CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005504
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
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
55QLRQTMAKFLQEHLAubiquitination[1]
75IDRSNEFKNLREFWKacetylation[2, 3]
239PGFSTSKKLDKLGMRubiquitination[4]
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] 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]
 [3] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [4] 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
Functional Description
  
Sequence Annotation
 NP_BIND 162 171 FAD.
 NP_BIND 195 197 FAD.
 NP_BIND 377 381 FAD.
 NP_BIND 406 408 FAD.
 REGION 219 220 Substrate binding.
 REGION 281 284 Substrate binding.
 REGION 404 405 Substrate binding.
 ACT_SITE 283 283 Proton acceptor.
 BINDING 171 171 Substrate; via carbonyl oxygen.
 BINDING 274 274 Substrate.
 BINDING 309 309 FAD.
 BINDING 320 320 FAD.
 MOD_RES 75 75 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Complete proteome; Direct protein sequencing; Disease mutation; FAD; Flavoprotein; Mitochondrion; Oxidoreductase; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 423 AA 
Protein Sequence
MATATRLLGW RVASWRLRPP LAGFVSQRAH SLLPVDDAIN GLSEEQRQLR QTMAKFLQEH 60
LAPKAQEIDR SNEFKNLREF WKQLGNLGVL GITAPVQYGG SGLGYLEHVL VMEEISRASG 120
AVGLSYGAHS NLCINQLVRN GNEAQKEKYL PKLISGEYIG ALAMSEPNAG SDVVSMKLKA 180
EKKGNHYILN GNKFWITNGP DADVLIVYAK TDLAAVPASR GITAFIVEKG MPGFSTSKKL 240
DKLGMRGSNT CELIFEDCKI PAANILGHEN KGVYVLMSGL DLERLVLAGG PLGLMQAVLD 300
HTIPYLHVRE AFGQKIGHFQ LMQGKMADMY TRLMACRQYV YNVAKACDEG HCTAKDCAGV 360
ILYSAECATQ VALDGIQCFG GNGYINDFPM GRFLRDAKLY EIGAGTSEVR RLVIGRAFNA 420
DFH 423 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; ISS:BHF-UCL.
 GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
 GO:0008470; F:isovaleryl-CoA dehydrogenase activity; ISS:BHF-UCL.
 GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome.
 GO:0006552; P:leucine catabolic process; ISS:BHF-UCL. 
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