Protein adenylyltransferase SelO, mitochondrial (SELO)
The protein contains 669 amino acids for an estimated molecular weight of 73489 Da.
Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr and Tyr residues of target proteins (AMPylation) (PubMed:30270044). May be a redox-active mitochondrial selenoprotein which interacts with a redox target protein (PubMed:24751718). (updated: Feb. 13, 2019)
Protein identification was indicated in the following studies:
- 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.
- 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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| Variant | Description |
|---|---|
| dbSNP:rs5771225 | |
| dbSNP:rs2272846 | |
| dbSNP:rs2272852 | |
| dbSNP:rs17013238 |
No binding partner found
The reference OMIM entry for this protein is 607917
Selenoprotein o
Selo
DESCRIPTION
Selenoproteins, such as SELO, contain the rare twenty-first amino acid, selenocysteine (sec). These proteins lack common amino acid sequence motifs, but the 3-prime untranslated regions of selenoprotein genes have a common stem-loop structure, the sec insertion sequence (SECIS), that is necessary for the recognition of UGA as a sec codon rather than as a stop signal (summary by Kryukov et al., 1999 and Kryukov et al., 2003).CLONING
By searching databases using a SECIS-based method to identify putative selenoproteins, Kryukov et al. (2003) identified SELO. The deduced 669-amino acid globular protein contains a sec at position 667, near the C terminus. SELO mRNA was detected in a variety of tissues and cell types.GENE STRUCTURE
Kryukov et al. (2003) reported that the SELO gene contains 9 exons.MAPPING
Kryukov et al. (2003) reported that the SELO gene maps to chromosome 22q13.33. ... More on the omim web site
Feb. 22, 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. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 607917 was added.