PDK1_HUMAN - dbPTM
PDK1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PDK1_HUMAN
UniProt AC Q15118
Protein Name [Pyruvate dehydrogenase (acetyl-transferring)] kinase isozyme 1, mitochondrial
Gene Name PDK1
Organism Homo sapiens (Human).
Sequence Length 436
Subcellular Localization Mitochondrion matrix .
Protein Description Kinase that plays a key role in regulation of glucose and fatty acid metabolism and homeostasis via phosphorylation of the pyruvate dehydrogenase subunits PDHA1 and PDHA2. This inhibits pyruvate dehydrogenase activity, and thereby regulates metabolite flux through the tricarboxylic acid cycle, down-regulates aerobic respiration and inhibits the formation of acetyl-coenzyme A from pyruvate. Plays an important role in cellular responses to hypoxia and is important for cell proliferation under hypoxia. Protects cells against apoptosis in response to hypoxia and oxidative stress..
Protein Sequence MRLARLLRGAALAGPGPGLRAAGFSRSFSSDSGSSPASERGVPGQVDFYARFSPSPLSMKQFLDFGSVNACEKTSFMFLRQELPVRLANIMKEISLLPDNLLRTPSVQLVQSWYIQSLQELLDFKDKSAEDAKAIYDFTDTVIRIRNRHNDVIPTMAQGVIEYKESFGVDPVTSQNVQYFLDRFYMSRISIRMLLNQHSLLFGGKGKGSPSHRKHIGSINPNCNVLEVIKDGYENARRLCDLYYINSPELELEELNAKSPGQPIQVVYVPSHLYHMVFELFKNAMRATMEHHANRGVYPPIQVHVTLGNEDLTVKMSDRGGGVPLRKIDRLFNYMYSTAPRPRVETSRAVPLAGFGYGLPISRLYAQYFQGDLKLYSLEGYGTDAVIYIKALSTDSIERLPVYNKAAWKHYNTNHEADDWCVPSREPKDMTTFRSA
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
25PhosphorylationGLRAAGFSRSFSSDS
CCCHHCCEECCCCCC
26.5412177059
35PhosphorylationFSSDSGSSPASERGV
CCCCCCCCCHHHCCC
28.1926437602
49PhosphorylationVPGQVDFYARFSPSP
CCCCEEEEEECCCCC
7.7528060719
67PhosphorylationKQFLDFGSVNACEKT
HHHHCCCCCCCCCCC
16.5219835603
133UbiquitinationDKSAEDAKAIYDFTD
CCCHHHHHHHHHHHH
47.87-
136PhosphorylationAEDAKAIYDFTDTVI
HHHHHHHHHHHHHHH
15.1825147952
230UbiquitinationCNVLEVIKDGYENAR
CCEEHHHHHHHHHHH
50.72-
243PhosphorylationARRLCDLYYINSPEL
HHHHHHEEEECCCCC
6.7725147952
244PhosphorylationRRLCDLYYINSPELE
HHHHHEEEECCCCCC
10.8318083107
268PhosphorylationGQPIQVVYVPSHLYH
CCCCEEEEECHHHHH
14.0522817900
319MethylationLTVKMSDRGGGVPLR
EEEEECCCCCCCCHH
38.05-
336PhosphorylationDRLFNYMYSTAPRPR
HHHHHHHHCCCCCCC
7.78-
338PhosphorylationLFNYMYSTAPRPRVE
HHHHHHCCCCCCCCC
24.16-
346PhosphorylationAPRPRVETSRAVPLA
CCCCCCCCCCCCCCC
22.2119835603
347PhosphorylationPRPRVETSRAVPLAG
CCCCCCCCCCCCCCC
12.5319835603
357PhosphorylationVPLAGFGYGLPISRL
CCCCCCCCCCCHHHH
17.1519835603
366PhosphorylationLPISRLYAQYFQGDL
CCHHHHHHHHHCCCE
11.3727251275
393PhosphorylationVIYIKALSTDSIERL
EEEEEECCCCCHHHC
34.7212177059
396PhosphorylationIKALSTDSIERLPVY
EEECCCCCHHHCCCC
26.8312177059
403PhosphorylationSIERLPVYNKAAWKH
CHHHCCCCCHHHHHH
14.7028060719
405UbiquitinationERLPVYNKAAWKHYN
HHCCCCCHHHHHHCC
23.07-
405SuccinylationERLPVYNKAAWKHYN
HHCCCCCHHHHHHCC
23.07-
405SuccinylationERLPVYNKAAWKHYN
HHCCCCCHHHHHHCC
23.07-
431PhosphorylationSREPKDMTTFRSA--
CCCCCCCCCCCCC--
32.6824719451

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
136YPhosphorylationKinaseFGFR1P11362
Uniprot
243YPhosphorylationKinaseABLP00519
PSP
243YPhosphorylationKinaseFGFR1P11362
Uniprot
243YPhosphorylationKinaseFLT3P36888
Uniprot
243YPhosphorylationKinaseJAK2O60674
Uniprot
244YPhosphorylationKinaseFGFR1P11362
Uniprot
338TPhosphorylationKinasePGK1P00558
PSP
346TPhosphorylationKinaseAKT1P31749
PSP
346TPhosphorylationKinaseAKT2P31751
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PDK1_HUMAN !!

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 PDK1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PDK2_HUMANPDK2physical
12573248
GNDS_HUMANRALGDSphysical
11889038
KS6B1_HUMANRPS6KB1physical
11733037
RPTOR_HUMANRPTORphysical
12150926
PKN2_HUMANPKN2physical
10753910
PKN1_HUMANPKN1physical
10753910
SGK1_HUMANSGK1physical
17314099
XRCC6_HUMANXRCC6physical
21900206
UBP4_HUMANUSP4physical
22347420
PDK1_HUMANPDK1physical
18003900
PDK2_HUMANPDK2physical
26186194
PDK3_HUMANPDK3physical
26186194
ODPX_HUMANPDHXphysical
26186194
ODPA_HUMANPDHA1physical
26186194
RPTOR_HUMANRPTORphysical
24516643
MTOR_HUMANMTORphysical
24516643
CO4A5_HUMANCOL4A5physical
26496610
HMGN1_HUMANHMGN1physical
26496610
MYH1_HUMANMYH1physical
26496610
PDK2_HUMANPDK2physical
26496610
PDK3_HUMANPDK3physical
26496610
SPG7_HUMANSPG7physical
26496610
STXB2_HUMANSTXBP2physical
26496610
MKNK1_HUMANMKNK1physical
26496610
CELF2_HUMANCELF2physical
26496610
SRCAP_HUMANSRCAPphysical
26496610
RASF8_HUMANRASSF8physical
26496610
RIMS1_HUMANRIMS1physical
26496610
VWA8_HUMANVWA8physical
26496610
COG4_HUMANCOG4physical
26496610
NECT3_HUMANPVRL3physical
26496610
P5CR2_HUMANPYCR2physical
26496610
NSF1C_HUMANNSFL1Cphysical
26496610
ZNFX1_HUMANZNFX1physical
26496610
VKOR1_HUMANVKORC1physical
26496610
ILKAP_HUMANILKAPphysical
26496610
TRI47_HUMANTRIM47physical
26496610
ATG4A_HUMANATG4Aphysical
26496610
NRBP2_HUMANNRBP2physical
26496610
ODPA_HUMANPDHA1physical
24486017
PDK2_HUMANPDK2physical
28514442
CRBN_HUMANCRBNphysical
28514442
ODPX_HUMANPDHXphysical
28514442
DENR_HUMANDENRphysical
28514442
ITB3_HUMANITGB3physical
10896934

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PDK1_HUMAN

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Related Literatures of Post-Translational Modification

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