shows prognostic value for patients with glioma
Wang C, Fang M, Zhang M, Li W, Guan H, Sun Y, Xie S, Zhong X
Neuropathology 2013 Dec;33(6):628-36
PMID 23714193
 
The 1
Wilson MA, Collins JL, Hod Y, Ringe D, Petsko GA
1-A resolution crystal structure of DJ-1, the protein mutated in autosomal recessive early onset Parkinson's disease Proc Natl Acad Sci U S A
PMID 12855764
 
The Parkinson's disease-associated DJ-1 protein is a transcriptional co-activator that protects against neuronal apoptosis
Xu J, Zhong N, Wang H, Elias JE, Kim CY, Woldman I, Pifl C, Gygi SP, Geula C, Yankner BA
Hum Mol Genet 2005 May 1;14(9):1231-41
PMID 15790595
 
DJ-1 could predict worse prognosis in esophageal squamous cell carcinoma
Yuen HF, Chan YP, Law S, Srivastava G, El-Tanani M, Mak TW, Chan KW
Cancer Epidemiol Biomarkers Prev 2008 Dec;17(12):3593-602
PMID 19064576
 
Tumorigenesis role and clinical significance of DJ-1, a negative regulator of PTEN, in supraglottic squamous cell carcinoma
Zhu XL, Wang ZF, Lei WB, Zhuang HW, Hou WJ, Wen YH, Wen WP
J Exp Clin Cancer Res 2012 Nov 14;31:94
PMID 23151319
 
Park7, a novel locus for autosomal recessive early-onset parkinsonism, on chromosome 1p36
van Duijn CM, Dekker MC, Bonifati V, Galjaard RJ, Houwing-Duistermaat JJ, Snijders PJ, Testers L, Breedveld GJ, Horstink M, Sandkuijl LA, van Swieten JC, Oostra BA, Heutink P
Am J Hum Genet 2001 Sep;69(3):629-34
PMID 11462174
 

Citation

This paper should be referenced as such :
La Cognata V, Cavallaro S
PARK7 (Parkinsonism associated deglycase);
Atlas Genet Cytogenet Oncol Haematol. in press
On line version : http://AtlasGeneticsOncology.org/Genes/PARK7ID41639ch1p36.html


Other Leukemias implicated (Data extracted from papers in the Atlas) [ 1 ]
  t(1;9)(p13;p12) PAX5/HIPK1

External links

Nomenclature
HGNC (Hugo)PARK7   16369
Cards
AtlasPARK7ID41639ch1p36.txt
Entrez_Gene (NCBI)PARK7  11315  Parkinsonism associated deglycase
AliasesDJ-1; DJ1; HEL-S-67p
GeneCards (Weizmann)PARK7
Ensembl hg19 (Hinxton)ENSG00000116288 [Gene_View]  chr1:8021714-8045342 [Contig_View]  PARK7 [Vega]
Ensembl hg38 (Hinxton)ENSG00000116288 [Gene_View]  chr1:8021714-8045342 [Contig_View]  PARK7 [Vega]
ICGC DataPortalENSG00000116288
TCGA cBioPortalPARK7
AceView (NCBI)PARK7
Genatlas (Paris)PARK7
WikiGenes11315
SOURCE (Princeton)PARK7
Genomic and cartography
GoldenPath hg19 (UCSC)PARK7  -     chr1:8021714-8045342 +  1p36.23   [Description]    (hg19-Feb_2009)
GoldenPath hg38 (UCSC)PARK7  -     1p36.23   [Description]    (hg38-Dec_2013)
EnsemblPARK7 - 1p36.23 [CytoView hg19]  PARK7 - 1p36.23 [CytoView hg38]
Mapping of homologs : NCBIPARK7 [Mapview hg19]  PARK7 [Mapview hg38]
OMIM602533   606324   
Gene and transcription
Genbank (Entrez)AB073864 AF021819 AK091679 AK130886 AK312000
RefSeq transcript (Entrez)NM_001123377 NM_007262
RefSeq genomic (Entrez)NC_000001 NC_018912 NG_008271 NT_032977 NW_004929289
Consensus coding sequences : CCDS (NCBI)PARK7
Cluster EST : UnigeneHs.419640 [ NCBI ]
CGAP (NCI)Hs.419640
Alternative Splicing GalleryENSG00000116288
Gene ExpressionPARK7 [ NCBI-GEO ]   PARK7 [ EBI - ARRAY_EXPRESS ]   PARK7 [ SEEK ]   PARK7 [ MEM ]
Gene Expression Viewer (FireBrowse)PARK7 [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)11315
GTEX Portal (Tissue expression)PARK7
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ99497 (Uniprot)
NextProtQ99497  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ99497
Splice isoforms : SwissVarQ99497 (Swissvar)
PhosPhoSitePlusQ99497
Domains : Interpro (EBI)Class_I_gatase-like    DJ-1/PfpI    DJ1   
Domain families : Pfam (Sanger)DJ-1_PfpI (PF01965)   
Domain families : Pfam (NCBI)pfam01965   
DMDM Disease mutations11315
Blocks (Seattle)PARK7
PDB (SRS)1J42    1P5F    1PDV    1PDW    1PE0    1Q2U    1SOA    1UCF    2OR3    2R1T    2R1U    2R1V    2RK3    2RK4    2RK6    3B36    3B38    3B3A    3BWE    3CY6    3CYF    3CZ9    3CZA    3EZG    3F71    3SF8    4BTE    4MNT    4MTC    4N0M    4N12    4OGF    4OQ4    4P2G    4P34    4P35    4P36    4RKW    4RKY    4S0Z    4ZGG   
PDB (PDBSum)1J42    1P5F    1PDV    1PDW    1PE0    1Q2U    1SOA    1UCF    2OR3    2R1T    2R1U    2R1V    2RK3    2RK4    2RK6    3B36    3B38    3B3A    3BWE    3CY6    3CYF    3CZ9    3CZA    3EZG    3F71    3SF8    4BTE    4MNT    4MTC    4N0M    4N12    4OGF    4OQ4    4P2G    4P34    4P35    4P36    4RKW    4RKY    4S0Z    4ZGG   
PDB (IMB)1J42    1P5F    1PDV    1PDW    1PE0    1Q2U    1SOA    1UCF    2OR3    2R1T    2R1U    2R1V    2RK3    2RK4    2RK6    3B36    3B38    3B3A    3BWE    3CY6    3CYF    3CZ9    3CZA    3EZG    3F71    3SF8    4BTE    4MNT    4MTC    4N0M    4N12    4OGF    4OQ4    4P2G    4P34    4P35    4P36    4RKW    4RKY    4S0Z    4ZGG   
PDB (RSDB)1J42    1P5F    1PDV    1PDW    1PE0    1Q2U    1SOA    1UCF    2OR3    2R1T    2R1U    2R1V    2RK3    2RK4    2RK6    3B36    3B38    3B3A    3BWE    3CY6    3CYF    3CZ9    3CZA    3EZG    3F71    3SF8    4BTE    4MNT    4MTC    4N0M    4N12    4OGF    4OQ4    4P2G    4P34    4P35    4P36    4RKW    4RKY    4S0Z    4ZGG   
Structural Biology KnowledgeBase1J42    1P5F    1PDV    1PDW    1PE0    1Q2U    1SOA    1UCF    2OR3    2R1T    2R1U    2R1V    2RK3    2RK4    2RK6    3B36    3B38    3B3A    3BWE    3CY6    3CYF    3CZ9    3CZA    3EZG    3F71    3SF8    4BTE    4MNT    4MTC    4N0M    4N12    4OGF    4OQ4    4P2G    4P34    4P35    4P36    4RKW    4RKY    4S0Z    4ZGG   
SCOP (Structural Classification of Proteins)1J42    1P5F    1PDV    1PDW    1PE0    1Q2U    1SOA    1UCF    2OR3    2R1T    2R1U    2R1V    2RK3    2RK4    2RK6    3B36    3B38    3B3A    3BWE    3CY6    3CYF    3CZ9    3CZA    3EZG    3F71    3SF8    4BTE    4MNT    4MTC    4N0M    4N12    4OGF    4OQ4    4P2G    4P34    4P35    4P36    4RKW    4RKY    4S0Z    4ZGG   
CATH (Classification of proteins structures)1J42    1P5F    1PDV    1PDW    1PE0    1Q2U    1SOA    1UCF    2OR3    2R1T    2R1U    2R1V    2RK3    2RK4    2RK6    3B36    3B38    3B3A    3BWE    3CY6    3CYF    3CZ9    3CZA    3EZG    3F71    3SF8    4BTE    4MNT    4MTC    4N0M    4N12    4OGF    4OQ4    4P2G    4P34    4P35    4P36    4RKW    4RKY    4S0Z    4ZGG   
SuperfamilyQ99497
Human Protein AtlasENSG00000116288
Peptide AtlasQ99497
HPRD03961
IPIIPI00298547   IPI00983313   
Protein Interaction databases
DIP (DOE-UCLA)Q99497
IntAct (EBI)Q99497
FunCoupENSG00000116288
BioGRIDPARK7
STRING (EMBL)PARK7
ZODIACPARK7
Ontologies - Pathways
QuickGOQ99497
Ontology : AmiGOchromatin  core promoter binding  negative regulation of protein phosphorylation  double-stranded DNA binding  single-stranded DNA binding  transcription coactivator activity  transcription coactivator activity  mRNA binding  receptor binding  copper ion binding  protein binding  nucleus  cytoplasm  mitochondrion  mitochondrion  mitochondrial respiratory chain complex I  mitochondrial intermembrane space  mitochondrial matrix  endoplasmic reticulum  cytosol  cytosol  plasma membrane  negative regulation of protein kinase activity  proteolysis  protein deglycosylation  autophagy  inflammatory response  mitochondrion organization  Ras protein signal transduction  single fertilization  transcription factor binding  peptidase activity  adult locomotory behavior  detoxification of copper ion  positive regulation of gene expression  negative regulation of gene expression  superoxide dismutase copper chaperone activity  PML body  oxidoreductase activity, acting on peroxide as acceptor  enzyme active site formation via L-cysteine sulfinic acid  glyoxalase III activity  methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione  lactate biosynthetic process  lactate biosynthetic process  enzyme binding  kinase binding  cytokine binding  axon  negative regulation of protein ubiquitination  negative regulation of protein binding  negative regulation of protein binding  negative regulation of protein binding  activation of protein kinase B activity  negative regulation of proteasomal ubiquitin-dependent protein catabolic process  positive regulation of interleukin-8 production  positive regulation of peptidyl-serine phosphorylation  negative regulation of protein sumoylation  cellular response to oxidative stress  cellular response to oxidative stress  tyrosine 3-monooxygenase activator activity  cellular response to glyoxal  L-dopa decarboxylase activator activity  response to drug  hydrogen peroxide metabolic process  identical protein binding  protein homodimerization activity  negative regulation of apoptotic process  regulation of neuron apoptotic process  negative regulation of neuron apoptotic process  cell body  small protein activating enzyme binding  ubiquitin-like protein conjugating enzyme binding  membrane raft  mercury ion binding  regulation of TRAIL receptor biosynthetic process  positive regulation of transcription from RNA polymerase II promoter  positive regulation of transcription from RNA polymerase II promoter  positive regulation of transcription from RNA polymerase II promoter  glycolate biosynthetic process  negative regulation of protein export from nucleus  androgen receptor binding  regulation of inflammatory response  detoxification of mercury ion  protein stabilization  protein stabilization  positive regulation of sequence-specific DNA binding transcription factor activity  positive regulation of sequence-specific DNA binding transcription factor activity  negative regulation of ubiquitin-protein transferase activity  dopamine uptake involved in synaptic transmission  regulation of mitochondrial membrane potential  positive regulation of protein kinase B signaling  membrane depolarization  peroxiredoxin activity  membrane hyperpolarization  negative regulation of cell death  regulation of androgen receptor signaling pathway  extracellular exosome  cellular response to hydrogen peroxide  repressing transcription factor binding  positive regulation of protein homodimerization activity  scaffold protein binding  presynapse  cellular oxidant detoxification  positive regulation of protein localization to nucleus  positive regulation of protein localization to nucleus  negative regulation of neuron death  positive regulation of superoxide dismutase activity  negative regulation of protein acetylation  positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway  negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway  regulation of fibril organization  positive regulation of mitochondrial electron transport, NADH to ubiquinone  negative regulation of death-inducing signaling complex assembly  negative regulation of protein K48-linked deubiquitination  negative regulation of TRAIL-activated apoptotic signaling pathway  cupric ion binding  cuprous ion binding  positive regulation of pyrroline-5-carboxylate reductase activity  positive regulation of tyrosine 3-monooxygenase activity  positive regulation of dopamine biosynthetic process  positive regulation of dopamine biosynthetic process  glyoxal catabolic process  positive regulation of L-dopa biosynthetic process  positive regulation of L-dopa decarboxylase activity  negative regulation of oxidative stress-induced cell death  negative regulation of hydrogen peroxide-induced cell death  negative regulation of hydrogen peroxide-induced neuron death  negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway  negative regulation of hydrogen peroxide-induced neuron intrinsic apoptotic signaling pathway  positive regulation of reactive oxygen species biosynthetic process  positive regulation of mitophagy  ubiquitin-specific protease binding  glyoxalase (glycolic acid-forming) activity  negative regulation of ubiquitin-specific protease activity  positive regulation of oxidative phosphorylation uncoupler activity  positive regulation of transcription regulatory region DNA binding  positive regulation of androgen receptor activity  negative regulation of extrinsic apoptotic signaling pathway  negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway  
Ontology : EGO-EBIchromatin  core promoter binding  negative regulation of protein phosphorylation  double-stranded DNA binding  single-stranded DNA binding  transcription coactivator activity  transcription coactivator activity  mRNA binding  receptor binding  copper ion binding  protein binding  nucleus  cytoplasm  mitochondrion  mitochondrion  mitochondrial respiratory chain complex I  mitochondrial intermembrane space  mitochondrial matrix  endoplasmic reticulum  cytosol  cytosol  plasma membrane  negative regulation of protein kinase activity  proteolysis  protein deglycosylation  autophagy  inflammatory response  mitochondrion organization  Ras protein signal transduction  single fertilization  transcription factor binding  peptidase activity  adult locomotory behavior  detoxification of copper ion  positive regulation of gene expression  negative regulation of gene expression  superoxide dismutase copper chaperone activity  PML body  oxidoreductase activity, acting on peroxide as acceptor  enzyme active site formation via L-cysteine sulfinic acid  glyoxalase III activity  methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione  lactate biosynthetic process  lactate biosynthetic process  enzyme binding  kinase binding  cytokine binding  axon  negative regulation of protein ubiquitination  negative regulation of protein binding  negative regulation of protein binding  negative regulation of protein binding  activation of protein kinase B activity  negative regulation of proteasomal ubiquitin-dependent protein catabolic process  positive regulation of interleukin-8 production  positive regulation of peptidyl-serine phosphorylation  negative regulation of protein sumoylation  cellular response to oxidative stress  cellular response to oxidative stress  tyrosine 3-monooxygenase activator activity  cellular response to glyoxal  L-dopa decarboxylase activator activity  response to drug  hydrogen peroxide metabolic process  identical protein binding  protein homodimerization activity  negative regulation of apoptotic process  regulation of neuron apoptotic process  negative regulation of neuron apoptotic process  cell body  small protein activating enzyme binding  ubiquitin-like protein conjugating enzyme binding  membrane raft  mercury ion binding  regulation of TRAIL receptor biosynthetic process  positive regulation of transcription from RNA polymerase II promoter  positive regulation of transcription from RNA polymerase II promoter  positive regulation of transcription from RNA polymerase II promoter  glycolate biosynthetic process  negative regulation of protein export from nucleus  androgen receptor binding  regulation of inflammatory response  detoxification of mercury ion  protein stabilization  protein stabilization  positive regulation of sequence-specific DNA binding transcription factor activity  positive regulation of sequence-specific DNA binding transcription factor activity  negative regulation of ubiquitin-protein transferase activity  dopamine uptake involved in synaptic transmission  regulation of mitochondrial membrane potential  positive regulation of protein kinase B signaling  membrane depolarization  peroxiredoxin activity  membrane hyperpolarization  negative regulation of cell death  regulation of androgen receptor signaling pathway  extracellular exosome  cellular response to hydrogen peroxide  repressing transcription factor binding  positive regulation of protein homodimerization activity  scaffold protein binding  presynapse  cellular oxidant detoxification  positive regulation of protein localization to nucleus  positive regulation of protein localization to nucleus  negative regulation of neuron death  positive regulation of superoxide dismutase activity  negative regulation of protein acetylation  positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway  negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway  regulation of fibril organization  positive regulation of mitochondrial electron transport, NADH to ubiquinone  negative regulation of death-inducing signaling complex assembly  negative regulation of protein K48-linked deubiquitination  negative regulation of TRAIL-activated apoptotic signaling pathway  cupric ion binding  cuprous ion binding  positive regulation of pyrroline-5-carboxylate reductase activity  positive regulation of tyrosine 3-monooxygenase activity  positive regulation of dopamine biosynthetic process  positive regulation of dopamine biosynthetic process  glyoxal catabolic process  positive regulation of L-dopa biosynthetic process  positive regulation of L-dopa decarboxylase activity  negative regulation of oxidative stress-induced cell death  negative regulation of hydrogen peroxide-induced cell death  negative regulation of hydrogen peroxide-induced neuron death  negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway  negative regulation of hydrogen peroxide-induced neuron intrinsic apoptotic signaling pathway  positive regulation of reactive oxygen species biosynthetic process  positive regulation of mitophagy  ubiquitin-specific protease binding  glyoxalase (glycolic acid-forming) activity  negative regulation of ubiquitin-specific protease activity  positive regulation of oxidative phosphorylation uncoupler activity  positive regulation of transcription regulatory region DNA binding  positive regulation of androgen receptor activity  negative regulation of extrinsic apoptotic signaling pathway  negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway  
Pathways : KEGGParkinson's disease   
NDEx NetworkPARK7
Atlas of Cancer Signalling NetworkPARK7
Wikipedia pathwaysPARK7
Orthology - Evolution
OrthoDB11315
GeneTree (enSembl)ENSG00000116288
Phylogenetic Trees/Animal Genes : TreeFamPARK7
Homologs : HomoloGenePARK7
Homology/Alignments : Family Browser (UCSC)PARK7
Gene fusions - Rearrangements
Polymorphisms : SNP, variants
NCBI Variation ViewerPARK7 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)PARK7
dbVarPARK7
ClinVarPARK7
1000_GenomesPARK7 
Exome Variant ServerPARK7
ExAC (Exome Aggregation Consortium)PARK7 (select the gene name)
Genetic variants : HAPMAP11315
Genomic Variants (DGV)PARK7 [DGVbeta]
Mutations
ICGC Data PortalPARK7 
TCGA Data PortalPARK7 
Broad Tumor PortalPARK7
OASIS PortalPARK7 [ Somatic mutations - Copy number]
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
LOVD (Leiden Open Variation Database)MSeqDR-LSDB Mitochondrial Disease Locus Specific Database
LOVD (Leiden Open Variation Database)Parkinson's disease Mutation Database
BioMutasearch PARK7
DgiDB (Drug Gene Interaction Database)PARK7
DoCM (Curated mutations)PARK7 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)PARK7 (select a term)
intoGenPARK7
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] 
Diseases
DECIPHER (Syndromes)1:8021714-8045342  ENSG00000116288
CONAN: Copy Number AnalysisPARK7 
Mutations and Diseases : HGMDPARK7
OMIM602533    606324   
MedgenPARK7
Genetic Testing Registry PARK7
NextProtQ99497 [Medical]
TSGene11315
GENETestsPARK7
Huge Navigator PARK7 [HugePedia]
snp3D : Map Gene to Disease11315
BioCentury BCIQPARK7
ClinGenPARK7
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD11315
Chemical/Pharm GKB GenePA32946
Clinical trialPARK7
Miscellaneous
canSAR (ICR)PARK7 (select the gene name)
Probes
Litterature
PubMed320 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMinePARK7
EVEXPARK7
GoPubMedPARK7
iHOPPARK7
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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