Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 149 (18 Sep 2019)
Sequence version 1 (01 Oct 2000)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

E3 ubiquitin-protein ligase parkin

Gene

Prkn

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Functions within a multiprotein E3 ubiquitin ligase complex, catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins, such as BCL2, SYT11, CCNE1, GPR37, RHOT1/MIRO1, MFN1, MFN2, STUB1, SNCAIP, SEPTIN5, TOMM20, USP30, ZNF746 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. Promotes the autophagic degradation of dysfunctional depolarized mitochondria (mitophagy) by promoting the ubiquitination of mitochondrial proteins such as TOMM20, RHOT1/MIRO1 and USP30. Preferentially assembles 'Lys-6'-, 'Lys-11'- and 'Lys-63'-linked polyubiquitin chains following mitochondrial damage, leading to mitophagy. Mediates 'Lys-48'-linked polyubiquitination of ZNF746, followed by degradation of ZNF746 by the proteasome; possibly playing a role in the regulation of neuron death. 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 similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

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. 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. 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.By similarity1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein ubiquitination

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 keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi238Zinc 1PROSITE-ProRule annotation1
Metal bindingi241Zinc 1PROSITE-ProRule annotation1
Metal bindingi253Zinc 2PROSITE-ProRule annotation1
Metal bindingi257Zinc 2; via pros nitrogenPROSITE-ProRule annotation1
Metal bindingi260Zinc 1PROSITE-ProRule annotation1
Metal bindingi263Zinc 1PROSITE-ProRule annotation1
Metal bindingi289Zinc 2PROSITE-ProRule annotation1
Metal bindingi293Zinc 2PROSITE-ProRule annotation1
Metal bindingi332Zinc 3PROSITE-ProRule annotation1
Metal bindingi337Zinc 3PROSITE-ProRule annotation1
Metal bindingi352Zinc 3PROSITE-ProRule annotation1
Metal bindingi360Zinc 3PROSITE-ProRule annotation1
Metal bindingi365Zinc 4PROSITE-ProRule annotation1
Metal bindingi368Zinc 4PROSITE-ProRule annotation1
Metal bindingi373Zinc 4; via tele nitrogenPROSITE-ProRule annotation1
Metal bindingi377Zinc 4PROSITE-ProRule annotation1
Metal bindingi418Zinc 5PROSITE-ProRule annotation1
Metal bindingi421Zinc 5PROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei431PROSITE-ProRule annotation1 Publication1
Metal bindingi436Zinc 5PROSITE-ProRule annotation1
Metal bindingi441Zinc 5PROSITE-ProRule annotation1
Metal bindingi446Zinc 6PROSITE-ProRule annotation1
Metal bindingi449Zinc 6PROSITE-ProRule annotation1
Metal bindingi457Zinc 6PROSITE-ProRule annotation1
Metal bindingi461Zinc 6; via tele nitrogenPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri141 – 225RING-type 0; atypicalAdd BLAST85
Zinc fingeri238 – 293RING-type 1PROSITE-ProRule annotationAdd BLAST56
Zinc fingeri313 – 377IBR-typePROSITE-ProRule annotationAdd BLAST65
Zinc fingeri418 – 449RING-type 2; atypicalPROSITE-ProRule annotationAdd BLAST32

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionTransferase
Biological processAutophagy, Transcription, Transcription regulation, Ubl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00143

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:PrknBy similarity
Synonyms:Park2Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
61797 Prkn

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Endoplasmic reticulum, Membrane, Mitochondrion, Nucleus, Postsynaptic cell membrane, Synapse

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi403W → A: Increased autoubiquitination. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000585781 – 465E3 ubiquitin-protein ligase parkinAdd BLAST465

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei65Phosphoserine; by PINK1By similarity1
Modified residuei80PhosphothreonineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Auto-ubiquitinates in an E2-dependent manner leading to its own degradation.1 Publication
S-nitrosylated.By similarity
Phosphorylation at Ser-65 by PINK1 contributes to activate PRKN activity. It is however not sufficient and requires binding to phosphorylated ubiquitin as well (By similarity).By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q9JK66

PRoteomics IDEntifications database

More...
PRIDEi
Q9JK66

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q9JK66

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q9JK66

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Largely confined to neuronal elements, including fibers and neuropil. Highly expressed at the forebrain level, in pyramidal cells of layer V, in various cortical regions and cerebellum. Expressed in the nucleus of diagonal band of Broca, nucleus basalis, bed nucleus of the stria terminalis, and olfactory tubercle. Moderate expression is seen in most neurons of the subthalamic nucleus, heart, skeletal muscle and testis. Moderate expression was found in frontal cortex, parietal cortex, cerebellum, heart, skeletal muscle and testis.1 Publication

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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.

Interacts with CHPF, the interaction 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 (By similarity).

Interacts with heat shock protein 70 family members, including HSPA1L, HSPA1A and HSPA8; interaction HSPA1L promotes translocation to damaged mitochondria (By similarity).

Interacts with BAG4 and, to a lesser extent, BAG5; interaction with BAG4 inhibits translocation to damaged mitochondria.

Interacts (when phosphorylated at Ser-65) with ubiquitin (phosphorylated); binding to phosphorylated ubiquitin is required to activate PRKN.

Forms a complex with PINK1 and PARK7 (By similarity).

By similarity

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
Ranbp2D4A0542EBI-973793,EBI-973937

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
248590, 16 interactors

Database of interacting proteins

More...
DIPi
DIP-37656N

Protein interaction database and analysis system

More...
IntActi
Q9JK66, 1 interactor

Molecular INTeraction database

More...
MINTi
Q9JK66

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000040511

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1465
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q9JK66

Database of comparative protein structure models

More...
ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q9JK66

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1 – 76Ubiquitin-likePROSITE-ProRule annotationAdd BLAST76

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni204 – 238SYT11 binding 1By similarityAdd BLAST35
Regioni234 – 465TRIAD supradomainPROSITE-ProRule annotationAdd BLAST232
Regioni257 – 293SYT11 binding 2By similarityAdd BLAST37
Regioni378 – 410REPAdd BLAST33

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The ubiquitin-like domain binds the PSMD4 subunit of 26S proteasomes.By similarity
The RING-type 1 zinc finger domain is required to repress p53/TP53 transcription.By similarity

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the RBR family. Parkin subfamily.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri141 – 225RING-type 0; atypicalAdd BLAST85
Zinc fingeri238 – 293RING-type 1PROSITE-ProRule annotationAdd BLAST56
Zinc fingeri313 – 377IBR-typePROSITE-ProRule annotationAdd BLAST65
Zinc fingeri418 – 449RING-type 2; atypicalPROSITE-ProRule annotationAdd BLAST32

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0006 Eukaryota
ENOG410YG4B LUCA

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q9JK66

KEGG Orthology (KO)

More...
KOi
K04556

Database of Orthologous Groups

More...
OrthoDBi
1140368at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q9JK66

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR031127 E3_UB_ligase_RBR
IPR002867 IBR_dom
IPR003977 Parkin
IPR041565 Parkin_Znf-RING
IPR029071 Ubiquitin-like_domsf
IPR000626 Ubiquitin_dom
IPR041170 Znf-RING_14

The PANTHER Classification System

More...
PANTHERi
PTHR11685 PTHR11685, 1 hit

Pfam protein domain database

More...
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

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF037880 Parkin, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01475 PARKIN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00647 IBR, 2 hits
SM00213 UBQ, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF54236 SSF54236, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51873 TRIAD, 1 hit
PS50053 UBIQUITIN_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (6)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 6 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: Q9JK66-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        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
Length:465
Mass (Da):51,709
Last modified:October 1, 2000 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iE13CF170AD6D042B
GO
Isoform 2 (identifier: Q9JK66-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     429-446: GGCMHMKCPQPQCKLEWC → ERMHVQYTMCIPGAHGGY
     447-465: Missing.

Show »
Length:446
Mass (Da):49,368
Checksum:iF06FAF788531DF5C
GO
Isoform 3 (identifier: Q9JK66-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-191: Missing.

Show »
Length:274
Mass (Da):30,642
Checksum:iB29BB58E86EB5DFE
GO
Isoform 4 (identifier: Q9JK66-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     57-57: Q → QHPQDGFCHKSHLAVHNLSQQDVTQ

Show »
Length:489
Mass (Da):54,418
Checksum:i49F53B8F358E2AB5
GO
Isoform 5 (identifier: Q9JK66-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     179-206: Missing.

Show »
Length:437
Mass (Da):48,734
Checksum:i3227286E41EBE5E3
GO
Isoform 6 (identifier: Q9JK66-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-191: Missing.
     390-394: AYRVD → EDVCT
     395-465: Missing.

Show »
Length:203
Mass (Da):22,288
Checksum:i3CFF551C49EB0783
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti24F → C in AAF34874 (PubMed:10686358).Curated1
Sequence conflicti138E → A in BAA92431 (Ref. 3) Curated1
Sequence conflicti348K → R in BAA92431 (Ref. 3) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0117171 – 191Missing in isoform 3 and isoform 6. 1 PublicationAdd BLAST191
Alternative sequenceiVSP_01171857Q → QHPQDGFCHKSHLAVHNLSQ QDVTQ in isoform 4. 1 Publication1
Alternative sequenceiVSP_011719179 – 206Missing in isoform 5. 1 PublicationAdd BLAST28
Alternative sequenceiVSP_011720390 – 394AYRVD → EDVCT in isoform 6. 1 Publication5
Alternative sequenceiVSP_011721395 – 465Missing in isoform 6. 1 PublicationAdd BLAST71
Alternative sequenceiVSP_011722429 – 446GGCMH…KLEWC → ERMHVQYTMCIPGAHGGY in isoform 2. 1 PublicationAdd BLAST18
Alternative sequenceiVSP_011723447 – 465Missing in isoform 2. 1 PublicationAdd BLAST19

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

NCBI Reference Sequences

More...
RefSeqi
NP_064478.1, NM_020093.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
56816

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:56816

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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
RefSeqiNP_064478.1, NM_020093.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KNBNMR-A1-76[»]
4K7DX-ray2.80A/B/C141-465[»]
4K95X-ray6.50A/B/C/D/E/F/G/H/I/J/K/L1-465[»]
4ZYNX-ray2.54A/B1-465[»]
SMRiQ9JK66
ModBaseiSearch...

Protein-protein interaction databases

BioGridi248590, 16 interactors
DIPiDIP-37656N
IntActiQ9JK66, 1 interactor
MINTiQ9JK66
STRINGi10116.ENSRNOP00000040511

PTM databases

iPTMnetiQ9JK66
PhosphoSitePlusiQ9JK66

Proteomic databases

PaxDbiQ9JK66
PRIDEiQ9JK66

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi56816
KEGGirno:56816

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5071
RGDi61797 Prkn

Phylogenomic databases

eggNOGiKOG0006 Eukaryota
ENOG410YG4B LUCA
InParanoidiQ9JK66
KOiK04556
OrthoDBi1140368at2759
PhylomeDBiQ9JK66

Enzyme and pathway databases

UniPathwayiUPA00143

Miscellaneous databases

EvolutionaryTraceiQ9JK66

Protein Ontology

More...
PROi
PR:Q9JK66

Family and domain databases

InterProiView protein in InterPro
IPR031127 E3_UB_ligase_RBR
IPR002867 IBR_dom
IPR003977 Parkin
IPR041565 Parkin_Znf-RING
IPR029071 Ubiquitin-like_domsf
IPR000626 Ubiquitin_dom
IPR041170 Znf-RING_14
PANTHERiPTHR11685 PTHR11685, 1 hit
PfamiView protein in Pfam
PF01485 IBR, 1 hit
PF00240 ubiquitin, 1 hit
PF17976 zf-RING_12, 1 hit
PF17978 zf-RING_14, 1 hit
PIRSFiPIRSF037880 Parkin, 1 hit
PRINTSiPR01475 PARKIN
SMARTiView protein in SMART
SM00647 IBR, 2 hits
SM00213 UBQ, 1 hit
SUPFAMiSSF54236 SSF54236, 1 hit
PROSITEiView protein in PROSITE
PS51873 TRIAD, 1 hit
PS50053 UBIQUITIN_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPRKN_RAT
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9JK66
Secondary accession number(s): Q8K5C3
, Q8K5C4, Q8K5C5, Q8K5C6, Q8VHY6, Q9JLL1, Q9JM64
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 1, 2000
Last modified: September 18, 2019
This is version 149 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again