PINK1_HUMAN » Serine/threonine-protein kinase PINK1, mitochondrial

PINK1_HUMAN » Serine/threonine-protein kinase PINK1, mitochondrial
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Topology in Mitochondrial outer membrane
Topologyintermembrane space
cytoplasmic side
PINK1_HUMAN » Serine/threonine-protein kinase PINK1, mitochondrial » BRPK;PTEN-induced putative kinase protein 1;
Hydrophobic Thickness 30.6 ± 2.9 Å
Tilt Angle 5 ± 6°
ΔGtransfer -14.0 kcal/mol
ΔGfold -0.6 kcal/mol
Links UniProtKB, Pfam, Interpro, iHOP, STRING, HGNC, HMDB
Topology Out
TM Segments 95-116 (95-121)
Pathways

Parkinson's disease (KEGG)

PDB none
OPM none
Complexes none
Interactions

B2CL1, Complex: B2CL1:PINK1

B2CL2, Complex: B2CL2:PINK1

HTRA2, Complex: PINK1:HTRA2, PubMed

MCL1, Complex: MCL1:PINK1

MIRO1, Complex: PINK1:MIRO1, PubMed

MIRO2, Complex: MIRO2:TRAK1:PINK1

PGAM5, Complex: PINK1:PGAM5, PubMed

TOM20, Complex: PINK1:PRKN2:TOM20, PubMed

TOM22, Complex: PINK1:TOM22, PubMed

TOM70, Complex: TOM70:PINK1, PubMed

Domains

AA: 264-509, PDBID: 2HW6, Subunit B, Seq Identity:92%, Protein kinase domain

UniProt annotation for PINK1_HUMAN » Serine/threonine-protein kinase PINK1, mitochondrial
FUNCTION: 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 (PubMed, PubMed, PubMed, PubMed).

CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.

SUBUNIT: Interacts with PARK2. Interacts with FBXO7. Forms a complex with PARK2 and PARK7 (PubMed).

TISSUE SPECIFICITY: 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.

DISEASE: Parkinson disease 6 (PARK6) OMIM: 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. mutations affecting the gene represented in this entry.

UniProt features for PINK1_HUMAN » Serine/threonine-protein kinase PINK1, mitochondrial
TRANSIT 1 77 Mitochondrion (Potential).
CHAIN 78 581 Serine/threonine-protein kinase PINK1, mitochondrial.
DOMAIN 156 511 Protein kinase.
ACT_SITE 362 362 Proton acceptor (By similarity).
Amino Acid Sequence for PINK1_HUMAN » Serine/threonine-protein kinase PINK1, mitochondrial
MAVRQALGRG LQLGRALLLR FTGKPGRAYG LGRPGPAAGC VRGERPGWAA GPGAEPRRVG LGLPNRLRFF RQSVAGLAAR LQRQFVVRAW GCAGPCGRAV FLAFGLGLGL IEEKQAESRR AVSACQEIQA IFTQKSKPGP DPLDTRRLQG FRLEEYLIGQ SIGKGCSAAV YEATMPTLPQ NLEVTKSTGL LPGRGPGTSA PGEGQERAPG APAFPLAIKM MWNISAGSSS EAILNTMSQE LVPASRVALA GEYGAVTYRK SKRGPKQLAP HPNIIRVLRA FTSSVPLLPG ALVDYPDVLP SRLHPEGLGH GRTLFLVMKN YPCTLRQYLC VNTPSPRLAA MMLLQLLEGV DHLVQQGIAH RDLKSDNILV ELDPDGCPWL VIADFGCCLA DESIGLQLPF SSWYVDRGGN GCLMAPEVST ARPGPRAVID YSKADAWAVG AIAYEIFGLV NPFYGQGKAH LESRSYQEAQ LPALPESVPP DVRQLVRALL QREASKRPSA RVAANVLHLS LWGEHILALK NLKLDKMVGW LLQQSAATLL ANRLTEKCCV ETKMKMLFLA NLECETLCQA ALLLCSWRAA L