dbPTM

ODPA_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ODPA_MOUSE
UniProt AC	P35486
Protein Name	Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
Gene Name	Pdha1
Organism	Mus musculus (Mouse).
Sequence Length	390
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	MRKMLAAVSRVLAGSAQKPASRVLVASRNFANDATFEIKKCDLHRLEEGPPVTTVLTREDGLKYYRMMQTVRRMELKADQLYKQKIIRGFCHLCDGQEACCVGLEAGINPTDHLITAYRAHGFTFTRGLPVRAILAELTGRRGGCAKGKGGSMHMYAKNFYGGNGIVGAQVPLGAGIALACKYNGKDEVCLTLYGDGAANQGQIFEAYNMAALWKLPCIFICENNRYGMGTSVERAAASTDYYKRGDFIPGLRVDGMDILCVREATKFAAAYCRSGKGPILMELQTYRYHGHSMSDPGVSYRTREEIQEVRSKSDPIMLLKDRMVNSNLASVEELKEIDVEVRKEIEDAAQFATADPEPPLEELGYHIYSSDPPFEVRGANQWIKFKSVS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
39	Acetylation	NDATFEIKKCDLHRL CCCEEEEEECCHHHC	39.90	23576753
41	S-nitrosylation	ATFEIKKCDLHRLEE CEEEEEECCHHHCCC	5.98	21278135
41	S-nitrosocysteine	ATFEIKKCDLHRLEE CEEEEEECCHHHCCC	5.98	-
41	S-palmitoylation	ATFEIKKCDLHRLEE CEEEEEECCHHHCCC	5.98	26165157
63	Succinylation	LTREDGLKYYRMMQT EECHHHHHHHHHHHH	45.85	23806337
63	Acetylation	LTREDGLKYYRMMQT EECHHHHHHHHHHHH	45.85	23576753
63	Succinylation	LTREDGLKYYRMMQT EECHHHHHHHHHHHH	45.85	-
70	Phosphorylation	KYYRMMQTVRRMELK HHHHHHHHHHHHHHC	9.70	28576409
77	Acetylation	TVRRMELKADQLYKQ HHHHHHHCHHHHHHH	36.29	23864654
77	Succinylation	TVRRMELKADQLYKQ HHHHHHHCHHHHHHH	36.29	23806337
83	Succinylation	LKADQLYKQKIIRGF HCHHHHHHHHHHHHH	54.42	23806337
83	Acetylation	LKADQLYKQKIIRGF HCHHHHHHHHHHHHH	54.42	23864654
83	Glutarylation	LKADQLYKQKIIRGF HCHHHHHHHHHHHHH	54.42	24703693
83	Malonylation	LKADQLYKQKIIRGF HCHHHHHHHHHHHHH	54.42	26320211
85	Acetylation	ADQLYKQKIIRGFCH HHHHHHHHHHHHHHH	35.63	6269763
91	S-nitrosylation	QKIIRGFCHLCDGQE HHHHHHHHHHCCCCC	2.39	24895380
94	S-nitrosylation	IRGFCHLCDGQEACC HHHHHHHCCCCCEEE	2.16	24895380
100	S-nitrosylation	LCDGQEACCVGLEAG HCCCCCEEEEEECCC	1.58	24895380
101	S-nitrosylation	CDGQEACCVGLEAGI CCCCCEEEEEECCCC	3.33	24895380
181	S-nitrosylation	GAGIALACKYNGKDE CCCEEEEEEECCCCE	5.10	21278135
181	S-palmitoylation	GAGIALACKYNGKDE CCCEEEEEEECCCCE	5.10	28680068
181	S-nitrosocysteine	GAGIALACKYNGKDE CCCEEEEEEECCCCE	5.10	-
218	S-nitrosylation	AALWKLPCIFICENN HHHHCCCEEEEECCC	6.02	22588120
222	S-nitrosylation	KLPCIFICENNRYGM CCCEEEEECCCCCCC	2.97	22588120
227	Phosphorylation	FICENNRYGMGTSVE EEECCCCCCCCCHHH	17.37	23527152
231	Phosphorylation	NNRYGMGTSVERAAA CCCCCCCCHHHHHHC	22.25	27742792
232	Phosphorylation	NRYGMGTSVERAAAS CCCCCCCHHHHHHCC	19.09	26824392
239	Phosphorylation	SVERAAASTDYYKRG HHHHHHCCCCHHHCC	19.65	23984901
240	Phosphorylation	VERAAASTDYYKRGD HHHHHCCCCHHHCCC	24.24	23984901
242	Phosphorylation	RAAASTDYYKRGDFI HHHCCCCHHHCCCCC	15.81	26643407
243	Phosphorylation	AAASTDYYKRGDFIP HHCCCCHHHCCCCCC	9.30	25367039
244	Succinylation	AASTDYYKRGDFIPG HCCCCHHHCCCCCCC	43.61	-
244	Succinylation	AASTDYYKRGDFIPG HCCCCHHHCCCCCCC	43.61	23806337
244	Acetylation	AASTDYYKRGDFIPG HCCCCHHHCCCCCCC	43.61	23576753
261	S-palmitoylation	VDGMDILCVREATKF CCCEEEEEEEHHHHH	2.50	28526873
261	S-nitrosylation	VDGMDILCVREATKF CCCEEEEEEEHHHHH	2.50	24895380
261	S-nitrosocysteine	VDGMDILCVREATKF CCCEEEEEEEHHHHH	2.50	-
266	Phosphorylation	ILCVREATKFAAAYC EEEEEHHHHHHHHHH	23.18	22418434
267	Acetylation	LCVREATKFAAAYCR EEEEHHHHHHHHHHH	39.80	23576753
273	S-nitrosocysteine	TKFAAAYCRSGKGPI HHHHHHHHHCCCCCE	2.09	-
273	S-nitrosylation	TKFAAAYCRSGKGPI HHHHHHHHHCCCCCE	2.09	21278135
273	S-palmitoylation	TKFAAAYCRSGKGPI HHHHHHHHHCCCCCE	2.09	28526873
277	Succinylation	AAYCRSGKGPILMEL HHHHHCCCCCEEEEE	63.86	-
277	Succinylation	AAYCRSGKGPILMEL HHHHHCCCCCEEEEE	63.86	23806337
277	Acetylation	AAYCRSGKGPILMEL HHHHHCCCCCEEEEE	63.86	23806337
289	Phosphorylation	MELQTYRYHGHSMSD EEEEEEEECCCCCCC	11.18	27087446
293	Phosphorylation	TYRYHGHSMSDPGVS EEEECCCCCCCCCCC	25.27	27087446
295	Phosphorylation	RYHGHSMSDPGVSYR EECCCCCCCCCCCHH	43.60	27087446
300	Phosphorylation	SMSDPGVSYRTREEI CCCCCCCCHHCHHHH	18.14	27087446
301	Phosphorylation	MSDPGVSYRTREEIQ CCCCCCCHHCHHHHH	17.38	25521595
303	Phosphorylation	DPGVSYRTREEIQEV CCCCCHHCHHHHHHH	33.91	26643407
313	Acetylation	EIQEVRSKSDPIMLL HHHHHHHCCCCEEHH	48.60	23806337
313	Succinylation	EIQEVRSKSDPIMLL HHHHHHHCCCCEEHH	48.60	-
313	Succinylation	EIQEVRSKSDPIMLL HHHHHHHCCCCEEHH	48.60	23806337
314	Phosphorylation	IQEVRSKSDPIMLLK HHHHHHCCCCEEHHH	50.28	22817900
321	Acetylation	SDPIMLLKDRMVNSN CCCEEHHHHHHHCCC	39.05	23576753
321	Glutarylation	SDPIMLLKDRMVNSN CCCEEHHHHHHHCCC	39.05	24703693
321	Succinylation	SDPIMLLKDRMVNSN CCCEEHHHHHHHCCC	39.05	-
321	Ubiquitination	SDPIMLLKDRMVNSN CCCEEHHHHHHHCCC	39.05	-
331	Phosphorylation	MVNSNLASVEELKEI HHCCCCCCHHHHHHC	32.97	27180971
336	Acetylation	LASVEELKEIDVEVR CCCHHHHHHCCHHHH	56.77	23835326
336	Succinylation	LASVEELKEIDVEVR CCCHHHHHHCCHHHH	56.77	26388266
344	Succinylation	EIDVEVRKEIEDAAQ HCCHHHHHHHHHHHH	69.12	23954790
385	Succinylation	RGANQWIKFKSVS-- CCCCCEEEEEECC--	43.72	-
385	Acetylation	RGANQWIKFKSVS-- CCCCCEEEEEECC--	43.72	23954790
385	Succinylation	RGANQWIKFKSVS-- CCCCCEEEEEECC--	43.72	23806337
385	Ubiquitination	RGANQWIKFKSVS-- CCCCCEEEEEECC--	43.72	-

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
232	S	Phosphorylation	Kinase	PDHK1	Q15118	PSP
232	S	Phosphorylation	Kinase	PDK1	Q8BFP9	Uniprot
232	S	Phosphorylation	Kinase	PDHK2	Q15119	PSP
293	S	Phosphorylation	Kinase	PDK1	Q8BFP9	Uniprot
293	S	Phosphorylation	Kinase	PDK2	Q9JK42	Uniprot
293	S	Phosphorylation	Kinase	PDHK3	Q15120	PSP
293	S	Phosphorylation	Kinase	PDK3	Q922H2	Uniprot
293	S	Phosphorylation	Kinase	PDHK4	Q16654	PSP
293	S	Phosphorylation	Kinase	PDK4	O70571	Uniprot
300	S	Phosphorylation	Kinase	PDK1	Q8BFP9	Uniprot
300	S	Phosphorylation	Kinase	PDK2	Q9JK42	Uniprot
300	S	Phosphorylation	Kinase	PDK3	Q922H2	Uniprot
300	S	Phosphorylation	Kinase	PDHK4	Q16654	PSP
300	S	Phosphorylation	Kinase	PDK4	O70571	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
232	S	Phosphorylation	17208939
Phosphorylation at Ser-232, Ser-293 and Ser-300 by PDK family kinases inactivates the enzyme; for this phosphorylation at a single site is sufficient.
293	S	Phosphorylation	17208939
Phosphorylation at Ser-232, Ser-293 and Ser-300 by PDK family kinases inactivates the enzyme; for this phosphorylation at a single site is sufficient.
293	S	Phosphorylation	17208939
Phosphorylation at Ser-293 interferes with access to active site, and thereby inactivates the enzyme.
300	S	Phosphorylation	17242355
Phosphorylation at Ser-232, Ser-293 and Ser-300 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 ODPA_MOUSE !!

Protein-Protein Interaction

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

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of ODPA_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293 AND SER-300, ANDMASS SPECTROMETRY.	19367708 [Abstract]
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232; TYR-289; SER-293AND SER-300, AND MASS SPECTROMETRY.	17242355 [Abstract]
"Mitochondrial phosphoproteome revealed by an improved IMAC method andMS/MS/MS."; Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.; Mol. Cell. Proteomics 6:669-676(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-232; SER-293 ANDSER-300, AND MASS SPECTROMETRY.	17208939 [Abstract]
"Proteomic analysis of in vivo phosphorylated synaptic proteins."; Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I.,Blackstock W.P., Choudhary J.S., Grant S.G.; J. Biol. Chem. 280:5972-5982(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293, AND MASSSPECTROMETRY.	15572359 [Abstract]
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain."; Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; J. Proteome Res. 7:311-318(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-301, AND MASSSPECTROMETRY.	18034455 [Abstract]

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