CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006485
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial 
Protein Synonyms/Alias
 PDHE1-A type I 
Gene Name
 Pdha1 
Gene Synonyms/Alias
 Pdha-1 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
39NDATFEIKKCDLHRLacetylation[1]
63LTREDGLKYYRMMQTacetylation[1, 2, 3, 4]
63LTREDGLKYYRMMQTsuccinylation[3]
77TVRRMELKADQLYKQacetylation[1, 2, 3, 4, 5, 6, 7]
77TVRRMELKADQLYKQsuccinylation[3]
83LKADQLYKQKIIRGFacetylation[1, 2, 3, 4, 5]
83LKADQLYKQKIIRGFsuccinylation[3]
244AASTDYYKRGDFIPGacetylation[1, 2, 3, 4]
244AASTDYYKRGDFIPGsuccinylation[3]
267LCVREATKFAAAYCRacetylation[1, 2, 4, 6]
277AAYCRSGKGPILMELacetylation[3]
277AAYCRSGKGPILMELsuccinylation[3]
313EIQEVRSKSDPIMLLacetylation[1, 2, 3, 4, 6]
313EIQEVRSKSDPIMLLsuccinylation[3]
321SDPIMLLKDRMVNSNacetylation[1, 2, 3, 4, 5, 6, 7, 8, 9, 10]
321SDPIMLLKDRMVNSNsuccinylation[3]
321SDPIMLLKDRMVNSNubiquitination[11]
385RGANQWIKFKSVS**acetylation[1, 2, 3]
385RGANQWIKFKSVS**succinylation[3]
385RGANQWIKFKSVS**ubiquitination[11]
Reference
 [1] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [2] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [4] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [5] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [6] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [7] 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]
 [8] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
 Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
 J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379]
 [9] Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice.
 Fritz KS, Galligan JJ, Hirschey MD, Verdin E, Petersen DR.
 J Proteome Res. 2012 Mar 2;11(3):1633-43. [PMID: 22309199]
 [10] Circadian acetylome reveals regulation of mitochondrial metabolic pathways.
 Masri S, Patel VR, Eckel-Mahan KL, Peleg S, Forne I, Ladurner AG, Baldi P, Imhof A, Sassone-Corsi P.
 Proc Natl Acad Sci U S A. 2013 Feb 26;110(9):3339-44. [PMID: 23341599]
 [11] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023
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. 
Sequence Annotation
 MOD_RES 232 232 Phosphoserine; by PDK1.
 MOD_RES 289 289 Phosphotyrosine.
 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.
 MOD_RES 321 321 N6-acetyllysine (By similarity).  
Keyword
 Acetylation; Carbohydrate metabolism; Complete proteome; Direct protein sequencing; Glucose metabolism; Mitochondrion; Oxidoreductase; Phosphoprotein; Pyruvate; Reference proteome; Thiamine pyrophosphate; Transit peptide; Tricarboxylic acid cycle. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 390 AA 
Protein Sequence
MRKMLAAVSR VLAGSAQKPA SRVLVASRNF ANDATFEIKK CDLHRLEEGP PVTTVLTRED 60
GLKYYRMMQT VRRMELKADQ LYKQKIIRGF CHLCDGQEAC CVGLEAGINP TDHLITAYRA 120
HGFTFTRGLP VRAILAELTG RRGGCAKGKG GSMHMYAKNF YGGNGIVGAQ VPLGAGIALA 180
CKYNGKDEVC LTLYGDGAAN QGQIFEAYNM AALWKLPCIF ICENNRYGMG TSVERAAAST 240
DYYKRGDFIP GLRVDGMDIL CVREATKFAA AYCRSGKGPI LMELQTYRYH GHSMSDPGVS 300
YRTREEIQEV RSKSDPIMLL KDRMVNSNLA SVEELKEIDV EVRKEIEDAA QFATADPEPP 360
LEELGYHIYS SDPPFEVRGA NQWIKFKSVS 390 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0045254; C:pyruvate dehydrogenase complex; ISS:UniProtKB.
 GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:EC.
 GO:0004738; F:pyruvate dehydrogenase activity; IMP:MGI.
 GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; ISS:UniProtKB.
 GO:0006096; P:glycolysis; IEA:InterPro.
 GO:0006099; P:tricarboxylic acid cycle; ISS:UniProtKB. 
Interpro
 IPR001017; DH_E1.
 IPR017597; Pyrv_DH_E1_asu_subgrp-y. 
Pfam
 PF00676; E1_dh 
SMART
  
PROSITE
  
PRINTS