Acylphosphatase-1 (ACYP1)
The protein contains 99 amino acids for an estimated molecular weight of 11261 Da.
Its physiological role is not yet clear. (updated: Sept. 12, 2018)
Protein identification was indicated in the following studies:
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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No binding partner found
Cellular Component
The reference OMIM entry for this protein is 600875
Acylphosphatase, erythrocyte; acyp1
Acype
DESCRIPTION
Acylphosphatase (EC 3.6.1.7) is a small cytosolic enzyme with a molecular mass of 11 kD that is expressed in many vertebrate tissues. The enzyme catalyzes the hydrolysis of the carboxyl-phosphate bond of acyl phosphates. Two isoenzymes have been isolated, called muscle acylphosphatase (102595) and erythrocyte acylphosphatase on the basis of their tissue localization (summary by Fiaschi et al., 1995).CLONING
Liguri et al. (1986) reported the isolation and characterization of a human erythrocyte acylphosphatase isoenzyme. The protein contains 98 amino acid residues; it has an acetylated N terminus and does not contain cysteine. It shares 56% sequence identity with human muscle acylphosphatase. The erythrocyte enzyme showed hydrolytic activity on acyl phosphates with higher affinity than the muscle enzyme for some substrates and phosphorylated inhibitors. Fiaschi et al. (1995) isolated and characterized 3 independent cDNAs coding for the erythrocyte isoform. All the clones were incomplete at the 5-prime end, but Northern blot analysis using cDNA as a probe showed the presence of an unusually long 5-prime untranslated region in the mRNA.MAPPING
By analysis of somatic cell hybrids and FISH, Fiaschi et al. (1998) mapped the ACYP1 gene to human chromosome 14q24.3. ... More on the omim web site
Oct. 19, 2018: Protein entry updated
Automatic update: OMIM entry 600875 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).