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DROME:Q0KHV6

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Species (Taxon ID) Drosophila melanogaster (Fruit fly). (7227)
Gene Name(s) No Information Provided. (synonyms: Pink1-RE (ECO:0000313 with EMBL:AFA28429.1))
Protein Name(s) FI19430p1 (ECO:0000313 with EMBL:AFA28429.1)

PTEN-induced putative kinase 1, isoform A (ECO:0000313 with EMBL:AAN09178.1) PTEN-induced putative kinase 1, isoform B (ECO:0000313 with EMBL:AAF46188.1) PTEN-induced putative kinase 1, isoform C (ECO:0000313 with EMBL:AAZ52497.1) PTEN-induced putative kinase 1, isoform D (ECO:0000313 with EMBL:AAZ52498.1) PTEN-induced putative kinase 1, isoform E (ECO:0000313 with EMBL:AAZ52499.1) PTEN-induced putative kinase 1, isoform F (ECO:0000313 with EMBL:AAZ52500.1) PTEN-induced putative kinase 1, isoform G (ECO:0000313 with EMBL:AAZ52501.1) PTEN-induced putative kinase 1, isoform H (ECO:0000313 with EMBL:AAZ52502.1) PTEN-induced putative kinase 1, isoform I (ECO:0000313 with EMBL:AHN59423.1)

External Links
UniProt Q0KHV6
EMBL AE014298
AE014298
AE014298
AE014298
AE014298
AE014298
AE014298
AE014298
BT133188
AE014298
RefSeq NP_001027049.1
NP_001027050.1
NP_001027051.1
NP_001027052.1
NP_001027053.1
NP_001027054.1
NP_572340.2
NP_727110.1
UniGene Dm.56
SMR Q0KHV6
IntAct Q0KHV6
STRING 7227.FBpp0099833
EnsemblMetazoa FBtr0070956
FBtr0070957
FBtr0100413
FBtr0100414
FBtr0100415
FBtr0100416
FBtr0100419
FBtr0100420
GeneID 31607
KEGG dme:Dmel_CG4523
UCSC CG4523-RA
CTD 65018
FlyBase FBgn0029891
GeneTree ENSGT00390000001206
OMA LKMMFNY
OrthoDB EOG7TBC1R
GenomeRNAi 31607
NextBio 774437
PRO PR:Q0KHV6
Proteomes UP000000803
GO GO:0005737
GO:0005739
GO:0016006
GO:0005524
GO:0004672
GO:0004674
GO:0048749
GO:0035234
GO:0000266
GO:0000422
GO:0007005
GO:0010637
GO:0043524
GO:0043069
GO:0007274
GO:0048078
GO:0090141
GO:0042787
GO:0010821
GO:0006979
GO:0030382
InterPro IPR011009
IPR000719
IPR008271
Pfam PF00069
SUPFAM SSF56112
PROSITE PS50011
PS00108

Annotations

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status
GO:0000266

mitochondrial fission

PMID:18230723[1]

IGI: Inferred from Genetic Interaction

FB:FBgn0026479

P

Seeded From UniProt

complete

GO:0000266

mitochondrial fission

PMID:18230723[1]

IGI: Inferred from Genetic Interaction

FB:FBgn0029870

P

Seeded From UniProt

complete

GO:0047497

mitochondrion transport along microtubule

PMID:22396657[2]

IMP: Inferred from Mutant Phenotype

P

Figure 3

complete
CACAO 3953

GO:0000266

mitochondrial fission

PMID:18230723[1]

IGI: Inferred from Genetic Interaction

FB:FBgn0261276

P

Seeded From UniProt

complete

GO:0048312

intracellular distribution of mitochondria

PMID:22396657[2]

IMP: Inferred from Mutant Phenotype

P

Figure 4

complete
CACAO 3954

GO:0000266

mitochondrial fission

PMID:18443288[3]

IGI: Inferred from Genetic Interaction

FB:FBgn0026479

P

Seeded From UniProt

complete

GO:0000266

mitochondrial fission

PMID:18443288[3]

IGI: Inferred from Genetic Interaction

FB:FBgn0261276

P

Seeded From UniProt

complete

GO:0000422

mitophagy

PMID:20194754[4]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0004672

protein kinase activity

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000719
InterPro:IPR008271

F

Seeded From UniProt

complete

GO:0004672

protein kinase activity

PMID:22645651[5]

IDA: Inferred from Direct Assay

F

Seeded From UniProt

complete

GO:0004674

protein serine/threonine kinase activity

GO_REF:0000033

IBA: Inferred from Biological aspect of Ancestor

PANTHER:PTN001121970

F

Seeded From UniProt

complete

GO:0004674

protein serine/threonine kinase activity

PMID:24901221[6]

IDA: Inferred from Direct Assay

F

Seeded From UniProt

complete

GO:0005515

protein binding

PMID:19048081[7]

IPI: Inferred from Physical Interaction

FB:FBgn0033672

F

Seeded From UniProt

complete

GO:0005515

protein binding

PMID:21151955[8]

IPI: Inferred from Physical Interaction

FB:FBgn0023517

F

Seeded From UniProt

complete

GO:0005524

ATP binding

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000719

F

Seeded From UniProt

complete

GO:0005737

cytoplasm

PMID:19048081[7]

IDA: Inferred from Direct Assay

C

Seeded From UniProt

complete

GO:0005739

mitochondrion

PMID:19048081[7]

IDA: Inferred from Direct Assay

C

Seeded From UniProt

complete

GO:0006468

protein phosphorylation

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR000719
InterPro:IPR008271

P

Seeded From UniProt

complete

GO:0006468

protein phosphorylation

GO_REF:0000033

IBA: Inferred from Biological aspect of Ancestor

PANTHER:PTN000540563

P

Seeded From UniProt

complete

GO:0006468

protein phosphorylation

PMID:24901221[6]

IDA: Inferred from Direct Assay

P

Seeded From UniProt

complete

GO:0006979

response to oxidative stress

PMID:16938835[9]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0007005

mitochondrion organization

PMID:16672980[10]

IGI: Inferred from Genetic Interaction

FB:FBgn0040491

P

Seeded From UniProt

complete

GO:0007005

mitochondrion organization

PMID:16672980[10]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0007005

mitochondrion organization

PMID:16672981[11]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0007005

mitochondrion organization

PMID:16818890[12]

IDA: Inferred from Direct Assay

P

Seeded From UniProt

complete

GO:0007005

mitochondrion organization

PMID:18230723[1]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0007005

mitochondrion organization

PMID:18443288[3]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0007005

mitochondrion organization

PMID:18799731[13]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0007005

mitochondrion organization

PMID:24901221[6]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0007274

neuromuscular synaptic transmission

PMID:20049710[14]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0010637

negative regulation of mitochondrial fusion

PMID:20194754[4]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0010821

regulation of mitochondrion organization

PMID:19546216[15]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0016006

Nebenkern

PMID:16672981[11]

IDA: Inferred from Direct Assay

C

Seeded From UniProt

complete

GO:0016301

kinase activity

GO_REF:0000038

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0418

F

Seeded From UniProt

complete

GO:0016310

phosphorylation

GO_REF:0000038

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0418

P

Seeded From UniProt

complete

GO:0016740

transferase activity

GO_REF:0000038

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0808

F

Seeded From UniProt

complete

GO:0030382

sperm mitochondrion organization

PMID:16672980[10]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0030382

sperm mitochondrion organization

PMID:16672981[11]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0030382

sperm mitochondrion organization

PMID:18799731[13]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0035234

ectopic germ cell programmed cell death

PMID:23523076[16]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0042787

protein ubiquitination involved in ubiquitin-dependent protein catabolic process

PMID:20194754[4]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0043069

negative regulation of programmed cell death

PMID:16938835[9]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0043524

negative regulation of neuron apoptotic process

PMID:16818890[12]

IDA: Inferred from Direct Assay

P

Seeded From UniProt

complete

GO:0047497

mitochondrion transport along microtubule

PMID:22396657[2]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0048078

positive regulation of compound eye pigmentation

PMID:19692353[17]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0048312

intracellular distribution of mitochondria

PMID:22396657[2]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0048749

compound eye development

PMID:16938835[9]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0090141

positive regulation of mitochondrial fission

PMID:20194754[4]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:1902956

regulation of mitochondrial electron transport, NADH to ubiquinone

PMID:24652937[18]

IGI: Inferred from Genetic Interaction

FB:FBgn0019957

P

Seeded From UniProt

complete

GO:1902956

regulation of mitochondrial electron transport, NADH to ubiquinone

PMID:25412178[19]

IGI: Inferred from Genetic Interaction

FB:FBgn0019957

P

Seeded From UniProt

complete

Notes

References

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

  1. 1.0 1.1 1.2 1.3 Poole, AC et al. (2008) The PINK1/Parkin pathway regulates mitochondrial morphology. Proc. Natl. Acad. Sci. U.S.A. 105 1638-43 PubMed GONUTS page
  2. 2.0 2.1 2.2 2.3 Liu, S et al. (2012) Parkinson's disease-associated kinase PINK1 regulates Miro protein level and axonal transport of mitochondria. PLoS Genet. 8 e1002537 PubMed GONUTS page
  3. 3.0 3.1 3.2 Yang, Y et al. (2008) Pink1 regulates mitochondrial dynamics through interaction with the fission/fusion machinery. Proc. Natl. Acad. Sci. U.S.A. 105 7070-5 PubMed GONUTS page
  4. 4.0 4.1 4.2 4.3 Ziviani, E et al. (2010) Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin. Proc. Natl. Acad. Sci. U.S.A. 107 5018-23 PubMed GONUTS page
  5. Woodroof, HI et al. (2011) Discovery of catalytically active orthologues of the Parkinson's disease kinase PINK1: analysis of substrate specificity and impact of mutations. Open Biol 1 110012 PubMed GONUTS page
  6. 6.0 6.1 6.2 Shiba-Fukushima, K et al. (2014) PINK1-mediated phosphorylation of Parkin boosts Parkin activity in Drosophila. PLoS Genet. 10 e1004391 PubMed GONUTS page
  7. 7.0 7.1 7.2 Whitworth, AJ et al. () Rhomboid-7 and HtrA2/Omi act in a common pathway with the Parkinson's disease factors Pink1 and Parkin. Dis Model Mech 1 168-74; discussion 173 PubMed GONUTS page
  8. Imai, Y et al. (2010) The loss of PGAM5 suppresses the mitochondrial degeneration caused by inactivation of PINK1 in Drosophila. PLoS Genet. 6 e1001229 PubMed GONUTS page
  9. 9.0 9.1 9.2 Wang, D et al. (2006) Antioxidants protect PINK1-dependent dopaminergic neurons in Drosophila. Proc. Natl. Acad. Sci. U.S.A. 103 13520-5 PubMed GONUTS page
  10. 10.0 10.1 10.2 Park, J et al. (2006) Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin. Nature 441 1157-61 PubMed GONUTS page
  11. 11.0 11.1 11.2 Clark, IE et al. (2006) Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin. Nature 441 1162-6 PubMed GONUTS page
  12. 12.0 12.1 Yang, Y et al. (2006) Mitochondrial pathology and muscle and dopaminergic neuron degeneration caused by inactivation of Drosophila Pink1 is rescued by Parkin. Proc. Natl. Acad. Sci. U.S.A. 103 10793-8 PubMed GONUTS page
  13. 13.0 13.1 Deng, H et al. (2008) The Parkinson's disease genes pink1 and parkin promote mitochondrial fission and/or inhibit fusion in Drosophila. Proc. Natl. Acad. Sci. U.S.A. 105 14503-8 PubMed GONUTS page
  14. Morais, VA et al. (2009) Parkinson's disease mutations in PINK1 result in decreased Complex I activity and deficient synaptic function. EMBO Mol Med 1 99-111 PubMed GONUTS page
  15. Lutz, AK et al. (2009) Loss of parkin or PINK1 function increases Drp1-dependent mitochondrial fragmentation. J. Biol. Chem. 284 22938-51 PubMed GONUTS page
  16. Yacobi-Sharon, K et al. (2013) Alternative germ cell death pathway in Drosophila involves HtrA2/Omi, lysosomes, and a caspase-9 counterpart. Dev. Cell 25 29-42 PubMed GONUTS page
  17. Venderova, K et al. (2009) Leucine-Rich Repeat Kinase 2 interacts with Parkin, DJ-1 and PINK-1 in a Drosophila melanogaster model of Parkinson's disease. Hum. Mol. Genet. 18 4390-404 PubMed GONUTS page
  18. Morais, VA et al. (2014) PINK1 loss-of-function mutations affect mitochondrial complex I activity via NdufA10 ubiquinone uncoupling. Science 344 203-7 PubMed GONUTS page
  19. Pogson, JH et al. (2014) The complex I subunit NDUFA10 selectively rescues Drosophila pink1 mutants through a mechanism independent of mitophagy. PLoS Genet. 10 e1004815 PubMed GONUTS page