Adenylate kinase isoenzyme 1 (AK1)
The protein contains 194 amino acids for an estimated molecular weight of 21635 Da.
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Also displays broad nucleoside diphosphate kinase activity. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. (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.
- 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.
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.
This protein is annotated as membranous in Gene Ontology.
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| Variant | Description |
|---|---|
| HAAKD | |
| HAAKD | |
| dbSNP:rs8192462 | |
| HAAKD | |
| HAAKD |
Biological Process
ADP biosynthetic process
AMP metabolic process
ATP metabolic process
Cell cycle arrest
Nucleobase-containing small molecule interconversion
Nucleobase-containing small molecule metabolic process
Nucleoside diphosphate phosphorylation
Nucleoside triphosphate biosynthetic process
Purine nucleotide metabolic process
Small molecule metabolic process
Cellular Component
Cytoplasm
Cytosol
Extracellular exosome
Outer dense fiber
Plasma membrane
Sperm flagellum
The reference OMIM entry for this protein is 103000
Adenylate kinase 1; ak1
Adenylate kinase, soluble
DESCRIPTION
Adenylate kinase (EC 2.7.4.3) is a ubiquitous monomeric enzyme that catalyzes the reversible conversion of MgATP plus AMP to MgADP plus ADP and contributes to homeostasis of the adenine nucleotide composition in the cell (Matsuura et al., 1989).CLONING
By screening a human genomic library with chicken Ak1 cDNA, Matsuura et al. (1989) cloned the AK1 gene. The deduced protein contains 194 amino acids. Northern blot analysis of human skeletal muscle RNA revealed transcripts of 0.9 and 2.5 kb that differed in their 3-prime tails.GENE STRUCTURE
Matsuura et al. (1989) determined that the AK1 gene spans 12 kb and has 7 exons. The 5-prime flanking region contains a TATA box and 3 putative SP1 (189906)-binding sites within a GC-rich region, but it has no typical CAAT box. The 3-prime region contains 3 canonical polyadenylation signals. Alu sequences are located in the large intron 5 and in the noncoding region of exon 7.MAPPING
Rapley et al. (1968) concluded that the AK locus is linked to the ABO (110300) locus with a recombination value of about 0.20. Schleutermann et al. (1969) found that the nail-patella syndrome locus (NPS1; 161200) and the AK locus are closely linked. No recombination was found in 53 opportunities. Fenger and Sorensen (1975) found a 1.33 to 1 ratio for the female to male recombination fractions between ABO and AK, but the difference between the recombination fractions was not significantly different from zero. All published data combined showed the most likely recombination fraction to be about 14%. Westerveld et al. (1976) found evidence that the AK locus assigned to chromosome 9 is the AK1 locus, or so-called red cell AK. In an early instance of deletion mapping, Ferguson-Smith et al. (1976) localized the ABO-NPS1-AK1 linkage group to 9q34 by regional assignment of AK1 in studies of a chromosome deletion. Cook et al. (1978) collated evidence that ABO-AK1 lie in band 9q34. They could exclude MNSs, GPT, and Gc from chromosome 9. AK1 is proximal to the break in the Philadelphia chromosome rearrangement (Geurts van Kessel et al., 1982). On the basis of a chromosome 9 aberration, an inverted paracentric insertion, inv ins(9)(q22.1q34.3q34.1), Allderdice et al. (1986) concluded that AK1 is located in 9q34.1-q34.3. Since AK1 is in 9q34 and is proximal to the breakpoint that creates the Philadelphia chromosome in chronic myeloid leukemia, located in band 9q34.1, AK1 and probably the linked ABO locus may be in the proximal part of 9q34.1.MOLECULAR GENETICS
Fildes and Harris (1966) found electrophoretic variation in red cells and defined 3 phenotypes, designated AK1, AK2-1 and AK2. All of the 141 children of 2 AK1 parents (62 such matings) were also AK1. Among the 136 children of AK1 by AK2-1 matings, 72 were AK1 and 64 AK2-1. AK1 and AK2 persons were thought to be homozygotes for a 2-allele system and AK2-1 persons heterozygotes. The frequency of the rarer AK2 allele was about 0.05 in the English and about 1 in 400 persons would be expected to be homozygous for this allele. Survey and family data were consistent. Singer and Brock (1971) identified a probably silent allele at the AK locus. Data on gene frequencies of allelic variants were tabulated by Roychoudhury and Nei (1988). In a patient with hemolytic anemia and adenylate kinase deficiency (612631), Matsuura et al. (1989) identified an arg128-to-trp mutation (103000.0001) in the AK1 gene. In 2 sibs of Ital ... 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 103000 was added.
Jan. 27, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed