Damage-control phosphatase ARMT1 (C6orf211)
The protein contains 441 amino acids for an estimated molecular weight of 51172 Da.
Metal-dependent phosphatase that shows phosphatase activity against several substrates, including fructose-1-phosphate and fructose-6-phosphate (By similarity). Its preference for fructose-1-phosphate, a strong glycating agent that causes DNA damage rather than a canonical yeast metabolite, suggests a damage-control function in hexose phosphate metabolism (By similarity). Has also been shown to have O-methyltransferase activity that methylates glutamate residues of target proteins to form gamma-glutamyl methyl ester residues (PubMed:25732820). Possibly methylates PCNA, suggesting it is involved in the DNA damage response (PubMed:25732820). (updated: July 3, 2019)
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
Cellular response to DNA damage stimulus
Methylation
Regulation of response to DNA damage stimulus
Cellular Component
The reference OMIM entry for this protein is 616332
Acidic residue methyltransferase 1; armt1
Chromosome 6 open reading frame 211; c6orf211
DESCRIPTION
ARMT1 is a protein-glutamate O-methyltransferase (EC 2.1.1.80) that transfers the methyl group from the cofactor S-adenosyl methionine (SAM) onto protein substrates. ARMT1 may play a role in DNA damage response (summary by Perry et al., 2015).CLONING
By performing assays for carboxyl methyltransferase activity in fractionated human breast cancer cells, followed by mass spectrometric and database analyses, Perry et al. (2015) identified ARMT1. The deduced 441-amino acid protein shares significant structural similarity with SAM-dependent methyltransferases.GENE FUNCTION
By assaying recombinant protein expressed in bacteria, Perry et al. (2015) found that ARMT1 showed carboxyl methyltransferase activity directed toward PCNA (176740), which functions as a sliding clamp during DNA replication and repair. ARMT1 also showed automethylation activity that appeared to function in a negative-feedback loop. Knockdown of ARMT1 via short hairpin RNA sensitized SK-Br-3 human breast cancer cells to DNA damage, but it induced resistance to DNA damage in MCF7 human breast cancer cells.MAPPING
Hartz (2015) mapped the ARMT1 gene to chromosome 6q25.1 based on an alignment of the ARMT1 sequence (GenBank GENBANK AK022972) with the genomic sequence (GRCh38). ... More on the omim web site
July 4, 2019: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 10, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 10, 2018: Protein entry updated
Automatic update: OMIM entry 616332 was added.
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated