CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015091
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 3-hydroxyisobutyryl-CoA hydrolase, mitochondrial 
Protein Synonyms/Alias
 3-hydroxyisobutyryl-coenzyme A hydrolase; HIB-CoA hydrolase; HIBYL-CoA-H 
Gene Name
 HIBCH 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
92IIKGAGGKAFCAGGDacetylation[1]
112EAEKAKQKIAPVFFRubiquitination[2, 3, 4]
252ENYHTESKIDRDKSFubiquitination[5]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 
Functional Description
 Hydrolyzes 3-hydroxyisobutyryl-CoA (HIBYL-CoA), a saline catabolite. Has high activity toward isobutyryl-CoA. Could be an isobutyryl-CoA dehydrogenase that functions in valine catabolism. Also hydrolyzes 3-hydroxypropanoyl-CoA. 
Sequence Annotation
 BINDING 121 121 Substrate.
 BINDING 146 146 Substrate; via amide nitrogen.
 BINDING 169 169 Substrate.
 BINDING 177 177 Substrate.
 MOD_RES 92 92 N6-acetyllysine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Branched-chain amino acid catabolism; Complete proteome; Disease mutation; Hydrolase; Mitochondrion; Polymorphism; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 386 AA 
Protein Sequence
MGQREMWRLM SRFNAFKRTN TILHHLRMSK HTDAAEEVLL EKKGCTGVIT LNRPKFLNAL 60
TLNMIRQIYP QLKKWEQDPE TFLIIIKGAG GKAFCAGGDI RVISEAEKAK QKIAPVFFRE 120
EYMLNNAVGS CQKPYVALIH GITMGGGVGL SVHGQFRVAT EKCLFAMPET AIGLFPDVGG 180
GYFLPRLQGK LGYFLALTGF RLKGRDVYRA GIATHFVDSE KLAMLEEDLL ALKSPSKENI 240
ASVLENYHTE SKIDRDKSFI LEEHMDKINS CFSANTVEEI IENLQQDGSS FALEQLKVIN 300
KMSPTSLKIT LRQLMEGSSK TLQEVLTMEY RLSQACMRGH DFHEGVRAVL IDKDQSPKWK 360
PADLKEVTEE DLNNHFKSLG SSDLKF 386 
Gene Ontology
 GO:0005759; C:mitochondrial matrix; TAS:Reactome.
 GO:0003860; F:3-hydroxyisobutyryl-CoA hydrolase activity; IDA:UniProtKB.
 GO:0009083; P:branched-chain amino acid catabolic process; TAS:Reactome.
 GO:0034641; P:cellular nitrogen compound metabolic process; TAS:Reactome.
 GO:0006574; P:valine catabolic process; IEA:UniProtKB-UniPathway. 
Interpro
 IPR014748; Crontonase_C. 
Pfam
  
SMART
  
PROSITE
 PS00166; ENOYL_COA_HYDRATASE 
PRINTS