Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-01293
Entry Name
UniProt Accession
Theoretical PI
8.35
Molecular Weight
43295.63
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial
Protein Synonyms/Alias
1.2.4.1; PDHE1-A type I;
Gene Name
PDHA1
Gene Synonyms/Alias
PHE1A;
Created Date
01-AUG-1988
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
91
Canonical
QKIIRGFCHLCDGQE
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Predicted from GPS-Lipid
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
Modified residue: 63 63 N6-acetyllysine; alternate.
Modified residue: 63 63 N6-succinyllysine; alternate.
Modified residue: 232 232 Phosphoserine; by PDK1.
Modified residue: 244 244 N6-acetyllysine; alternate.
Modified residue: 244 244 N6-succinyllysine; alternate.
Modified residue: 277 277 N6-succinyllysine.
Modified residue: 293 293 Phosphoserine; by PDK1, PDK2, PDK3 andPDK4.
Modified residue: 295 295 Phosphoserine.
Modified residue: 300 300 Phosphoserine; by PDK1, PDK2, PDK3 andPDK4.
Modified residue: 301 301 Phosphotyrosine.
Modified residue: 313 313 N6-acetyllysine; alternate.
Modified residue: 313 313 N6-succinyllysine; alternate.
Modified residue: 321 321 N6-acetyllysine.
Modified residue: 336 336 N6-acetyllysine.
Modified residue: 385 385 N6-succinyllysine.
Protein Length
390 AA.
Protein Sequence
(Canonical)
MRKMLAAVSR VLSGASQKPA SRVLVASRNF ANDATFEIKK CDLHRLEEGP PVTTVLTRED  60
GLKYYRMMQT VRRMELKADQ LYKQKIIRGF CHLCDGQEAC CVGLEAGINP TDHLITAYRA  120
HGFTFTRGLS VREILAELTG RKGGCAKGKG GSMHMYAKNF YGGNGIVGAQ VPLGAGIALA  180
CKYNGKDEVC LTLYGDGAAN QGQIFEAYNM AALWKLPCIF ICENNRYGMG TSVERAAAST  240
DYYKRGDFIP GLRVDGMDIL CVREATRFAA AYCRSGKGPI LMELQTYRYH GHSMSDPGVS  300
YRTREEIQEV RSKSDPIMLL KDRMVNSNLA SVEELKEIDV EVRKEIEDAA QFATADPEPP  360
LEELGYHIYS SDPPFEVRGA NQWIKFKSVS                                   390
FASTA
(Canonical)
>LipidDB-9606-01293|P08559
MRKMLAAVSRVLSGASQKPASRVLVASRNFANDATFEIKKCDLHRLEEGPPVTTVLTRED
GLKYYRMMQTVRRMELKADQLYKQKIIRGFCHLCDGQEACCVGLEAGINPTDHLITAYRA
HGFTFTRGLSVREILAELTGRKGGCAKGKGGSMHMYAKNFYGGNGIVGAQVPLGAGIALA
CKYNGKDEVCLTLYGDGAANQGQIFEAYNMAALWKLPCIFICENNRYGMGTSVERAAAST
DYYKRGDFIPGLRVDGMDILCVREATRFAAAYCRSGKGPILMELQTYRYHGHSMSDPGVS
YRTREEIQEVRSKSDPIMLLKDRMVNSNLASVEELKEIDVEVRKEIEDAAQFATADPEPP
LEELGYHIYSSDPPFEVRGANQWIKFKSVS
Gene Ontology
GO:0005759; C:mitochondrial matrix; TAS:Reactome
GO:0005739; C:mitochondrion; IDA:UniProt
GO:0005634; C:nucleus; IDA:UniProt
GO:0045254; C:pyruvate dehydrogenase complex; IDA:UniProtKB
GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC
GO:0004738; F:pyruvate dehydrogenase activity; IDA:UniProtKB
GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IDA:UniProtKB
GO:0044237; P:cellular metabolic process; TAS:Reactome
GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW
GO:0006096; P:glycolytic process; IEA:InterPro
GO:0006090; P:pyruvate metabolic process; TAS:Reactome
GO:0010510; P:regulation of acetyl-CoA biosynthetic process from pyruvate; TAS:Reactome
GO:0044281; P:small molecule metabolic process; TAS:Reactome
GO:0006099; P:tricarboxylic acid cycle; IDA:UniProtKB
Interpro
InterPro; IPR001017; DH_E1
InterPro; IPR017597; Pyrv_DH_E1_asu_subgrp-y
InterPro; IPR029061; THDP-binding
Pfam
Pfam; PF00676; E1_dh;
SMART
PROSITE
PRINTS