CPLM-002673

Genbank Nucleotide ID

Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial

Protein Synonyms/Alias

Homo sapiens (Human)

Position	Peptide	Type	References
39	NDATFEIKKCDLHRL	ubiquitination	[1]
63	LTREDGLKYYRMMQT	ubiquitination	[1]
77	TVRRMELKADQLYKQ	acetylation	[2, 3, 4]
77	TVRRMELKADQLYKQ	ubiquitination	[1]
83	LKADQLYKQKIIRGF	acetylation	[2, 4]
85	ADQLYKQKIIRGFCH	acetylation	[4]
244	AASTDYYKRGDFIPG	acetylation	[4]
244	AASTDYYKRGDFIPG	ubiquitination	[5, 6]
277	AAYCRSGKGPILMEL	ubiquitination	[1]
313	EIQEVRSKSDPIMLL	ubiquitination	[1]
321	SDPIMLLKDRMVNSN	acetylation	[2, 3, 4, 6]
321	SDPIMLLKDRMVNSN	ubiquitination	[1]
336	LASVEELKEIDVEVR	acetylation	[2, 4]
336	LASVEELKEIDVEVR	ubiquitination	[7]
385	RGANQWIKFKSVS**	acetylation	[4]
385	RGANQWIKFKSVS**	ubiquitination	[8]

[1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
[2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
[3] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
[4] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
PLoS One. 2012;7(12):e50545. [PMID: 23236377]
[5] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[6] Integrated proteomic analysis of post-translational modifications by serial enrichment.
Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
[7] Global identification of modular cullin-RING ligase substrates.
Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
[8] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]

Functional 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.

MOD_RES 232 232 Phosphoserine; by PDK1.
MOD_RES 289 289 Phosphotyrosine (By similarity).
MOD_RES 293 293 Phosphoserine; by PDK1, PDK2, PDK3 and
MOD_RES 300 300 Phosphoserine; by PDK1, PDK2, PDK3 and
MOD_RES 301 301 Phosphotyrosine (By similarity).
MOD_RES 321 321 N6-acetyllysine.

3D-structure; Acetylation; Alternative splicing; Carbohydrate metabolism; Complete proteome; Disease mutation; Glucose metabolism; Leigh syndrome; Mitochondrion; Oxidoreductase; Phosphoprotein; Polymorphism; Pyruvate; Reference proteome; Thiamine pyrophosphate; Transit peptide; Tricarboxylic acid cycle.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO:0045254; C:pyruvate dehydrogenase complex; IDA:UniProtKB.
GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:EC.
GO:0004738; F:pyruvate dehydrogenase activity; IDA:UniProtKB.
GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IDA:UniProtKB.
GO:0006096; P:glycolysis; IEA:InterPro.
GO:0010510; P:regulation of acetyl-CoA biosynthetic process from pyruvate; TAS:Reactome.
GO:0006099; P:tricarboxylic acid cycle; IDA:UniProtKB.

IPR001017; DH_E1.
IPR017597; Pyrv_DH_E1_asu_subgrp-y.