CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-003887
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Pyruvate dehydrogenase E1 component subunit beta, mitochondrial 
Protein Synonyms/Alias
 PDHE1-B 
Gene Name
 PDHB 
Gene Synonyms/Alias
 PHE1B 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
184PWNSEDAKGLIKSAIubiquitination[1, 2, 3]
188EDAKGLIKSAIRDNNubiquitination[2]
229LIPIGKAKIERQGTHubiquitination[2]
336DVPMPYAKILEDNSIacetylation[4, 5]
336DVPMPYAKILEDNSIubiquitination[1, 2, 3, 6]
347DNSIPQVKDIIFAIKubiquitination[2, 6]
354KDIIFAIKKTLNI**acetylation[4, 7]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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] 
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
 BINDING 89 89 Thiamine pyrophosphate.
 MOD_RES 67 67 Phosphotyrosine (By similarity).  
Keyword
 3D-structure; Alternative splicing; Carbohydrate metabolism; Complete proteome; Direct protein sequencing; Disease mutation; Glucose metabolism; Mitochondrion; Oxidoreductase; Phosphoprotein; Polymorphism; Pyruvate; Reference proteome; Thiamine pyrophosphate; Transit peptide; Tricarboxylic acid cycle. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 359 AA 
Protein Sequence
MAAVSGLVRR PLREVSGLLK RRFHWTAPAA LQVTVRDAIN QGMDEELERD EKVFLLGEEV 60
AQYDGAYKVS RGLWKKYGDK RIIDTPISEM GFAGIAVGAA MAGLRPICEF MTFNFSMQAI 120
DQVINSAAKT YYMSGGLQPV PIVFRGPNGA SAGVAAQHSQ CFAAWYGHCP GLKVVSPWNS 180
EDAKGLIKSA IRDNNPVVVL ENELMYGVPF EFPPEAQSKD FLIPIGKAKI ERQGTHITVV 240
SHSRPVGHCL EAAAVLSKEG VECEVINMRT IRPMDMETIE ASVMKTNHLV TVEGGWPQFG 300
VGAEICARIM EGPAFNFLDA PAVRVTGADV PMPYAKILED NSIPQVKDII FAIKKTLNI 359 
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; TAS:ProtInc.
 GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IDA:UniProtKB.
 GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
 GO:0010510; P:regulation of acetyl-CoA biosynthetic process from pyruvate; TAS:Reactome.
 GO:0006099; P:tricarboxylic acid cycle; IDA:UniProtKB. 
Interpro
 IPR027110; PDHB.
 IPR009014; Transketo_C/Pyr-ferredox_oxred.
 IPR015941; Transketolase-like_C.
 IPR005475; Transketolase-like_Pyr-bd.
 IPR005476; Transketolase_C. 
Pfam
 PF02779; Transket_pyr
 PF02780; Transketolase_C 
SMART
 SM00861; Transket_pyr 
PROSITE
  
PRINTS