Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9BXM7

- PINK1_HUMAN

UniProt

Q9BXM7 - PINK1_HUMAN

Protein

Serine/threonine-protein kinase PINK1, mitochondrial

Gene

PINK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 PARK2. Targets PARK2 to dysfunctional depolarized mitochondria through the phosphorylation of MFN2. Activates PARK2 in 2 steps: (1) by mediating phosphorylation at 'Ser-65' of PARK2 and (2) mediating phosphorylation of ubiquitin, converting PARK2 to its fully-active form.10 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.1 Publication

    Cofactori

    Magnesium.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei186 – 1861ATPPROSITE-ProRule annotation
    Active sitei362 – 3621Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi162 – 1709ATPBy similarityPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. C3HC4-type RING finger domain binding Source: BHF-UCL
    3. calcium-dependent protein kinase activity Source: BHF-UCL
    4. kinase activity Source: MGI
    5. magnesium ion binding Source: UniProtKB
    6. protein binding Source: IntAct
    7. protein serine/threonine kinase activity Source: UniProtKB
    8. ubiquitin protein ligase binding Source: UniProtKB

    GO - Biological processi

    1. cell death Source: UniProtKB-KW
    2. cellular response to toxic substance Source: Ensembl
    3. intracellular signal transduction Source: UniProtKB
    4. mitochondrion degradation Source: UniProtKB
    5. negative regulation of neuron apoptotic process Source: Ensembl
    6. negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway Source: ParkinsonsUK-UCL
    7. peptidyl-serine phosphorylation Source: BHF-UCL
    8. positive regulation of dopamine secretion Source: Ensembl
    9. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: BHF-UCL
    10. positive regulation of release of cytochrome c from mitochondria Source: BHF-UCL
    11. positive regulation of synaptic transmission, dopaminergic Source: Ensembl
    12. protein phosphorylation Source: UniProtKB
    13. protein ubiquitination Source: UniProtKB
    14. regulation of protein complex assembly Source: BHF-UCL
    15. regulation of protein ubiquitination Source: BHF-UCL
    16. response to stress Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Autophagy

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    SignaLinkiQ9BXM7.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase PINK1, mitochondrial (EC:2.7.11.1)
    Alternative name(s):
    BRPK
    PTEN-induced putative kinase protein 1
    Gene namesi
    Name:PINK1
    OrganismiHomo sapiens (Human)Imported
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:14581. PINK1.

    Subcellular locationi

    GO - Cellular componenti

    1. chromatin Source: ParkinsonsUK-UCL
    2. cytoskeleton Source: ParkinsonsUK-UCL
    3. cytosol Source: UniProtKB
    4. integral component of membrane Source: UniProtKB-KW
    5. membrane Source: ParkinsonsUK-UCL
    6. mitochondrial inner membrane Source: ParkinsonsUK-UCL
    7. mitochondrial intermembrane space Source: ParkinsonsUK-UCL
    8. mitochondrial outer membrane Source: UniProtKB-SubCell
    9. mitochondrion Source: UniProtKB
    10. nucleus Source: ParkinsonsUK-UCL

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Mitochondrion, Mitochondrion outer membrane

    Pathology & Biotechi

    Involvement in diseasei

    Parkinson disease 6 (PARK6) [MIM:605909]: 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.17 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti92 – 921C → F in PARK6. 1 Publication
    VAR_046568
    Natural varianti125 – 1251C → G in PARK6. 1 Publication
    VAR_062773
    Natural varianti126 – 1261Q → P in PARK6; strongly reduces interaction with PARK2. 1 Publication
    VAR_064344
    Natural varianti147 – 1471R → H in PARK6; unknown pathological significance. 1 Publication
    VAR_046574
    Natural varianti168 – 1681A → P in PARK6; has reduced autophosphorylation activity compared to wild-type; localizes to the mitochondria and immunogold experiments reveal that both wild-type and mutant proteins face the mitochondrial intermembrane space. 2 Publications
    VAR_046575
    Natural varianti196 – 1961P → L in PARK6. 1 Publication
    VAR_046577
    Natural varianti217 – 2171A → D in PARK6. 1 Publication
    VAR_046578
    Natural varianti240 – 2401E → K in PARK6. 2 Publications
    VAR_046581
    Natural varianti268 – 2681L → V in PARK6. 2 Publications
    VAR_046584
    Natural varianti271 – 2711H → Q in PARK6. 1 Publication
    VAR_046585
    Natural varianti279 – 2791R → H in PARK6. 1 Publication
    VAR_046587
    Natural varianti280 – 2801A → T in PARK6; early-onset. 1 Publication
    VAR_062774
    Natural varianti309 – 3091G → D in PARK6; fails to maintain mitochondrial membrane potential; has reduced autophosphorylation activity compared to wild-type; strongly reduces interaction with PARK2. 1 Publication
    VAR_018994
    Natural varianti313 – 3131T → M in PARK6. 1 Publication
    VAR_046589
    Natural varianti347 – 3471L → P in PARK6; strongly reduces interaction with PARK2. 3 Publications
    VAR_046593
    Natural varianti369 – 3691L → P in PARK6. 1 Publication
    VAR_062775
    Natural varianti386 – 3861G → A in PARK6; abolishes kinase activity. 1 Publication
    VAR_062776
    Natural varianti388 – 3881C → R in PARK6. 1 Publication
    VAR_046596
    Natural varianti399 – 3991P → L in PARK6; digenic inheritance; associated with Ser-39 mutation in PARK7 gene. 1 Publication
    VAR_062777
    Natural varianti407 – 4071R → Q in PARK6; early-onset. 1 Publication
    VAR_062778
    Natural varianti409 – 4091G → V in PARK6. 1 Publication
    VAR_062779
    Natural varianti417 – 4171E → G in PARK6. 1 Publication
    VAR_046599
    Natural varianti464 – 4641R → H in PARK6. 1 Publication
    VAR_046605
    Natural varianti489 – 4891L → P in PARK6. 1 Publication
    VAR_046607
    Natural varianti534 – 5341Q → QQ in PARK6. 1 Publication
    VAR_046610

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi219 – 2191K → A: Abolishes MFN2 phosphorylation and interaction with PARK2; when associated with ALA-362 and ALA-384. 1 Publication
    Mutagenesisi362 – 3621D → A: Abolishes MFN2 phosphorylation and interaction with PARK2; when associated with ALA-219 and ALA-384. 1 Publication
    Mutagenesisi384 – 3841D → A: Abolishes MFN2 phosphorylation and interaction with PARK2; when associated with ALA-219 and ALA-362. 1 Publication

    Keywords - Diseasei

    Disease mutation, Neurodegeneration, Parkinson disease, Parkinsonism

    Organism-specific databases

    MIMi168600. phenotype.
    605909. phenotype.
    Orphaneti2828. Young adult-onset Parkinsonism.
    PharmGKBiPA33325.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 7777MitochondrionSequence AnalysisAdd
    BLAST
    Chaini78 – 581504Serine/threonine-protein kinase PINK1, mitochondrialPRO_0000024369Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei228 – 2281Phosphoserine; by autocatalysis1 Publication
    Modified residuei402 – 4021Phosphoserine; by autocatalysis1 Publication

    Post-translational modificationi

    Autophosphorylation at Ser-228 and Ser-402 is essential for Parkin/PARK2 recruitment to depolarized mitochondria.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ9BXM7.
    PRIDEiQ9BXM7.

    PTM databases

    PhosphoSiteiQ9BXM7.

    Expressioni

    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

    BgeeiQ9BXM7.
    CleanExiHS_PINK1.
    GenevestigatoriQ9BXM7.

    Organism-specific databases

    HPAiCAB026191.
    HPA001931.

    Interactioni

    Subunit structurei

    Interacts with PARK2. Interacts with FBXO7.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EEDO755306EBI-2846068,EBI-923794
    FBXO7Q9Y3I18EBI-2846068,EBI-1161222
    FBXO7Q9Y3I1-12EBI-2846068,EBI-9102965
    MAP1LC3BQ9GZQ83EBI-2846068,EBI-373144
    PARK2O602607EBI-2846068,EBI-716346
    RHOT1Q8IXI23EBI-2846068,EBI-1396430

    Protein-protein interaction databases

    BioGridi122376. 50 interactions.
    DIPiDIP-29427N.
    IntActiQ9BXM7. 11 interactions.
    MINTiMINT-6781189.
    STRINGi9606.ENSP00000364204.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9BXM7.
    SMRiQ9BXM7. Positions 246-545.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini78 – 9316Mitochondrial intermembraneSequence AnalysisAdd
    BLAST
    Topological domaini111 – 581471CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei94 – 11017HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini156 – 511356Protein kinaseCuratedPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transit peptide, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000231649.
    HOVERGENiHBG053601.
    InParanoidiQ9BXM7.
    KOiK05688.
    OMAiGPKQLAP.
    OrthoDBiEOG7TBC1R.
    PhylomeDBiQ9BXM7.
    TreeFamiTF313183.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 2 hits.
    PROSITEiPS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    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.

    « Hide

    MAVRQALGRG LQLGRALLLR FTGKPGRAYG LGRPGPAAGC VRGERPGWAA    50
    GPGAEPRRVG LGLPNRLRFF RQSVAGLAAR LQRQFVVRAW GCAGPCGRAV 100
    FLAFGLGLGL IEEKQAESRR AVSACQEIQA IFTQKSKPGP DPLDTRRLQG 150
    FRLEEYLIGQ SIGKGCSAAV YEATMPTLPQ NLEVTKSTGL LPGRGPGTSA 200
    PGEGQERAPG APAFPLAIKM MWNISAGSSS EAILNTMSQE LVPASRVALA 250
    GEYGAVTYRK SKRGPKQLAP HPNIIRVLRA FTSSVPLLPG ALVDYPDVLP 300
    SRLHPEGLGH GRTLFLVMKN YPCTLRQYLC VNTPSPRLAA MMLLQLLEGV 350
    DHLVQQGIAH RDLKSDNILV ELDPDGCPWL VIADFGCCLA DESIGLQLPF 400
    SSWYVDRGGN GCLMAPEVST ARPGPRAVID YSKADAWAVG AIAYEIFGLV 450
    NPFYGQGKAH LESRSYQEAQ LPALPESVPP DVRQLVRALL QREASKRPSA 500
    RVAANVLHLS LWGEHILALK NLKLDKMVGW LLQQSAATLL ANRLTEKCCV 550
    ETKMKMLFLA NLECETLCQA ALLLCSWRAA L 581
    Length:581
    Mass (Da):62,769
    Last modified:June 1, 2001 - v1
    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)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti209 – 2091P → A in AAH28215. (PubMed:15489334)Curated
    Sequence conflicti419 – 4191S → P in BAC11484. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti67 – 671L → F.1 Publication
    VAR_046566
    Natural varianti68 – 681R → P.1 Publication
    VAR_046567
    Natural varianti92 – 921C → F in PARK6. 1 Publication
    VAR_046568
    Natural varianti98 – 981R → W.1 Publication
    VAR_046569
    Natural varianti111 – 1111I → S.1 Publication
    VAR_046570
    Natural varianti115 – 1151Q → L.2 Publications
    Corresponds to variant rs148871409 [ dbSNP | Ensembl ].
    VAR_046571
    Natural varianti124 – 1241A → V.1 Publication
    VAR_046572
    Natural varianti125 – 1251C → G in PARK6. 1 Publication
    VAR_062773
    Natural varianti126 – 1261Q → P in PARK6; strongly reduces interaction with PARK2. 1 Publication
    VAR_064344
    Natural varianti145 – 1451T → M.1 Publication
    Corresponds to variant rs45604240 [ dbSNP | Ensembl ].
    VAR_046573
    Natural varianti147 – 1471R → H in PARK6; unknown pathological significance. 1 Publication
    VAR_046574
    Natural varianti148 – 1481L → W.1 Publication
    Corresponds to variant rs56297806 [ dbSNP | Ensembl ].
    VAR_041010
    Natural varianti168 – 1681A → P in PARK6; has reduced autophosphorylation activity compared to wild-type; localizes to the mitochondria and immunogold experiments reveal that both wild-type and mutant proteins face the mitochondrial intermembrane space. 2 Publications
    VAR_046575
    Natural varianti186 – 1861K → N.1 Publication
    VAR_046576
    Natural varianti196 – 1961P → L in PARK6. 1 Publication
    VAR_046577
    Natural varianti196 – 1961P → S.1 Publication
    Corresponds to variant rs35802484 [ dbSNP | Ensembl ].
    VAR_041011
    Natural varianti209 – 2091P → L.1 Publication
    Corresponds to variant rs34677717 [ dbSNP | Ensembl ].
    VAR_041012
    Natural varianti215 – 2151P → L in a glioblastoma multiforme sample; somatic mutation. 1 Publication
    VAR_041013
    Natural varianti217 – 2171A → D in PARK6. 1 Publication
    VAR_046578
    Natural varianti231 – 2311E → G.1 Publication
    VAR_046579
    Natural varianti235 – 2351N → I.1 Publication
    VAR_046580
    Natural varianti240 – 2401E → K in PARK6. 2 Publications
    VAR_046581
    Natural varianti257 – 2571T → I.
    VAR_046582
    Natural varianti263 – 2631R → G.1 Publication
    VAR_046583
    Natural varianti268 – 2681L → V in PARK6. 2 Publications
    VAR_046584
    Natural varianti271 – 2711H → Q in PARK6. 1 Publication
    VAR_046585
    Natural varianti276 – 2761R → Q.1 Publication
    VAR_046586
    Natural varianti279 – 2791R → H in PARK6. 1 Publication
    VAR_046587
    Natural varianti280 – 2801A → T in PARK6; early-onset. 1 Publication
    VAR_062774
    Natural varianti296 – 2961P → L.2 Publications
    VAR_046588
    Natural varianti305 – 3051P → L.
    Corresponds to variant rs7349186 [ dbSNP | Ensembl ].
    VAR_018993
    Natural varianti309 – 3091G → D in PARK6; fails to maintain mitochondrial membrane potential; has reduced autophosphorylation activity compared to wild-type; strongly reduces interaction with PARK2. 1 Publication
    VAR_018994
    Natural varianti313 – 3131T → M in PARK6. 1 Publication
    VAR_046589
    Natural varianti317 – 3171V → I.2 Publications
    Corresponds to variant rs200949139 [ dbSNP | Ensembl ].
    VAR_046590
    Natural varianti318 – 3181M → L.1 Publication
    VAR_046591
    Natural varianti322 – 3221P → L.1 Publication
    VAR_046592
    Natural varianti339 – 3391A → T.4 Publications
    Corresponds to variant rs55831733 [ dbSNP | Ensembl ].
    VAR_041014
    Natural varianti340 – 3401A → T.7 Publications
    Corresponds to variant rs3738136 [ dbSNP | Ensembl ].
    VAR_018995
    Natural varianti341 – 3411M → I.1 Publication
    Corresponds to variant rs35813094 [ dbSNP | Ensembl ].
    VAR_041015
    Natural varianti347 – 3471L → P in PARK6; strongly reduces interaction with PARK2. 3 Publications
    VAR_046593
    Natural varianti362 – 3621D → H.1 Publication
    VAR_046594
    Natural varianti369 – 3691L → P in PARK6. 1 Publication
    VAR_062775
    Natural varianti377 – 3771C → F.1 Publication
    Corresponds to variant rs34203620 [ dbSNP | Ensembl ].
    VAR_041016
    Natural varianti383 – 3831A → T.2 Publications
    Corresponds to variant rs45515602 [ dbSNP | Ensembl ].
    VAR_046595
    Natural varianti386 – 3861G → A in PARK6; abolishes kinase activity. 1 Publication
    VAR_062776
    Natural varianti388 – 3881C → R in PARK6. 1 Publication
    VAR_046596
    Natural varianti395 – 3951G → V.1 Publication
    VAR_046597
    Natural varianti399 – 3991P → L in PARK6; digenic inheritance; associated with Ser-39 mutation in PARK7 gene. 1 Publication
    VAR_062777
    Natural varianti407 – 4071R → Q in PARK6; early-onset. 1 Publication
    VAR_062778
    Natural varianti409 – 4091G → V in PARK6. 1 Publication
    VAR_062779
    Natural varianti411 – 4111G → S.1 Publication
    Corresponds to variant rs45478900 [ dbSNP | Ensembl ].
    VAR_046598
    Natural varianti417 – 4171E → G in PARK6. 1 Publication
    VAR_046599
    Natural varianti425 – 4251P → S.1 Publication
    VAR_046600
    Natural varianti431 – 4311Y → H May predispose to Parkinson disease development; shows decreased mitochondrial membrane potential under stress conditions. 1 Publication
    VAR_046601
    Natural varianti442 – 4421I → T.2 Publications
    VAR_046602
    Natural varianti451 – 4511N → S May predispose to Parkinson disease development; shows decreased mitochondrial membrane potential under stress conditions. 1 Publication
    VAR_046603
    Natural varianti461 – 4611L → S.1 Publication
    VAR_046604
    Natural varianti464 – 4641R → H in PARK6. 1 Publication
    VAR_046605
    Natural varianti476 – 4761E → K May predispose to Parkinson disease development; shows decreased mitochondrial membrane potential under stress conditions. 5 Publications
    Corresponds to variant rs115477764 [ dbSNP | Ensembl ].
    VAR_046606
    Natural varianti477 – 4771S → T.1 Publication
    Corresponds to variant rs34416410 [ dbSNP | Ensembl ].
    VAR_041017
    Natural varianti489 – 4891L → P in PARK6. 1 Publication
    VAR_046607
    Natural varianti501 – 5011R → P May predispose to Parkinson disease development; shows decreased mitochondrial membrane potential under stress conditions. 1 Publication
    VAR_046608
    Natural varianti521 – 5211N → T.7 Publications
    Corresponds to variant rs1043424 [ dbSNP | Ensembl ].
    VAR_018996
    Natural varianti525 – 5251D → N.2 Publications
    VAR_046609
    Natural varianti534 – 5341Q → QQ in PARK6. 1 Publication
    VAR_046610
    Natural varianti537 – 5371A → T.1 Publication
    VAR_046611
    Natural varianti575 – 5751C → R May predispose to Parkinson disease development; shows decreased mitochondrial membrane potential under stress conditions. 1 Publication
    VAR_046612

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 307307Missing in isoform 2. 1 PublicationVSP_050754Add
    BLAST
    Alternative sequencei308 – 32013LGHGR…LVMKN → MCGSQRPSPLSTS in isoform 2. 1 PublicationVSP_050755Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB053323 mRNA. Translation: BAB55647.1.
    AF316873 mRNA. Translation: AAK28062.1.
    AK075225 mRNA. Translation: BAC11484.1.
    AL391357 Genomic DNA. Translation: CAH73475.1.
    BC009534 mRNA. Translation: AAH09534.1.
    BC028215 mRNA. Translation: AAH28215.1.
    CCDSiCCDS211.1. [Q9BXM7-1]
    RefSeqiNP_115785.1. NM_032409.2. [Q9BXM7-1]
    UniGeneiHs.389171.

    Genome annotation databases

    EnsembliENST00000321556; ENSP00000364204; ENSG00000158828. [Q9BXM7-1]
    GeneIDi65018.
    KEGGihsa:65018.
    UCSCiuc001bdm.3. human. [Q9BXM7-1]
    uc001bdn.3. human. [Q9BXM7-2]

    Polymorphism databases

    DMDMi48428484.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB053323 mRNA. Translation: BAB55647.1 .
    AF316873 mRNA. Translation: AAK28062.1 .
    AK075225 mRNA. Translation: BAC11484.1 .
    AL391357 Genomic DNA. Translation: CAH73475.1 .
    BC009534 mRNA. Translation: AAH09534.1 .
    BC028215 mRNA. Translation: AAH28215.1 .
    CCDSi CCDS211.1. [Q9BXM7-1 ]
    RefSeqi NP_115785.1. NM_032409.2. [Q9BXM7-1 ]
    UniGenei Hs.389171.

    3D structure databases

    ProteinModelPortali Q9BXM7.
    SMRi Q9BXM7. Positions 246-545.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122376. 50 interactions.
    DIPi DIP-29427N.
    IntActi Q9BXM7. 11 interactions.
    MINTi MINT-6781189.
    STRINGi 9606.ENSP00000364204.

    PTM databases

    PhosphoSitei Q9BXM7.

    Polymorphism databases

    DMDMi 48428484.

    Proteomic databases

    PaxDbi Q9BXM7.
    PRIDEi Q9BXM7.

    Protocols and materials databases

    DNASUi 65018.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000321556 ; ENSP00000364204 ; ENSG00000158828 . [Q9BXM7-1 ]
    GeneIDi 65018.
    KEGGi hsa:65018.
    UCSCi uc001bdm.3. human. [Q9BXM7-1 ]
    uc001bdn.3. human. [Q9BXM7-2 ]

    Organism-specific databases

    CTDi 65018.
    GeneCardsi GC01P020959.
    GeneReviewsi PINK1.
    HGNCi HGNC:14581. PINK1.
    HPAi CAB026191.
    HPA001931.
    MIMi 168600. phenotype.
    605909. phenotype.
    608309. gene.
    neXtProti NX_Q9BXM7.
    Orphaneti 2828. Young adult-onset Parkinsonism.
    PharmGKBi PA33325.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000231649.
    HOVERGENi HBG053601.
    InParanoidi Q9BXM7.
    KOi K05688.
    OMAi GPKQLAP.
    OrthoDBi EOG7TBC1R.
    PhylomeDBi Q9BXM7.
    TreeFami TF313183.

    Enzyme and pathway databases

    SignaLinki Q9BXM7.

    Miscellaneous databases

    ChiTaRSi PINK1. human.
    GeneWikii PINK1.
    GenomeRNAii 65018.
    NextBioi 67218.
    PROi Q9BXM7.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9BXM7.
    CleanExi HS_PINK1.
    Genevestigatori Q9BXM7.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 2 hits.
    PROSITEi PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Growth-suppressive effects of BPOZ and EGR2, two genes involved in the PTEN signaling pathway."
      Unoki M., Nakamura Y.
      Oncogene 20:4457-4465(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Endometrium1 Publication.
    2. "BRPK, a novel protein kinase showing increased expression in mouse cancer cell lines with higher metastatic potential."
      Nakajima A., Kataoka K., Hong M., Sakaguchi M., Huh N.-H.
      Cancer Lett. 201:195-201(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AUTOPHOSPHORYLATION.
      Tissue: PlacentaImported.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANTS THR-340 AND THR-521.
      Tissue: PlacentaImported.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: LeukocyteImported and LungImported.
    6. Cited for: SUBCELLULAR LOCATION, MEMBRANE TOPOLOGY.
    7. "The PINK1/Parkin-mediated mitophagy is compromised by PD-associated mutations."
      Geisler S., Holmstrom K.M., Treis A., Skujat D., Weber S.S., Fiesel F.C., Kahle P.J., Springer W.
      Autophagy 6:871-878(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MITOCHONDRIAL AUTOPHAGY, SUBCELLULAR LOCATION, INTERACTION WITH PARK2, CHARACTERIZATION OF VARIANTS PARK6 PRO-126; ASP-309 AND PRO-347.
    8. "PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy."
      Matsuda N., Sato S., Shiba K., Okatsu K., Saisho K., Gautier C.A., Sou Y.S., Saiki S., Kawajiri S., Sato F., Kimura M., Komatsu M., Hattori N., Tanaka K.
      J. Cell Biol. 189:211-221(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MITOCHONDRIAL AUTOPHAGY.
    9. Cited for: FUNCTION IN MITOCHONDRIAL AUTOPHAGY, INTERACTION WITH PARK2.
    10. "PINK1 autophosphorylation upon membrane potential dissipation is essential for Parkin recruitment to damaged mitochondria."
      Okatsu K., Oka T., Iguchi M., Imamura K., Kosako H., Tani N., Kimura M., Go E., Koyano F., Funayama M., Shiba-Fukushima K., Sato S., Shimizu H., Fukunaga Y., Taniguchi H., Komatsu M., Hattori N., Mihara K., Tanaka K., Matsuda N.
      Nat. Commun. 3:1016-1016(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-228 AND SER-402.
    11. "Parkin-catalyzed ubiquitin-ester transfer is triggered by PINK1-dependent phosphorylation."
      Iguchi M., Kujuro Y., Okatsu K., Koyano F., Kosako H., Kimura M., Suzuki N., Uchiyama S., Tanaka K., Matsuda N.
      J. Biol. Chem. 288:22019-22032(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH FBXO7.
    13. "PINK1-phosphorylated mitofusin 2 is a Parkin receptor for culling damaged mitochondria."
      Chen Y., Dorn G.W. II
      Science 340:471-475(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MITOPHAGY, MUTAGENESIS OF LYS-219; ASP-362 AND ASP-384.
    14. Cited for: FUNCTION, CATALYTIC ACTIVITY, CHARACTERIZATION OF VARIANTS PARK6 PRO-168 AND ALA-386.
    15. "The mitochondrial deubiquitinase USP30 opposes parkin-mediated mitophagy."
      Bingol B., Tea J.S., Phu L., Reichelt M., Bakalarski C.E., Song Q., Foreman O., Kirkpatrick D.S., Sheng M.
      Nature 0:0-0(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. Cited for: VARIANTS PARK6 PHE-92; PRO-168 AND HIS-464, VARIANTS LEU-296; THR-340; THR-442; LYS-476; THR-521 AND ASN-525.
    17. Cited for: VARIANTS PARK6 GLN-271; PRO-347 AND GLY-417.
    18. Cited for: VARIANTS PARK6 LYS-240; PRO-347 AND PRO-489, VARIANTS GLY-231; ILE-235; GLY-263; LEU-318; THR-339; THR-340; HIS-362; SER-425; LYS-476 AND THR-521.
    19. Cited for: VARIANT PARK6 HIS-147.
    20. Cited for: VARIANT PARK6 ASP-309, CHARACTERIZATION OF VARIANT PARK6 ASP-309, FUNCTION, SUBCELLULAR LOCATION.
    21. Cited for: VARIANT PARK6 VAL-268.
    22. Cited for: VARIANTS PARK6 HIS-279 AND GLN-534 INS, VARIANT LEU-115.
    23. "Mitochondrial import and enzymatic activity of PINK1 mutants associated to recessive parkinsonism."
      Silvestri L., Caputo V., Bellacchio E., Atorino L., Dallapiccola B., Valente E.M., Casari G.
      Hum. Mol. Genet. 14:3477-3492(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANTS PARK6 PRO-168 AND ASP-309.
    24. "Clinicogenetic study of PINK1 mutations in autosomal recessive early-onset parkinsonism."
      Li Y., Tomiyama H., Sato K., Hatano Y., Yoshino H., Atsumi M., Kitaguchi M., Sasaki S., Kawaguchi S., Miyajima H., Toda T., Mizuno Y., Hattori N.
      Neurology 64:1955-1957(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PARK6 ARG-388.
    25. Cited for: VARIANTS PARK6 PRO-168 AND LEU-196, VARIANTS LEU-115; THR-340; LYS-476 AND THR-521.
    26. Cited for: VARIANTS ILE-317; THR-339; THR-383; SER-411; HIS-431; SER-451; SER-461; LYS-476; PRO-501 AND ARG-575, CHARACTERIZATION OF VARIANTS HIS-431; SER-451; LYS-476; PRO-501 AND ARG-575.
    27. "Juvenile-onset Parkinsonism as a result of the first mutation in the adenosine triphosphate orientation domain of PINK1."
      Leutenegger A.-L., Salih M.A.M., Ibanez P., Mukhtar M.M., Lesage S., Arabi A., Lohmann E., Duerr A., Ahmed A.E.M., Brice A.
      Arch. Neurol. 63:1257-1261(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PARK6 ASP-217.
    28. "T313M PINK1 mutation in an extended highly consanguineous Saudi family with early-onset Parkinson disease."
      Chishti M.A., Bohlega S., Ahmed M., Loualich A., Carroll P., Sato C., St George-Hyslop P., Westaway D., Rogaeva E.
      Arch. Neurol. 63:1483-1485(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PARK6 MET-313.
    29. "Mutational analysis of the PINK1 gene in early-onset parkinsonism in Europe and North Africa."
      The French Parkinson's disease genetics study group
      Ibanez P., Lesage S., Lohmann E., Thobois S., De Michele G., Borg M., Agid Y., Durr A., Brice A.
      Brain 129:686-694(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS PARK6 GLY-125; LYS-240; PRO-369; ALA-386 AND VAL-409.
    30. "Association of PINK1 and DJ-1 confers digenic inheritance of early-onset Parkinson's disease."
      Tang B., Xiong H., Sun P., Zhang Y., Wang D., Hu Z., Zhu Z., Ma H., Pan Q., Xia J.-H., Xia K., Zhang Z.
      Hum. Mol. Genet. 15:1816-1825(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PARK6 LEU-399.
    31. Cited for: VARIANT PARK6 THR-280, VARIANTS THR-340 AND THR-521.
    32. "Analysis of the PINK1 gene in a cohort of patients with sporadic early-onset parkinsonism in Taiwan."
      Fung H.-C., Chen C.-M., Hardy J., Singleton A.B., Lee-Chen G.-J., Wu Y.-R.
      Neurosci. Lett. 394:33-36(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PARK6 GLN-407, VARIANTS THR-340 AND THR-521.
    33. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] TRP-148; SER-196; LEU-209; LEU-215; THR-339; THR-340; ILE-341; PHE-377; THR-477 AND THR-521.
    34. Cited for: VARIANTS PHE-67; PRO-68; TRP-98; SER-111; VAL-124; MET-145; ASN-186; ILE-257 VAL-268; GLN-276; LEU-296; ILE-317; LEU-322; THR-339; THR-383; VAL-395; THR-442; LYS-476; ASN-525 AND THR-537.
    35. "Clinical and molecular characterisation of a Parkinson family with a novel PINK1 mutation."
      Prestel J., Gempel K., Hauser T.K., Schweitzer K., Prokisch H., Ahting U., Freudenstein D., Bueltmann E., Naegele T., Berg D., Klopstock T., Gasser T.
      J. Neurol. 255:643-648(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT PARK6 PRO-126.
    36. Cited for: VARIANT PARK6 PRO-347.

    Entry informationi

    Entry nameiPINK1_HUMAN
    AccessioniPrimary (citable) accession number: Q9BXM7
    Secondary accession number(s): Q8N6T9, Q8NBU3, Q96DE4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2004
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 131 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3