PRKN
entrez
5071
canonical
uniprot
O60260
canonical
ensembl
ENSG00000185345
resolver
ensp
ENSP00000355862
resolver
ensp
ENSP00000355863
resolver
ensp
ENSP00000355865
resolver
genesymbol
PARK2
resolver
genesymbol
PRKN
resolver
genesymbol_syn
PARK2
resolver
hgnc
HGNC:8607
resolver
uniprot
A3FG77
resolver
uniprot
A8K975
resolver
uniprot
D3JZW7
resolver
uniprot
D3K2X0
resolver
uniprot
Q5TFV8
resolver
uniprot
Q5VVX4
resolver
uniprot
Q6Q2I6
resolver
uniprot
Q8NI41
resolver
uniprot
Q8NI43
resolver
uniprot
Q8NI44
resolver
uniprot
Q8WW07
resolver
uniprot
X5DR79
resolver
uniprot_entry
PRKN_HUMAN
resolver
uniprot_entry
X5DR79_HUMAN
resolver
uniprot_sec
A3FG77
resolver
uniprot_sec
A8K975
resolver
uniprot_sec
D3JZW7
resolver
uniprot_sec
D3K2X0
resolver
uniprot_sec
Q5TFV8
resolver
uniprot_sec
Q5VVX4
resolver
uniprot_sec
Q6Q2I6
resolver
uniprot_sec
Q8NI41
resolver
uniprot_sec
Q8NI43
resolver
uniprot_sec
Q8NI44
resolver
uniprot_sec
Q8WW07
resolver
activity_regulation
ACTIVITY REGULATION: In the autoinhibited state the side chain of Phe-463 inserts into a hydrophobic groove in RING-0, occluding the ubiquitin acceptor site Cys-431, whereas the REP repressor element binds RING-1 and blocks its E2-binding site (PubMed:23727886, PubMed:23770887). Activation of PRKN requires 2 steps: (1) phosphorylation at Ser-65 by PINK1 and (2) binding to phosphorylated ubiquitin, leading to unlock repression of the catalytic Cys-431 by the RING-0 region via an allosteric mechanism and converting PRKN to its fully-active form (PubMed:24660806, PubMed:24784582, PubMed:25474007, PubMed:25527291). According to another report, phosphorylation at Ser-65 by PINK1 is not essential for activation and only binding to phosphorylated ubiquitin is essential to unlock repression (PubMed:24751536). In addition, ISG15 conjugation positively regulates its ubiquitin E3 ligase activity by suppressing the intramolecular interaction that maintains its autoinhibited conformation (PubMed:27534820). {ECO:0000269|PubMed:23727886, ECO:0000269|PubMed:23770887, ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25474007, ECO:0000269|PubMed:25527291, ECO:0000269|PubMed:27534820}.
uniprot
proteins
amino_acid_sequence
MIVFVRFNSSHGFPVEVDSDTSIFQLKEVVAKRQGVPADQLRVIFAGKELRNDWTVQNCDLDQQSIVHIVQRPWRKGQEMNATGGDDPRNAAGGCEREPQSLTRVDLSSSVLPGDSVGLAVILHTDSRKDSPPAGSPAGRSIYNSFYVYCKGPCQRVQPGKLRVQCSTCRQATLTLTQGPSCWDDVLIPNRMSGECQSPHCPGTSAEFFFKCGAHPTSDKETSVALHLIATNSRNITCITCTDVRSPVLVFQCNSRHVICLDCFHLYCVTRLNDRQFVHDPQLGYSLPCVAGCPNSLIKELHHFRILGEEQYNRYQQYGAEECVLQMGGVLCPRPGCGAGLLPEPDQRKVTCEGGNGLGCGFAFCRECKEAYHEGECSAVFEASGTTTQAYRVDERAAEQARWEAASKETIKKTTKPCPRCHVPVEKNGGCMHMKCPQPQCRLEWCWNCGCEWNRVCMGDHWFDV
uniprot
proteins
disease_involvement
DISEASE: Parkinson disease (PARK) [MIM:168600]: A complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability. Additional features are characteristic postural abnormalities, dysautonomia, dystonic cramps, and dementia. The pathology of Parkinson disease involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain. The disease is progressive and usually manifests after the age of 50 years, although early-onset cases (before 50 years) are known. The majority of the cases are sporadic suggesting a multifactorial etiology based on environmental and genetic factors. However, some patients present with a positive family history for the disease. Familial forms of the disease usually begin at earlier ages and are associated with atypical clinical features. {ECO:0000269|PubMed:12629236, ECO:0000269|PubMed:12730996, ECO:0000269|PubMed:19966284, ECO:0000269|PubMed:29311685}. Note=Disease susceptibility may be associated with variants affecting the gene represented in this entry. Heterozygous mutations act as susceptibility alleles for late-onset Parkinson disease (PubMed:12629236, PubMed:12730996).; DISEASE: Parkinson disease 2 (PARK2) [MIM:600116]: An autosomal recessive form of Parkinson disease, a complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability. PARK2 differs from classic forms of Parkinson disease by early DOPA-induced dyskinesia, diurnal fluctuation of the symptoms, sleep benefit, dystonia and hyper-reflexia. Dementia is absent. Pathologically, patients show loss of dopaminergic neurons in the substantia nigra, similar to that seen in classic Parkinson disease; however, Lewy bodies (intraneuronal accumulations of aggregated proteins) are absent. Disease onset is usually before age 40 years. {ECO:0000269|PubMed:10072423, ECO:0000269|PubMed:10824074, ECO:0000269|PubMed:10888878, ECO:0000269|PubMed:10939576, ECO:0000269|PubMed:11163284, ECO:0000269|PubMed:11179010, ECO:0000269|PubMed:11431533, ECO:0000269|PubMed:11487568, ECO:0000269|PubMed:11590439, ECO:0000269|PubMed:11971093, ECO:0000269|PubMed:12056932, ECO:0000269|PubMed:12112109, ECO:0000269|PubMed:12114481, ECO:0000269|PubMed:12116199, ECO:0000269|PubMed:12362318, ECO:0000269|PubMed:12397156, ECO:0000269|PubMed:12629236, ECO:0000269|PubMed:12730996, ECO:0000269|PubMed:12925569, ECO:0000269|PubMed:15584030, ECO:0000269|PubMed:17360614, ECO:0000269|PubMed:19229105, ECO:0000269|PubMed:19801972, ECO:0000269|PubMed:20404107, ECO:0000269|PubMed:20889486, ECO:0000269|PubMed:20889974, ECO:0000269|PubMed:21376232, ECO:0000269|PubMed:22396657, ECO:0000269|PubMed:22956510, ECO:0000269|PubMed:23770917, ECO:0000269|PubMed:32047033, ECO:0000269|PubMed:9560156, ECO:0000269|PubMed:9731209}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Note=Defects in PRKN may be involved in the development and/or progression of ovarian cancer.
uniprot
proteins
ec_number
2.3.2.31
uniprot
proteins
function
FUNCTION: Functions within a multiprotein E3 ubiquitin ligase complex, catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins (PubMed:10888878, PubMed:10973942, PubMed:11431533, PubMed:12150907, PubMed:12628165, PubMed:15105460, PubMed:16135753, PubMed:21376232, PubMed:21532592, PubMed:22396657, PubMed:23620051, PubMed:23754282, PubMed:24660806, PubMed:24751536, PubMed:29311685, PubMed:32047033). Substrates include SYT11 and VDAC1 (PubMed:29311685, PubMed:32047033). Other substrates are BCL2, CCNE1, GPR37, RHOT1/MIRO1, MFN1, MFN2, STUB1, SNCAIP, SEPTIN5, TOMM20, USP30, ZNF746, MIRO1 and AIMP2 (PubMed:10888878, PubMed:10973942, PubMed:11431533, PubMed:12150907, PubMed:12628165, PubMed:15105460, PubMed:16135753, PubMed:21376232, PubMed:21532592, PubMed:22396657, PubMed:23620051, PubMed:23754282, PubMed:24660806, PubMed:24751536). Mediates monoubiquitination as well as 'Lys-6', 'Lys-11', 'Lys-48'-linked and 'Lys-63'-linked polyubiquitination of substrates depending on the context (PubMed:19229105, PubMed:20889974, PubMed:25474007, PubMed:25621951, PubMed:32047033). Participates in the removal and/or detoxification of abnormally folded or damaged protein by mediating 'Lys-63'-linked polyubiquitination of misfolded proteins such as PARK7: 'Lys-63'-linked polyubiquitinated misfolded proteins are then recognized by HDAC6, leading to their recruitment to aggresomes, followed by degradation (PubMed:17846173, PubMed:19229105). Mediates 'Lys-63'-linked polyubiquitination of a 22 kDa O-linked glycosylated isoform of SNCAIP, possibly playing a role in Lewy-body formation (PubMed:11431533, PubMed:11590439, PubMed:15105460, PubMed:15728840, PubMed:19229105). Mediates monoubiquitination of BCL2, thereby acting as a positive regulator of autophagy (PubMed:20889974). 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:11439185, PubMed:18957282, PubMed:19029340, PubMed:19966284, PubMed:21376232, PubMed:22082830, PubMed:22396657, PubMed:23620051, PubMed:23933751, PubMed:24660806, PubMed:24784582, PubMed:24896179, PubMed:25474007, PubMed:25527291, 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:11439185, PubMed:19029340, PubMed:19801972, PubMed:19966284, PubMed:21376232, PubMed:22082830, PubMed:22396657, PubMed:23620051, PubMed:23685073, PubMed:23933751, PubMed:24896179, PubMed:25527291, PubMed:32047033, PubMed:33499712). Activation and recruitment onto the outer membrane of damaged/dysfunctional mitochondria (OMM) requires PINK1-mediated phosphorylation of both PRKN and ubiquitin (PubMed:24660806, PubMed:24784582, PubMed:25474007, PubMed:25527291). After mitochondrial damage, functions with PINK1 to mediate the decision between mitophagy or preventing apoptosis by inducing either the poly- or monoubiquitination of VDAC1, respectively; polyubiquitination of VDAC1 promotes mitophagy, while monoubiquitination of VDAC1 decreases mitochondrial calcium influx which ultimately inhibits apoptosis (PubMed:27534820, 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 such as TOMM20, RHOT1/MIRO1, MFN1 and USP30 (PubMed:19029340, PubMed:19966284, PubMed:21753002, PubMed:22396657, PubMed:23620051, PubMed:23685073, PubMed:23933751, PubMed:24896179, PubMed:25527291). Preferentially assembles 'Lys-6'-, 'Lys-11'- and 'Lys-63'-linked polyubiquitin chains, leading to mitophagy (PubMed:25621951, PubMed:32047033). The PINK1-PRKN pathway also promotes fission of damaged mitochondria by PINK1-mediated phosphorylation which promotes the PRKN-dependent degradation of mitochondrial proteins involved in fission such as MFN2 (PubMed:23620051). This prevents the refusion of unhealthy mitochondria with the mitochondrial network or initiates mitochondrial fragmentation facilitating their later engulfment by autophagosomes (PubMed:23620051). Regulates motility of damaged mitochondria via the ubiquitination and subsequent degradation of MIRO1 and MIRO2; in motor neurons, this likely inhibits mitochondrial intracellular anterograde transport along the axons which probably increases the chance of the mitochondria undergoing mitophagy in the soma (PubMed:22396657). Involved in mitochondrial biogenesis via the 'Lys-48'-linked polyubiquitination of transcriptional repressor ZNF746/PARIS which leads to its subsequent proteasomal degradation and allows activation of the transcription factor PPARGC1A (PubMed:21376232). Limits the production of reactive oxygen species (ROS) (PubMed:18541373). Regulates cyclin-E during neuronal apoptosis (PubMed:12628165). In collaboration with CHPF isoform 2, may enhance cell viability and protect cells from oxidative stress (PubMed:22082830). Independently of its ubiquitin ligase activity, protects from apoptosis by the transcriptional repression of p53/TP53 (PubMed:19801972). May protect neurons against alpha synuclein toxicity, proteasomal dysfunction, GPR37 accumulation, and kainate-induced excitotoxicity (PubMed:11439185). May play a role in controlling neurotransmitter trafficking at the presynaptic terminal and in calcium-dependent exocytosis. May represent a tumor suppressor gene (PubMed:12719539). {ECO:0000269|PubMed:10888878, ECO:0000269|PubMed:10973942, ECO:0000269|PubMed:11431533, ECO:0000269|PubMed:11439185, ECO:0000269|PubMed:11590439, ECO:0000269|PubMed:12150907, ECO:0000269|PubMed:12628165, ECO:0000269|PubMed:12719539, ECO:0000269|PubMed:15105460, ECO:0000269|PubMed:15728840, ECO:0000269|PubMed:16135753, ECO:0000269|PubMed:17846173, ECO:0000269|PubMed:18541373, ECO:0000269|PubMed:18957282, ECO:0000269|PubMed:19029340, ECO:0000269|PubMed:19229105, ECO:0000269|PubMed:19801972, ECO:0000269|PubMed:19966284, ECO:0000269|PubMed:20889974, ECO:0000269|PubMed:21376232, ECO:0000269|PubMed:21532592, ECO:0000269|PubMed:21753002, ECO:0000269|PubMed:22082830, ECO:0000269|PubMed:22396657, ECO:0000269|PubMed:23620051, ECO:0000269|PubMed:23685073, ECO:0000269|PubMed:23754282, ECO:0000269|PubMed:23933751, ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:24896179, ECO:0000269|PubMed:25474007, ECO:0000269|PubMed:25527291, ECO:0000269|PubMed:25621951, ECO:0000269|PubMed:27534820, ECO:0000269|PubMed:29311685, ECO:0000269|PubMed:32047033, ECO:0000269|PubMed:33499712}.
uniprot
proteins
mass_dalton
51641
uniprot
proteins
mutagenesis
MUTAGEN 65; /note="S->A: Loss of phosphorylation. Undergoes autoubiquitination in the presence of phosphorylated ubiquitin."; /evidence="ECO:0000269|PubMed:25474007"; MUTAGEN 65; /note="S->E: Phosphomimetic mutant; still requires PINK1 for activation. PRKN is activated in presence of phosphorylated ubiquitin."; /evidence="ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25474007"; MUTAGEN 175; /note="T->A: Loss of phosphorylation. Reduced mitochondrial localization; when associated with A-217."; /evidence="ECO:0000269|PubMed:18957282"; MUTAGEN 175; /note="T->E: Phosphomimetic mutant. Mostly localizes to the mitochondria; when associated with E-217."; /evidence="ECO:0000269|PubMed:18957282"; MUTAGEN 217; /note="T->A: Loss of phosphorylation. Reduced mitochondrial localization; when associated with A-175."; /evidence="ECO:0000269|PubMed:18957282"; MUTAGEN 217; /note="T->E: Phosphomimetic mutant. Mostly localizes to the mitochondria; when associated with E-175."; /evidence="ECO:0000269|PubMed:18957282"; MUTAGEN 238; /note="C->S: Loss of mitochondrial localization."; /evidence="ECO:0000269|PubMed:18957282"; MUTAGEN 332; /note="C->S: Impairs folding of IBR domain."; /evidence="ECO:0000269|PubMed:17360614"; MUTAGEN 337; /note="C->A: Impairs the ability to ubiquitinate SNCAIP."; /evidence="ECO:0000269|PubMed:11590439"; MUTAGEN 365; /note="C->S: Impairs protein folding."; /evidence="ECO:0000269|PubMed:17360614"; MUTAGEN 403; /note="W->A: Decreased autoinhibition and increased E3 activity."; /evidence="ECO:0000269|PubMed:24784582"; MUTAGEN 421; /note="C->A: Impairs the ability of self-ubiquitination and to ubiquitinate SNCAIP."; /evidence="ECO:0000269|PubMed:11590439, ECO:0000269|PubMed:18541373"; MUTAGEN 429; /note="G->E: Reduced self-ubiquitination."; /evidence="ECO:0000269|PubMed:23770917"; MUTAGEN 431; /note="C->A: Loss of activity."; /evidence="ECO:0000269|PubMed:23770917"; MUTAGEN 431; /note="C->S: Impairs the ability to ubiquitinate target proteins. No effect on translocation to mitochondria."; /evidence="ECO:0000269|PubMed:11590439, ECO:0000269|PubMed:23727886, ECO:0000269|PubMed:23770887, ECO:0000269|PubMed:25474007, ECO:0000269|PubMed:32047033"; MUTAGEN 433; /note="H->N,A: Impaired activity."; /evidence="ECO:0000269|PubMed:23727886, ECO:0000269|PubMed:23770887"; MUTAGEN 444; /note="E->Q,A: Impaired activity."; /evidence="ECO:0000269|PubMed:23727886, ECO:0000269|PubMed:23770887
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination.
uniprot
proteins
post_translational_modification
PTM: ISGylated. Conjugated to ubiquitin-like protein ISG15 upon IFN-beta stimulation. ISGylation positively regulates its E3 ligase activity. {ECO:0000269|PubMed:27534820}.; PTM: Auto-ubiquitinates in an E2-dependent manner leading to its own degradation (PubMed:19229105, PubMed:23770917, PubMed:25474007). Also polyubiquitinated by RNF41 for proteasomal degradation (PubMed:19229105). {ECO:0000269|PubMed:19229105, ECO:0000269|PubMed:23770917, ECO:0000269|PubMed:25474007}.; PTM: S-nitrosylated. The inhibition of PRKN ubiquitin E3 ligase activity by S-nitrosylation could contribute to the degenerative process in PD by impairing the ubiquitination of PRKN substrates. {ECO:0000269|PubMed:15105460}.; PTM: Phosphorylated (PubMed:18957282, PubMed:23754282, PubMed:24660806, PubMed:24784582, PubMed:25474007). Activation requires phosphorylation at Ser-65 by PINK1 and binding to PINK1 phosphorylated ubiquitin (PubMed:18957282, PubMed:23754282, PubMed:24660806, PubMed:24784582, PubMed:25474007). Phosphorylation at Thr-175 by PINK1 and at Thr-217 is important for mitochondrial localization (PubMed:18957282). {ECO:0000269|PubMed:18957282, ECO:0000269|PubMed:23754282, ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25474007}.
uniprot
proteins
protein_family
Parkin subfamily
uniprot
proteins
protein_family
RBR family
uniprot
proteins
pubmed
10072423
uniprot
proteins
pubmed
10319893
uniprot
proteins
pubmed
10511432
uniprot
proteins
pubmed
10824074
uniprot
proteins
pubmed
10888878
uniprot
proteins
pubmed
10939576
uniprot
proteins
pubmed
10965160
uniprot
proteins
pubmed
10973942
uniprot
proteins
pubmed
11078524
uniprot
proteins
pubmed
11163284
uniprot
proteins
pubmed
11179010
uniprot
proteins
pubmed
11431533
uniprot
proteins
pubmed
11439185
uniprot
proteins
pubmed
11487568
uniprot
proteins
pubmed
11590439
uniprot
proteins
pubmed
11971093
uniprot
proteins
pubmed
12056932
uniprot
proteins
pubmed
12112109
uniprot
proteins
pubmed
12114481
uniprot
proteins
pubmed
12116199
uniprot
proteins
pubmed
12150907
uniprot
proteins
pubmed
12362318
uniprot
proteins
pubmed
12397156
uniprot
proteins
pubmed
12446796
uniprot
proteins
pubmed
12628165
uniprot
proteins
pubmed
12629236
uniprot
proteins
pubmed
12634850
uniprot
proteins
pubmed
12719539
uniprot
proteins
pubmed
12730996
uniprot
proteins
pubmed
12781599
uniprot
proteins
pubmed
12925569
uniprot
proteins
pubmed
14532270
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
14614460
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14976155
uniprot
proteins
pubmed
15105460
uniprot
proteins
pubmed
15229644
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15584030
uniprot
proteins
pubmed
15728840
uniprot
proteins
pubmed
15987638
uniprot
proteins
pubmed
16135753
uniprot
proteins
pubmed
16332688
uniprot
proteins
pubmed
16352719
uniprot
proteins
pubmed
16955485
uniprot
proteins
pubmed
17360614
uniprot
proteins
pubmed
17846173
uniprot
proteins
pubmed
18541373
uniprot
proteins
pubmed
18957282
uniprot
proteins
pubmed
19029340
uniprot
proteins
pubmed
19229105
uniprot
proteins
pubmed
19501131
uniprot
proteins
pubmed
19801972
uniprot
proteins
pubmed
19966284
uniprot
proteins
pubmed
20404107
uniprot
proteins
pubmed
20798600
uniprot
proteins
pubmed
20889486
uniprot
proteins
pubmed
20889974
uniprot
proteins
pubmed
21376232
uniprot
proteins
pubmed
21532592
uniprot
proteins
pubmed
21753002
uniprot
proteins
pubmed
22082830
uniprot
proteins
pubmed
22396657
uniprot
proteins
pubmed
22956510
uniprot
proteins
pubmed
23620051
uniprot
proteins
pubmed
23685073
uniprot
proteins
pubmed
23727886
uniprot
proteins
pubmed
23754282
uniprot
proteins
pubmed
23770887
uniprot
proteins
pubmed
23770917
uniprot
proteins
pubmed
23933751
uniprot
proteins
pubmed
24270810
uniprot
proteins
pubmed
24660806
uniprot
proteins
pubmed
24751536
uniprot
proteins
pubmed
24784582
uniprot
proteins
pubmed
24896179
uniprot
proteins
pubmed
24898855
uniprot
proteins
pubmed
25474007
uniprot
proteins
pubmed
25527291
uniprot
proteins
pubmed
25621951
uniprot
proteins
pubmed
27534820
uniprot
proteins
pubmed
27535533
uniprot
proteins
pubmed
29311685
uniprot
proteins
pubmed
32047033
uniprot
proteins
pubmed
33499712
uniprot
proteins
pubmed
9560156
uniprot
proteins
pubmed
9731209
uniprot
proteins
sequence_length
465
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:10319893, ECO:0000269|PubMed:16955485, ECO:0000269|PubMed:17846173, ECO:0000269|PubMed:18957282, ECO:0000269|PubMed:19029340, ECO:0000269|PubMed:19229105, ECO:0000269|PubMed:19501131, ECO:0000269|PubMed:22082830, ECO:0000269|PubMed:23620051, ECO:0000269|PubMed:23933751, ECO:0000269|PubMed:24898855}. Nucleus {ECO:0000269|PubMed:16955485}. Endoplasmic reticulum {ECO:0000269|PubMed:19501131}. Mitochondrion {ECO:0000269|PubMed:18957282, ECO:0000269|PubMed:19029340, ECO:0000269|PubMed:19229105, ECO:0000269|PubMed:20889974, ECO:0000269|PubMed:22082830, ECO:0000269|PubMed:23620051, ECO:0000269|PubMed:23754282, ECO:0000269|PubMed:23933751, ECO:0000269|PubMed:24898855}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q9WVS6}. Cell projection, neuron projection {ECO:0000269|PubMed:12925569}. Postsynaptic density {ECO:0000250|UniProtKB:Q9WVS6}. Presynapse {ECO:0000250|UniProtKB:Q9WVS6}. Note=Mainly localizes in the cytosol (PubMed:19029340, PubMed:19229105). Co-localizes with SYT11 in neutrites (PubMed:12925569). Co-localizes with SNCAIP in brainstem Lewy bodies (PubMed:10319893, PubMed:11431533). Translocates to dysfunctional mitochondria that have lost the mitochondrial membrane potential; recruitment to mitochondria is PINK1-dependent (PubMed:18957282, PubMed:19966284, PubMed:23620051, PubMed:24898855). Mitochondrial localization also gradually increases with cellular growth (PubMed:22082830). {ECO:0000269|PubMed:10319893, ECO:0000269|PubMed:11431533, ECO:0000269|PubMed:12925569, ECO:0000269|PubMed:18957282, ECO:0000269|PubMed:19029340, ECO:0000269|PubMed:19229105, ECO:0000269|PubMed:19966284, ECO:0000269|PubMed:22082830, ECO:0000269|PubMed:23620051, ECO:0000269|PubMed:24898855}.
uniprot
proteins