CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-037326
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 2-oxoglutarate dehydrogenase, mitochondrial 
Protein Synonyms/Alias
  
Gene Name
 OGDH 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
74ENPKSVHKSWDIFFRubiquitination[1]
404PVVMGKTKAEQFYCGubiquitination[2]
914AQNPENVKRLLFCTGubiquitination[2]
985QGYYDYVKPRLRTTIacetylation[3, 4]
1015APATGNKKTHLTELQubiquitination[2]
Reference
 [1] 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]
 [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] 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]
 [4] 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] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1038 AA 
Protein Sequence
MFHLRTCAAK LRPLTASQTV KTFSQNRPAA ARTFQQIRCY SAPVAAEPFL SGTSSNYVEE 60
MYCAWLENPK SVHKSWDIFF RNTNAGAPPG TAYQSPLPLS RGSLAAVAHA QSLVEAQPNV 120
DKLVEDHLAV QSLIRAYQIR GHHVAQLDPL GILDADLDSS VPADIISSTD KLDLAVFKER 180
LRMLTVGGFY GLDESDLDKV FHLPTTTFIG GQESALPLRE IIRRLEMAYC QHIGVEFMFI 240
NDLEQCQWIR QKFETPGIMQ FTNEEKRTLL ARLVRSTRFE EFLQRKWSSE KRFGLEGCEV 300
LIPALKTIID KSSENGVDYV IMGMPHRGRL NVLANVIRKE LEQIFCQFDS KLEAADEGSG 360
DVKYHLGMYH RRINRVTDRN ITLSLVANPS HLEAADPVVM GKTKAEQFYC GDTEGKKVMS 420
ILLHGDAAFA GQGIVYETFH LSDLPSYTTH GTVHVVVNNQ IGFTTDPRMA RSSPYPTDVA 480
RVVNAPIFHV NSDDPEAVMY VCKVAAEWRS TFHKDVVVDL VCYRRNGHNE MDEPMFTQPL 540
MYKQIRKQKP VLQKYAELLV SQGVVNQPEY EEEISKYDKI CEEAFARSKD EKILHIKHWL 600
DSPWPGFFTL DGQPRSMSCP STGLTEDILT HIGNVASSVP VENFTIHGGL SRILKTRGEM 660
VKNRTVDWAL AEYMAFGSLL KEGIHIRLSG QDVERGTFSH RHHVLHDQNV DKRTCIPMNH 720
LWPNQAPYTV CNSSLSEYGV LGFELGFAMA SPNALVLWEA QFGDFHNTAQ CIIDQFICPG 780
QAKWVRQNGI VLLLPHGMEG MGPEHSSARP ERFLQMCNDD PDVLPDLKEA NFDINQLYDC 840
NWVVVNCSTP GNFFHVLRRQ ILLPFRKPLI IFTPKSLLRH PEARSSFDEM LPGTHFQRVI 900
PEDGPAAQNP ENVKRLLFCT GKVYYDLTRE RKARDMVGQV AITRIEQLSP FPFDLLLKEV 960
QKYPNAELAW CQEEHKNQGY YDYVKPRLRT TISRAKPVWY AGRDPAAAPA TGNKKTHLTE 1020
LQRLLDTAFD LDVFKNFS 1038 
Gene Ontology
 GO:0005739; C:mitochondrion; IDA:HPA.
 GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:InterPro.
 GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
 GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. 
Interpro
 IPR011603; 2oxoglutarate_DH_E1.
 IPR001017; DH_E1.
 IPR005475; Transketolase-like_Pyr-bd. 
Pfam
 PF00676; E1_dh
 PF02779; Transket_pyr 
SMART
 SM00861; Transket_pyr 
PROSITE
  
PRINTS