You are using an unsupported browser. Please upgrade your browser to a newer version to get the best experience on Human Metabolome Database.
Identification
HMDB Protein ID HMDBP01493
Secondary Accession Numbers
  • 6789
Name [3-methyl-2-oxobutanoate dehydrogenase [lipoamide]] kinase, mitochondrial
Synonyms
  1. BCKD-kinase
  2. BCKDHKIN
  3. Branched-chain alpha-ketoacid dehydrogenase kinase
Gene Name BCKDK
Protein Type Enzyme
Biological Properties
General Function Involved in ATP binding
Specific Function Catalyzes the phosphorylation and inactivation of the branched-chain alpha-ketoacid dehydrogenase complex, the key regulatory enzyme of the valine, leucine and isoleucine catabolic pathways. Key enzyme that regulate the activity state of the BCKD complex
Pathways Not Available
Reactions Not Available
GO Classification
Function
binding
catalytic activity
transferase activity
transferase activity, transferring phosphorus-containing groups
kinase activity
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
adenyl ribonucleotide binding
atp binding
protein histidine kinase activity
two-component sensor activity
protein kinase activity
Process
phosphorus metabolic process
phosphate metabolic process
metabolic process
peptidyl-histidine phosphorylation
biological regulation
regulation of biological process
cellular metabolic process
regulation of cellular process
signal transduction
protein amino acid phosphorylation
phosphorylation
Cellular Location
  1. Mitochondrion matrix
Gene Properties
Chromosome Location Chromosome:1
Locus 16p11.2
SNPs BCKDK
Gene Sequence
>1239 bp
ATGATCCTGGCGTCGGTGCTGAGGAGCGGTCCCGGGGGCGGGCTTCCGCTCCGGCCCCTC
CTGGGACCCGCACTCGCGCTCCGGGCCCGCTCGACGTCGGCCACCGACACACACCACGTG
GAGATGGCTCGGGAGCGCTCCAAGACCGTCACCTCCTTTTACAACCAGTCGGCCATCGAC
GCGGCAGCGGAGAAGCCCTCAGTCCGCCTAACGCCCACCATGATGCTCTACGCTGGCCGC
TCTCAGGACGGCAGCCACCTTCTGAAAAGTGCTCGGTACCTGCAGCAAGAACTTCCAGTG
AGGATTGCTCACCGCATCAAGGGCTTCCGCTGCCTTCCTTTCATCATTGGCTGCAACCCC
ACCATACTGCACGTGCATGAGCTATATATCCGTGCCTTCCAGAAGCTGACAGACTTCCCT
CCGATCAAGGACCAGGCGGACGAGGCCCAGTACTGCCAGCTGGTGCGACAGCTGCTGGAT
GACCACAAGGATGTGGTGACCCTCTTGGCAGAGGGCCTACGTGAGAGCCGGAAGCACATA
GAGGATGAAAAGCTCGTCCGCTACTTCTTGGACAAGACGCTGACTTCGAGGCTTGGAATC
CGCATGTTGGCCACGCATCACCTGGCGCTGCATGAGGACAAGCCTGACTTTTTCGGCATC
ATCTGTACTCGTCTCTCACCAAAGAAGATTATTGAGAAGTGGGTGGACTTTGCCAGACGC
CTGTGTGAGCACAAGTATGGCAATGCGCCCCGTGTCCGCATCAATGGCCATGTGGCTGCC
CGGTTCCCCTTCATCCCTATGCCACTGGACTACATCCTGCCGGAGCTGCTCAAGAATGCC
ATGAGAGCCACAATGGAGAGTCACCTAGACACTCCCTACAATGTCCCAGATGTGGTCATC
ACCATCGCCAACAATGATGTCGATCTGATCATCAGGATCTCAGACCGTGGTGGAGGAATC
GCTCACAAAGATCTGGACCGGGTCATGGACTACCACTTCACTACTGCTGAGGCCAGCACA
CAGGACCCCCGGATCAGCCCCCTCTTTGGCCATCTGGACATGCATAGTGGCGCCCAGTCA
GGACCCATGCACGGCTTTGGCTTCGGGTTGCCCACGTCACGGGCCTACGCGGAGTACCTC
GGTGGGTCTCTGCAGCTGCAGTCCCTGCAGGGCATTGGCACGGACGTCTACCTGCGGCTC
CGCCACATCGATGGCCGGGAGGAAAGCTTCCGGATCTGA
Protein Properties
Number of Residues 412
Molecular Weight 46360.0
Theoretical pI 9.06
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>[3-methyl-2-oxobutanoate dehydrogenase [lipoamide]] kinase, mitochondrial
MILASVLRSGPGGGLPLRPLLGPALALRARSTSATDTHHVEMARERSKTVTSFYNQSAID
AAAEKPSVRLTPTMMLYAGRSQDGSHLLKSARYLQQELPVRIAHRIKGFRCLPFIIGCNP
TILHVHELYIRAFQKLTDFPPIKDQADEAQYCQLVRQLLDDHKDVVTLLAEGLRESRKHI
EDEKLVRYFLDKTLTSRLGIRMLATHHLALHEDKPDFVGIICTRLSPKKIIEKWVDFARR
LCEHKYGNAPRVRINGHVAARFPFIPMPLDYILPELLKNAMRATMESHLDTPYNVPDVVI
TIANNDVDLIIRISDRGGGIAHKDLDRVMDYHFTTAEASTQDPRISPLFGHLDMHSGAQS
GPMHGFGFGLPTSRAYAEYLGGSLQLQSLQGIGTDVYLRLRHIDGREESFRI
GenBank ID Protein 2583173
UniProtKB/Swiss-Prot ID O14874
UniProtKB/Swiss-Prot Entry Name BCKD_HUMAN
PDB IDs
GenBank Gene ID AF026548
GeneCard ID BCKDK
GenAtlas ID BCKDK
HGNC ID HGNC:16902
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  3. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. doi: 10.1016/j.molcel.2008.07.007. [PubMed:18691976 ]
  4. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. doi: 10.1021/pr0705441. Epub 2008 Jan 26. [PubMed:18220336 ]