HK1

From Wikipedia, the free encyclopedia


Hexokinase 1
PDB rendering based on 1bg3.
Available structures: 1bg3, 1cza, 1dgk, 1hkb, 1hkc, 1qha
Identifiers
Symbol(s) HK1; HK1-ta; HK1-tb; HK1-tc; HKI; HXK1
External IDs OMIM: 142600 MGI: 96103 HomoloGene: 37270
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 3098 15275
Ensembl ENSG00000156515 ENSMUSG00000037012
Uniprot P19367 Q3TJE3
Refseq NM_000188 (mRNA)
NP_000179 (protein)		 XM_978893 (mRNA)
XP_983987 (protein)
Location Chr 10: 70.7 - 70.83 Mb Chr 10: 61.66 - 61.76 Mb
Pubmed search [1] [2]

Hexokinase 1, also known as HK1, is a human gene.

Hexokinases phosphorylate glucose to produce glucose-6-phosphate, thus committing glucose to the glycolytic pathway. This gene encodes a ubiquitous form of hexokinase which localizes to the outer membrane of mitochondria. Mutations in this gene have been associated with hemolytic anemia due to hexokinase deficiency. Alternative splicing of this gene results in five transcript variants which encode different isoforms, some of which are tissue-specific. Each isoform has a distinct N-terminus; the remainder of the protein is identical among all the isoforms. A sixth transcript variant has been described, but due to the presence of several stop codons, it is not thought to encode a protein.[1]

[edit] References

  1. ^ Entrez Gene: HK1 hexokinase 1.

[edit] Further reading

  • Murakami K, Kanno H, Tancabelic J, Fujii H (2003). "Gene expression and biological significance of hexokinase in erythroid cells.". Acta Haematol. 108 (4): 204–9. PMID 12432216. 
  • Daniele A, Altruda F, Ferrone M, et al. (1992). "Mapping of human hexokinase 1 gene to 10q11----qter.". Hum. Hered. 42 (2): 107–10. PMID 1572668. 
  • Magnani M, Bianchi M, Casabianca A, et al. (1992). "A recombinant human 'mini'-hexokinase is catalytically active and regulated by hexose 6-phosphates.". Biochem. J. 285 ( Pt 1): 193–9. PMID 1637300. 
  • Magnani M, Serafini G, Bianchi M, et al. (1991). "Human hexokinase type I microheterogeneity is due to different amino-terminal sequences.". J. Biol. Chem. 266 (1): 502–5. PMID 1985912. 
  • Adams V, Griffin LD, Gelb BD, McCabe ER (1991). "Protein kinase activity of rat brain hexokinase.". Biochem. Biophys. Res. Commun. 177 (3): 1101–6. PMID 2059200. 
  • Murakami K, Blei F, Tilton W, et al. (1990). "An isozyme of hexokinase specific for the human red blood cell (HKR)". Blood 75 (3): 770–5. PMID 2297576. 
  • Nishi S, Seino S, Bell GI (1989). "Human hexokinase: sequences of amino- and carboxyl-terminal halves are homologous.". Biochem. Biophys. Res. Commun. 157 (3): 937–43. PMID 3207429. 
  • Rijksen G, Akkerman JW, van den Wall Bake AW, et al. (1983). "Generalized hexokinase deficiency in the blood cells of a patient with nonspherocytic hemolytic anemia.". Blood 61 (1): 12–8. PMID 6848140. 
  • Bianchi M, Magnani M (1995). "Hexokinase mutations that produce nonspherocytic hemolytic anemia.". Blood Cells Mol. Dis. 21 (1): 2–8. doi:10.1006/bcmd.1995.0002. PMID 7655856. 
  • Blachly-Dyson E, Zambronicz EB, Yu WH, et al. (1993). "Cloning and functional expression in yeast of two human isoforms of the outer mitochondrial membrane channel, the voltage-dependent anion channel.". J. Biol. Chem. 268 (3): 1835–41. PMID 8420959. 
  • Aleshin AE, Zeng C, Fromm HJ, Honzatko RB (1996). "Crystallization and preliminary X-ray analysis of human brain hexokinase.". FEBS Lett. 391 (1-2): 9–10. PMID 8706938. 
  • Visconti PE, Olds-Clarke P, Moss SB, et al. (1996). "Properties and localization of a tyrosine phosphorylated form of hexokinase in mouse sperm.". Mol. Reprod. Dev. 43 (1): 82–93. doi:10.1002/(SICI)1098-2795(199601)43:1<82::AID-MRD11>3.0.CO;2-6. PMID 8720117. 
  • Mori C, Nakamura N, Welch JE, et al. (1997). "Testis-specific expression of mRNAs for a unique human type 1 hexokinase lacking the porin-binding domain.". Mol. Reprod. Dev. 44 (1): 14–22. doi:10.1002/(SICI)1098-2795(199605)44:1<14::AID-MRD2>3.0.CO;2-W. PMID 8722688. 
  • Murakami K, Piomelli S (1997). "Identification of the cDNA for human red blood cell-specific hexokinase isozyme.". Blood 89 (3): 762–6. PMID 9028305. 
  • Ruzzo A, Andreoni F, Magnani M (1998). "An erythroid-specific exon is present in the human hexokinase gene.". Blood 91 (1): 363–4. PMID 9414310. 
  • Travis AJ, Foster JA, Rosenbaum NA, et al. (1998). "Targeting of a germ cell-specific type 1 hexokinase lacking a porin-binding domain to the mitochondria as well as to the head and fibrous sheath of murine spermatozoa.". Mol. Biol. Cell 9 (2): 263–76. PMID 9450953. 
  • Aleshin AE, Zeng C, Bourenkov GP, et al. (1998). "The mechanism of regulation of hexokinase: new insights from the crystal structure of recombinant human brain hexokinase complexed with glucose and glucose-6-phosphate.". Structure 6 (1): 39–50. PMID 9493266. 
  • Ruzzo A, Andreoni F, Magnani M (1998). "Structure of the human hexokinase type I gene and nucleotide sequence of the 5' flanking region.". Biochem. J. 331 ( Pt 2): 607–13. PMID 9531504. 
  • Aleshin AE, Zeng C, Bartunik HD, et al. (1998). "Regulation of hexokinase I: crystal structure of recombinant human brain hexokinase complexed with glucose and phosphate.". J. Mol. Biol. 282 (2): 345–57. doi:10.1006/jmbi.1998.2017. PMID 9735292. 
  • Murakami K, Kanno H, Miwa S, Piomelli S (1999). "Human HKR isozyme: organization of the hexokinase I gene, the erythroid-specific promoter, and transcription initiation site.". Mol. Genet. Metab. 67 (2): 118–30. doi:10.1006/mgme.1999.2842. PMID 10356311. 
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