PFKP

Phosphofructokinase, platelet

Available structures

Ortholog search: PDBe, RCSB

List of PDB id codes
4U1R, 4WL0, 4XYJ, 4XYK, 4XZ2

Identifiers

Symbols

PFKP ; ATP-PFK; PFK-C; PFK-P; PFKF

External IDs

OMIM: 171840 MGI: 1891833 HomoloGene: 20579 ChEMBL: 2972 GeneCards: PFKP Gene

EC number

2.7.1.11

Gene ontology
Molecular function	• 6-phosphofructokinase activity • ATP binding • protein complex binding • metal ion binding
Cellular component	• nucleus • cytosol • membrane • extracellular exosome
Biological process	• carbohydrate metabolic process • fructose 6-phosphate metabolic process • glucose metabolic process • small molecule metabolic process • carbohydrate phosphorylation • canonical glycolysis • activation of mitophagy in response to mitochondrial depolarization
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 10:
3.07 – 3.14 Mb

Chr 13:
6.58 – 6.65 Mb

PubMed search

Phosphofructokinase, platelet, also known as PFKP is an enzyme which in humans is encoded by the PFKP gene.^[1]

Function

The PFKP gene encodes the platelet isoform of phosphofructokinase (PFK) (ATP:D-fructose-6-phosphate-1-phosphotransferase, EC 2.7.1.11). PFK catalyzes the irreversible conversion of fructose 6-phosphate to fructose 1,6-bisphosphate and is a key regulatory enzyme in glycolysis. The PFKP gene, which maps to chromosome 10p, is also expressed in fibroblasts. See also the muscle (PFKM) and liver (PFKL) isoforms of phosphofructokinase, which map to chromosomes 12q13 and 21q22, respectively. Full tetrameric phosphofructokinase enzyme expressed in platelets can be composed of subunits P4, P3L, and P2L2.^[2]^[1]

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles. ^{[§ 1]}

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|{{{bSize}}}px|alt=Glycolysis and Gluconeogenesis edit]]

Glycolysis and Gluconeogenesis edit

↑ The interactive pathway map can be edited at WikiPathways: "GlycolysisGluconeogenesis_WP534".

References

1 2 "Entrez Gene: PFKP phosphofructokinase, platelet".
↑ Vora S (April 1981). "Isozymes of human phosphofructokinase in blood cells and cultured cell lines: molecular and genetic evidence for a trigenic system". Blood 57 (4): 724–32. PMID 6451249.

Meienhofer MC, Lagrange JL, Cottreau D, et al. (1979). "Phosphofructokinase in human blood cells". Blood 54 (2): 389–400. PMID 156568.
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. doi:10.1007/bf00273280. PMID 156693.
Morrison N, Simpson C, Fothergill-Gilmore L, et al. (1992). "Regional chromosomal assignment of the human platelet phosphofructokinase gene to 10p15". Hum. Genet. 89 (1): 105–6. doi:10.1007/BF00207053. PMID 1533608.
Simpson CJ, Fothergill-Gilmore LA (1991). "Isolation and sequence of a cDNA encoding human platelet phosphofructokinase". Biochem. Biophys. Res. Commun. 180 (1): 197–203. doi:10.1016/S0006-291X(05)81276-8. PMID 1834056.
Nakajima H, Noguchi T, Yamasaki T, et al. (1987). "Cloning of human muscle phosphofructokinase cDNA". FEBS Lett. 223 (1): 113–6. doi:10.1016/0014-5793(87)80519-7. PMID 2822475.
Eto K, Sakura H, Yasuda K, et al. (1994). "Cloning of a complete protein-coding sequence of human platelet-type phosphofructokinase isozyme from pancreatic islet". Biochem. Biophys. Res. Commun. 198 (3): 990–8. doi:10.1006/bbrc.1994.1141. PMID 8117307.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
Adam GC, Sorensen EJ, Cravatt BF (2003). "Trifunctional chemical probes for the consolidated detection and identification of enzyme activities from complex proteomes". Mol. Cell Proteomics 1 (10): 828–35. doi:10.1074/mcp.T200007-MCP200. PMID 12438565.
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. PMC 139241. PMID 12477932.
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.
Navarro-Lérida I, Martínez Moreno M, Roncal F, et al. (2004). "Proteomic identification of brain proteins that interact with dynein light chain LC8". Proteomics 4 (2): 339–46. doi:10.1002/pmic.200300528. PMID 14760703.
Beausoleil SA, Jedrychowski M, Schwartz D, et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
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. PMC 528928. 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.
Hannemann A, Jandrig B, Gaunitz F, et al. (2005). "Characterization of the human P-type 6-phosphofructo-1-kinase gene promoter in neural cell lines". Gene 345 (2): 237–47. doi:10.1016/j.gene.2004.11.018. PMID 15716112.
Beausoleil SA, Villén J, Gerber SA, et al. (2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". Nat. Biotechnol. 24 (10): 1285–92. doi:10.1038/nbt1240. PMID 16964243.
Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein–protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
Martínez-Costa OH, Sánchez-Martínez C, Sánchez V, Aragón JJ (2007). "Chimeric phosphofructokinases involving exchange of the N- and C-terminal halves of mammalian isozymes: implications for ligand binding sites". FEBS Lett. 581 (16): 3033–8. doi:10.1016/j.febslet.2007.05.059. PMID 17544406.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

Transferases: phosphorus-containing groups (EC 2.7)

2.7.1-2.7.4:
phosphotransferase/kinase
(PO₄)

2.7.1: OH acceptor	Hexo- Gluco- Fructo- Hepatic Galacto- Phosphofructo- 1 Liver Muscle Platelet 2 Riboflavin Shikimate Thymidine ADP-thymidine NAD⁺ Glycerol Pantothenate Mevalonate Pyruvate Deoxycytidine PFP Diacylglycerol Phosphoinositide 3 Class I PI 3 Class II PI 3 Sphingosine Glucose-1,6-bisphosphate synthase

2.7.2: COOH acceptor	Phosphoglycerate Aspartate kinase

2.7.3: N acceptor	Creatine

2.7.4: PO₄ acceptor	Phosphomevalonate Adenylate Nucleoside-diphosphate Uridylate Guanylate Thiamine-diphosphate

2.7.6: diphosphotransferase
(P₂O₇)

2.7.7: nucleotidyltransferase
(PO₄-nucleoside)

Polymerase

DNA polymerase	DNA-directed DNA polymerase I II III IV V RNA-directed DNA polymerase Reverse transcriptase Telomerase DNA nucleotidylexotransferase/Terminal deoxynucleotidyl transferase

RNA nucleotidyltransferase	RNA polymerase/DNA-directed RNA polymerase RNA polymerase I RNA polymerase II RNA polymerase III RNA polymerase IV Primase RNA-dependent RNA polymerase PNPase

Phosphorolytic
3' to 5' exoribonuclease

Nucleotidyltransferase

Guanylyltransferase

mRNA capping enzyme

Other

2.7.8: miscellaneous

Phosphatidyltransferases	CDP-diacylglycerol—glycerol-3-phosphate 3-phosphatidyltransferase CDP-diacylglycerol—serine O-phosphatidyltransferase CDP-diacylglycerol—inositol 3-phosphatidyltransferase CDP-diacylglycerol—choline O-phosphatidyltransferase

Glycosyl-1-phosphotransferase	N-acetylglucosamine-1-phosphate transferase

2.7.10-2.7.13: protein kinase
(PO₄; protein acceptor)

2.7.10: protein-tyrosine	see tyrosine kinases

2.7.11: protein-serine/threonine	see serine/threonine-specific protein kinases

2.7.12: protein-dual-specificity	see serine/threonine-specific protein kinases

2.7.13: protein-histidine	Protein-histidine pros-kinase Protein-histidine tele-kinase Histidine kinase

Metabolism: carbohydrate metabolism: glycolysis/gluconeogenesis enzymes

Glycolysis

Gluconeogenesis only

to oxaloacetate:	Pyruvate carboxylase Phosphoenolpyruvate carboxykinase

from lactate (Cori cycle):	Lactate dehydrogenase

from alanine (Alanine cycle):	Alanine transaminase

from glycerol:	Glycerol kinase Glycerol dehydrogenase

Regulatory

This article is issued from Wikipedia - version of the Monday, July 27, 2015. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.

PFKP

Function

Interactive pathway map

References

Further reading