HUMAN:PRKN2

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Species (Taxon ID)	Homo sapiens (Human). (taxon:9606)
Gene Name(s)	PARK2 ( synonyms: PRKN )
Protein Name(s)	E3 ubiquitin-protein ligase parkin Parkinson juvenile disease protein 2 Parkinson disease protein 2
External Links
UniProt Identifier	PRKN2_HUMAN
UniProt Accessions	O60260, A3FG77, A8K975, Q5TFV8, Q6Q2I6, Q8NI41, Q8NI43, Q8NI44, Q8WW07,
EMBL	AB009973, EF375726, AF381282, AF381283, AF381286, AK292590, AL445215, AL035697, AL132982, AP000886, AP000887, AP001576, AP001577, AP001578, AP003699, AL035697, AL132982, AL445215, AP000886, AP000887, AP001576, AP001577, AP001578, AP003699, AL132982, AL035697, AL445215, AP000886, AP000887, AP001576, AP001577, AP001578, AP003699, CH471051, BC022014, AY564225,
RefSeq	NP_004553.2, NP_054642.2, NP_054643.2,
PDB	1IYF, 2JMO,
IntAct	O60260,
Ensembl	ENST00000366898,
Pfam	PF01485, PF00240,

Annotations

Qualifier	GO ID	GO term name	Reference	Evidence Code	with/from	Aspect	Notes	Status
	GO:0004842	ubiquitin-protein ligase activity	PMID:10888878^[1]	IDA: Inferred from Direct Assay		F	Figure 5a. Incubation of immunoprecipitated Parkin with ATP, E1, E2, and ubiquitin results in an ubiquitinated signal at 30 kD.	complete
	GO:0000422	mitochondrion degradation	PMID:19029340^[2]	IDA: Inferred from Direct Assay		P	Figure 4. HeLa cells transfected with the gene for PRKN2 have less mitochondrial mass under depolarizing conditions compared to cells that do not have the parkin gene.	complete
	GO:0000209	protein polyubiquitination	PMID:16227987^[3]	IDA: Inferred from Direct Assay		P
	GO:0005739	mitochondrion	PMID:19029340^[2]	IDA: Inferred from Direct Assay		C	Figure 1a and 1b. Human cells treated with CCCP (to depolarize the mitochondrial membrane) have increased levels of Parkin associated with them.	complete
	GO:0000209	protein polyubiquitination	PMID:18541373^[4]	IDA: Inferred from Direct Assay		P
	GO:0000209	protein polyubiquitination	PMID:19880420^[5]	IDA: Inferred from Direct Assay		P
	GO:0004842	ubiquitin-protein ligase activity	PMID:11078524^[6]	IDA: Inferred from Direct Assay		F	Figure 3C shows that Cys421Ala and Cys431Ala mutations significantly decrease the self-ubiquitination of Parkin.	complete
	GO:0000422	mitochondrion degradation	PMID:19029340^[2]	IMP: Inferred from Mutant Phenotype		P
	GO:0004842	ubiquitin-protein ligase activity	PMID:11078524^[6]	IDA: Inferred from Direct Assay		F	Figure 1B shows that Parkin selectively interacts with UbcH8.	complete
	GO:0001933	negative regulation of protein phosphorylation	PMID:17512523^[7]	IDA: Inferred from Direct Assay		P
	GO:0004842	ubiquitin-protein ligase activity	PMID:11078524^[6]	IDA: Inferred from Direct Assay		F	Figure 4C shows that ubiquitination of CDCrel-1 is significantly increased in the presence of Parkin.	complete
	GO:0001963	synaptic transmission, dopaminergic	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000063644	P
	GO:0005829	cytosol	PMID:19029340^[2]	IDA: Inferred from Direct Assay		C	Figure 1 a and c. Immunostained cells show that parkin is located in the cytosol.	complete
	GO:0001964	startle response	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000063644	P
	GO:0004842	ubiquitin-protein ligase activity	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000063644	F
	GO:0004842	ubiquitin-protein ligase activity	PMID:15728840^[8]	IDA: Inferred from Direct Assay		F
	GO:0004842	ubiquitin-protein ligase activity	PMID:16227987^[3]	IDA: Inferred from Direct Assay		F
	GO:0004842	ubiquitin-protein ligase activity	PMID:17097639^[9]	IDA: Inferred from Direct Assay		F
	GO:0004842	ubiquitin-protein ligase activity	PMID:18541373^[4]	IDA: Inferred from Direct Assay		F
	GO:0004842	ubiquitin-protein ligase activity	PMID:19880420^[5]	IDA: Inferred from Direct Assay		F
	GO:0004842	ubiquitin-protein ligase activity	PMID:20889974^[10]	IDA: Inferred from Direct Assay		F
	GO:0004842	ubiquitin-protein ligase activity	PMID:21376232^[11]	IDA: Inferred from Direct Assay		F
	GO:0005515	protein binding	PMID:10888878^[1]	IPI: Inferred from Physical Interaction	UniProtKB:P68036	F
	GO:0005515	protein binding	PMID:11590439^[12]	IPI: Inferred from Physical Interaction	UniProtKB:Q9Y6H5	F
	GO:0005515	protein binding	PMID:12364339^[13]	IPI: Inferred from Physical Interaction	UniProtKB:Q9Y6H5	F
	GO:0005515	protein binding	PMID:15603737^[14]	IPI: Inferred from Physical Interaction	UniProtKB:Q5QJC9	F
	GO:0005515	protein binding	PMID:15728840^[8]	IPI: Inferred from Physical Interaction	UniProtKB:Q9Y6H5	F
	GO:0005515	protein binding	PMID:16189514^[15]	IPI: Inferred from Physical Interaction	UniProtKB:Q15645	F
	GO:0005515	protein binding	PMID:16332688^[16]	IPI: Inferred from Physical Interaction	UniProtKB:P49792	F
	GO:0005515	protein binding	PMID:16352719^[17]	IPI: Inferred from Physical Interaction	UniProtKB:Q5S007	F
	GO:0005515	protein binding	PMID:17097639^[9]	IPI: Inferred from Physical Interaction	UniProtKB:Q99700	F
	GO:0005515	protein binding	PMID:20889974^[10]	IPI: Inferred from Physical Interaction	UniProtKB:P10415	F
	GO:0005515	protein binding	PMID:21376232^[11]	IPI: Inferred from Physical Interaction	UniProtKB:Q6NUN9	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:0005737	cytoplasm	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0963	C
	GO:0005737	cytoplasm	PMID:17512523^[7]	IDA: Inferred from Direct Assay		C
	GO:0005737	cytoplasm	PMID:21376232^[11]	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:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0173	C
	GO:0005739	mitochondrion	PMID:19029340^[2]	IMP: Inferred from Mutant Phenotype		C
	GO:0005739	mitochondrion	PMID:20889974^[10]	IDA: Inferred from Direct Assay		C
	GO:0005783	endoplasmic reticulum	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0256	C
	GO:0005783	endoplasmic reticulum	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0095	C
	GO:0005794	Golgi apparatus	PMID:17097639^[9]	IDA: Inferred from Direct Assay		C
	GO:0005829	cytosol	GO_REF:0000023	IEA: Inferred from Electronic Annotation	SP_SL:SL-0091	C
	GO:0005829	cytosol	PMID:19029340^[2]	IDA: Inferred from Direct Assay		C
	GO:0005829	cytosol	PMID:19880420^[5]	IDA: Inferred from Direct Assay		C
	GO:0005829	cytosol	PMID:20889974^[10]	IDA: Inferred from Direct Assay		C
	GO:0006511	ubiquitin-dependent protein catabolic process	PMID:10888878^[1]	TAS: Traceable Author Statement		P
	GO:0006511	ubiquitin-dependent protein catabolic process	PMID:21376232^[11]	IDA: Inferred from Direct Assay		P
	GO:0006513	protein monoubiquitination	PMID:20889974^[10]	IDA: Inferred from Direct Assay		P
	GO:0006914	autophagy	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0072	P
	GO:0007417	central nervous system development	PMID:9560156^[18]	TAS: Traceable Author Statement		P
	GO:0007612	learning	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000063644	P
	GO:0007626	locomotory behavior	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000063644	P
	GO:0008219	cell death	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0523	P
	GO:0008219	cell death	PMID:21376232^[11]	IDA: Inferred from Direct Assay		P
	GO:0008270	zinc ion binding	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR002867	F
	GO:0008344	adult locomotory behavior	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000063644	P
	GO:0010506	regulation of autophagy	PMID:20889974^[10]	IDA: Inferred from Direct Assay		P
	GO:0016235	aggresome	PMID:14645198^[19]	IDA: Inferred from Direct Assay		C
	GO:0016567	protein ubiquitination	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000063644	P
	GO:0016874	ligase activity	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0436	F
	GO:0016881	acid-amino acid ligase activity	GO_REF:0000002	IEA: Inferred from Electronic Annotation	InterPro:IPR003977	F
	GO:0019538	protein metabolic process	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000063644	P
	GO:0019900	kinase binding	PMID:17512523^[7]	IPI: Inferred from Physical Interaction	UniProtKB:P53667	F
	GO:0019900	kinase binding	PMID:19880420^[5]	IPI: Inferred from Physical Interaction	UniProtKB:Q9BXM7	F
	GO:0019901	protein kinase binding	PMID:20798600^[20]	IPI: Inferred from Physical Interaction	UniProtKB:Q9BXM7	F
	GO:0030165	PDZ domain binding	PMID:17512523^[7]	IPI: Inferred from Physical Interaction	UniProtKB:P53667	F
	GO:0031625	ubiquitin protein ligase binding	PMID:21532592^[21]	IPI: Inferred from Physical Interaction	UniProtKB:P68036	F
	GO:0032232	negative regulation of actin filament bundle assembly	PMID:17512523^[7]	IDA: Inferred from Direct Assay		P
	GO:0035249	synaptic transmission, glutamatergic	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000063644	P
	GO:0042415	norepinephrine metabolic process	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000063644	P
	GO:0042417	dopamine metabolic process	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000063644	P
	GO:0042787	protein ubiquitination involved in ubiquitin-dependent protein catabolic process	PMID:17097639^[9]	IDA: Inferred from Direct Assay		P
	GO:0043005	neuron projection	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000063644	C
	GO:0043123	positive regulation of I-kappaB kinase/NF-kappaB cascade	PMID:19880420^[5]	IDA: Inferred from Direct Assay		P
	GO:0043234	protein complex	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000063644	C
	GO:0046872	metal ion binding	GO_REF:0000004	IEA: Inferred from Electronic Annotation	SP_KW:KW-0479	F
	GO:0046928	regulation of neurotransmitter secretion	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000063644	P
	GO:0048471	perinuclear region of cytoplasm	PMID:17097639^[9]	IDA: Inferred from Direct Assay		C
	GO:0050804	regulation of synaptic transmission	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000063644	P
	GO:0051087	chaperone binding	PMID:15603737^[14]	IPI: Inferred from Physical Interaction	UniProtKB:P08107	F
	GO:0051583	dopamine uptake	GO_REF:0000019	IEA: Inferred from Electronic Annotation	Ensembl:ENSMUSP00000063644	P
	GO:0051865	protein autoubiquitination	PMID:15728840^[8]	IDA: Inferred from Direct Assay		P
	GO:0051865	protein autoubiquitination	PMID:17512523^[7]	IDA: Inferred from Direct Assay		P
	GO:0060548	negative regulation of cell death	PMID:15603737^[14]	IDA: Inferred from Direct Assay		P
	GO:0070534	protein K63-linked ubiquitination	PMID:15728840^[8]	IDA: Inferred from Direct Assay		P
	GO:0070534	protein K63-linked ubiquitination	PMID:19880420^[5]	IDA: Inferred from Direct Assay		P
	GO:0070842	aggresome assembly	PMID:14645198^[19]	IMP: Inferred from Mutant Phenotype		P
	GO:0070936	protein K48-linked ubiquitination	PMID:21376232^[11]	IDA: Inferred from Direct Assay		P
	GO:0070997	neuron death	PMID:21376232^[11]	IDA: Inferred from Direct Assay		P
	GO:0090201	negative regulation of release of cytochrome c from mitochondria	PMID:19880420^[5]	IDA: Inferred from Direct Assay		P
	GO:2000377	regulation of reactive oxygen species metabolic process	PMID:18541373^[4]	IMP: Inferred from Mutant Phenotype		P
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Notes

References

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

↑ ^1.0 ^1.1 ^1.2 Shimura H et al. (2000) Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase. Nat Genet 25: 302-5 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 Narendra D et al. (2008) Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. J Cell Biol 183: 795-803 PubMed GONUTS page
↑ ^3.0 ^3.1 LaVoie MJ et al. (2005) Dopamine covalently modifies and functionally inactivates parkin. Nat Med 11: 1214-21 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 Yu F & Zhou J (2008) Parkin is ubiquitinated by Nrdp1 and abrogates Nrdp1-induced oxidative stress. Neurosci Lett 440: 4-8 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 ^5.3 ^5.4 ^5.5 ^5.6 Sha D et al. (2010) Phosphorylation of parkin by Parkinson disease-linked kinase PINK1 activates parkin E3 ligase function and NF-kappaB signaling. Hum Mol Genet 19: 352-63 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 Zhang Y et al. (2000) Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1. Proc Natl Acad Sci U S A 97: 13354-9 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 ^7.4 ^7.5 Lim MK et al. (2007) Parkin interacts with LIM Kinase 1 and reduces its cofilin-phosphorylation activity via ubiquitination. Exp Cell Res 313: 2858-74 PubMed GONUTS page
↑ ^8.0 ^8.1 ^8.2 ^8.3 Lim KL et al. (2005) Parkin mediates nonclassical, proteasomal-independent ubiquitination of synphilin-1: implications for Lewy body formation. J Neurosci 25: 2002-9 PubMed GONUTS page
↑ ^9.0 ^9.1 ^9.2 ^9.3 ^9.4 Huynh DP et al. (2007) Parkin is an E3 ubiquitin-ligase for normal and mutant ataxin-2 and prevents ataxin-2-induced cell death. Exp Neurol 203: 531-41 PubMed GONUTS page
↑ ^10.0 ^10.1 ^10.2 ^10.3 ^10.4 ^10.5 Chen D et al. (2010) Parkin mono-ubiquitinates Bcl-2 and regulates autophagy. J Biol Chem 285: 38214-23 PubMed GONUTS page
↑ ^11.0 ^11.1 ^11.2 ^11.3 ^11.4 ^11.5 ^11.6 Shin JH et al. (2011) PARIS (ZNF746) repression of PGC-1α contributes to neurodegeneration in Parkinson's disease. Cell 144: 689-702 PubMed GONUTS page
↑ Chung KK et al. (2001) Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease. Nat Med 7: 1144-50 PubMed GONUTS page
↑ Junn E et al. (2002) Parkin accumulation in aggresomes due to proteasome impairment. J Biol Chem 277: 47870-7 PubMed GONUTS page
↑ ^14.0 ^14.1 ^14.2 Kalia SK et al. (2004) BAG5 inhibits parkin and enhances dopaminergic neuron degeneration. Neuron 44: 931-45 PubMed GONUTS page
↑ Rual JF et al. (2005) Towards a proteome-scale map of the human protein-protein interaction network. Nature 437: 1173-8 PubMed GONUTS page
↑ Um JW et al. (2006) Parkin ubiquitinates and promotes the degradation of RanBP2. J Biol Chem 281: 3595-603 PubMed GONUTS page
↑ Smith WW et al. (2005) Leucine-rich repeat kinase 2 (LRRK2) interacts with parkin, and mutant LRRK2 induces neuronal degeneration. Proc Natl Acad Sci U S A 102: 18676-81 PubMed GONUTS page
↑ Kitada T et al. (1998) Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Nature 392: 605-8 PubMed GONUTS page
↑ ^19.0 ^19.1 Muqit MM et al. (2004) Parkin is recruited into aggresomes in a stress-specific manner: over-expression of parkin reduces aggresome formation but can be dissociated from parkin's effect on neuronal survival. Hum Mol Genet 13: 117-35 PubMed GONUTS page
↑ Geisler S et al. (2010) The PINK1/Parkin-mediated mitophagy is compromised by PD-associated mutations. Autophagy 6: 871-8 PubMed GONUTS page
↑ Wenzel DM et al. (2011) UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids. Nature 474: 105-8 PubMed GONUTS page

[PMID:10888878-0] 1.0 ^1.1 ^1.2 Shimura H et al. (2000) Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase. Nat Genet 25: 302-5 PubMed GONUTS page

[PMID:19029340-1] 2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 Narendra D et al. (2008) Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. J Cell Biol 183: 795-803 PubMed GONUTS page

[PMID:16227987-2] 3.0 ^3.1 LaVoie MJ et al. (2005) Dopamine covalently modifies and functionally inactivates parkin. Nat Med 11: 1214-21 PubMed GONUTS page

[PMID:18541373-3] 4.0 ^4.1 ^4.2 Yu F & Zhou J (2008) Parkin is ubiquitinated by Nrdp1 and abrogates Nrdp1-induced oxidative stress. Neurosci Lett 440: 4-8 PubMed GONUTS page

[PMID:19880420-4] 5.0 ^5.1 ^5.2 ^5.3 ^5.4 ^5.5 ^5.6 Sha D et al. (2010) Phosphorylation of parkin by Parkinson disease-linked kinase PINK1 activates parkin E3 ligase function and NF-kappaB signaling. Hum Mol Genet 19: 352-63 PubMed GONUTS page

[PMID:11078524-5] 6.0 ^6.1 ^6.2 Zhang Y et al. (2000) Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1. Proc Natl Acad Sci U S A 97: 13354-9 PubMed GONUTS page

[PMID:17512523-6] 7.0 ^7.1 ^7.2 ^7.3 ^7.4 ^7.5 Lim MK et al. (2007) Parkin interacts with LIM Kinase 1 and reduces its cofilin-phosphorylation activity via ubiquitination. Exp Cell Res 313: 2858-74 PubMed GONUTS page

[PMID:15728840-7] 8.0 ^8.1 ^8.2 ^8.3 Lim KL et al. (2005) Parkin mediates nonclassical, proteasomal-independent ubiquitination of synphilin-1: implications for Lewy body formation. J Neurosci 25: 2002-9 PubMed GONUTS page

[PMID:17097639-8] 9.0 ^9.1 ^9.2 ^9.3 ^9.4 Huynh DP et al. (2007) Parkin is an E3 ubiquitin-ligase for normal and mutant ataxin-2 and prevents ataxin-2-induced cell death. Exp Neurol 203: 531-41 PubMed GONUTS page

[PMID:20889974-9] 10.0 ^10.1 ^10.2 ^10.3 ^10.4 ^10.5 Chen D et al. (2010) Parkin mono-ubiquitinates Bcl-2 and regulates autophagy. J Biol Chem 285: 38214-23 PubMed GONUTS page

[PMID:21376232-10] 11.0 ^11.1 ^11.2 ^11.3 ^11.4 ^11.5 ^11.6 Shin JH et al. (2011) PARIS (ZNF746) repression of PGC-1α contributes to neurodegeneration in Parkinson's disease. Cell 144: 689-702 PubMed GONUTS page

[PMID:11590439-11] Chung KK et al. (2001) Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease. Nat Med 7: 1144-50 PubMed GONUTS page

[PMID:12364339-12] Junn E et al. (2002) Parkin accumulation in aggresomes due to proteasome impairment. J Biol Chem 277: 47870-7 PubMed GONUTS page

[PMID:15603737-13] 14.0 ^14.1 ^14.2 Kalia SK et al. (2004) BAG5 inhibits parkin and enhances dopaminergic neuron degeneration. Neuron 44: 931-45 PubMed GONUTS page

[PMID:16189514-14] Rual JF et al. (2005) Towards a proteome-scale map of the human protein-protein interaction network. Nature 437: 1173-8 PubMed GONUTS page

[PMID:16332688-15] Um JW et al. (2006) Parkin ubiquitinates and promotes the degradation of RanBP2. J Biol Chem 281: 3595-603 PubMed GONUTS page

[PMID:16352719-16] Smith WW et al. (2005) Leucine-rich repeat kinase 2 (LRRK2) interacts with parkin, and mutant LRRK2 induces neuronal degeneration. Proc Natl Acad Sci U S A 102: 18676-81 PubMed GONUTS page

[PMID:9560156-17] Kitada T et al. (1998) Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Nature 392: 605-8 PubMed GONUTS page

[PMID:14645198-18] 19.0 ^19.1 Muqit MM et al. (2004) Parkin is recruited into aggresomes in a stress-specific manner: over-expression of parkin reduces aggresome formation but can be dissociated from parkin's effect on neuronal survival. Hum Mol Genet 13: 117-35 PubMed GONUTS page

[PMID:20798600-19] Geisler S et al. (2010) The PINK1/Parkin-mediated mitophagy is compromised by PD-associated mutations. Autophagy 6: 871-8 PubMed GONUTS page

[PMID:21532592-20] Wenzel DM et al. (2011) UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids. Nature 474: 105-8 PubMed GONUTS page

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HUMAN:PRKN2

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