CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004037
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial 
Protein Synonyms/Alias
 Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain; BCKDE1A; BCKDH E1-alpha 
Gene Name
 BCKDHA 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
311FAVYNATKEARRRAVubiquitination[1, 2]
356DEVNYWDKQDHPISRubiquitination[2]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] 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] 
Functional Description
 The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). 
Sequence Annotation
 REGION 157 159 Thiamine pyrophosphate binding.
 METAL 206 206 Potassium.
 METAL 211 211 Potassium.
 METAL 212 212 Potassium.
 MOD_RES 337 337 Phosphoserine.
 MOD_RES 347 347 Phosphoserine.  
Keyword
 3D-structure; Complete proteome; Direct protein sequencing; Disease mutation; Maple syrup urine disease; Metal-binding; Mitochondrion; Oxidoreductase; Phosphoprotein; Polymorphism; Potassium; Reference proteome; Thiamine pyrophosphate; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 445 AA 
Protein Sequence
MAVAIAAARV WRLNRGLSQA ALLLLRQPGA RGLARSHPPR QQQQFSSLDD KPQFPGASAE 60
FIDKLEFIQP NVISGIPIYR VMDRQGQIIN PSEDPHLPKE KVLKLYKSMT LLNTMDRILY 120
ESQRQGRISF YMTNYGEEGT HVGSAAALDN TDLVFGQYRE AGVLMYRDYP LELFMAQCYG 180
NISDLGKGRQ MPVHYGCKER HFVTISSPLA TQIPQAVGAA YAAKRANANR VVICYFGEGA 240
ASEGDAHAGF NFAATLECPI IFFCRNNGYA ISTPTSEQYR GDGIAARGPG YGIMSIRVDG 300
NDVFAVYNAT KEARRRAVAE NQPFLIEAMT YRIGHHSTSD DSSAYRSVDE VNYWDKQDHP 360
ISRLRHYLLS QGWWDEEQEK AWRKQSRRKV MEAFEQAERK PKPNPNLLFS DVYQEMPAQL 420
RKQQESLARH LQTYGEHYPL DHFDK 445 
Gene Ontology
 GO:0005947; C:mitochondrial alpha-ketoglutarate dehydrogenase complex; IDA:HGNC.
 GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; TAS:ProtInc.
 GO:0003826; F:alpha-ketoacid dehydrogenase activity; IDA:HGNC.
 GO:0016831; F:carboxy-lyase activity; TAS:HGNC.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0009083; P:branched-chain amino acid catabolic process; IDA:HGNC.
 GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome. 
Interpro
 IPR001017; DH_E1. 
Pfam
 PF00676; E1_dh 
SMART
  
PROSITE
  
PRINTS