Pyruvate kinase PKLR (PKLR)
The protein contains 574 amino acids for an estimated molecular weight of 61830 Da.
Plays a key role in glycolysis. (updated: April 1, 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.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- 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.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- 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.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
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
ATP biosynthetic process
Canonical glycolysis
Carbohydrate metabolic process
Cellular response to epinephrine stimulus
Cellular response to insulin stimulus
Endocrine pancreas development
Energy reserve metabolic process
Glucose metabolic process
Glycolytic process
Pathogenesis
Positive regulation of cellular metabolic process
Pyruvate biosynthetic process
Response to ATP
Response to cAMP
Response to glucose
Response to heat
Response to hypoxia
Response to lithium ion
Response to nutrient
Response to other organism
Small molecule metabolic process
Molecular Function
ATP binding
Kinase activity
Magnesium ion binding
Potassium ion binding
Pyruvate kinase activity
The reference OMIM entry for this protein is 102900
Adenosine triphosphate, elevated, of erythrocytes
Pyruvate kinase hyperactivity
A number sign (#) is used with this entry because of evidence that the phenotype of hereditary increase of red blood cell ATP is caused by a specific mutation in the gene for red cell pyruvate kinase (PKLR; 609712.0008). Brewer (1965) in the United States and Zurcher et al. (1965) in Holland described high erythrocyte adenosine triphosphate as a dominantly inherited trait. 'High red cell ATP syndrome' may be a heterogeneous category. For example, pyrimidine-5-prime-nucleotidase deficiency (266120) hemolytic anemia shows this feature. Max-Audit et al. (1980) described a family in which 4 persons had polycythemia and pyruvate kinase hyperactivity. They showed low 2,3-diphosphoglycerate (2,3-DPG) and high adenosine triphosphate (ATP) levels. The PK electrophoretic patterns in these persons were abnormal by the presence of several additional bands. Beutler et al. (1997) restudied the family described by Zurcher et al. (1965) and by SSCP analysis found a band shift in exon 2 of the red cell pyruvate kinase gene resulting from a point mutation at nucleotide 110. Beutler (1997) verified the mutation as a G-to-A transition resulting in a gly37-to-glu amino acid substitution (609712.0008). The mutation was present in heterozygous state. Beutler et al. (1997) stated it is possible that different mutations in the PKLR gene are responsible for the finding in other families with elevated red cell ATP levels, because the enzyme kinetics in other families have been different from those in the family reported by Zurcher et al. (1965). ... 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
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 102900 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 25, 2016: Protein entry updated
Automatic update: model status changed