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Entry version 177 (05 Jun 2019)
Sequence version 1 (01 Jun 2001)
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Protein

Serine/threonine-protein kinase PINK1, mitochondrial

Gene

PINK1

Organism
Homo sapiens (Human)
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

Protects against mitochondrial dysfunction during cellular stress by phosphorylating mitochondrial proteins. Involved in the clearance of damaged mitochondria via selective autophagy (mitophagy) by mediating activation and translocation of PRKN (PubMed:14607334, PubMed:15087508, PubMed:19229105, PubMed:19966284, PubMed:20404107, PubMed:20798600, PubMed:23620051, PubMed:23754282, PubMed:23933751, PubMed:24660806, PubMed:24751536, PubMed:24784582, PubMed:24896179, PubMed:25527291). Targets PRKN to dysfunctional depolarized mitochondria through the phosphorylation of MFN2 (PubMed:23620051). Activates PRKN in 2 steps: (1) by mediating phosphorylation at 'Ser-65' of PRKN and (2) mediating phosphorylation of ubiquitin, converting PRKN to its fully-active form (PubMed:24660806, PubMed:24751536, PubMed:24784582, PubMed:25527291). Required for ubiquinone reduction by mitochondrial complex I by mediating phosphorylation of complex I subunit NDUFA10 (By similarity).By similarity14 Publications

<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 ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei186ATPPROSITE-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 sitei362Proton acceptorPROSITE-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 describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi162 – 170ATPPROSITE-ProRule annotationBy similarity9

<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 functionKinase, Serine/threonine-protein kinase, Transferase
Biological processAutophagy
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-5205685 Pink/Parkin Mediated Mitophagy
R-HSA-9614657 FOXO-mediated transcription of cell death genes

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...
SignaLinki
Q9BXM7

SIGNOR Signaling Network Open Resource

More...
SIGNORi
Q9BXM7

<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:
Serine/threonine-protein kinase PINK1, mitochondrial (EC:2.7.11.13 Publications)
Alternative name(s):
BRPK
PTEN-induced putative kinase protein 1
<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:PINK1
<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>OrganismiHomo sapiens (Human)Imported
<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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <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: Chromosome 1

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:14581 PINK1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
608309 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q9BXM7

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini78 – 93Mitochondrial intermembraneSequence analysisAdd BLAST16
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei94 – 110HelicalSequence analysisAdd BLAST17
Topological domaini111 – 581CytoplasmicSequence analysisAdd BLAST471

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion, Mitochondrion inner membrane, Mitochondrion outer membrane

<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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Parkinson disease 6 (PARK6)23 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn early-onset form of Parkinson disease, a neurodegenerative disorder characterized by parkinsonian signs such as rigidity, resting tremor and bradykinesia. A subset of patients manifest additional symptoms including hyperreflexia, autonomic instability, dementia and psychiatric disturbances. Symptoms show diurnal fluctuation and can improve after sleep. PARK6 pathogenesis involves respiratory complex I deficiency causing mitochondrial depolarization and dysfunction. Inheritance is autosomal recessive.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_04656892C → F in PARK6. 1 Publication1
Natural variantiVAR_062773125C → G in PARK6. 1 Publication1
Natural variantiVAR_064344126Q → P in PARK6; strongly reduces interaction with PRKN. 2 PublicationsCorresponds to variant dbSNP:rs775809722Ensembl.1
Natural variantiVAR_046574147R → H in PARK6; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs138050841Ensembl.1
Natural variantiVAR_046575168A → P in PARK6; no effect on autophosphorylation; localizes to the mitochondria and immunogold experiments reveal that both wild-type and mutant proteins face the mitochondrial intermembrane space. 4 PublicationsCorresponds to variant dbSNP:rs768091663EnsemblClinVar.1
Natural variantiVAR_078934170V → G in PARK6. 1 Publication1
Natural variantiVAR_046577196P → L in PARK6. 1 PublicationCorresponds to variant dbSNP:rs138302371EnsemblClinVar.1
Natural variantiVAR_046578217A → D in PARK6. 1 PublicationCorresponds to variant dbSNP:rs74315360EnsemblClinVar.1
Natural variantiVAR_046581240E → K in PARK6. 2 PublicationsCorresponds to variant dbSNP:rs573931674Ensembl.1
Natural variantiVAR_046584268L → V in PARK6. 2 PublicationsCorresponds to variant dbSNP:rs372280083EnsemblClinVar.1
Natural variantiVAR_046585271H → Q in PARK6. 1 PublicationCorresponds to variant dbSNP:rs28940284EnsemblClinVar.1
Natural variantiVAR_046587279R → H in PARK6. 1 PublicationCorresponds to variant dbSNP:rs74315358EnsemblClinVar.1
Natural variantiVAR_062774280A → T in PARK6; early-onset. 1 PublicationCorresponds to variant dbSNP:rs772510148Ensembl.1
Natural variantiVAR_018994309G → D in PARK6; fails to maintain mitochondrial membrane potential; full-length mutant has no effect on autophosphorylation; strongly reduces interaction with PRKN; decreases PRKN and SNCAIP ubiquitination and degradation. 4 PublicationsCorresponds to variant dbSNP:rs74315355EnsemblClinVar.1
Natural variantiVAR_046589313T → M in PARK6; decreases PRKN and SNCAIP ubiquitination and degradation. 2 PublicationsCorresponds to variant dbSNP:rs74315359EnsemblClinVar.1
Natural variantiVAR_046593347L → P in PARK6; strongly reduces interaction with PRKN. 4 PublicationsCorresponds to variant dbSNP:rs28940285EnsemblClinVar.1
Natural variantiVAR_062775369L → P in PARK6. 1 PublicationCorresponds to variant dbSNP:rs1195888869Ensembl.1
Natural variantiVAR_062776386G → A in PARK6; abolishes kinase activity. 2 Publications1
Natural variantiVAR_046596388C → R in PARK6. 1 Publication1
Natural variantiVAR_062778407R → Q in PARK6; early-onset. 1 PublicationCorresponds to variant dbSNP:rs556540177Ensembl.1
Natural variantiVAR_062779409G → V in PARK6. 1 Publication1
Natural variantiVAR_046599417E → G in PARK6. 1 Publication1
Natural variantiVAR_078935456 – 581Missing in PARK6. 1 PublicationAdd BLAST126
Natural variantiVAR_046605464R → H in PARK6. 1 PublicationCorresponds to variant dbSNP:rs764328076Ensembl.1
Natural variantiVAR_046607489L → P in PARK6. 1 Publication1
Natural variantiVAR_046610534Q → QQ in PARK6. 1 Publication1

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>Mutagenesisi219K → A: Abolishes MFN2 phosphorylation and interaction with PRKN; when associated with ALA-362 and ALA-384. 1 Publication1
Mutagenesisi362D → A: Abolishes MFN2 phosphorylation and interaction with PRKN; when associated with ALA-219 and ALA-384. 1 Publication1
Mutagenesisi384D → A: Abolishes MFN2 phosphorylation and interaction with PRKN; when associated with ALA-219 and ALA-362. 1 Publication1

Keywords - Diseasei

Disease mutation, Neurodegeneration, Parkinson disease, Parkinsonism, Primary mitochondrial disease

Organism-specific databases

DisGeNET

More...
DisGeNETi
65018

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
PINK1

MalaCards human disease database

More...
MalaCardsi
PINK1
MIMi168600 phenotype
605909 phenotype

Open Targets

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OpenTargetsi
ENSG00000158828

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
2828 Young-onset Parkinson disease

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA33325

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL3337330

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
PINK1

Domain mapping of disease mutations (DMDM)

More...
DMDMi
48428484

<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 transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 77MitochondrionSequence analysisAdd BLAST77
<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_000002436978 – 581Serine/threonine-protein kinase PINK1, mitochondrialAdd BLAST504

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 residuei228Phosphoserine; by autocatalysis1 Publication1
Modified residuei402Phosphoserine; by autocatalysis1 Publication1

<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

Autophosphorylation at Ser-228 and Ser-402 is essential for Parkin/PRKN recruitment to depolarized mitochondria.1 Publication
Two shorter forms of 55 kDa and 48 kDa seem to be produced by proteolytic cleavage and localize mainly in cytosol.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q9BXM7

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

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PaxDbi
Q9BXM7

PeptideAtlas

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PeptideAtlasi
Q9BXM7

PRoteomics IDEntifications database

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PRIDEi
Q9BXM7

ProteomicsDB human proteome resource

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ProteomicsDBi
79455
79456 [Q9BXM7-2]

PTM databases

CarbonylDB database of protein carbonylation sites

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CarbonylDBi
Q9BXM7

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q9BXM7

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

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PhosphoSitePlusi
Q9BXM7

<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

Highly expressed in heart, skeletal muscle and testis, and at lower levels in brain, placenta, liver, kidney, pancreas, prostate, ovary and small intestine. Present in the embryonic testis from an early stage of development.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000158828 Expressed in 236 organ(s), highest expression level in tendon

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q9BXM7 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB026191
HPA001931

<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

Interacts with PRKN. Interacts with FBXO7. Forms a complex with PRKN and PARK7 (PubMed:19229105).4 Publications

<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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
122376, 64 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q9BXM7

Database of interacting proteins

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DIPi
DIP-29427N

Protein interaction database and analysis system

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IntActi
Q9BXM7, 18 interactors

Molecular INTeraction database

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MINTi
Q9BXM7

STRING: functional protein association networks

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STRINGi
9606.ENSP00000364204

<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

3D structure databases

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

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SMRi
Q9BXM7

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<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>Domaini156 – 511Protein kinasePROSITE-ProRule annotationCuratedAdd BLAST356

<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 protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG4158 Eukaryota
ENOG410YE6P LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00390000001206

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000231649

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9BXM7

KEGG Orthology (KO)

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KOi
K05688

Identification of Orthologs from Complete Genome Data

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OMAi
CPWLVIT

Database of Orthologous Groups

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OrthoDBi
314975at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9BXM7

TreeFam database of animal gene trees

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TreeFami
TF313183

Family and domain databases

Conserved Domains Database

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CDDi
cd14018 STKc_PINK1, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR040110 PINK1_STKc
IPR000719 Prot_kinase_dom
IPR008271 Ser/Thr_kinase_AS

Pfam protein domain database

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Pfami
View protein in Pfam
PF00069 Pkinase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00220 S_TKc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 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 (2)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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <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 11 Publication (identifier: Q9BXM7-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

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MAVRQALGRG LQLGRALLLR FTGKPGRAYG LGRPGPAAGC VRGERPGWAA
60 70 80 90 100
GPGAEPRRVG LGLPNRLRFF RQSVAGLAAR LQRQFVVRAW GCAGPCGRAV
110 120 130 140 150
FLAFGLGLGL IEEKQAESRR AVSACQEIQA IFTQKSKPGP DPLDTRRLQG
160 170 180 190 200
FRLEEYLIGQ SIGKGCSAAV YEATMPTLPQ NLEVTKSTGL LPGRGPGTSA
210 220 230 240 250
PGEGQERAPG APAFPLAIKM MWNISAGSSS EAILNTMSQE LVPASRVALA
260 270 280 290 300
GEYGAVTYRK SKRGPKQLAP HPNIIRVLRA FTSSVPLLPG ALVDYPDVLP
310 320 330 340 350
SRLHPEGLGH GRTLFLVMKN YPCTLRQYLC VNTPSPRLAA MMLLQLLEGV
360 370 380 390 400
DHLVQQGIAH RDLKSDNILV ELDPDGCPWL VIADFGCCLA DESIGLQLPF
410 420 430 440 450
SSWYVDRGGN GCLMAPEVST ARPGPRAVID YSKADAWAVG AIAYEIFGLV
460 470 480 490 500
NPFYGQGKAH LESRSYQEAQ LPALPESVPP DVRQLVRALL QREASKRPSA
510 520 530 540 550
RVAANVLHLS LWGEHILALK NLKLDKMVGW LLQQSAATLL ANRLTEKCCV
560 570 580
ETKMKMLFLA NLECETLCQA ALLLCSWRAA L
Length:581
Mass (Da):62,769
Last modified:June 1, 2001 - 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:i721FE01F63263A64
GO
Isoform 2Curated (identifier: Q9BXM7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-307: Missing.
     308-320: LGHGRTLFLVMKN → MCGSQRPSPLSTS

Note: No experimental confirmation available.Curated
Show »
Length:274
Mass (Da):30,104
Checksum:iC54C628F879B4BED
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 conflicti209P → A in AAH28215 (PubMed:15489334).Curated1
Sequence conflicti419S → P in BAC11484 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04656667L → F1 PublicationCorresponds to variant dbSNP:rs763142730Ensembl.1
Natural variantiVAR_04656768R → P1 PublicationCorresponds to variant dbSNP:rs1385309950Ensembl.1
Natural variantiVAR_04656892C → F in PARK6. 1 Publication1
Natural variantiVAR_04656998R → W1 PublicationCorresponds to variant dbSNP:rs575668171Ensembl.1
Natural variantiVAR_046570111I → S1 Publication1
Natural variantiVAR_046571115Q → L2 PublicationsCorresponds to variant dbSNP:rs148871409EnsemblClinVar.1
Natural variantiVAR_046572124A → V1 PublicationCorresponds to variant dbSNP:rs1274588239Ensembl.1
Natural variantiVAR_062773125C → G in PARK6. 1 Publication1
Natural variantiVAR_064344126Q → P in PARK6; strongly reduces interaction with PRKN. 2 PublicationsCorresponds to variant dbSNP:rs775809722Ensembl.1
Natural variantiVAR_046573145T → M1 PublicationCorresponds to variant dbSNP:rs45604240EnsemblClinVar.1
Natural variantiVAR_046574147R → H in PARK6; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs138050841Ensembl.1
Natural variantiVAR_041010148L → W1 PublicationCorresponds to variant dbSNP:rs56297806Ensembl.1
Natural variantiVAR_046575168A → P in PARK6; no effect on autophosphorylation; localizes to the mitochondria and immunogold experiments reveal that both wild-type and mutant proteins face the mitochondrial intermembrane space. 4 PublicationsCorresponds to variant dbSNP:rs768091663EnsemblClinVar.1
Natural variantiVAR_078934170V → G in PARK6. 1 Publication1
Natural variantiVAR_046576186K → N1 PublicationCorresponds to variant dbSNP:rs143204084Ensembl.1
Natural variantiVAR_046577196P → L in PARK6. 1 PublicationCorresponds to variant dbSNP:rs138302371EnsemblClinVar.1
Natural variantiVAR_041011196P → S1 PublicationCorresponds to variant dbSNP:rs35802484Ensembl.1
Natural variantiVAR_041012209P → L1 PublicationCorresponds to variant dbSNP:rs34677717Ensembl.1
Natural variantiVAR_041013215P → L in a glioblastoma multiforme sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs371854396EnsemblClinVar.1
Natural variantiVAR_046578217A → D in PARK6. 1 PublicationCorresponds to variant dbSNP:rs74315360EnsemblClinVar.1
Natural variantiVAR_046579231E → G1 PublicationCorresponds to variant dbSNP:rs1303935100Ensembl.1
Natural variantiVAR_046580235N → I1 Publication1
Natural variantiVAR_046581240E → K in PARK6. 2 PublicationsCorresponds to variant dbSNP:rs573931674Ensembl.1
Natural variantiVAR_046582257T → I. Corresponds to variant dbSNP:rs370906995EnsemblClinVar.1
Natural variantiVAR_046583263R → G1 Publication1
Natural variantiVAR_046584268L → V in PARK6. 2 PublicationsCorresponds to variant dbSNP:rs372280083EnsemblClinVar.1
Natural variantiVAR_046585271H → Q in PARK6. 1 PublicationCorresponds to variant dbSNP:rs28940284EnsemblClinVar.1
Natural variantiVAR_046586276R → Q1 PublicationCorresponds to variant dbSNP:rs548506734Ensembl.1
Natural variantiVAR_046587279R → H in PARK6. 1 PublicationCorresponds to variant dbSNP:rs74315358EnsemblClinVar.1
Natural variantiVAR_062774280A → T in PARK6; early-onset. 1 PublicationCorresponds to variant dbSNP:rs772510148Ensembl.1
Natural variantiVAR_046588296P → L2 PublicationsCorresponds to variant dbSNP:rs779060308Ensembl.1
Natural variantiVAR_018993305P → L. Corresponds to variant dbSNP:rs7349186Ensembl.1
Natural variantiVAR_018994309G → D in PARK6; fails to maintain mitochondrial membrane potential; full-length mutant has no effect on autophosphorylation; strongly reduces interaction with PRKN; decreases PRKN and SNCAIP ubiquitination and degradation. 4 PublicationsCorresponds to variant dbSNP:rs74315355EnsemblClinVar.1
Natural variantiVAR_046589313T → M in PARK6; decreases PRKN and SNCAIP ubiquitination and degradation. 2 PublicationsCorresponds to variant dbSNP:rs74315359EnsemblClinVar.1
Natural variantiVAR_046590317V → I2 PublicationsCorresponds to variant dbSNP:rs200949139Ensembl.1
Natural variantiVAR_046591318M → L1 PublicationCorresponds to variant dbSNP:rs139226733EnsemblClinVar.1
Natural variantiVAR_046592322P → L1 PublicationCorresponds to variant dbSNP:rs768019187Ensembl.1
Natural variantiVAR_041014339A → T4 PublicationsCorresponds to variant dbSNP:rs55831733EnsemblClinVar.1
Natural variantiVAR_018995340A → T7 PublicationsCorresponds to variant dbSNP:rs3738136EnsemblClinVar.1
Natural variantiVAR_041015341M → I1 PublicationCorresponds to variant dbSNP:rs35813094Ensembl.1
Natural variantiVAR_046593347L → P in PARK6; strongly reduces interaction with PRKN. 4 PublicationsCorresponds to variant dbSNP:rs28940285EnsemblClinVar.1
Natural variantiVAR_046594362D → H1 Publication1
Natural variantiVAR_062775369L → P in PARK6. 1 PublicationCorresponds to variant dbSNP:rs1195888869Ensembl.1
Natural variantiVAR_041016377C → F1 PublicationCorresponds to variant dbSNP:rs34203620Ensembl.1
Natural variantiVAR_046595383A → T2 PublicationsCorresponds to variant dbSNP:rs45515602EnsemblClinVar.1
Natural variantiVAR_062776386G → A in PARK6; abolishes kinase activity. 2 Publications1
Natural variantiVAR_046596388C → R in PARK6. 1 Publication1
Natural variantiVAR_046597395G → V1 PublicationCorresponds to variant dbSNP:rs1035071310Ensembl.1
Natural variantiVAR_062777399P → L Probable disease-associated mutation found in early-onset Parkinson disease with digenic inheritance; found in a patient also carrying mutation S-39 in PARK7; decreases PRKN and SNCAIP ubiquitination and degradation. 2 PublicationsCorresponds to variant dbSNP:rs119451946EnsemblClinVar.1
Natural variantiVAR_062778407R → Q in PARK6; early-onset. 1 PublicationCorresponds to variant dbSNP:rs556540177Ensembl.1
Natural variantiVAR_062779409G → V in PARK6. 1 Publication1
Natural variantiVAR_046598411G → S1 PublicationCorresponds to variant dbSNP:rs45478900Ensembl.1
Natural variantiVAR_046599417E → G in PARK6. 1 Publication1
Natural variantiVAR_046600425P → S1 PublicationCorresponds to variant dbSNP:rs554114655Ensembl.1
Natural variantiVAR_046601431Y → H May predispose to Parkinson disease development; shows decreased mitochondrial membrane potential under stress conditions. 1 PublicationCorresponds to variant dbSNP:rs74315361EnsemblClinVar.1
Natural variantiVAR_046602442I → T2 Publications1
Natural variantiVAR_046603451N → S May predispose to Parkinson disease development; shows decreased mitochondrial membrane potential under stress conditions. 1 Publication