CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-030827
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Dihydrolipoyl dehydrogenase, mitochondrial 
Protein Synonyms/Alias
 cDNA FLJ50515, highly similar to Dihydrolipoyl dehydrogenase, mitochondrial (EC 1.8.1.4) 
Gene Name
 DLD 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
23EVRLNLDKMMEQKSTacetylation[1]
28LDKMMEQKSTAVKALubiquitination[2]
33EQKSTAVKALTGGIAubiquitination[2, 3]
44GGIAHLFKQNKVVHVacetylation[1]
44GGIAHLFKQNKVVHVubiquitination[2, 3]
60GYGKITGKNQVTATKubiquitination[2, 4]
67KNQVTATKADGGTQVacetylation[1]
67KNQVTATKADGGTQVubiquitination[4, 5, 6]
168NFQRILQKQGFKFKLacetylation[1, 7, 8]
221IGRRPFTKNLGLEELacetylation[1]
221IGRRPFTKNLGLEELubiquitination[2, 3, 4]
247VNTRFQTKIPNIYAIacetylation[1]
247VNTRFQTKIPNIYAIubiquitination[3, 4, 5]
311GKSEEQLKEEGIEYKacetylation[1, 7, 8]
311GKSEEQLKEEGIEYKubiquitination[4, 5]
318KEEGIEYKVGKFPFAacetylation[7]
318KEEGIEYKVGKFPFAubiquitination[4]
321GIEYKVGKFPFAANSacetylation[1, 7, 8]
321GIEYKVGKFPFAANSubiquitination[2, 4]
331FAANSRAKTNADTDGubiquitination[2]
341ADTDGMVKILGQKSTubiquitination[3, 4]
346MVKILGQKSTDRVLGubiquitination[2, 4]
406NLAASFGKSINF***ubiquitination[4]
Reference
 [1] 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]
 [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] 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]
 [4] 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]
 [5] 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]
 [6] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [7] 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]
 [8] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 410 AA 
Protein Sequence
MAHGKDFASR GIEMSEVRLN LDKMMEQKST AVKALTGGIA HLFKQNKVVH VNGYGKITGK 60
NQVTATKADG GTQVIDTKNI LIATGSEVTP FPGITIDEDT IVSSTGALSL KKVPEKMVVI 120
GAGVIGVELG SVWQRLGADV TAVEFLGHVG GVGIDMEISK NFQRILQKQG FKFKLNTKVT 180
GATKKSDGKI DVSIEAASGG KAEVITCDVL LVCIGRRPFT KNLGLEELGI ELDPRGRIPV 240
NTRFQTKIPN IYAIGDVVAG PMLAHKAEDE GIICVEGMAG GAVHIDYNCV PSVIYTHPEV 300
AWVGKSEEQL KEEGIEYKVG KFPFAANSRA KTNADTDGMV KILGQKSTDR VLGAHILGPG 360
AGEMVNEAAL ALEYGASCED IARVCHAHPT LSEAFREANL AASFGKSINF 410 
Gene Ontology
 GO:0043159; C:acrosomal matrix; IEA:Compara.
 GO:0005739; C:mitochondrion; IDA:HPA.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0004148; F:dihydrolipoyl dehydrogenase activity; IEA:Compara.
 GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
 GO:0045454; P:cell redox homeostasis; IEA:InterPro.
 GO:0007369; P:gastrulation; IEA:Compara.
 GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IEA:Compara.
 GO:0006508; P:proteolysis; IEA:Compara.
 GO:0042391; P:regulation of membrane potential; IEA:Compara.
 GO:0048240; P:sperm capacitation; IEA:Compara. 
Interpro
 IPR016156; FAD/NAD-linked_Rdtase_dimer.
 IPR013027; FAD_pyr_nucl-diS_OxRdtase.
 IPR006258; Lipoamide_DH.
 IPR004099; Pyr_nucl-diS_OxRdtase_dimer.
 IPR023753; Pyr_nucl-diS_OxRdtase_FAD/NAD.
 IPR001327; Pyr_OxRdtase_NAD-bd_dom. 
Pfam
 PF00070; Pyr_redox
 PF07992; Pyr_redox_2
 PF02852; Pyr_redox_dim 
SMART
  
PROSITE
  
PRINTS
 PR00368; FADPNR.