PFKL

From Wikipedia, the free encyclopedia

Phosphofructokinase, liver

Identifiers

PFKL; DKFZp686G1648; DKFZp686L2097; FLJ30173; FLJ40909; PFK-B

External IDs

OMIM: 171860 MGI: 97547 HomoloGene: 55668

Gene ontology
Molecular Function:	• nucleotide binding • magnesium ion binding • 6-phosphofructokinase activity • ATP binding • kinase activity • transferase activity
Cellular Component:	• cytoplasm • 6-phosphofructokinase complex
Biological Process:	• fructose 6-phosphate metabolic process • glycolysis • regulation of glycolysis

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001002021 (mRNA)
NP_001002021 (protein)

NM_008826 (mRNA)
NP_032852 (protein)

Location

Chr 21: 44.54 - 44.57 Mb

Chr 10: 77.39 - 77.41 Mb

Pubmed search

[1]

[2]

Phosphofructokinase, liver, also known as PFKL, is a human gene.^[1]

Phosphofructokinase (PFK) is a tetrameric enzyme that catalyzes a key step in glycolysis, namely the conversion of D-fructose 6-phosphate to D-fructose 1,6-bisphosphate. Separate genes encode a muscle subunit (M) and a liver subunit (L). PFK from muscle is a homotetramer of M subunits, PFK from liver is a homotetramer of L-subunits, while PFK from platelets can be composed of any tetrameric combination of M and L subunits. The protein encoded by this gene represents the L subunit. Two transcript variants encoding different isoforms have been found for this gene.^[1]

[edit] References

^ ^a ^b Entrez Gene: PFKL phosphofructokinase, liver.

[edit] Further reading

Kahn A, Meienhofer MC, Cottreau D, et al. (1979). "Phosphofructokinase (PFK) isozymes in man. I. Studies of adult human tissues.". Hum. Genet. 48 (1): 93–108. PMID 156693.
Kristensen T, Lopez R, Prydz H (1992). "An estimate of the sequencing error frequency in the DNA sequence databases.". DNA Seq. 2 (6): 343–6. PMID 1446073.
Wang D, Fang H, Cantor CR, Smith CL (1992). "A contiguous Not I restriction map of band q22.3 of human chromosome 21.". Proc. Natl. Acad. Sci. U.S.A. 89 (8): 3222–6. PMID 1565613.
Elson A, Levanon D, Brandeis M, et al. (1990). "The structure of the human liver-type phosphofructokinase gene.". Genomics 7 (1): 47–56. PMID 2139864.
Levanon D, Danciger E, Dafni N, et al. (1990). "The primary structure of human liver type phosphofructokinase and its comparison with other types of PFK.". DNA 8 (10): 733–43. PMID 2533063.
Van Keuren M, Drabkin H, Hart I, et al. (1986). "Regional assignment of human liver-type 6-phosphofructokinase to chromosome 21q22.3 by using somatic cell hybrids and a monoclonal anti-L antibody.". Hum. Genet. 74 (1): 34–40. PMID 2944814.
Levanon D, Danciger E, Dafni N, Groner Y (1987). "Genomic clones of the human liver-type phosphofructokinase.". Biochem. Biophys. Res. Commun. 141 (1): 374–80. PMID 2948503.
Vora S, Davidson M, Seaman C, et al. (1984). "Heterogeneity of the molecular lesions in inherited phosphofructokinase deficiency.". J. Clin. Invest. 72 (6): 1995–2006. PMID 6227635.
Vora S, Seaman C, Durham S, Piomelli S (1980). "Isozymes of human phosphofructokinase: identification and subunit structural characterization of a new system.". Proc. Natl. Acad. Sci. U.S.A. 77 (1): 62–6. PMID 6444721.
Koster JF, Slee RG, Van Berkel TJ (1980). "Isoenzymes of human phosphofructokinase.". Clin. Chim. Acta 103 (2): 169–73. PMID 6445244.
Vora S, Francke U (1981). "Assignment of the human gene for liver-type 6-phosphofructokinase isozyme (PFKL) to chromosome 21 by using somatic cell hybrids and monoclonal anti-L antibody.". Proc. Natl. Acad. Sci. U.S.A. 78 (6): 3738–42. PMID 6455664.
Zeitschel U, Bigl M, Eschrich K, Bigl V (1996). "Cellular distribution of 6-phosphofructo-1-kinase isoenzymes in rat brain.". J. Neurochem. 67 (6): 2573–80. PMID 8931492.
Hattori M, Fujiyama A, Taylor TD, et al. (2000). "The DNA sequence of human chromosome 21.". Nature 405 (6784): 311–9. doi:10.1038/35012518. PMID 10830953.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Gevaert K, Goethals M, Martens L, et al. (2004). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801.
Zhang C, Dowd DR, Staal A, et al. (2003). "Nuclear coactivator-62 kDa/Ski-interacting protein is a nuclear matrix-associated coactivator that may couple vitamin D receptor-mediated transcription and RNA splicing.". J. Biol. Chem. 278 (37): 35325–36. doi:10.1074/jbc.M305191200. PMID 12840015.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Colland F, Jacq X, Trouplin V, et al. (2004). "Functional proteomics mapping of a human signaling pathway.". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMID 15231748.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
Rush J, Moritz A, Lee KA, et al. (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.". Nat. Biotechnol. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455.