UniProtKB - Q9JK66 (PRKN_RAT)
E3 ubiquitin-protein ligase parkin
Prkn
Functioni
Functions within a multiprotein E3 ubiquitin ligase complex, catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. Substrates include SYT11 and VDAC1. Other substrates are BCL2, CCNE1, GPR37, RHOT1/MIRO1, MFN1, MFN2, STUB1, SNCAIP, SEPTIN5, TOMM20, USP30, ZNF746, MIRO1 and AIMP2. Mediates monoubiquitination as well as 'Lys-6', 'Lys-11', 'Lys-48'-linked and 'Lys-63'-linked polyubiquitination of substrates depending on the context. 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. Mediates 'Lys-63'-linked polyubiquitination of a 22 kDa O-linked glycosylated isoform of SNCAIP, possibly playing a role in Lewy-body formation. Mediates monoubiquitination of BCL2, thereby acting as a positive regulator of autophagy. 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. 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. Activation and recruitment onto the outer membrane of damaged/dysfunctional mitochondria (OMM) requires PINK1-mediated phosphorylation of both PRKN and ubiquitin. 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. 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. Preferentially assembles 'Lys-6'-, 'Lys-11'- and 'Lys-63'-linked polyubiquitin chains, leading to mitophagy. 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. This prevents the refusion of unhealthy mitochondria with the mitochondrial network or initiates mitochondrial fragmentation facilitating their later engulfment by autophagosomes. 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. 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. Limits the production of reactive oxygen species (ROS). Regulates cyclin-E during neuronal apoptosis. In collaboration with CHPF isoform 2, may enhance cell viability and protect cells from oxidative stress. Independently of its ubiquitin ligase activity, protects from apoptosis by the transcriptional repression of p53/TP53. May protect neurons against alpha synuclein toxicity, proteasomal dysfunction, GPR37 accumulation, and kainate-induced excitotoxicity. May play a role in controlling neurotransmitter trafficking at the presynaptic terminal and in calcium-dependent exocytosis. May represent a tumor suppressor gene.
By similarityCatalytic activityi
- [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.1 Publication EC:2.3.2.31
Activity regulationi
: protein ubiquitination Pathwayi
This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 238 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 241 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 253 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 257 | Zinc 2; via pros nitrogenPROSITE-ProRule annotation | 1 | |
Metal bindingi | 260 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 263 | Zinc 1PROSITE-ProRule annotation | 1 | |
Metal bindingi | 289 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 293 | Zinc 2PROSITE-ProRule annotation | 1 | |
Metal bindingi | 332 | Zinc 3PROSITE-ProRule annotation | 1 | |
Metal bindingi | 337 | Zinc 3PROSITE-ProRule annotation | 1 | |
Metal bindingi | 352 | Zinc 3PROSITE-ProRule annotation | 1 | |
Metal bindingi | 360 | Zinc 3PROSITE-ProRule annotation | 1 | |
Metal bindingi | 365 | Zinc 4PROSITE-ProRule annotation | 1 | |
Metal bindingi | 368 | Zinc 4PROSITE-ProRule annotation | 1 | |
Metal bindingi | 373 | Zinc 4; via tele nitrogenPROSITE-ProRule annotation | 1 | |
Metal bindingi | 377 | Zinc 4PROSITE-ProRule annotation | 1 | |
Metal bindingi | 418 | Zinc 5PROSITE-ProRule annotation | 1 | |
Metal bindingi | 421 | Zinc 5PROSITE-ProRule annotation | 1 | |
Active sitei | 431 | PROSITE-ProRule annotation1 Publication | 1 | |
Metal bindingi | 436 | Zinc 5PROSITE-ProRule annotation | 1 | |
Metal bindingi | 441 | Zinc 5PROSITE-ProRule annotation | 1 | |
Metal bindingi | 446 | Zinc 6PROSITE-ProRule annotation | 1 | |
Metal bindingi | 449 | Zinc 6PROSITE-ProRule annotation | 1 | |
Metal bindingi | 457 | Zinc 6PROSITE-ProRule annotation | 1 | |
Metal bindingi | 461 | Zinc 6; via tele nitrogenPROSITE-ProRule annotation | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 141 – 225 | RING-type 0; atypicalAdd BLAST | 85 | |
Zinc fingeri | 238 – 293 | RING-type 1PROSITE-ProRule annotationAdd BLAST | 56 | |
Zinc fingeri | 313 – 377 | IBR-typePROSITE-ProRule annotationAdd BLAST | 65 | |
Zinc fingeri | 418 – 449 | RING-type 2; atypicalPROSITE-ProRule annotationAdd BLAST | 32 |
GO - Molecular functioni
- actin binding Source: RGD
- beta-catenin binding Source: RGD
- chaperone binding Source: RGD
- cullin family protein binding Source: ParkinsonsUK-UCL
- enzyme binding Source: RGD
- F-box domain binding Source: ParkinsonsUK-UCL
- G protein-coupled receptor binding Source: ParkinsonsUK-UCL
- heat shock protein binding Source: RGD
- histone deacetylase binding Source: RGD
- Hsp70 protein binding Source: RGD
- identical protein binding Source: ParkinsonsUK-UCL
- kinase binding Source: RGD
- metal ion binding Source: UniProtKB-KW
- PDZ domain binding Source: ParkinsonsUK-UCL
- phospholipase binding Source: RGD
- protein-containing complex binding Source: RGD
- protein kinase binding Source: RGD
- transcription corepressor activity Source: RGD
- tubulin binding Source: RGD
- ubiquitin binding Source: UniProtKB
- ubiquitin conjugating enzyme binding Source: ParkinsonsUK-UCL
- ubiquitin protein ligase activity Source: UniProtKB
- ubiquitin protein ligase binding Source: RGD
- ubiquitin-protein transferase activity Source: UniProtKB
- ubiquitin-specific protease binding Source: RGD
GO - Biological processi
- adult locomotory behavior Source: ParkinsonsUK-UCL
- aggresome assembly Source: ParkinsonsUK-UCL
- autophagy of mitochondrion Source: ParkinsonsUK-UCL
- brain development Source: RGD
- cellular protein catabolic process Source: RGD
- cellular response to hydrogen sulfide Source: RGD
- cellular response to L-glutamate Source: RGD
- cellular response to L-glutamine Source: RGD
- cellular response to manganese ion Source: RGD
- cellular response to toxic substance Source: ParkinsonsUK-UCL
- dopamine metabolic process Source: RGD
- dopamine uptake involved in synaptic transmission Source: RGD
- free ubiquitin chain polymerization Source: RGD
- learning Source: RGD
- locomotory behavior Source: RGD
- mitochondrial fission Source: ParkinsonsUK-UCL
- mitochondrial fragmentation involved in apoptotic process Source: RGD
- mitochondrion localization Source: ParkinsonsUK-UCL
- mitochondrion organization Source: ParkinsonsUK-UCL
- mitochondrion to lysosome transport Source: RGD
- mitophagy Source: RGD
- modulation of chemical synaptic transmission Source: RGD
- negative regulation by host of viral genome replication Source: RGD
- negative regulation of actin filament bundle assembly Source: RGD
- negative regulation of canonical Wnt signaling pathway Source: RGD
- negative regulation of cell death Source: RGD
- negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway Source: ParkinsonsUK-UCL
- negative regulation of endoplasmic reticulum stress-induced neuron intrinsic apoptotic signaling pathway Source: RGD
- negative regulation of excitatory postsynaptic potential Source: RGD
- negative regulation of exosomal secretion Source: RGD
- negative regulation of gene expression Source: RGD
- negative regulation of glucokinase activity Source: ParkinsonsUK-UCL
- negative regulation of insulin secretion Source: ParkinsonsUK-UCL
- negative regulation of intralumenal vesicle formation Source: RGD
- negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator Source: RGD
- negative regulation of JNK cascade Source: ParkinsonsUK-UCL
- negative regulation of mitochondrial fission Source: RGD
- negative regulation of mitochondrial fusion Source: ParkinsonsUK-UCL
- negative regulation of neuron apoptotic process Source: RGD
- negative regulation of neuron death Source: MGI
- negative regulation of oxidative stress-induced neuron death Source: ParkinsonsUK-UCL
- negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway Source: ParkinsonsUK-UCL
- negative regulation of primary amine oxidase activity Source: RGD
- negative regulation of protein phosphorylation Source: ParkinsonsUK-UCL
- negative regulation of reactive oxygen species biosynthetic process Source: RGD
- negative regulation of reactive oxygen species metabolic process Source: ParkinsonsUK-UCL
- negative regulation of release of cytochrome c from mitochondria Source: ParkinsonsUK-UCL
- negative regulation of spontaneous neurotransmitter secretion Source: RGD
- negative regulation of synaptic transmission, glutamatergic Source: RGD
- negative regulation of transcription by RNA polymerase II Source: RGD
- neuron cellular homeostasis Source: ParkinsonsUK-UCL
- norepinephrine metabolic process Source: RGD
- parkin-mediated stimulation of mitophagy in response to mitochondrial depolarization Source: RGD
- positive regulation of apoptotic process Source: RGD
- positive regulation of ATP biosynthetic process Source: RGD
- positive regulation of autophagy of mitochondrion Source: RGD
- positive regulation of dendrite extension Source: RGD
- positive regulation of DNA binding Source: ParkinsonsUK-UCL
- positive regulation of gene expression Source: RGD
- positive regulation of I-kappaB kinase/NF-kappaB signaling Source: ParkinsonsUK-UCL
- positive regulation of insulin secretion involved in cellular response to glucose stimulus Source: RGD
- positive regulation of mitochondrial fission Source: ParkinsonsUK-UCL
- positive regulation of mitochondrial fusion Source: ParkinsonsUK-UCL
- positive regulation of mitochondrial membrane potential Source: RGD
- positive regulation of mitophagy Source: RGD
- positive regulation of mitophagy in response to mitochondrial depolarization Source: RGD
- positive regulation of neurotransmitter uptake Source: RGD
- positive regulation of proteasomal protein catabolic process Source: RGD
- positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: RGD
- positive regulation of protein binding Source: RGD
- positive regulation of protein linear polyubiquitination Source: RGD
- positive regulation of protein localization to membrane Source: RGD
- positive regulation of transcription by RNA polymerase II Source: ParkinsonsUK-UCL
- positive regulation of tumor necrosis factor-mediated signaling pathway Source: ParkinsonsUK-UCL
- proteasomal protein catabolic process Source: RGD
- proteasome-mediated ubiquitin-dependent protein catabolic process Source: ParkinsonsUK-UCL
- protein autoubiquitination Source: ParkinsonsUK-UCL
- protein destabilization Source: UniProtKB
- protein K11-linked ubiquitination Source: UniProtKB
- protein K48-linked ubiquitination Source: UniProtKB
- protein K63-linked ubiquitination Source: ParkinsonsUK-UCL
- protein K6-linked ubiquitination Source: UniProtKB
- protein localization to mitochondrion Source: ParkinsonsUK-UCL
- protein metabolic process Source: RGD
- protein monoubiquitination Source: UniProtKB
- protein polyubiquitination Source: ParkinsonsUK-UCL
- protein stabilization Source: RGD
- protein ubiquitination Source: ParkinsonsUK-UCL
- regulation of apoptotic process Source: GO_Central
- regulation of autophagy Source: UniProtKB
- regulation of cellular response to oxidative stress Source: ParkinsonsUK-UCL
- regulation of dopamine metabolic process Source: RGD
- regulation of gene expression Source: RGD
- regulation of mitochondrial membrane potential Source: RGD
- regulation of mitochondrion organization Source: ParkinsonsUK-UCL
- regulation of neurotransmitter secretion Source: RGD
- regulation of protein stability Source: RGD
- regulation of protein ubiquitination Source: RGD
- regulation of reactive oxygen species metabolic process Source: RGD
- response to corticosterone Source: RGD
- response to curcumin Source: RGD
- response to endoplasmic reticulum stress Source: RGD
- response to muscle activity Source: RGD
- response to oxidative stress Source: ParkinsonsUK-UCL
- response to unfolded protein Source: RGD
- response to xenobiotic stimulus Source: RGD
- startle response Source: RGD
- synaptic transmission, dopaminergic Source: RGD
- synaptic transmission, glutamatergic Source: RGD
- ubiquitin-dependent protein catabolic process Source: ParkinsonsUK-UCL
- zinc ion homeostasis Source: ParkinsonsUK-UCL
Keywordsi
Molecular function | Transferase |
Biological process | Autophagy, Transcription, Transcription regulation, Ubl conjugation pathway |
Ligand | Metal-binding, Zinc |
Enzyme and pathway databases
UniPathwayi | UPA00143 |
Names & Taxonomyi
Protein namesi | Recommended name: E3 ubiquitin-protein ligase parkinCurated (EC:2.3.2.311 Publication)Alternative name(s): Parkin RBR E3 ubiquitin-protein ligaseBy similarity |
Gene namesi | |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 61797, Prkn |
Subcellular locationi
Nucleus
- Nucleus By similarity
Endoplasmic reticulum
- Endoplasmic reticulum By similarity
Cytoplasm and Cytosol
- cytosol 1 Publication
Mitochondrion
- Mitochondrion By similarity
- Mitochondrion outer membrane By similarity
Other locations
- neuron projection 1 Publication
- postsynaptic density By similarity
- presynapse By similarity
Note: Mainly localizes in the cytosol. Co-localizes with SYT11 in neutrites. Co-localizes with SNCAIP in brainstem Lewy bodies. Translocates to dysfunctional mitochondria that have lost the mitochondrial membrane potential; recruitment to mitochondria is PINK1-dependent. Mitochondrial localization also gradually increases with cellular growth.By similarity
Cytosol
- cytosol Source: ParkinsonsUK-UCL
Endoplasmic reticulum
- endoplasmic reticulum Source: RGD
- endoplasmic reticulum membrane Source: ParkinsonsUK-UCL
Golgi apparatus
- Golgi apparatus Source: RGD
- Golgi membrane Source: ParkinsonsUK-UCL
Mitochondrion
- mitochondrial outer membrane Source: UniProtKB-SubCell
- mitochondrion Source: RGD
Nucleus
- nucleus Source: RGD
Other locations
- aggresome Source: ParkinsonsUK-UCL
- axon Source: RGD
- cytoplasm Source: ParkinsonsUK-UCL
- cytoplasmic vesicle Source: RGD
- intracellular vesicle Source: RGD
- membrane raft Source: RGD
- neuron projection Source: ParkinsonsUK-UCL
- neuronal cell body Source: RGD
- Parkin-FBXW7-Cul1 ubiquitin ligase complex Source: ParkinsonsUK-UCL
- perinuclear region of cytoplasm Source: ParkinsonsUK-UCL
- postsynaptic density Source: RGD
- presynapse Source: RGD
- protein-containing complex Source: RGD
- synapse Source: ParkinsonsUK-UCL
- synaptic vesicle Source: RGD
- synaptic vesicle membrane Source: RGD
- terminal bouton Source: ParkinsonsUK-UCL
- ubiquitin ligase complex Source: ParkinsonsUK-UCL
Keywords - Cellular componenti
Cell junction, Cell projection, Cytoplasm, Endoplasmic reticulum, Membrane, Mitochondrion, Mitochondrion outer membrane, Nucleus, SynapsePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 403 | W → A: Increased autoubiquitination. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000058578 | 1 – 465 | E3 ubiquitin-protein ligase parkinAdd BLAST | 465 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 65 | Phosphoserine; by PINK1By similarity | 1 | |
Modified residuei | 80 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 175 | Phosphothreonine; by PINK1By similarity | 1 | |
Modified residuei | 217 | PhosphothreonineBy similarity | 1 |
Post-translational modificationi
Keywords - PTMi
Phosphoprotein, Ubl conjugationProteomic databases
PaxDbi | Q9JK66 |
PTM databases
iPTMneti | Q9JK66 |
PhosphoSitePlusi | Q9JK66 |
Expressioni
Tissue specificityi
Interactioni
Subunit structurei
Forms an E3 ubiquitin ligase complex with UBE2L3 or UBE2L6. Mediates 'Lys-63'-linked polyubiquitination by associating with UBE2V1.
Part of a SCF-like complex, consisting of PRKN, CUL1 and FBXW7.
Interacts with SNCAIP. Binds to the C2A and C2B domains of SYT11.
Interacts and regulates the turnover of SEPTIN5. Part of a complex, including STUB1, HSP70 and GPR37. The amount of STUB1 in the complex increases during ER stress. STUB1 promotes the dissociation of HSP70 from PRKN and GPR37, thus facilitating PRKN-mediated GPR37 ubiquitination. HSP70 transiently associates with unfolded GPR37 and inhibits the E3 activity of PRKN, whereas, STUB1 enhances the E3 activity of PRKN through promotion of dissociation of HSP70 from PRKN-GPR37 complexes.
Interacts with PSMD4 and PACRG.
Interacts with LRRK2.
Interacts with RANBP2.
Interacts with SUMO1 but not SUMO2, which promotes nuclear localization and autoubiquitination.
Interacts (via first RING-type domain) with AIMP2 (via N-terminus).
Interacts with PSMA7 and RNF41.
Interacts with PINK1.
Forms a complex with PINK1 and PARK7.
Interacts with CHPF, the interaction with isoform 2 may facilitate PRKN transport into the mitochondria.
Interacts with MFN2 (phosphorylated), promotes PRKN localization in dysfunctional depolarized mitochondria.
Interacts with FBXO7; this promotes translocation to dysfunctional depolarized mitochondria.
Interacts with ZNF746.
Interacts with heat shock protein 70 family members, including HSPA1L, HSPA1A and HSPA8; interaction HSPA1L promotes translocation to damaged mitochondria.
Interacts with BAG4 and, to a lesser extent, BAG5; interaction with BAG4 inhibits translocation to damaged mitochondria.
Forms a complex with PRKN and PARK7.
Interacts with AMBRA1 (By similarity).
By similarityBinary interactionsi
Q9JK66
With | #Exp. | IntAct |
---|---|---|
Ranbp2 [D4A054] | 2 | EBI-973793,EBI-973937 |
GO - Molecular functioni
- actin binding Source: RGD
- beta-catenin binding Source: RGD
- chaperone binding Source: RGD
- cullin family protein binding Source: ParkinsonsUK-UCL
- enzyme binding Source: RGD
- F-box domain binding Source: ParkinsonsUK-UCL
- G protein-coupled receptor binding Source: ParkinsonsUK-UCL
- heat shock protein binding Source: RGD
- histone deacetylase binding Source: RGD
- Hsp70 protein binding Source: RGD
- identical protein binding Source: ParkinsonsUK-UCL
- kinase binding Source: RGD
- PDZ domain binding Source: ParkinsonsUK-UCL
- phospholipase binding Source: RGD
- protein kinase binding Source: RGD
- tubulin binding Source: RGD
- ubiquitin binding Source: UniProtKB
- ubiquitin conjugating enzyme binding Source: ParkinsonsUK-UCL
- ubiquitin protein ligase binding Source: RGD
- ubiquitin-specific protease binding Source: RGD
Protein-protein interaction databases
BioGRIDi | 248590, 17 interactors |
DIPi | DIP-37656N |
IntActi | Q9JK66, 1 interactor |
MINTi | Q9JK66 |
STRINGi | 10116.ENSRNOP00000040511 |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | Q9JK66 |
BMRBi | Q9JK66 |
SMRi | Q9JK66 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q9JK66 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 1 – 76 | Ubiquitin-likePROSITE-ProRule annotationAdd BLAST | 76 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 71 – 96 | DisorderedSequence analysisAdd BLAST | 26 | |
Regioni | 77 – 237 | Necessary for PINK1-dependent localization to mitochondriaBy similarityAdd BLAST | 161 | |
Regioni | 204 – 238 | SYT11 binding 1By similarityAdd BLAST | 35 | |
Regioni | 234 – 465 | TRIAD supradomainPROSITE-ProRule annotationAdd BLAST | 232 | |
Regioni | 257 – 293 | SYT11 binding 2By similarityAdd BLAST | 37 | |
Regioni | 378 – 410 | REP1 PublicationAdd BLAST | 33 |
Domaini
Sequence similaritiesi
Zinc finger
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 141 – 225 | RING-type 0; atypicalAdd BLAST | 85 | |
Zinc fingeri | 238 – 293 | RING-type 1PROSITE-ProRule annotationAdd BLAST | 56 | |
Zinc fingeri | 313 – 377 | IBR-typePROSITE-ProRule annotationAdd BLAST | 65 | |
Zinc fingeri | 418 – 449 | RING-type 2; atypicalPROSITE-ProRule annotationAdd BLAST | 32 |
Keywords - Domaini
Repeat, Zinc-fingerPhylogenomic databases
eggNOGi | KOG0006, Eukaryota |
InParanoidi | Q9JK66 |
OrthoDBi | 1140368at2759 |
PhylomeDBi | Q9JK66 |
Family and domain databases
DisProti | DP01850 |
InterProi | View protein in InterPro IPR002867, IBR_dom IPR003977, Parkin IPR041565, Parkin_Znf-RING IPR044066, TRIAD_supradom IPR000626, Ubiquitin-like_dom IPR029071, Ubiquitin-like_domsf IPR041170, Znf-RING_14 |
Pfami | View protein in Pfam PF01485, IBR, 1 hit PF00240, ubiquitin, 1 hit PF17976, zf-RING_12, 1 hit PF17978, zf-RING_14, 1 hit |
PIRSFi | PIRSF037880, Parkin, 1 hit |
PRINTSi | PR01475, PARKIN |
SMARTi | View protein in SMART SM00647, IBR, 2 hits SM00213, UBQ, 1 hit |
SUPFAMi | SSF54236, SSF54236, 1 hit |
PROSITEi | View protein in PROSITE PS51873, TRIAD, 1 hit PS50053, UBIQUITIN_2, 1 hit |
s (6+)i Sequence
Sequence statusi: Complete.
This entry describes 6 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 6 described isoforms and 8 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MIVFVRFNSS YGFPVEVDSD TSIFQLKEVV AKRQGVPADQ LRVIFAGKEL
60 70 80 90 100
QNHLTVQNCD LEQQSIVHIV QRPQRKSHET NASGGDKPQS TPEGSIWEPR
110 120 130 140 150
SLTRVDLSSH ILPADSVGLA VILDTDSKSD SEAARGPEAK PTYHSFFVYC
160 170 180 190 200
KGPCHKVQPG KLRVQCGTCR QATLTLAQGP SCWDDVLIPN RMSGECQSPD
210 220 230 240 250
CPGTRAEFFF KCGAHPTSDK DTSVALNLIT NNSRSIPCIA CTDVRNPVLV
260 270 280 290 300
FQCNHRHVIC LDCFHLYCVT RLNDRQFVHD AQLGYSLPCV AGCPNSLIKE
310 320 330 340 350
LHHFRILGEE QYNRYQQYGA EECVLQMGGV LCPRPGCGAG LLPEQGQKKV
360 370 380 390 400
TCEGGNGLGC GFVFCRDCKE AYHEGECDSM FEASGATSQA YRVDQRAAEQ
410 420 430 440 450
ARWEEASKET IKKTTKPCPR CNVPIEKNGG CMHMKCPQPQ CKLEWCWNCG
460
CEWNRACMGD HWFDV
Computationally mapped potential isoform sequencesi
There are 8 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketD3JVU5 | D3JVU5_RAT | E3 ubiquitin-protein ligase parkin | Prkn Park2 | 79 | Annotation score: | ||
A0A0G2JY87 | A0A0G2JY87_RAT | RBR-type E3 ubiquitin transferase | Prkn | 210 | Annotation score: | ||
A0A0G2K740 | A0A0G2K740_RAT | RBR-type E3 ubiquitin transferase | Prkn | 488 | Annotation score: | ||
A0A0G2K2J2 | A0A0G2K2J2_RAT | RBR-type E3 ubiquitin transferase | Prkn | 182 | Annotation score: | ||
A0A0G2JZS8 | A0A0G2JZS8_RAT | E3 ubiquitin-protein ligase parkin | Prkn | 343 | Annotation score: | ||
A0A8I5ZN83 | A0A8I5ZN83_RAT | E3 ubiquitin-protein ligase parkin | Prkn | 101 | Annotation score: | ||
A0A8I6A5N7 | A0A8I6A5N7_RAT | E3 ubiquitin-protein ligase parkin | Prkn | 493 | Annotation score: | ||
A0A8I6GIU4 | A0A8I6GIU4_RAT | E3 ubiquitin-protein ligase parkin | Prkn | 436 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 24 | F → C in AAF34874 (PubMed:10686358).Curated | 1 | |
Sequence conflicti | 138 | E → A in BAA92431 (Ref. 3) Curated | 1 | |
Sequence conflicti | 348 | K → R in BAA92431 (Ref. 3) Curated | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_011717 | 1 – 191 | Missing in isoform 3 and isoform 6. 1 PublicationAdd BLAST | 191 | |
Alternative sequenceiVSP_011718 | 57 | Q → QHPQDGFCHKSHLAVHNLSQ QDVTQ in isoform 4. 1 Publication | 1 | |
Alternative sequenceiVSP_011719 | 179 – 206 | Missing in isoform 5. 1 PublicationAdd BLAST | 28 | |
Alternative sequenceiVSP_011720 | 390 – 394 | AYRVD → EDVCT in isoform 6. 1 Publication | 5 | |
Alternative sequenceiVSP_011721 | 395 – 465 | Missing in isoform 6. 1 PublicationAdd BLAST | 71 | |
Alternative sequenceiVSP_011722 | 429 – 446 | GGCMH…KLEWC → ERMHVQYTMCIPGAHGGY in isoform 2. 1 PublicationAdd BLAST | 18 | |
Alternative sequenceiVSP_011723 | 447 – 465 | Missing in isoform 2. 1 PublicationAdd BLAST | 19 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF343574 mRNA Translation: AAL73348.1 AF381277 mRNA Translation: AAM21452.1 AF381278 mRNA Translation: AAM21453.1 AF381279 mRNA Translation: AAM21454.1 AF381280 mRNA Translation: AAM21455.1 AF381281 mRNA Translation: AAM21456.1 AF168004 mRNA Translation: AAF34874.1 AF210434 mRNA Translation: AAG37013.1 AF257234 mRNA Translation: AAF68666.1 AB039878 mRNA Translation: BAA92431.1 |
RefSeqi | NP_064478.1, NM_020093.1 |
Genome annotation databases
Ensembli | ENSRNOT00000096213; ENSRNOP00000077507; ENSRNOG00000055547 [Q9JK66-1] ENSRNOT00000107769; ENSRNOP00000088932; ENSRNOG00000055547 [Q9JK66-3] |
GeneIDi | 56816 |
KEGGi | rno:56816 |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF343574 mRNA Translation: AAL73348.1 AF381277 mRNA Translation: AAM21452.1 AF381278 mRNA Translation: AAM21453.1 AF381279 mRNA Translation: AAM21454.1 AF381280 mRNA Translation: AAM21455.1 AF381281 mRNA Translation: AAM21456.1 AF168004 mRNA Translation: AAF34874.1 AF210434 mRNA Translation: AAG37013.1 AF257234 mRNA Translation: AAF68666.1 AB039878 mRNA Translation: BAA92431.1 |
RefSeqi | NP_064478.1, NM_020093.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2KNB | NMR | - | A | 1-76 | [»] | |
4K7D | X-ray | 2.80 | A/B/C | 141-465 | [»] | |
4K95 | X-ray | 6.50 | A/B/C/D/E/F/G/H/I/J/K/L | 1-465 | [»] | |
4ZYN | X-ray | 2.54 | A/B | 1-465 | [»] | |
AlphaFoldDBi | Q9JK66 | |||||
BMRBi | Q9JK66 | |||||
SMRi | Q9JK66 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 248590, 17 interactors |
DIPi | DIP-37656N |
IntActi | Q9JK66, 1 interactor |
MINTi | Q9JK66 |
STRINGi | 10116.ENSRNOP00000040511 |
PTM databases
iPTMneti | Q9JK66 |
PhosphoSitePlusi | Q9JK66 |
Proteomic databases
PaxDbi | Q9JK66 |
Genome annotation databases
Ensembli | ENSRNOT00000096213; ENSRNOP00000077507; ENSRNOG00000055547 [Q9JK66-1] ENSRNOT00000107769; ENSRNOP00000088932; ENSRNOG00000055547 [Q9JK66-3] |
GeneIDi | 56816 |
KEGGi | rno:56816 |
Organism-specific databases
CTDi | 5071 |
RGDi | 61797, Prkn |
Phylogenomic databases
eggNOGi | KOG0006, Eukaryota |
InParanoidi | Q9JK66 |
OrthoDBi | 1140368at2759 |
PhylomeDBi | Q9JK66 |
Enzyme and pathway databases
UniPathwayi | UPA00143 |
Miscellaneous databases
EvolutionaryTracei | Q9JK66 |
PROi | PR:Q9JK66 |
Family and domain databases
DisProti | DP01850 |
InterProi | View protein in InterPro IPR002867, IBR_dom IPR003977, Parkin IPR041565, Parkin_Znf-RING IPR044066, TRIAD_supradom IPR000626, Ubiquitin-like_dom IPR029071, Ubiquitin-like_domsf IPR041170, Znf-RING_14 |
Pfami | View protein in Pfam PF01485, IBR, 1 hit PF00240, ubiquitin, 1 hit PF17976, zf-RING_12, 1 hit PF17978, zf-RING_14, 1 hit |
PIRSFi | PIRSF037880, Parkin, 1 hit |
PRINTSi | PR01475, PARKIN |
SMARTi | View protein in SMART SM00647, IBR, 2 hits SM00213, UBQ, 1 hit |
SUPFAMi | SSF54236, SSF54236, 1 hit |
PROSITEi | View protein in PROSITE PS51873, TRIAD, 1 hit PS50053, UBIQUITIN_2, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | PRKN_RAT | |
Accessioni | Q9JK66Primary (citable) accession number: Q9JK66 Secondary accession number(s): Q8K5C3 Q9JM64 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 11, 2004 |
Last sequence update: | October 1, 2000 | |
Last modified: | May 25, 2022 | |
This is version 163 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families