ATP-dependent 6-phosphofructokinase, platelet type (PFKP)
The protein contains 784 amino acids for an estimated molecular weight of 85596 Da.
Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. (updated: March 4, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
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Biological Process
Canonical glycolysis
Carbohydrate metabolic process
Carbohydrate phosphorylation
Cellular response to leukemia inhibitory factor
Fructose 1,6-bisphosphate metabolic process
Fructose 6-phosphate metabolic process
Glucose catabolic process
Glucose metabolic process
Glycolytic process
Pathogenesis
Protein homotetramerization
Small molecule metabolic process
The reference OMIM entry for this protein is 171840
Phosphofructokinase, platelet type; pfkp
Pfk, platelet type
Pfk, fibroblast type; pfkf
DESCRIPTION
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; 610681) and liver (PFKL; 171860) isoforms of phosphofructokinase, which map to chromosomes 12q13 and 21q22, respectively. Vora (1981) determined that full tetrameric phophofructokinase enzyme expressed in platelets can be composed of subunits P4, P3L, and P2L2.CLONING
Simpson and Fothergill-Gilmore (1991) isolated a cDNA corresponding to the PFKP gene from a human lymphocyte Raji cell line cDNA library using a cDNA for human muscle PFK as a probe. The deduced amino acid sequence showed 71% identity to the amino acid sequence for the human muscle isoenzyme and 63% identity to the human liver isoenzyme.GENE FUNCTION
Yi et al. (2012) demonstrated that the dynamic posttranslational modification of proteins by O-linked beta-N-acetylglucosamine (O-GlcNAcylation) is a key metabolic regulator of glucose metabolism. O-GlcNAcylation was induced at ser529 of phosphofructokinase-1 (PFK1) in response to hypoxia. Glycosylation inhibited PFK1 activity and redirected glucose flux through the pentose phosphate pathway, thereby conferring a selective growth advantage on cancer cells. Blocking glycosylation of PFK1 at ser529 reduced cancer cell proliferation in vitro and impaired tumor formation in vivo.MAPPING
Weil et al. (1980) developed a method of specific immunoprecipitation of human PFK and used it to locate the structural gene for fibroblast PFK (PFKF) to chromosome 10 in somatic cell hybrids. Vora et al. (1983) assigned the PFKP gene to 10p by use of a mouse antihuman P-subunit-specific antiserum in the study of human/rodent somatic cell hybrids. A single discordant hybrid cell containing only 10q did not express PFKP, and fibroblasts from a patient with duplication of 10p exhibited PFK activity values 180% of normal. Schwartz et al. (1984) confirmed the assignment of PFKP and hexokinase-1 (HK1; 142600) to 10p by dosage effects in a case of 10p partial trisomy. The synteny of PFKP and HK1 may have functional significance because the enzymes which they encode are the primary and secondary control points of the glycolytic pathway. By use of the cDNA clone as a biotinylated probe for in situ hybridization to human chromosome spreads, Morrison et al. (1992) assigned the PFKP gene to chromosome 10p15.3-p15.2.NOMENCLATURE
Francke (1983) suggested that this form of PFK is best called the 'platelet' type and symbolized PFKP because it is the only form made by platelets, whereas fibroblasts have more than one form of PFK. ... More on the omim web site
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 171840 was added.