Serine/threonine-protein kinase PINK1, mitochondrial

UniProt data

UniProt name: PINK1_HUMAN (Q9BXM7)

Gene name: PINK1

Organism: Homo sapiens (Human).

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:24660806, PubMed:24751536, PubMed:24784582, PubMed:25527291). {ECO:0000269|PubMed:14607334, ECO:0000269|PubMed:15087508, ECO:0000269|PubMed:19229105, ECO:0000269|PubMed:19966284, ECO:0000269|PubMed:20404107, ECO:0000269|PubMed:20798600, ECO:0000269|PubMed:23620051, ECO:0000269|PubMed:23754282, ECO:0000269|PubMed:23933751, ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:24896179, ECO:0000269|PubMed:25527291}.

Subcellular location: Mitochondrion outer membrane; Single-pass membrane protein {ECO:0000269|PubMed:15087508, ECO:0000269|PubMed:18687899, ECO:0000269|PubMed:19229105, ECO:0000269|PubMed:20798600, ECO:0000269|PubMed:23933751}. Cytoplasm, cytosol {ECO:0000269|PubMed:19229105, ECO:0000269|PubMed:20798600}. Note=Localizes mostly in mitochondrion and the 2 proteolytic processed fragments of 55 kDa and 48 kDa localize mainly in cytosol. {ECO:0000269|PubMed:19229105}.

Transmembrane domains:

  1. 94-110, 17 AA, Helical. {ECO:0000255}.

Sequence: 581 AA

10 20 30 40 50 60 MAVRQALGRG LQLGRALLLR FTGKPGRAYG LGRPGPAAGC VRGERPGWAA GPGAEPRRVG 70 80 90 100 110 120 LGLPNRLRFF RQSVAGLAAR LQRQFVVRAW GCAGPCGRAV FLAFGLGLGL IEEKQAESRR 130 140 150 160 170 180 AVSACQEIQA IFTQKSKPGP DPLDTRRLQG FRLEEYLIGQ SIGKGCSAAV YEATMPTLPQ 190 200 210 220 230 240 NLEVTKSTGL LPGRGPGTSA PGEGQERAPG APAFPLAIKM MWNISAGSSS EAILNTMSQE 250 260 270 280 290 300 LVPASRVALA GEYGAVTYRK SKRGPKQLAP HPNIIRVLRA FTSSVPLLPG ALVDYPDVLP 310 320 330 340 350 360 SRLHPEGLGH GRTLFLVMKN YPCTLRQYLC VNTPSPRLAA MMLLQLLEGV DHLVQQGIAH 370 380 390 400 410 420 RDLKSDNILV ELDPDGCPWL VIADFGCCLA DESIGLQLPF SSWYVDRGGN GCLMAPEVST 430 440 450 460 470 480 ARPGPRAVID YSKADAWAVG AIAYEIFGLV NPFYGQGKAH LESRSYQEAQ LPALPESVPP 490 500 510 520 530 540 DVRQLVRALL QREASKRPSA RVAANVLHLS LWGEHILALK NLKLDKMVGW LLQQSAATLL 550 560 570 580 ANRLTEKCCV ETKMKMLFLA NLECETLCQA ALLLCSWRAA L

CATM prediction

The sequence of PINK1_HUMAN returned 3 potential models

The positions at the dimer's interface are highlighted in yellow. The position at the crossing point is highlighted in orange.

# Sequence and interface d θ Z' ω' Score
           100       110 
    +    |    +    |   		 (Å) (°) (Å) (°)  
Model 1 GCAGACGRAVFLAFGLGLGLIEE 7.2 -28.0° 2.4 49.9 -32.5
Model 2 GCAGACGRAVFLAFGLGLGLIEE 6.6 -45.0° 0.2 44.9 -16.4
Model 3 GCAGACGRAVFLAFGLGLGLIEE 7.0 -46.0° 3.6 37.0 -15.3
Prolines* GCAGPCGRAVFLAFGLGLGLIEE          

* Note: this sequence contains Pro residues. CATM substituted them with Ala during the modeling. The positions are marked.

Click on the model number to visualize its details below.

MODEL 1 DETAILS

Precited structure:


Click on the image to enlarge

Download model 1 structure: PDB, PyMOL session

List of hydrogen bonds:

Donor Acceptor Distance
B, 102, LEU, HA A, 101, PHE, O 3.08Å
B, 105, GLY, HA1 A, 102, LEU, O 3.33Å
B, 106, LEU, HA A, 105, GLY, O 3.43Å
A, 102, LEU, HA B, 101, PHE, O 3.08Å
A, 105, GLY, HA1 B, 102, LEU, O 3.33Å
A, 106, LEU, HA B, 105, GLY, O 3.43Å