FB2026_01 , released March 12, 2026
FB2026_01 , released March 12, 2026
Gene: Dmel\park
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General Information
Symbol
Dmel\park
Species
D. melanogaster
Name
parkin
Annotation Symbol
CG10523
Feature Type
FlyBase ID
FBgn0041100
Gene Model Status
Stock Availability
Enzyme Name (EC)
Gene Summary
parkin (park) encodes an E3 ubiquitin ligase with a key role in protein ubiquitination. It is involved in mitochondrion organization, oxidative stress and locomotion. [Date last reviewed: 2019-06-13] (FlyBase Gene Snapshot)
Also Known As

dParkin, D-parkin, dpk

Key Links
Genomic Location
Cytogenetic map
Sequence location
Recombination map
3-47
RefSeq locus
NT_037436 REGION:21194754..21196853
Sequence
Genomic Maps
Other Genome Views
The following external sites may use different assemblies or annotations than FlyBase.
Function
Gene Ontology (GO) Annotations (38 terms)
Molecular Function (5 terms)
Terms Based on Experimental Evidence (2 terms)
CV Term
Evidence
References
inferred from physical interaction with UniProtKB:Q9VR05
inferred from direct assay
inferred from mutant phenotype
inferred from direct assay
Terms Based on Predictions or Assertions (4 terms)
CV Term
Evidence
References
Biological Process (27 terms)
Terms Based on Experimental Evidence (26 terms)
CV Term
Evidence
References
inferred from mutant phenotype
inferred from mutant phenotype
inferred from genetic interaction with FLYBASE:Drp1; FB:FBgn0026479
inferred from genetic interaction with FLYBASE:Marf; FB:FBgn0029870
inferred from genetic interaction with FLYBASE:Opa1; FB:FBgn0261276
involved_in mitophagy
inferred from mutant phenotype
inferred from direct assay
inferred from genetic interaction with FLYBASE:bsk; FB:FBgn0000229
inferred from genetic interaction with FLYBASE:hep; FB:FBgn0010303
inferred from mutant phenotype
inferred from genetic interaction with FLYBASE:fzo; FB:FBgn0011596
inferred from mutant phenotype
involved_in oogenesis
inferred from mutant phenotype
inferred from mutant phenotype
inferred from genetic interaction with UniProtKB:Q0KHV6
inferred from mutant phenotype
inferred from mutant phenotype
inferred from direct assay
inferred from direct assay
inferred from mutant phenotype
inferred from direct assay
inferred from mutant phenotype
inferred from mutant phenotype
inferred from direct assay
inferred from mutant phenotype
inferred from mutant phenotype
inferred from mutant phenotype
inferred from mutant phenotype
inferred from mutant phenotype
involved_in spermatogenesis
inferred from mutant phenotype
involved_in type 2 mitophagy
inferred from mutant phenotype
inferred from mutant phenotype
inferred from mutant phenotype
Terms Based on Predictions or Assertions (4 terms)
CV Term
Evidence
References
involved_in mitophagy
inferred from biological aspect of ancestor with PANTHER:PTN000188399
inferred from electronic annotation with InterPro:IPR031127
Cellular Component (6 terms)
Terms Based on Experimental Evidence (2 terms)
CV Term
Evidence
References
located_in cytoplasm
inferred from direct assay
inferred from direct assay
colocalizes_with mitochondrion
inferred from direct assay
located_in mitochondrion
inferred from direct assay
inferred from direct assay
Terms Based on Predictions or Assertions (6 terms)
CV Term
Evidence
References
is_active_in cytoplasm
inferred from biological aspect of ancestor with PANTHER:PTN000188395
is_active_in cytosol
inferred from biological aspect of ancestor with PANTHER:PTN000188399
located_in cytosol
inferred from electronic annotation with InterPro:IPR003977
inferred from biological aspect of ancestor with PANTHER:PTN000188399
is_active_in Golgi apparatus
inferred from biological aspect of ancestor with PANTHER:PTN000188399
located_in mitochondrion
inferred from electronic annotation with InterPro:IPR003977
inferred from biological aspect of ancestor with PANTHER:PTN000188395
Protein Family (UniProt)
Belongs to the RBR family. Parkin subfamily. (Q7KTX7)
Catalytic Activity (EC/Rhea)
ubiquitin protein ligase activity
Summaries
Gene Snapshot
parkin (park) encodes an E3 ubiquitin ligase with a key role in protein ubiquitination. It is involved in mitochondrion organization, oxidative stress and locomotion. [Date last reviewed: 2019-06-13]
Gene Group (FlyBase)
RING-BETWEEN-RING UBIQUITIN LIGASES -
E3 (ubiquitin) ligases interact with ubiquitin-E2 (ubiquitin-conjugating) enzymes and the target protein, transferring the ubiquitin from the E2 to the substrate. RING-between-RING (RBR) E3 ligases are characterised by three closely spaced domains: RING1 (a classical RING finger domain), a In-Betweeen-RING (IBR) domain and a RING2 domain. The mechanism of action is described as RING/HECT-like, with the RING1 domain facilitating E2-transfer (E3 RING-like) to form a thioester intermediate with a cysteine in RING2 which then modifies the substrate protein (HECT-like). (Adapted from PMID:24469331).
Protein Function (UniProtKB)
E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes in the form of a thioester and then directly transfers the ubiquitin to targeted substrates, such as Paris, Marf, Opa1, Miro, pnut, Septin1, Tom20 and porin (PubMed:16002472, PubMed:17456438, PubMed:20194754, PubMed:23770917, PubMed:24192653, PubMed:24901221, PubMed:25474007, PubMed:27906179, PubMed:31714929, PubMed:32047033, PubMed:32138754). Mediates monoubiquitination as well as 'Lys-6', 'Lys-11', 'Lys-48'-linked and 'Lys-63'-linked polyubiquitination of substrates, depending on the context (PubMed:18957282, PubMed:23650379, PubMed:24901221, PubMed:25474007, PubMed:27906179, PubMed:31714929, PubMed:32047033). Protects against mitochondrial dysfunction during cellular stress, by acting downstream of Pink1, to coordinate mitochondrial quality control mechanisms that remove and replace dysfunctional mitochondrial components (PubMed:12642658, PubMed:15073152, PubMed:16672980, PubMed:16672981, PubMed:17123504, PubMed:18230723, PubMed:18443288, PubMed:18799731, PubMed:18957282, PubMed:20194754, PubMed:20496123, PubMed:23509287, PubMed:24192653, PubMed:24901221, PubMed:25474007, PubMed:27906179, PubMed:29497364, PubMed:32047033). Depending on the severity of mitochondrial damage and/or dysfunction, activity ranges from preventing apoptosis and stimulating mitochondrial biogenesis to regulating mitochondrial dynamics and eliminating severely damaged mitochondria via mitophagy (PubMed:12642658, PubMed:15073152, PubMed:16002472, PubMed:16672980, PubMed:16672981, PubMed:17123504, PubMed:18230723, PubMed:18443288, PubMed:18799731, PubMed:18957282, PubMed:20194754, PubMed:20496123, PubMed:23509287, PubMed:24192653, PubMed:24901221, PubMed:25474007, PubMed:27906179, PubMed:29497364, PubMed:32047033). Appears to be particularly important in maintaining the physiology and function of cells with high energy demands that are undergoing stress or altered metabolic environment, including spermatids, muscle cells and neurons such as the dopaminergic (DA) neurons (PubMed:12642658, PubMed:15073152, PubMed:16002472, PubMed:16672980, PubMed:17123504, PubMed:18799731, PubMed:20483372, PubMed:22396657, PubMed:24901221, PubMed:28435104, PubMed:29497364, PubMed:31714929). Activation and recruitment onto the outer membrane of damaged/dysfunctional mitochondria (OMM) requires Pink1-mediated phosphorylation of both park and ubiquitin (PubMed:18230723, PubMed:18799731, PubMed:18957282, PubMed:20194754, PubMed:22396657, PubMed:24901221, PubMed:25474007, PubMed:27906179). In depolarized mitochondria, mediates the decision between mitophagy or preventing apoptosis by inducing either the poly- or monoubiquitination of porin/VDAC; polyubiquitination of porin promotes mitophagy, while monoubiquitination of porin decreases mitochondrial calcium influx which ultimately inhibits apoptosis (PubMed:32047033). When cellular stress results in irreversible mitochondrial damage, promotes the autophagic degradation of dysfunctional depolarized mitochondria (mitophagy) by promoting the ubiquitination of mitochondrial proteins (PubMed:16672980, PubMed:16672981, PubMed:18957282, PubMed:20194754, PubMed:23509287, PubMed:24192653, PubMed:25474007, PubMed:29497364). Preferentially assembles 'Lys-6'-, 'Lys-11'- and 'Lys-63'-linked polyubiquitin chains following mitochondrial damage, leading to mitophagy (PubMed:23650379, PubMed:32047033). In developing tissues, inhibits JNK-mediated apoptosis by negatively regulating bsk transcription (PubMed:16002472, PubMed:20496123). The Pink1-park pathway also promotes fission and/or inhibits fusion of damaged mitochondria by mediating the ubiquitination and subsequent degradation of proteins involved in mitochondrial fusion/fission such as Marf, Opa1 and fzo (PubMed:17123504, PubMed:18230723, PubMed:18443288, PubMed:18799731, PubMed:20194754, PubMed:23650379, PubMed:24192653, PubMed:24901221, PubMed:29497364). This prevents the refusion of unhealthy mitochondria with the healthy mitochondrial network and/or initiates mitochondrial fragmentation facilitating their later engulfment by autophagosomes (PubMed:17123504, PubMed:18230723, PubMed:18443288, PubMed:18799731, PubMed:20194754, PubMed:23650379, PubMed:24192653, PubMed:24901221, PubMed:29497364). Regulates motility of damaged mitochondria by phosphorylating Miro which likely promotes its park-dependent degradation by the proteasome; in motor neurons, this inhibits mitochondrial intracellular anterograde transport along the axons which probably increases the chance of the mitochondria being eliminated in the soma (PubMed:22396657). The Pink1-park pathway is also involved in mitochondrial regeneration processes such as promoting mitochondrial biogenesis, activating localized mitochondrial repair, promoting selective turnover of mitochondrial proteins and initiating the mitochondrial import of endogenous proteins (PubMed:16672980, PubMed:20496123, PubMed:20869429, PubMed:23509287, PubMed:23650379, PubMed:24192653, PubMed:25565208, PubMed:29497364). Involved in mitochondrial biogenesis via the ubiquitination of transcriptional repressor Paris which leads to its subsequent proteasomal degradation and allows activation of the transcription factor srl (PubMed:23509287, PubMed:29497364, PubMed:32138754). Promotes localized mitochondrial repair by activating the translation of specific nuclear-encoded mitochondrial RNAs (nc-mtRNAs) on the mitochondrial surface, including several key electron transport chain component nc-mtRNAs (PubMed:23509287, PubMed:25565208).
(UniProt, Q7KTX7)
Summary (Interactive Fly)

ubiquitin protein ligase - degrades proteins with aberrant conformations - mutants exhibit muscle degeneration, male sterility, and defects in brain dopaminergic cells - PINK1 activates Parkin activity leading to ubiquitination of multiple proteins, which in turn promotes clearance of mitochondria by mitophagy

Gene Model and Products
Number of Transcripts
2
Number of Unique Polypeptides
1

Please see the JBrowse view of Dmel\park for information on other features

To submit a correction to a gene model please use the Contact FlyBase form

Protein Domains (via Pfam)
Isoform displayed:
Pfam protein domains
InterPro name
classification
start
end
Protein Domains (via SMART)
Isoform displayed:
SMART protein domains
InterPro name
classification
start
end
Structure
Protein 3D structure   (Predicted by AlphaFold)   (AlphaFold entry Q7KTX7)

If you don't see a structure in the viewer, refresh your browser.
Model Confidence:
  • Very high (pLDDT > 90)
  • Confident (90 > pLDDT > 70)
  • Low (70 > pLDDT > 50)
  • Very low (pLDDT < 50)

AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Some regions with low pLDDT may be unstructured in isolation.

Experimentally Determined Structures
Crossreferences
PDB - An information portal to biological macromolecular structures
Comments on Gene Model

Low-frequency RNA-Seq exon junction(s) not annotated.

Gene model reviewed during 5.45

Transcript Data
Annotated Transcripts
Name
FlyBase ID
RefSeq ID
Length (nt)
Assoc. CDS (aa)
FBtr0078318
1630
482
FBtr0078319
1609
482
Additional Transcript Data and Comments
Reported size (kB)
Comments
External Data
Crossreferences
Polypeptide Data
Annotated Polypeptides
Name
FlyBase ID
Predicted MW (kDa)
Length (aa)
Theoretical pI
UniProt
RefSeq ID
GenBank
FBpp0077974
54.1
482
6.08
FBpp0077975
54.1
482
6.08
Polypeptides with Identical Sequences

The group(s) of polypeptides indicated below share identical sequence to each other.

482 aa isoforms: park-PB, park-PC
Additional Polypeptide Data and Comments
Reported size (kDa)
Comments
External Data
Subunit Structure (UniProtKB)

Forms an E3 ubiquitin ligase complex with E2 ubiquitin-conjugating enzymes (PubMed:17456438). Interacts with Pink1 (PubMed:19048081). Interacts with Marf (PubMed:20194754, PubMed:24898855). Interacts with Paris (PubMed:32138754). Interacts with septins Septin1 and pnut (PubMed:17456438).

(UniProt, Q7KTX7)
Post Translational Modification

Auto-ubiquitinates in an E2-dependent manner leading to its own degradation.

Phosphorylated (PubMed:18957282, PubMed:24901221, PubMed:25474007, PubMed:27906179). Activation requires phosphorylation at Ser-94 by Pink1 and binding to Pink1-phosphorylated polyubiquitin chains (PubMed:18957282, PubMed:24901221, PubMed:25474007, PubMed:27906179). Phosphorylation at Thr-187 by Pink1 is also important for mitochondrial localization (PubMed:18957282).

(UniProt, Q7KTX7)
Domain

The RING-type 1 zinc finger domain is required for ubiquitination activity.

Members of the RBR family are atypical E3 ligases (PubMed:17456438, PubMed:23770917). They interact with E2 conjugating enzymes and function like HECT-type E3 enzymes: they bind E2s via the first RING domain, but require an obligate trans-thiolation step during the ubiquitin transfer, requiring a conserved cysteine residue in the second RING domain (PubMed:17456438, PubMed:23770917).

(UniProt, Q7KTX7)
Linkouts
Sequences Consistent with the Gene Model
Mapped Features

Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\park using the Feature Mapper tool.

External Data
Crossreferences
Eukaryotic Promoter Database - A collection of databases of experimentally validated promoters for selected model organisms.
Linkouts
Expression Data
Testis-specificity index

The testis specificity index was calculated from modENCODE tissue expression data by Vedelek et al., 2018 to indicate the degree of testis enrichment compared to other tissues. Scores range from -2.52 (underrepresented) to 5.2 (very high testis bias).

5.00

Transcript Expression
in situ
Stage
Tissue/Position (including subcellular localization)
Reference
organism | ubiquitous

Comment: maternally deposited

northern blot
Stage
Tissue/Position (including subcellular localization)
Reference
Additional Descriptive Data

park transcript is expressed in 0-2 hr embryos, and in third instar larvae through adults.

Marker for
 
Subcellular Localization
CV Term
Polypeptide Expression
immunolocalization
Stage
Tissue/Position (including subcellular localization)
Reference
western blot
Stage
Tissue/Position (including subcellular localization)
Reference
Additional Descriptive Data

In the germarium, park protein is specifially detected in germarium region 2b. In egg chambers park protein is detected up to stage 9-10 in the oocyte. It is preferentially localized at the posterior pole and is specifically expressed in the anterior margin of the oocyte. It colocalizes with eIF4E1 protein in the oocyte.

Marker for
 
Subcellular Localization
CV Term
Evidence
References
located_in cytoplasm
inferred from direct assay
inferred from direct assay
colocalizes_with mitochondrion
inferred from direct assay
located_in mitochondrion
inferred from direct assay
inferred from direct assay
Expression Deduced from Reporters
High-Throughput Expression Data
Associated Tools

JBrowse - Visual display of RNA-Seq signals

View Dmel\park in JBrowse
RNA-Seq by Region - Search RNA-Seq expression levels by exon or genomic region
Reference
See Gelbart and Emmert, 2013 for analysis details and data files for all genes.
Developmental Proteome: Life Cycle
Developmental Proteome: Embryogenesis
External Data and Images
Linkouts
BDGP expression data - Patterns of gene expression in Drosophila embryogenesis
DRscDB - A single-cell RNA-seq resource for data mining and data comparison across species
EMBL-EBI Single Cell Expression Atlas - Single cell expression across species
FlyAtlas - Adult expression by tissue, using Affymetrix Dros2 array
FlyAtlas2 - A Drosophila melanogaster expression atlas with RNA-Seq, miRNA-Seq and sex-specific data
Fly-FISH - A database of Drosophila embryo and larvae mRNA localization patterns
Flygut - An atlas of the Drosophila adult midgut
Images
Alleles, Insertions, Transgenic Constructs, and Aberrations
Classical and Insertion Alleles ( 22 )
For All Classical and Insertion Alleles Show
 
Other relevant insertions
Transgenic Constructs ( 56 )
For All Alleles Carried on Transgenic Constructs Show
Transgenic constructs containing/affecting coding region of park
Transgenic constructs containing regulatory region of park
Aberrations (Deficiencies and Duplications) ( 1 )
Inferred from experimentation ( 1 )
Inferred from location ( 5 )
Variants
Variant Molecular Consequences
Alleles Representing Disease-Implicated Variants
Phenotypes
For more details about a specific phenotype click on the relevant allele symbol.
Lethality
Allele
Sterility
Allele
Other Phenotypes
Allele
Phenotype manifest in
Allele
indirect flight muscle & mitochondrion
indirect flight muscle & nuclear membrane
mitochondrion & dorso-lateral dopaminergic neuron, with Scer\GAL4ple.PF
mitochondrion & skeletal muscle of thorax
myofibril & skeletal muscle of thorax
Orthologs
Human Orthologs (via DIOPT v9.1)
Species\Gene Symbol
Score
Best Score
Best Reverse Score
Alignment
Complementation?
Transgene?
Homo sapiens (Human) (13)
14 of 14
Yes
Yes
 
12  
2 of 14
No
Yes
1 of 14
No
No
1 of 14
No
No
 
4  
1 of 14
No
No
1 of 14
No
No
1 of 14
No
Yes
1 of 14
No
No
1 of 14
No
No
1 of 14
No
No
1 of 14
No
No
1 of 14
No
No
1 of 14
No
No
Model Organism Orthologs (via DIOPT v9.1)
Species\Gene Symbol
Score
Best Score
Best Reverse Score
Alignment
Complementation?
Transgene?
Rattus norvegicus (Norway rat) (11)
12 of 14
Yes
Yes
2 of 14
No
Yes
1 of 14
No
No
1 of 14
No
No
1 of 14
No
No
1 of 14
No
No
1 of 14
No
Yes
1 of 14
No
No
1 of 14
No
No
1 of 14
No
No
1 of 14
No
No
Mus musculus (laboratory mouse) (11)
14 of 14
Yes
Yes
1 of 14
No
No
1 of 14
No
No
1 of 14
No
No
1 of 14
No
No
1 of 14
No
Yes
1 of 14
No
No
1 of 14
No
No
1 of 14
No
No
1 of 14
No
No
1 of 14
No
No
Xenopus tropicalis (Western clawed frog) (7)
1 of 13
Yes
No
1 of 13
Yes
Yes
1 of 13
Yes
Yes
1 of 13
Yes
Yes
1 of 13
Yes
No
1 of 13
Yes
No
1 of 13
Yes
No
Danio rerio (Zebrafish) (17)
13 of 14
Yes
Yes
2 of 14
No
Yes
1 of 14
No
No
1 of 14
No
No
1 of 14
No
No
1 of 14
No
No
1 of 14
No
Yes
1 of 14
No
Yes
1 of 14
No
Yes
1 of 14
No
Yes
1 of 14
No
No
1 of 14
No
No
1 of 14
No
No
1 of 14
No
No
1 of 14
No
No
1 of 14
No
No
Caenorhabditis elegans (Nematode, roundworm) (12)
12 of 14
Yes
Yes
2 of 14
No
Yes
2 of 14
No
Yes
1 of 14
No
No
1 of 14
No
No
1 of 14
No
No
1 of 14
No
No
1 of 14
No
No
1 of 14
No
No
1 of 14
No
Yes
1 of 14
No
Yes
1 of 14
No
No
Anopheles gambiae (African malaria mosquito) (6)
12 of 12
Yes
Yes
Arabidopsis thaliana (thale-cress) (44)
2 of 13
Yes
No
2 of 13
Yes
No
2 of 13
Yes
No
2 of 13
Yes
No
2 of 13
Yes
No
2 of 13
Yes
No
2 of 13
Yes
No
2 of 13
Yes
No
2 of 13
Yes
No
2 of 13
Yes
No
2 of 13
Yes
No
2 of 13
Yes
Yes
2 of 13
Yes
Yes
2 of 13
Yes
Yes
2 of 13
Yes
Yes
2 of 13
Yes
Yes
2 of 13
Yes
Yes
2 of 13
Yes
Yes
2 of 13
Yes
Yes
2 of 13
Yes
No
2 of 13
Yes
Yes
2 of 13
Yes
Yes
2 of 13
Yes
Yes
2 of 13
Yes
Yes
2 of 13
Yes
No
2 of 13
Yes
Yes
2 of 13
Yes
Yes
2 of 13
Yes
Yes
2 of 13
Yes
Yes
1 of 13
No
No
1 of 13
No
No
1 of 13
No
No
1 of 13
No
No
1 of 13
No
No
1 of 13
No
Yes
1 of 13
No
No
1 of 13
No
No
1 of 13
No
No
1 of 13
No
No
1 of 13
No
No
1 of 13
No
No
1 of 13
No
No
1 of 13
No
No
1 of 13
No
No
Saccharomyces cerevisiae (Brewer's yeast) (1)
1 of 13
Yes
No
Schizosaccharomyces pombe (Fission yeast) (2)
1 of 12
Yes
Yes
1 of 12
Yes
No
Escherichia coli (enterobacterium) (0)
Other Organism Orthologs (via OrthoDB)
Data provided directly from OrthoDB:park. Refer to their site for version information.
Paralogs
Paralogs (via DIOPT v9.1)
Drosophila melanogaster (Fruit fly) (5)
3 of 13
3 of 13
3 of 13
2 of 13
1 of 13
Human Disease Associations
FlyBase Human Disease Model Reports
Disease Ontology (DO) Annotations
Models Based on Experimental Evidence ( 35 )
Allele
Disease
Evidence
References
Potential Models Based on Orthology ( 3 )
Human Ortholog
Disease
Evidence
References
Modifiers Based on Experimental Evidence ( 23 )
Allele
Disease
Interaction
References
is ameliorated by CisdGD15791
is ameliorated by CisdKO
is ameliorated by ItprGD1676
is ameliorated by AMPKαTD.UAS
is ameliorated by UchGD11265
is ameliorated by UchKK101723
is ameliorated by UchKO
is ameliorated by UchV96M
is ameliorated by UchC93S
is ameliorated by UchE8A
is ameliorated by GstO1UAS.cKa
is ameliorated by AMPKαTD.UAS
is ameliorated by Ucp4AUAS.cWa
is ameliorated by srlUAS.cTa
is ameliorated by CatUAS.cAa
is ameliorated by simaHMS00833
is exacerbated by ShmtGD8851
is ameliorated by Lrrke03680
is ameliorated by foxoUAS.cFa
is ameliorated by ThorUAS.cMa
is ameliorated by Opa1s3475
is ameliorated by Opa1f02779
is ameliorated by Parp1CH1
is ameliorated by MTF-1UAS.cSa
is exacerbated by MTF-1140-1R
is ameliorated by Trap1UAS.cCa
is NOT ameliorated by TER94UAS.cRa
is NOT ameliorated by Hsap\TRAP1UAS.cBa
is NOT ameliorated by ND-42UAS.cBa
is NOT ameliorated by ND-42UAS.Tag:HA
is NOT ameliorated by sicilyUAS.cZa
is NOT ameliorated by cluUASp.cSa
is NOT ameliorated by Hsap\CLUHUASp.cSa
is ameliorated by PEKGD5584
is exacerbated by Mul1A6
is ameliorated by TER94UAS.cCa
is ameliorated by prtpΔ1
is ameliorated by Usp8GD1285
is ameliorated by Usp8KO
is ameliorated by pntΔ88
is exacerbated by COX5Atend
is exacerbated by SdhA1110
is ameliorated by SdhA5
is exacerbated by blw1
is ameliorated by CisdKO.B
Disease Associations of Human Orthologs (via DIOPT v9.1 and OMIM)
Note that ortholog calls supported by only 1 or 2 algorithms (DIOPT score < 3) are not shown.
Functional Complementation Data
Functional complementation data is computed by FlyBase using a combination of the orthology data obtained from DIOPT and OrthoDB and the allele-level genetic interaction data curated from the literature.
Dmel gene
Ortholog showing functional complementation
Supporting References
Interactions
Summary of Physical Interactions
Interaction Browsers

Please see the Physical Interaction reports below for full details
protein-protein
Physical Interaction
Assay
References
Summary of Genetic Interactions
Interaction Browsers

Please look at the allele data for full details of the genetic interactions
Starting gene(s)
Interaction type
Interacting gene(s)
Reference
Starting gene(s)
Interaction type
Interacting gene(s)
Reference
External Data
Subunit Structure (UniProtKB)
Forms an E3 ubiquitin ligase complex with E2 ubiquitin-conjugating enzymes (PubMed:17456438). Interacts with Pink1 (PubMed:19048081). Interacts with Marf (PubMed:20194754, PubMed:24898855). Interacts with Paris (PubMed:32138754). Interacts with septins Septin1 and pnut (PubMed:17456438).
(UniProt, Q7KTX7 )
Linkouts
BioGRID - A database of protein and genetic interactions.
DroID - A comprehensive database of gene and protein interactions.
MIST (genetic) - An integrated Molecular Interaction Database
MIST (protein-protein) - An integrated Molecular Interaction Database
Pathways
Signaling Pathways (FlyBase)
Metabolic Pathways
FlyBase
External Links
External Data
Linkouts
KEGG Pathways - A collection of manually drawn pathway maps representing knowledge of molecular interaction, reaction and relation networks.
Reactome - An open-source, open access, manually curated and peer-reviewed pathway database.
Class of Gene
Genomic Location and Detailed Mapping Data
Chromosome (arm)
3L
Recombination map
3-47
Cytogenetic map
Sequence location
FlyBase Computed Cytological Location
Cytogenetic map
Evidence for location
78C2-78C2
Limits computationally determined from genome sequence between P{EP}chbEP3403 and P{PZ}ppl00217
Experimentally Determined Cytological Location
Cytogenetic map
Notes
References
Experimentally Determined Recombination Data
Left of (cM)
Right of (cM)
Notes
Stocks and Reagents
Stocks (21)
Genomic Clones (21)
cDNA Clones (24)
 

Please Note This section lists cDNAs and ESTs that fall within the genomic extent of the gene model, which may include cDNAs and ESTs of genes within introns, or of overlapping genes. Please see JBrowse for alignment of the cDNAs and ESTs to the gene model.

cDNA clones, fully sequenced
BDGP DGC clones
Other clones
Drosophila Genomics Resource Center cDNA clones

For each fully sequenced cDNA the DGRC maintains various forms of the cDNA (e.g tagged or untagged) in several different host vectors for subsequent cloning and expression in Drosophila and Drosophila cell lines.

cDNA Clones, End Sequenced (ESTs)
RNAi and Array Information
Linkouts
DRSC - Results frm RNAi screens
Antibody Information
Laboratory Generated Antibodies
Commercially Available Antibodies
 
Cell Line Information
Publicly Available Cell Lines
 
    Other Stable Cell Lines
     
      Other Comments

      park is required for the regulation of tubulin levels.

      The condition of park mutants raised on zinc-supplemented food is greatly improved.

      Flies mutant for park show significantly reduced lifespan but no difference in dopamine neuron numbers when raised on food supplemented with environmental pesticides or mitochondrial toxins.

      The increased lifespan of park mutants is due to metal chelation.

      park mutants display increased vulnerability to environmental pesticides and mitochondrial toxins associated with Parkinson's disease.

      park gene function is necessary for mitochondrial morphogenesis during earlier and later phases of spermiogenesis.

      In park mutants, the investment cones are scattered along the post-elongated spermatid bundles and fail to act properly in the process of sperm individualization.

      The level of dopamine is significantly reduced in park mutants compared to controls.

      Inhibition of park leads to a reduction of phospho-Akt levels.

      park appears to have a role in mitochondrial function.

      Relationship to Other Genes
      Source for database merge of

      Source for merge of: parkin CG10523

      Additional comments

      Source for merge of parkin CG10523 was sequence comparison ( date:020502 ).

      Nomenclature History
      Source for database identify of
      Nomenclature comments
      Etymology
      Synonyms and Secondary IDs (24)
      Reported As
      Symbol Synonym
      PARKIN
      park
      (Hunter-Manseau et al., 2025, Juba et al., 2025, Hunter-Manseau et al., 2024, Martinez et al., 2024, Rai et al., 2024, Zhang et al., 2024, Das et al., 2023, Ham et al., 2023, Hawrysh et al., 2023, Mauri et al., 2023, Moehlman et al., 2023, Sanchez-Martinez et al., 2023, Ecovoiu et al., 2022, Mannett et al., 2022, Miozzo et al., 2022, O'Hanlon et al., 2022, Paradis et al., 2022, Rai and Roy, 2022, Xue et al., 2022, Yang et al., 2022, Ham et al., 2021, Han et al., 2021, Ibaraki et al., 2021, Joy et al., 2021, Parker-Character et al., 2021, Sanz et al., 2021, Shen et al., 2021, Funk et al., 2020, Lee et al., 2020, Liu et al., 2020, Maddison et al., 2020, Pradhan et al., 2020, Wan et al., 2020, Aggarwal et al., 2019, Aryal and Lee, 2019, Bajracharya et al., 2019, Bajracharya et al., 2019, Bouska et al., 2019, Doktór et al., 2019, Doktór et al., 2019, Gumeni et al., 2019, Meltzer et al., 2019, Qiu et al., 2019, Vincow et al., 2019, von Stockum et al., 2019, Wu et al., 2019, Xu et al., 2019, Zhou et al., 2019, Bajracharya and Ballard, 2018, Baranski et al., 2018, Chakraborty et al., 2018, Kucherenko and Shcherbata, 2018, Lee et al., 2018, Liu et al., 2018, Steyaert et al., 2018, Tan et al., 2018, Thomas et al., 2018, Celardo et al., 2017, Galluzzi et al., 2017, Ketosugbo et al., 2017, Martinez et al., 2017, Ng et al., 2017, Transgenic RNAi Project members, 2017-, Zanon et al., 2017, Bajracharya and Ballard, 2016, Celardo et al., 2016, Dwivedi and Lakhotia, 2016, Sung et al., 2016, Zhang et al., 2016, Cagin et al., 2015, Choo et al., 2015, Gao et al., 2015, Khalil et al., 2015, Liu et al., 2015, Malik et al., 2015, Srivastav et al., 2015, Srivastav et al., 2015, Bhandari et al., 2014, Bingol et al., 2014, Klein et al., 2014, Ma et al., 2014, Pogson et al., 2014, Politi et al., 2014, Shiba-Fukushima et al., 2014, Wu et al., 2014, Burchell et al., 2013, Chambers et al., 2013, Costa et al., 2013, de Castro et al., 2013, Goh et al., 2013, Vos et al., 2013, Wu et al., 2013, Yacobi-Sharon et al., 2013, Zhang et al., 2013, Humphrey et al., 2012, Japanese National Institute of Genetics, 2012.5.21, Kim et al., 2012, Munoz-Soriano et al., 2012, Pezzulo et al., 2012, Pimenta de Castro et al., 2012, Vincent et al., 2012, Vos et al., 2012, Fernandes and Rao, 2011, Muñoz-Soriano and Paricio, 2011, Saini et al., 2011, Hao et al., 2010, Lorbeck et al., 2010, Saini and Schaffner, 2010, Saini et al., 2010, Schnorrer et al., 2010, Trinh et al., 2010, Ziviani et al., 2010, Cox and Spradling, 2009, Park et al., 2009, Tain et al., 2009, Tain et al., 2009, Kim et al., 2008, Poole et al., 2008, Riparbelli and Callaini, 2007, Wang et al., 2007, Kuo et al., 2006, Park et al., 2006, Cha et al., 2005)
      Name Synonyms
      parkin
      (Couto-Lima et al., 2025, Huang et al., 2023, Li et al., 2023, Adedara et al., 2022, Himalian et al., 2022, Leduc-Gaudet et al., 2022, Nayak and Mishra, 2022, Rai and Kumar Roy, 2022, Lin et al., 2021, Naz and Siddique, 2021, Ortega-Arellano et al., 2021, Pant et al., 2021, Bai et al., 2020, Cha et al., 2020, Denton et al., 2020, Ding et al., 2020, Kim et al., 2019, Kim et al., 2019, Ortega-Arellano et al., 2019, Si et al., 2019, Yadav and Srikrishna, 2019, Biosa et al., 2018, Shao et al., 2018, Valadas et al., 2018, Basil et al., 2017, M'Angale and Staveley, 2017, Meng et al., 2017, Wangler et al., 2017, Zhang et al., 2017, Brooks et al., 2016, Kandul et al., 2016, Kawasaki et al., 2016, Lehmann et al., 2016, Liu et al., 2016, Spinazzi and De Strooper, 2016, Sung et al., 2016, Wang et al., 2016, Wang et al., 2016, Zhang et al., 2016, Gehrke et al., 2015, Johnson et al., 2015, Khalil et al., 2015, Liu et al., 2015, Malik et al., 2015, Sen et al., 2015, van der Merwe et al., 2015, Vanhauwaert and Verstreken, 2015, Wang et al., 2015, Wangler et al., 2015, West et al., 2015, Zhu et al., 2015, Cornelissen et al., 2014, Hwang et al., 2014, Li et al., 2014, Ma et al., 2014, Tufi et al., 2014, Yun et al., 2014, Bonilla-Ramirez et al., 2013, Burchell et al., 2013, Chambers et al., 2013, Debattisti and Scorrano, 2013, Esposito et al., 2013, Goh et al., 2013, Kim et al., 2013, Manzanillo et al., 2013, Rana et al., 2013, Spratt et al., 2013, Vincow et al., 2013, Yacobi-Sharon et al., 2013, Elliott and Sparrow, 2012, Guo, 2012, Humphrey et al., 2012, Kim et al., 2012, Koh et al., 2012, Ng et al., 2012, Pimenta de Castro et al., 2012, Vilain et al., 2012, Vincent et al., 2012, Lee et al., 2011, Ottone et al., 2011, Saini et al., 2011, Hao et al., 2010, Hwang et al., 2010, Imai et al., 2010, Poole et al., 2010, Saini et al., 2010, Schnorrer et al., 2010, Ziviani et al., 2010, Lutz et al., 2009, Tain et al., 2009, Xun et al., 2009, Cox et al., 2008, Deng et al., 2008, Dodson et al., 2008, Kim et al., 2008, Whitworth et al., 2008, Whitworth et al., 2008, Guo et al., 2007, Korey, 2007, Muñoz-Soriano and Paricio, 2007, Riparbelli and Callaini, 2007, Wang et al., 2007, Clark et al., 2006, Kuo et al., 2006, Lin and Beal, 2006, Maricich and Zoghbi, 2006, Pallanck and Greenamyre, 2006, Greene et al., 2005, Greene et al., 2003, Fortini et al., 2000, Pallanck, 2000.3.3)
      Secondary FlyBase IDs
      • FBgn0037054
      Datasets (0)
      Study focus (0)
      Experimental Role
      Project
      Project Type
      Title
      Study result (0)
      Result
      Result Type
      Title
      External Crossreferences and Linkouts ( 69 )
      Sequence Crossreferences
      NCBI Gene - Gene integrates information from a wide range of species. A record may include nomenclature, Reference Sequences (RefSeqs), maps, pathways, variations, phenotypes, and links to genome-, phenotype-, and locus-specific resources worldwide.
      GenBank Nucleotide - A collection of sequences from several sources, including GenBank, RefSeq, TPA, and PDB.
      GenBank Protein - A collection of sequences from several sources, including translations from annotated coding regions in GenBank, RefSeq and TPA, as well as records from SwissProt, PIR, PRF, and PDB.
      RefSeq - A comprehensive, integrated, non-redundant, well-annotated set of reference sequences including genomic, transcript, and protein.
      UniProt/GCRP - The gene-centric reference proteome (GCRP) provides a 1:1 mapping between genes and UniProt accessions in which a single 'canonical' isoform represents the product(s) of each protein-coding gene.
      UniProt/Swiss-Prot - Manually annotated and reviewed records of protein sequence and functional information
      Other crossreferences
      AlphaFold DB - AlphaFold provides open access to protein structure predictions for the human proteome and other key proteins of interest, to accelerate scientific research.
      BDGP expression data - Patterns of gene expression in Drosophila embryogenesis
      DRscDB - A single-cell RNA-seq resource for data mining and data comparison across species
      EMBL-EBI Single Cell Expression Atlas - Single cell expression across species
      FlyAtlas2 - A Drosophila melanogaster expression atlas with RNA-Seq, miRNA-Seq and sex-specific data
      FlyMine - An integrated database for Drosophila genomics
      KEGG Genes - Molecular building blocks of life in the genomic space.
      MARRVEL_MODEL - MARRVEL (model organism gene)
      PDB - An information portal to biological macromolecular structures
      Linkouts
      BioGRID - A database of protein and genetic interactions.
      Drosophila Genomics Resource Center - Drosophila Genomics Resource Center (DGRC) cDNA clones
      DroID - A comprehensive database of gene and protein interactions.
      DRSC - Results frm RNAi screens
      Eukaryotic Promoter Database - A collection of databases of experimentally validated promoters for selected model organisms.
      FlyAtlas - Adult expression by tissue, using Affymetrix Dros2 array
      FlyCyc Genes - Genes from a BioCyc PGDB for Dmel
      Fly-FISH - A database of Drosophila embryo and larvae mRNA localization patterns
      Flygut - An atlas of the Drosophila adult midgut
      FlyMet - A comprehensive tissue-specific metabolomics resource for Drosophila.
      iBeetle-Base - RNAi phenotypes in the red flour beetle (Tribolium castaneum)
      Interactive Fly - A cyberspace guide to Drosophila development and metazoan evolution
      KEGG Pathways - A collection of manually drawn pathway maps representing knowledge of molecular interaction, reaction and relation networks.
      MIST (genetic) - An integrated Molecular Interaction Database
      MIST (protein-protein) - An integrated Molecular Interaction Database
      Reactome - An open-source, open access, manually curated and peer-reviewed pathway database.
      References (451)