dbPTM

ODPAT_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ODPAT_HUMAN
UniProt AC	P29803
Protein Name	Pyruvate dehydrogenase E1 component subunit alpha, testis-specific form, mitochondrial
Gene Name	PDHA2
Organism	Homo sapiens (Human).
Sequence Length	388
Subcellular Localization	Mitochondrion matrix.
Protein Description	The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links the glycolytic pathway to the tricarboxylic cycle..
Protein Sequence	MLAAFISRVLRRVAQKSARRVLVASRNSSNDATFEIKKCDLYLLEEGPPVTTVLTRAEGLKYYRMMLTVRRMELKADQLYKQKFIRGFCHLCDGQEACCVGLEAGINPSDHVITSYRAHGVCYTRGLSVRSILAELTGRRGGCAKGKGGSMHMYTKNFYGGNGIVGAQGPLGAGIALACKYKGNDEICLTLYGDGAANQGQIAEAFNMAALWKLPCVFICENNLYGMGTSTERAAASPDYYKRGNFIPGLKVDGMDVLCVREATKFAANYCRSGKGPILMELQTYRYHGHSMSDPGVSYRTREEIQEVRSKRDPIIILQDRMVNSKLATVEELKEIGAEVRKEIDDAAQFATTDPEPHLEELGHHIYSSDSSFEVRGANPWIKFKSVS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
16	Sumoylation	VLRRVAQKSARRVLV HHHHHHHHHHHEEEE	36.02	-
16	Sumoylation	VLRRVAQKSARRVLV HHHHHHHHHHHEEEE	36.02	-
37	Acetylation	NDATFEIKKCDLYLL CCCEEEEEECCEEEC	39.90	19864899
42	Phosphorylation	EIKKCDLYLLEEGPP EEEECCEEECCCCCC	8.93	-
62	Phosphorylation	TRAEGLKYYRMMLTV ECCCCHHHHHHHHHH	11.01	-
63	Phosphorylation	RAEGLKYYRMMLTVR CCCCHHHHHHHHHHH	7.16	-
75	Ubiquitination	TVRRMELKADQLYKQ HHHHHHHCHHHHHHH	36.29	23503661
75	Acetylation	TVRRMELKADQLYKQ HHHHHHHCHHHHHHH	36.29	2403231
81	Ubiquitination	LKADQLYKQKFIRGF HCHHHHHHHHCHHHH	56.45	23503661
81	Acetylation	LKADQLYKQKFIRGF HCHHHHHHHHCHHHH	56.45	2402041
128	Phosphorylation	VCYTRGLSVRSILAE EECCCCCCHHHHHHH	20.50	24719451
131	Phosphorylation	TRGLSVRSILAELTG CCCCCHHHHHHHHHC	21.57	28060719
150	Phosphorylation	CAKGKGGSMHMYTKN CCCCCCCCEEEEECC	17.74	30387612
154	Phosphorylation	KGGSMHMYTKNFYGG CCCCEEEEECCCCCC	10.41	22817900
155	Phosphorylation	GGSMHMYTKNFYGGN CCCEEEEECCCCCCC	16.37	30387612
180	Acetylation	AGIALACKYKGNDEI CCEEEEEEECCCCEE	44.37	25038526
225	Phosphorylation	FICENNLYGMGTSTE EEECCCCCCCCCCCC	13.74	25693802
229	Phosphorylation	NNLYGMGTSTERAAA CCCCCCCCCCCHHHC	24.47	25693802
230	Phosphorylation	NLYGMGTSTERAAAS CCCCCCCCCCHHHCC	23.65	22817900
231	Phosphorylation	LYGMGTSTERAAASP CCCCCCCCCHHHCCC	29.36	25693802
273	Phosphorylation	FAANYCRSGKGPILM HHHHHHHCCCCCEEE	41.10	21406692
275	Acetylation	ANYCRSGKGPILMEL HHHHHCCCCCEEEEE	63.86	30585241
284	Phosphorylation	PILMELQTYRYHGHS CEEEEEEEEEECCCC	23.69	26074081
285	Phosphorylation	ILMELQTYRYHGHSM EEEEEEEEEECCCCC	9.01	26074081
287	Phosphorylation	MELQTYRYHGHSMSD EEEEEEEECCCCCCC	11.18	22167270
291	Phosphorylation	TYRYHGHSMSDPGVS EEEECCCCCCCCCCC	25.27	20201521
293	Phosphorylation	RYHGHSMSDPGVSYR EECCCCCCCCCCCHH	43.60	29255136
298	Phosphorylation	SMSDPGVSYRTREEI CCCCCCCCHHCHHHH	18.14	22167270
299	Phosphorylation	MSDPGVSYRTREEIQ CCCCCCCHHCHHHHH	17.38	22167270
301	Phosphorylation	DPGVSYRTREEIQEV CCCCCHHCHHHHHHH	33.91	25884760
310	Phosphorylation	EEIQEVRSKRDPIII HHHHHHHHCCCCEEE	36.90	26437602
325	Phosphorylation	LQDRMVNSKLATVEE EEHHHCCCCCCCHHH	20.03	21406692
326	Acetylation	QDRMVNSKLATVEEL EHHHCCCCCCCHHHH	36.62	25038526
329	Phosphorylation	MVNSKLATVEELKEI HCCCCCCCHHHHHHH	38.60	21406692
334	Acetylation	LATVEELKEIGAEVR CCCHHHHHHHCHHHH	51.03	25038526
342	Acetylation	EIGAEVRKEIDDAAQ HHCHHHHHHHHHHHH	65.28	25038526

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
230	S	Phosphorylation	Kinase	PDK1	Q15118	GPS
291	S	Phosphorylation	Kinase	PDHK1	Q15118	PSP
291	S	Phosphorylation	Kinase	PDHK2	Q15119	PSP
291	S	Phosphorylation	Kinase	PDHK3	Q15120	PSP
291	S	Phosphorylation	Kinase	PDHK4	Q16654	PSP
298	S	Phosphorylation	Kinase	PDK1	Q15118	GPS
298	S	Phosphorylation	Kinase	PDK2	Q15119	GPS
298	S	Phosphorylation	Kinase	PDHK3	Q15120	PSP
298	S	Phosphorylation	Kinase	PDK4	Q16654	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
291	S	Phosphorylation	16436377
Phosphorylation at Ser-291, Ser-293 and Ser-298 by PDK family kinases inactivates the enzyme; for this phosphorylation at a single site is sufficient.
293	S	Phosphorylation	31536960
Phosphorylation at Ser-291, Ser-293 and Ser-298 by PDK family kinases inactivates the enzyme; for this phosphorylation at a single site is sufficient.
293	S	Phosphorylation	31536960
Phosphorylation at Ser-293 interferes with access to active site, and thereby inactivates the enzyme.
298	S	Phosphorylation	16436377
Phosphorylation at Ser-291, Ser-293 and Ser-298 by PDK family kinases inactivates the enzyme; for this phosphorylation at a single site is sufficient.

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 ODPAT_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of ODPAT_HUMAN !!

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 ODPAT_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291, AND MASSSPECTROMETRY.	19369195 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291 AND SER-298, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291, AND MASSSPECTROMETRY.	18088087 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291 AND SER-298, ANDMASS SPECTROMETRY.	17081983 [Abstract]
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-287 AND TYR-299, ANDMASS SPECTROMETRY.	18083107 [Abstract]

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