HUMAN:PARK7

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Species (Taxon ID)	Homo sapiens (Human). (taxon:9606)
Gene Name(s)	PARK7
Protein Name(s)	Protein DJ-1 Oncogene DJ1 Parkinson disease protein 7
External Links
UniProt Identifier	PARK7_HUMAN
UniProt Accessions	Q99497, B2R4Z1, O14805, Q6DR95, Q7LFU2,
EMBL	D61380, AF021819, AB073864, AK312000, AL034417, CH471130, BC008188, AB045294, AY648999,
PIR	JC5394,
RefSeq	NP_001116849.1, NP_009193.2,
PDB	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,
IntAct	Q99497,
Ensembl	ENST00000338639, ENST00000377488, ENST00000377491, ENST00000493678,
Pfam	PF01965,

Annotations

Qualifier	GO ID	GO term name	Reference	Evidence Code	with/from	Aspect	Notes	Status
	GO:0005634	nucleus		IDA: Inferred from Direct Assay		C	Source: UniProtKB
	GO:0005515	protein binding		IPI: Inferred from Physical Interaction		F	Source: UniProtKB
	GO:0008219	cell death		IEA: Inferred from Electronic Annotation		P	Source: UniProtKB-KW
	GO:0032091	negative regulation of protein binding		IDA: Inferred from Direct Assay		P	Source: UniProtKB
	GO:0034599	cellular response to oxidative stress	PMID:14662519^[1]	IMP: Inferred from Mutant Phenotype		P	Fig. 6	complete
	GO:0060765	regulation of androgen receptor signaling p...		IDA: Inferred from Direct Assay		P	Source: UniProtKB
	GO:0006979	response to oxidative stress	PMID:18309325^[2]	IDA: Inferred from Direct Assay		P	Figure 1: DJ-1 suppresses oxidative stress-induced JNK1 activation	complete
	GO:0001963	synaptic transmission, dopaminergic	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000030805	P
	GO:0003723	RNA binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0694	F
	GO:0003729	mRNA binding	PMID:18626009^[3]	IDA: Inferred from Direct Assay		F
	GO:0004601	peroxidase activity	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000030805	F
	GO:0004601	peroxidase activity	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:Q99LX0	F
	GO:0005515	protein binding	PMID:11477070^[4]	IPI: Inferred from Physical Interaction	UniProtKB:O75928	F
	GO:0005515	protein binding	PMID:11477070^[4]	IPI: Inferred from Physical Interaction	UniProtKB:Q9Y6X2	F
	GO:0005515	protein binding	PMID:15983381^[5]	IPI: Inferred from Physical Interaction	UniProtKB:Q9UER7	F
	GO:0005515	protein binding	PMID:17510388^[6]	IPI: Inferred from Physical Interaction	UniProtKB:P10275	F
	GO:0005515	protein binding	PMID:20127688^[7]	IPI: Inferred from Physical Interaction	UniProtKB:O94776	F
	GO:0005515	protein binding	PMID:21097510^[8]	IPI: Inferred from Physical Interaction	UniProtKB:Q6GQQ9	F
	GO:0005634	nucleus	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0539	C
	GO:0005634	nucleus	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0191	C
	GO:0005634	nucleus	PMID:11477070^[4]	IDA: Inferred from Direct Assay		C
	GO:0005634	nucleus	PMID:12446870^[9]	IDA: Inferred from Direct Assay		C
	GO:0005634	nucleus	PMID:18711745^[10]	IDA: Inferred from Direct Assay		C
	GO:0005737	cytoplasm	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0963	C
	GO:0005737	cytoplasm	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0086	C
	GO:0005737	cytoplasm	PMID:12446870^[9]	IDA: Inferred from Direct Assay		C
	GO:0005737	cytoplasm	PMID:18029348^[11]	IDA: Inferred from Direct Assay		C
	GO:0005737	cytoplasm	PMID:18711745^[10]	IDA: Inferred from Direct Assay		C
	GO:0005739	mitochondrion	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0496	C
	GO:0005739	mitochondrion	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000030805	C
	GO:0005739	mitochondrion	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0173	C
	GO:0005739	mitochondrion	PMID:18711745^[10]	IDA: Inferred from Direct Assay		C
	GO:0005829	cytosol	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000052374	C
	GO:0006914	autophagy	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0072	P
	GO:0006950	response to stress	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0346	P
	GO:0006950	response to stress	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000030805	P
	GO:0006954	inflammatory response	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0395	P
	GO:0006979	response to oxidative stress	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000052374	P
	GO:0007005	mitochondrion organization	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000030805	P
	GO:0007005	mitochondrion organization	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:Q99LX0	P
	GO:0007338	single fertilization	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0278	P
	GO:0008219	cell death	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0523	P
	GO:0008233	peptidase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0645	F
	GO:0008233	peptidase activity	PMID:20304780^[12]	IDA: Inferred from Direct Assay		F
	GO:0008344	adult locomotory behavior	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000030805	P
	GO:0016787	hydrolase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0378	F
	GO:0030424	axon	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000052374	C
	GO:0032091	negative regulation of protein binding	PMID:11477070^[4]	IDA: Inferred from Direct Assay		P
	GO:0034599	cellular response to oxidative stress	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000030805	P
	GO:0042493	response to drug	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSRNOP00000052374	P
	GO:0042542	response to hydrogen peroxide	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000030805	P
	GO:0042743	hydrogen peroxide metabolic process	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000030805	P
	GO:0042803	protein homodimerization activity	PMID:18711745^[10]	IDA: Inferred from Direct Assay		F
	GO:0043526	neuroprotection	PMID:18711745^[10]	IDA: Inferred from Direct Assay		P
	GO:0043526	neuroprotection	PMID:20304780^[12]	IDA: Inferred from Direct Assay		P
	GO:0050727	regulation of inflammatory response	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000030805	P
	GO:0050727	regulation of inflammatory response	GO_REF:0000024	ISS: Inferred from Sequence or Structural Similarity	UniProtKB:Q99LX0	P
	GO:0050821	protein stabilization	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000030805	P
	GO:0050821	protein stabilization	PMID:17015834^[13]	IMP: Inferred from Mutant Phenotype		P
	GO:0051583	dopamine uptake	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000030805	P
	GO:0051899	membrane depolarization	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000030805	P
	GO:0051920	peroxiredoxin activity	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000030805	F
	GO:0060081	membrane hyperpolarization	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000030805	P
	GO:0060548	negative regulation of cell death	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000030805	P
	GO:0060548	negative regulation of cell death	PMID:14749723^[14]	IDA: Inferred from Direct Assay		P
	GO:0060765	regulation of androgen receptor signaling pathway	PMID:11477070^[4]	IDA: Inferred from Direct Assay		P
	GO:0070301	cellular response to hydrogen peroxide	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000030805	P
	GO:0070301	cellular response to hydrogen peroxide	PMID:14749723^[14]	IDA: Inferred from Direct Assay		P
	GO:2000277	positive regulation of oxidative phosphorylation uncoupler activity	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000030805	P
	GO:0031647	regulation of protein stability	PMID:14713311^[15]	IDA: Inferred from Direct Assay		P	Figure 5. A missense mutation in DJ-1 causes reduced protein stability which manifests as the development of Parkinson's disease.	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ Bandopadhyay R et al. (2004) The expression of DJ-1 (PARK7) in normal human CNS and idiopathic Parkinson's disease. Brain 127: 420-30 PubMed GONUTS page
↑ Mo JS et al. (2008) DJ-1 modulates UV-induced oxidative stress signaling through the suppression of MEKK1 and cell death. Cell Death Differ 15: 1030-41 PubMed GONUTS page
↑ van der Brug MP et al. (2008) RNA binding activity of the recessive parkinsonism protein DJ-1 supports involvement in multiple cellular pathways. Proc Natl Acad Sci U S A 105: 10244-9 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 ^4.4 Takahashi K et al. (2001) DJ-1 positively regulates the androgen receptor by impairing the binding of PIASx alpha to the receptor. J Biol Chem 276: 37556-63 PubMed GONUTS page
↑ Junn E et al. (2005) Interaction of DJ-1 with Daxx inhibits apoptosis signal-regulating kinase 1 activity and cell death. Proc Natl Acad Sci U S A 102: 9691-6 PubMed GONUTS page
↑ Tillman JE et al. (2007) DJ-1 binds androgen receptor directly and mediates its activity in hormonally treated prostate cancer cells. Cancer Res 67: 4630-7 PubMed GONUTS page
↑ Opsahl JA et al. (2010) Increased interaction between DJ-1 and the Mi-2/ nucleosome remodelling and deacetylase complex during cellular stress. Proteomics 10: 1494-504 PubMed GONUTS page
↑ McNally RS et al. (2011) DJ-1 enhances cell survival through the binding of Cezanne, a negative regulator of NF-kappaB. J Biol Chem 286: 4098-106 PubMed GONUTS page
↑ ^9.0 ^9.1 Bonifati V et al. (2003) Mutations in the DJ-1 gene associated with autosomal recessive early-onset parkinsonism. Science 299: 256-9 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 ^10.3 ^10.4 Junn E et al. (2009) Mitochondrial localization of DJ-1 leads to enhanced neuroprotection. J Neurosci Res 87: 123-9 PubMed GONUTS page
↑ Barbe L et al. (2008) Toward a confocal subcellular atlas of the human proteome. Mol Cell Proteomics 7: 499-508 PubMed GONUTS page
↑ ^12.0 ^12.1 Chen J et al. (2010) Parkinson disease protein DJ-1 converts from a zymogen to a protease by carboxyl-terminal cleavage. Hum Mol Genet 19: 2395-408 PubMed GONUTS page
↑ Clements CM et al. (2006) DJ-1, a cancer- and Parkinson's disease-associated protein, stabilizes the antioxidant transcriptional master regulator Nrf2. Proc Natl Acad Sci U S A 103: 15091-6 PubMed GONUTS page
↑ ^14.0 ^14.1 Taira T et al. (2004) DJ-1 has a role in antioxidative stress to prevent cell death. EMBO Rep 5: 213-8 PubMed GONUTS page
↑ Moore DJ et al. (2003) A missense mutation (L166P) in DJ-1, linked to familial Parkinson's disease, confers reduced protein stability and impairs homo-oligomerization. J Neurochem 87: 1558-67 PubMed GONUTS page

[PMID:14662519-0] Bandopadhyay R et al. (2004) The expression of DJ-1 (PARK7) in normal human CNS and idiopathic Parkinson's disease. Brain 127: 420-30 PubMed GONUTS page

[PMID:18309325-1] Mo JS et al. (2008) DJ-1 modulates UV-induced oxidative stress signaling through the suppression of MEKK1 and cell death. Cell Death Differ 15: 1030-41 PubMed GONUTS page

[PMID:18626009-2] van der Brug MP et al. (2008) RNA binding activity of the recessive parkinsonism protein DJ-1 supports involvement in multiple cellular pathways. Proc Natl Acad Sci U S A 105: 10244-9 PubMed GONUTS page

[PMID:11477070-3] 4.0 ^4.1 ^4.2 ^4.3 ^4.4 Takahashi K et al. (2001) DJ-1 positively regulates the androgen receptor by impairing the binding of PIASx alpha to the receptor. J Biol Chem 276: 37556-63 PubMed GONUTS page

[PMID:15983381-4] Junn E et al. (2005) Interaction of DJ-1 with Daxx inhibits apoptosis signal-regulating kinase 1 activity and cell death. Proc Natl Acad Sci U S A 102: 9691-6 PubMed GONUTS page

[PMID:17510388-5] Tillman JE et al. (2007) DJ-1 binds androgen receptor directly and mediates its activity in hormonally treated prostate cancer cells. Cancer Res 67: 4630-7 PubMed GONUTS page

[PMID:20127688-6] Opsahl JA et al. (2010) Increased interaction between DJ-1 and the Mi-2/ nucleosome remodelling and deacetylase complex during cellular stress. Proteomics 10: 1494-504 PubMed GONUTS page

[PMID:21097510-7] McNally RS et al. (2011) DJ-1 enhances cell survival through the binding of Cezanne, a negative regulator of NF-kappaB. J Biol Chem 286: 4098-106 PubMed GONUTS page

[PMID:12446870-8] 9.0 ^9.1 Bonifati V et al. (2003) Mutations in the DJ-1 gene associated with autosomal recessive early-onset parkinsonism. Science 299: 256-9 PubMed GONUTS page

[PMID:18711745-9] 10.0 ^10.1 ^10.2 ^10.3 ^10.4 Junn E et al. (2009) Mitochondrial localization of DJ-1 leads to enhanced neuroprotection. J Neurosci Res 87: 123-9 PubMed GONUTS page

[PMID:18029348-10] Barbe L et al. (2008) Toward a confocal subcellular atlas of the human proteome. Mol Cell Proteomics 7: 499-508 PubMed GONUTS page

[PMID:20304780-11] 12.0 ^12.1 Chen J et al. (2010) Parkinson disease protein DJ-1 converts from a zymogen to a protease by carboxyl-terminal cleavage. Hum Mol Genet 19: 2395-408 PubMed GONUTS page

[PMID:17015834-12] Clements CM et al. (2006) DJ-1, a cancer- and Parkinson's disease-associated protein, stabilizes the antioxidant transcriptional master regulator Nrf2. Proc Natl Acad Sci U S A 103: 15091-6 PubMed GONUTS page

[PMID:14749723-13] 14.0 ^14.1 Taira T et al. (2004) DJ-1 has a role in antioxidative stress to prevent cell death. EMBO Rep 5: 213-8 PubMed GONUTS page

[PMID:14713311-14] Moore DJ et al. (2003) A missense mutation (L166P) in DJ-1, linked to familial Parkinson's disease, confers reduced protein stability and impairs homo-oligomerization. J Neurochem 87: 1558-67 PubMed GONUTS page

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HUMAN:PARK7

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