PFKP

Mammalian protein found in Homo sapiens
PFKP
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

4RH3, 4U1R, 4WL0, 4XYJ, 4XYK, 4XZ2

Identifiers
AliasesPFKP, ATP-PFK, PFK-C, PFK-P, PFKF, phosphofructokinase, platelet
External IDsOMIM: 171840; MGI: 1891833; HomoloGene: 20579; GeneCards: PFKP; OMA:PFKP - orthologs
Gene location (Human)
Chromosome 10 (human)
Chr.Chromosome 10 (human)[1]
Chromosome 10 (human)
Genomic location for PFKP
Genomic location for PFKP
Band10p15.2Start3,066,333 bp[1]
End3,137,718 bp[1]
Gene location (Mouse)
Chromosome 13 (mouse)
Chr.Chromosome 13 (mouse)[2]
Chromosome 13 (mouse)
Genomic location for PFKP
Genomic location for PFKP
Band13|13 A1Start6,629,804 bp[2]
End6,698,813 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • saphenous vein

  • spinal ganglia

  • Brodmann area 9

  • sperm

  • cingulate gyrus

  • prefrontal cortex

  • left ventricle

  • pons

  • ascending aorta

  • right coronary artery
Top expressed in
  • facial motor nucleus

  • superior frontal gyrus

  • anterior horn of spinal cord

  • cingulate gyrus

  • spermatocyte

  • pontine nuclei

  • cerebellar cortex

  • amygdala

  • intestinal villus

  • prefrontal cortex
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • transferase activity
  • nucleotide binding
  • protein-containing complex binding
  • metal ion binding
  • kinase activity
  • catalytic activity
  • ATP binding
  • 6-phosphofructokinase activity
  • cadherin binding
  • identical protein binding
  • AMP binding
  • monosaccharide binding
  • fructose-6-phosphate binding
Cellular component
  • cytosol
  • membrane
  • extracellular exosome
  • nucleus
  • cytoplasm
  • extracellular matrix
  • 6-phosphofructokinase complex
Biological process
  • fructose 6-phosphate metabolic process
  • glycolytic process
  • phosphorylation
  • canonical glycolysis
  • metabolism
  • cellular response to leukemia inhibitory factor
  • glucose catabolic process
  • fructose 1,6-bisphosphate metabolic process
  • protein complex oligomerization
  • protein homotetramerization
  • glycolytic process through fructose-6-phosphate
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

5214

56421

Ensembl

ENSG00000067057

ENSMUSG00000021196

UniProt

Q01813

Q9WUA3

RefSeq (mRNA)
NM_001242339
NM_002627
NM_001323067
NM_001323068
NM_001323069

NM_001323070
NM_001323071
NM_001323072
NM_001323073
NM_001323074
NM_001345944

NM_001291071
NM_019703

RefSeq (protein)
NP_001229268
NP_001309996
NP_001309997
NP_001309998
NP_001309999

NP_001310000
NP_001310001
NP_001310002
NP_001310003
NP_001332873
NP_002618

NP_001278000
NP_062677

Location (UCSC)Chr 10: 3.07 – 3.14 MbChr 13: 6.63 – 6.7 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Phosphofructokinase, platelet, also known as PFKP is an enzyme which in humans is encoded by the PFKP gene.[5]

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.[5][6]

Interactive pathway map

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

[[File:
GlycolysisGluconeogenesis_WP534go to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to WikiPathwaysgo to articlego to Entrezgo to article
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GlycolysisGluconeogenesis_WP534go to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to WikiPathwaysgo to articlego to Entrezgo to article
|alt=Glycolysis and Gluconeogenesis edit]]
Glycolysis and Gluconeogenesis edit
  1. ^ The interactive pathway map can be edited at WikiPathways: "GlycolysisGluconeogenesis_WP534".

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000067057 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000021196 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b "Entrez Gene: PFKP phosphofructokinase, platelet".
  6. ^ 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. doi:10.1182/blood.V57.4.724.724. PMID 6451249.

Further reading

  • Meienhofer MC, Lagrange JL, Cottreau D, et al. (1979). "Phosphofructokinase in human blood cells". Blood. 54 (2): 389–400. doi:10.1182/blood.V54.2.389.389. 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. S2CID 23300861.
  • 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. S2CID 42022687.
  • 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. S2CID 42849336.
  • 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. Bibcode:2002PNAS...9916899M. 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. S2CID 8868600.
  • 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. Bibcode:2004PNAS..10112130B. 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. S2CID 7200157.
  • 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. S2CID 14294292.
  • 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. S2CID 20271498.

External links

  • Overview of all the structural information available in the PDB for UniProt: Q01813 (Human ATP-dependent 6-phosphofructokinase, platelet type) at the PDBe-KB.

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


  • v
  • t
  • e
Transferases: phosphorus-containing groups (EC 2.7)
2.7.1-2.7.4:
phosphotransferase/kinase
(PO4)
2.7.1: OH acceptor
2.7.2: COOH acceptor
2.7.3: N acceptor
2.7.4: PO4 acceptor
2.7.6: diphosphotransferase
(P2O7)2.7.7: nucleotidyltransferase
(PO4-nucleoside)
Polymerase
DNA polymerase
DNA-directed DNA polymerase
I/A
γ
θ
ν
T7
Taq
II/B
α
δ
ε
ζ
Pfu
III/C
IV/X
β
λ
μ
TDT
V/Y
η
ι
κ
RNA-directed DNA polymerase
Reverse transcriptase
Telomerase
RNA polymerase
Phosphorolytic
3' to 5' exoribonuclease
Nucleotidyltransferase
Guanylyltransferase
Other
2.7.8: miscellaneous
Phosphatidyltransferases
Glycosyl-1-phosphotransferase
2.7.10-2.7.13: protein kinase
(PO4; protein acceptor)
2.7.10: protein-tyrosine
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
  • v
  • t
  • e
Glycolysis
Gluconeogenesis only
to oxaloacetate:
from lactate (Cori cycle):
from alanine (Alanine cycle):
from glycerol:
Regulatory


Stub icon

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  • v
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