Canmetcon
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Identification
HMDB Protein ID HMDBP03577
Secondary Accession Numbers
  • 9165
Name L-lactate dehydrogenase B chain
Synonyms
  1. LDH heart subunit
  2. LDH-B
  3. LDH-H
  4. Renal carcinoma antigen NY-REN-46
Gene Name LDHB
Protein Type Unknown
Biological Properties
General Function Involved in oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Specific Function Not Available
Pathways
  • Cysteine and methionine metabolism
  • Glycolysis / Gluconeogenesis
  • Propanoate metabolism
  • pyruvate fermentation to lactate
  • Pyruvate metabolism
Reactions
L-Lactic acid + NAD → Pyruvic acid + NADH details
L-Lactic acid + NAD → Pyruvic acid + NADH + Hydrogen Ion details
2-Hydroxybutyric acid + NAD → 2-Ketobutyric acid + NADH + Hydrogen Ion details
3-Mercaptolactic acid + NAD → 3-Mercaptopyruvic acid + NADH + Hydrogen Ion details
GO Classification
Biological Process
glycolysis
cellular carbohydrate metabolic process
pyruvate metabolic process
lactate metabolic process
NAD metabolic process
Cellular Component
cytosol
mitochondrion
Component
cell part
intracellular part
cytoplasm
Function
catalytic activity
lactate dehydrogenase activity
l-lactate dehydrogenase activity
oxidoreductase activity, acting on the ch-oh group of donors, nad or nadp as acceptor
oxidoreductase activity, acting on ch-oh group of donors
oxidoreductase activity
Molecular Function
NAD binding
L-lactate dehydrogenase activity
Process
metabolic process
primary metabolic process
carbohydrate metabolic process
cellular carbohydrate metabolic process
small molecule metabolic process
alcohol metabolic process
monosaccharide metabolic process
hexose metabolic process
glucose metabolic process
oxidation reduction
glucose catabolic process
glycolysis
Cellular Location
  1. Cytoplasm
Gene Properties
Chromosome Location 12
Locus 12p12.2-p12.1
SNPs LDHB
Gene Sequence
>1005 bp
ATGGCAACTCTTAAGGAAAAACTCATTGCACCAGTTGCGGAAGAAGAGGCAACAGTTCCA
AACAATAAGATCACTGTAGTGGGTGTTGGACAAGTTGGTATGGCGTGTGCTATCAGCATT
CTGGGAAAGTCTCTGGCTGATGAACTTGCTCTTGTGGATGTTTTGGAAGATAAGCTTAAA
GGAGAAATGATGGATCTGCAGCATGGGAGCTTATTTCTTCAGACACCTAAAATTGTGGCA
GATAAAGATTATTCTGTGACCGCCAATTCTAAGATTGTAGTGGTAACTGCAGGAGTCCGT
CAGCAAGAAGGGGAGAGTCGGCTCAATCTGGTGCAGAGAAATGTTAATGTCTTCAAATTC
ATTATTCCTCAGATCGTCAAGTACAGTCCTGATTGCATCATAATTGTGGTTTCCAACCCA
GTGGACATTCTTACGTATGTTACCTGGAAACTAAGTGGATTACCCAAACACCGCGTGATT
GGAAGTGGATGTAATCTGGATTCTGCTAGATTTCGCTACCTTATGGCTGAAAAACTTGGC
ATTCATCCCAGCAGCTGCCATGGATGGATTTTGGGGGAACATGGCGACTCAAGTGTGGCT
GTGTGGAGTGGTGTGAATGTGGCAGGTGTTTCTCTCCAGGAATTGAATCCAGAAATGGGA
ACTGACAATGATAGTGAAAATTGGAAGGAAGTGCATAAGATGGTGGTTGAAAGTGCCTAT
GAAGTCATCAAGCTAAAAGGATATACCAACTGGGCTATTGGATTAAGTGTGGCTGATCTT
ATTGAATCCATGTTGAAAAATCTATCCAGGATTCATCCCGTGTCAACAATGGTAAAGGGG
ATGTATGGCATTGAGAATGAAGTCTTCCTGAGCCTTCCATGTATCCTCAATGCCCGGGGA
TTAACCAGCGTTATCAACCAGAAGCTAAAGGATGATGAGGTTGCTCAGCTCAAGAAAAGT
GCAGATACCCTGTGGGACATCCAGAAGGACCTAAAAGACCTGTGA
Protein Properties
Number of Residues 334
Molecular Weight 36638.225
Theoretical pI 6.052
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>L-lactate dehydrogenase B chain
MATLKEKLIAPVAEEEATVPNNKITVVGVGQVGMACAISILGKSLADELALVDVLEDKLK
GEMMDLQHGSLFLQTPKIVADKDYSVTANSKIVVVTAGVRQQEGESRLNLVQRNVNVFKF
IIPQIVKYSPDCIIIVVSNPVDILTYVTWKLSGLPKHRVIGSGCNLDSARFRYLMAEKLG
IHPSSCHGWILGEHGDSSVAVWSGVNVAGVSLQELNPEMGTDNDSENWKEVHKMVVESAY
EVIKLKGYTNWAIGLSVADLIESMLKNLSRIHPVSTMVKGMYGIENEVFLSLPCILNARG
LTSVINQKLKDDEVAQLKKSADTLWDIQKDLKDL
GenBank ID Protein 34329
UniProtKB/Swiss-Prot ID P07195
UniProtKB/Swiss-Prot Entry Name LDHB_HUMAN
PDB IDs
GenBank Gene ID Y00711
GeneCard ID LDHB
GenAtlas ID LDHB
HGNC ID HGNC:6541
References
General References
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  2. Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed:15592455 ]
  3. 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 ]
  4. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [PubMed:19690332 ]
  5. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed:18083107 ]
  6. Scanlan MJ, Gordan JD, Williamson B, Stockert E, Bander NH, Jongeneel V, Gure AO, Jager D, Jager E, Knuth A, Chen YT, Old LJ: Antigens recognized by autologous antibody in patients with renal-cell carcinoma. Int J Cancer. 1999 Nov 12;83(4):456-64. [PubMed:10508479 ]
  7. Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. doi: 10.1021/pr900044c. [PubMed:19534553 ]
  8. Takeno T, Li SS: Structure of the human lactate dehydrogenase B gene. Biochem J. 1989 Feb 1;257(3):921-4. [PubMed:2930497 ]
  9. Sakai I, Sharief FS, Pan YC, Li SS: The cDNA and protein sequences of human lactate dehydrogenase B. Biochem J. 1987 Dec 15;248(3):933-6. [PubMed:3435492 ]
  10. Read JA, Winter VJ, Eszes CM, Sessions RB, Brady RL: Structural basis for altered activity of M- and H-isozyme forms of human lactate dehydrogenase. Proteins. 2001 May 1;43(2):175-85. [PubMed:11276087 ]
  11. Maekawa M, Sudo K, Kitajima M, Matsuura Y, Li SS, Kanno T: Analysis of a genetic mutation in an electrophoretic variant of the human lactate dehydrogenase-B(H) subunit. Hum Genet. 1993 Jun;91(5):423-6. [PubMed:8314553 ]
  12. Maekawa M, Sudo K, Kitajima M, Matsuura Y, Li SS, Kanno T: Detection and characterization of new genetic mutations in individuals heterozygous for lactate dehydrogenase-B(H) deficiency using DNA conformation polymorphism analysis and silver staining. Hum Genet. 1993 Mar;91(2):163-8. [PubMed:8462975 ]
  13. Sudo K, Maekawa M, Tomonaga A, Tsukada T, Nakayama T, Kitamura M, Li SS, Kanno T, Toriumi J: Molecular characterization of genetic mutations in human lactate dehydrogenase (LDH) B (H) variant. Hum Genet. 1992 May;89(2):158-62. [PubMed:1587525 ]
  14. Sudo K, Maekawa M, Ikawa S, Machida K, Kitamura M, Li SS: A missense mutation found in human lactate dehydrogenase-B (H) variant gene. Biochem Biophys Res Commun. 1990 Apr 30;168(2):672-6. [PubMed:2334429 ]
  15. Shonnard GC, Hud NV, Mohrenweiser HW: Arginine to tryptophan substitution in the active site of a human lactate dehydrogenase variant--LDHB GUA1: postulated effects on subunit structure and catalysis. Biochim Biophys Acta. 1996 Jan 17;1315(1):9-14. [PubMed:8611651 ]
  16. Sudo K, Maekawa M, Houki N, Okuda T, Akizuki S, Magara T, Kawano K: A novel in-frame deletion mutation in a case of lactate dehydrogenase (LD) H subunit deficiency showing an atypical LD isoenzyme pattern in serum and erythrocytes. Clin Biochem. 1999 Mar;32(2):137-41. [PubMed:10211631 ]
  17. Hidaka K, Ueda N, Hirata I, Watanabe Y, Minatogawa Y, Iuchi I: First case of missense mutation (LDH-H:R171P) in exon 4 of the lactate dehydrogenase gene detected in a Japanese patient. J Hum Genet. 1999;44(1):69-72. [PubMed:9929983 ]
  18. Takatani T, Takaoka N, Tatsumi M, Kawamoto H, Okuno Y, Morita K, Masutani T, Murakawa K, Okamoto Y: A novel missense mutation in human lactate dehydrogenase B-subunit gene. Mol Genet Metab. 2001 Aug;73(4):344-8. [PubMed:11509017 ]