PINK1_HUMAN - dbPTM
PINK1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PINK1_HUMAN
UniProt AC Q9BXM7
Protein Name Serine/threonine-protein kinase PINK1, mitochondrial
Gene Name PINK1
Organism Homo sapiens (Human).
Sequence Length 581
Subcellular Localization Mitochondrion outer membrane
Single-pass membrane protein . Mitochondrion inner membrane
Single-pass membrane protein . Cytoplasm, cytosol . Localizes mostly in mitochondrion and the 2 proteolytic processed fragments of 55 kDa and 48 kDa localize
Protein Description 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]
Protein Sequence MAVRQALGRGLQLGRALLLRFTGKPGRAYGLGRPGPAAGCVRGERPGWAAGPGAEPRRVGLGLPNRLRFFRQSVAGLAARLQRQFVVRAWGCAGPCGRAVFLAFGLGLGLIEEKQAESRRAVSACQEIQAIFTQKSKPGPDPLDTRRLQGFRLEEYLIGQSIGKGCSAAVYEATMPTLPQNLEVTKSTGLLPGRGPGTSAPGEGQERAPGAPAFPLAIKMMWNISAGSSSEAILNTMSQELVPASRVALAGEYGAVTYRKSKRGPKQLAPHPNIIRVLRAFTSSVPLLPGALVDYPDVLPSRLHPEGLGHGRTLFLVMKNYPCTLRQYLCVNTPSPRLAAMMLLQLLEGVDHLVQQGIAHRDLKSDNILVELDPDGCPWLVIADFGCCLADESIGLQLPFSSWYVDRGGNGCLMAPEVSTARPGPRAVIDYSKADAWAVGAIAYEIFGLVNPFYGQGKAHLESRSYQEAQLPALPESVPPDVRQLVRALLQREASKRPSARVAANVLHLSLWGEHILALKNLKLDKMVGWLLQQSAATLLANRLTEKCCVETKMKMLFLANLECETLCQAALLLCSWRAAL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
29PhosphorylationTGKPGRAYGLGRPGP
HCCCCCCCCCCCCCC
16.1227794612
135UbiquitinationIQAIFTQKSKPGPDP
HHHHHCCCCCCCCCC
58.3429967540
137UbiquitinationAIFTQKSKPGPDPLD
HHHCCCCCCCCCCCC
62.1129967540
161PhosphorylationEEYLIGQSIGKGCSA
HHHHHCCCCCCCCCH
28.2626471730
164UbiquitinationLIGQSIGKGCSAAVY
HHCCCCCCCCCHHHH
55.8929967540
186UbiquitinationPQNLEVTKSTGLLPG
CCCCEEEECCCCCCC
51.7221963094
198PhosphorylationLPGRGPGTSAPGEGQ
CCCCCCCCCCCCCCC
25.5026471730
199PhosphorylationPGRGPGTSAPGEGQE
CCCCCCCCCCCCCCC
38.0826471730
228PhosphorylationMWNISAGSSSEAILN
HHHCCCCCCHHHHHH
30.3322910362
257PhosphorylationAGEYGAVTYRKSKRG
CCCCCCCCEECCCCC
19.6426471730
258PhosphorylationGEYGAVTYRKSKRGP
CCCCCCCEECCCCCC
14.9426471730
262AcetylationAVTYRKSKRGPKQLA
CCCEECCCCCCCCCC
65.4930591343
284PhosphorylationVLRAFTSSVPLLPGA
HHHHHHCCCCCCCCC
25.38-
313PhosphorylationEGLGHGRTLFLVMKN
CCCCCCCEEEEEEEC
26.8422238344
319UbiquitinationRTLFLVMKNYPCTLR
CEEEEEEECCCCCHH
45.9421963094
402PhosphorylationGLQLPFSSWYVDRGG
CCCCCCCEEEEECCC
23.8619229105
433UbiquitinationRAVIDYSKADAWAVG
CEEEECCHHHHHHHH
44.02-
495PhosphorylationALLQREASKRPSARV
HHHHHHHHCCCCHHH
25.17-
547UbiquitinationLANRLTEKCCVETKM
HHHHHHHCHHHHHHH
27.9129967540

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
228SPhosphorylationKinasePRKAA2P54646
GPS
228SPhosphorylationKinasePINK1Q9BXM7
PSP
257TPhosphorylationKinasePINK1Q9BXM7
PSP
284SPhosphorylationKinasePRKAA2P54646
GPS
313TPhosphorylationKinaseMARK2Q7KZI7
PSP
402SPhosphorylationKinasePINK1Q9BXM7
PSP
495SPhosphorylationKinasePRKAA2P54646
GPS
-KUbiquitinationE3 ubiquitin ligasePRKNO60260
PMID:22724072
-KUbiquitinationE3 ubiquitin ligaseTRAF6Q9Y4K3
PMID:23885119

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
228SPhosphorylation

22910362
228Subiquitylation

22910362
402SPhosphorylation

22910362
402Subiquitylation

22910362

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PINK1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PRKN_HUMANPARK2physical
19358826
PINK1_HUMANPINK1physical
14607334
MAP1B_HUMANMAP1Bphysical
21151955
PRKDC_HUMANPRKDCphysical
21151955
IRS4_HUMANIRS4physical
21151955
KIF11_HUMANKIF11physical
21151955
PSMD1_HUMANPSMD1physical
21151955
PSMD2_HUMANPSMD2physical
21151955
HS90A_HUMANHSP90AA1physical
21151955
HSP74_HUMANHSPA4physical
21151955
TBA1A_HUMANTUBA1Aphysical
21151955
TBB5_HUMANTUBBphysical
21151955
CDC37_HUMANCDC37physical
21151955
PRS10_HUMANPSMC6physical
21151955
PGAM5_HUMANPGAM5physical
21151955
PARL_HUMANPARLphysical
21355049
MLP3A_HUMANMAP1LC3Aphysical
20153330
HS90A_HUMANHSP90AA1physical
18003639
CDC37_HUMANCDC37physical
18003639
HS90B_HUMANHSP90AB1physical
18003639
SYUA_HUMANSNCAphysical
19167501
HS90A_HUMANHSP90AA1physical
18359116
HSP74_HUMANHSPA4physical
18359116
CDC37_HUMANCDC37physical
18359116
PARK7_HUMANPARK7physical
16632486
HTRA2_HUMANHTRA2physical
17906618
PINK1_HUMANPINK1physical
22280891
TOM40_HUMANTOMM40physical
22280891
TOM70_HUMANTOMM70Aphysical
22280891
TOM22_HUMANTOMM22physical
22280891
TOM20_HUMANTOMM20physical
22280891
PRKN_HUMANPARK2physical
19229105
PARK7_HUMANPARK7physical
19229105
PRKN_HUMANPARK2physical
22724072
PINK1_HUMANPINK1physical
22724072
PRKN_HUMANPARK2physical
19880420
RICTR_HUMANRICTORphysical
21177249
SIN1_HUMANMAPKAP1physical
21177249
AKT1_HUMANAKT1physical
21177249
UBC12_HUMANUBE2Mphysical
22388932
CSN8_HUMANCOPS8physical
22388932
TRAF6_HUMANTRAF6physical
22643835
M3K7_HUMANMAP3K7physical
22643835
TOLIP_HUMANTOLLIPphysical
23244239
IRAK1_HUMANIRAK1physical
23244239
VIME_HUMANVIMphysical
23885119
SARM1_HUMANSARM1physical
23885119
RBCC1_HUMANRB1CC1physical
23885119
BAG2_HUMANBAG2physical
24513209
CRLS1_HUMANCRLS1physical
24703837
UBC_HUMANUBCphysical
24784582
UBC_HUMANUBCphysical
24751536
MIRO2_HUMANRHOT2physical
19152501
MIC60_HUMANIMMTphysical
19152501
ULA1_HUMANNAE1physical
22388932
PRKN_HUMANPARK2physical
24357652
PRKN_HUMANPARK2physical
19966284
TGM2_HUMANTGM2physical
25557247
PRKN_HUMANPARK2physical
25474007
UBC_HUMANUBCphysical
25474007
PRKN_HUMANPARK2physical
25591737
HCD2_HUMANHSD17B10physical
25591737
DNM1L_HUMANDNM1Lphysical
25591737
UBC_HUMANUBCphysical
25847540
PRKN_HUMANPARK2physical
26162776
UBC_HUMANUBCphysical
26162776
PRKN_HUMANPARK2physical
26116755
PRKN_HUMANPARK2physical
17052189
BAG5_HUMANBAG5physical
24475098
SYUA_HUMANSNCAphysical
27334109
BNIP3_HUMANBNIP3physical
27528605
HS90A_HUMANHSP90AA1physical
28438176
CDC37_HUMANCDC37physical
28438176
TOM40_HUMANTOMM40physical
28438176
UBC_HUMANUBCphysical
28438176

Drug and Disease Associations
Kegg Disease
H00057 Parkinson's disease (PD)
OMIM Disease
605909Parkinson disease 6 (PARK6)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PINK1_HUMAN

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Related Literatures of Post-Translational Modification

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