UniProt Accession

 ODPA_HUMAN; P08559; A5YVE9; B7Z3T7; B7Z3X5; Q53H41; Q5JPT8; Q9NP12; Q9UBJ8; Q9UBU0; Q9UNG4; Q9UNG5 

Genbank Protein ID

 D90084; M24848; X52709; X52710; M27257; M29155; M29156; M29157; M29158; M29159; M29160; M29161; M29162; M29163; M29164; L13318; J03503; J03575; L48690; EF590117; AK293250; AK296457; AK296341; AK222740; AL732326; CH471074; BC002406; AF125053; AF125054; AF125055; AF125056; AF125057; AF125058; AF125059; AF125060; AF125061; AF125062; AF125063; AF125064; AF125065; AF125066; AF125067; AF125068; AF125069; AF125070; AF125071; AF125072; AF125073; AF125074; AF125075; AF125076; AF125078; AF125079; AF125080; AF125081; AF125082; AF125083; AF125084; AF125085; AF125086; AF125087; AF125088 

Genbank Nucleotide ID

 BAA14121.1; AAA36533.1; CAA36933.1; CAA36934.1; AAA60051.1; AAA60051.1; AAA60051.1; AAA60051.1; AAA60051.1; AAA60051.1; AAA60051.1; AAA60051.1; AAA60051.1; AAA60051.1; AAA60051.1; AAA60227.1; AAA60055.1; AAA60050.1; AAB59581.1; ABQ59099.1; BAH11476.1; BAH12361.1; BAH12323.1; BAD96460.1; CAI41291.1; EAW98960.1; AAH02406.1; AAD23841.1; AAD23842.1; AAD23843.1; AAD23844.1; AAD23845.1; AAD23846.1; AAD23847.1; AAD23848.1; AAD23849.1; AAD23850.1; AAD23851.1; AAD23852.1; AAD23853.1; AAD23854.1; AAD23855.1; AAD23856.1; AAD23857.1; AAD23858.1; AAD23859.1; AAD23860.1; AAD23861.1; AAD23862.1; AAD23863.1; AAD23864.1; AAD23866.1; AAD23867.1; AAD23868.1; AAD23869.1; AAD23870.1; AAD23871.1; AAD23872.1; AAD23873.1; AAD23874.1; AAD23875.1; AAD23876.1 

Protein Name

 Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial 

Protein Synonyms/Alias

 PDHE1-A type I 

Gene Name

 PDHA1 

Gene Synonyms/Alias

 PHE1A 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
282	AASTDYYKRGDFIPG	ubiquitination	[1]
423	RGANQWIKFKSVS**	ubiquitination	[2]

Reference

 [1] 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]
 [2] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 

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 (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.  

Keyword

 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. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 390 AA 

Protein Sequence

Gene Ontology

 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. 

Interpro

 IPR001017; DH_E1.
 IPR017597; Pyrv_DH_E1_asu_subgrp-y. 

Pfam

 PF00676; E1_dh 

SMART

  

PROSITE

  

PRINTS