CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021715
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Isovaleryl-CoA dehydrogenase, mitochondrial 
Protein Synonyms/Alias
 IVD 
Gene Name
 Ivd 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
56QLRHTISKFLQENLAacetylation[1, 2, 3, 4, 5, 6, 7, 8, 9, 10]
56QLRHTISKFLQENLAsuccinylation[9]
56QLRHTISKFLQENLAubiquitination[11]
65LQENLAPKAQEIDQTacetylation[8, 9]
65LQENLAPKAQEIDQTsuccinylation[9]
65LQENLAPKAQEIDQTubiquitination[11]
76IDQTNDFKNLREFWKacetylation[1, 3, 5, 6, 7, 8, 9, 10, 12]
76IDQTNDFKNLREFWKsuccinylation[9]
76IDQTNDFKNLREFWKubiquitination[11]
147RNGNEAQKEKYLPKLacetylation[6, 10]
149GNEAQKEKYLPKLISacetylation[6, 8, 10]
183SMKLKAEKKGDHYVLacetylation[6]
230ITAFIVEKGMPGFSTacetylation[6, 10]
239MPGFSTSKKLDKLGMacetylation[6, 8, 9, 10]
239MPGFSTSKKLDKLGMsuccinylation[9]
260ELVFEDCKVPAANVLacetylation[3, 6, 8, 9, 10]
260ELVFEDCKVPAANVLsuccinylation[9]
272NVLSQESKGVYVLMSacetylation[8]
316VREAFGQKIGQFQLMacetylation[6, 9]
316VREAFGQKIGQFQLMsuccinylation[9]
346QYVYNVAKACDEGHIacetylation[10]
Reference
 [1] The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switching.
 Yang L, Vaitheesvaran B, Hartil K, Robinson AJ, Hoopmann MR, Eng JK, Kurland IJ, Bruce JE.
 J Proteome Res. 2011 Sep 2;10(9):4134-49. [PMID: 21728379]
 [2] Mitochondrial acetylome analysis in a mouse model of alcohol-induced liver injury utilizing SIRT3 knockout mice.
 Fritz KS, Galligan JJ, Hirschey MD, Verdin E, Petersen DR.
 J Proteome Res. 2012 Mar 2;11(3):1633-43. [PMID: 22309199]
 [3] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758]
 [4] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [5] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [6] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [7] Circadian acetylome reveals regulation of mitochondrial metabolic pathways.
 Masri S, Patel VR, Eckel-Mahan KL, Peleg S, Forne I, Ladurner AG, Baldi P, Imhof A, Sassone-Corsi P.
 Proc Natl Acad Sci U S A. 2013 Feb 26;110(9):3339-44. [PMID: 23341599]
 [8] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [9] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [10] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [11] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [12] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647
Functional Description
  
Sequence Annotation
 NP_BIND 163 172 FAD (By similarity).
 NP_BIND 196 198 FAD (By similarity).
 NP_BIND 378 382 FAD (By similarity).
 NP_BIND 407 409 FAD (By similarity).
 REGION 220 221 Substrate binding (By similarity).
 REGION 282 285 Substrate binding (By similarity).
 REGION 405 406 Substrate binding (By similarity).
 ACT_SITE 284 284 Proton acceptor (By similarity).
 BINDING 172 172 Substrate; via carbonyl oxygen (By
 BINDING 275 275 Substrate (By similarity).
 BINDING 310 310 FAD (By similarity).
 BINDING 321 321 FAD (By similarity).
 MOD_RES 76 76 N6-acetyllysine.  
Keyword
 Acetylation; Complete proteome; Direct protein sequencing; FAD; Flavoprotein; Mitochondrion; Oxidoreductase; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 424 AA 
Protein Sequence
MATAIRLLGR RVSSWRLRPS PSPLAVPRRA HSILPVDDDI NGLNEEQKQL RHTISKFLQE 60
NLAPKAQEID QTNDFKNLRE FWKQLGSLGV LGITAPVQYG GSGLGYLEHV LVMEEISRAS 120
GAVGLSYGAH SNLCVNQIVR NGNEAQKEKY LPKLISGEFI GALAMSEPNA GSDVVSMKLK 180
AEKKGDHYVL NGNKFWITNG PDADILVVYA KTDLTAVPAS RGITAFIVEK GMPGFSTSKK 240
LDKLGMRGSN TCELVFEDCK VPAANVLSQE SKGVYVLMSG LDLERLVLAG GPLGIMQAVL 300
DHTIPYLHVR EAFGQKIGQF QLMQGKMADM YTRLMASRQY VYNVAKACDE GHIIPKDCAG 360
VILYAAECAT QVALDGIQCL GGNGYINDFP MGRFLRDAKL YEIGAGTSEV RRLVIGRAFN 420
ADFR 424 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
 GO:0031966; C:mitochondrial membrane; IEA:Compara.
 GO:0005739; C:mitochondrion; IDA:MGI.
 GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
 GO:0008470; F:isovaleryl-CoA dehydrogenase activity; IEA:Compara.
 GO:0006552; P:leucine catabolic process; IEA:UniProtKB-UniPathway. 
Interpro
 IPR006089; Acyl-CoA_DH_CS.
 IPR006092; Acyl-CoA_DH_N.
 IPR006090; Acyl-CoA_Oxase/DH_1.
 IPR006091; Acyl-CoA_Oxase/DH_cen-dom.
 IPR009075; AcylCo_DH/oxidase_C.
 IPR013786; AcylCoA_DH/ox_N.
 IPR009100; AcylCoA_DH/oxidase. 
Pfam
 PF00441; Acyl-CoA_dh_1
 PF02770; Acyl-CoA_dh_M
 PF02771; Acyl-CoA_dh_N 
SMART
  
PROSITE
 PS00072; ACYL_COA_DH_1
 PS00073; ACYL_COA_DH_2 
PRINTS