Erythroid membrane-associated protein (ERMAP)
The protein contains 475 amino acids for an estimated molecular weight of 52605 Da.
Possible role as a cell-adhesion or receptor molecule of erythroid cells. (updated: Sept. 12, 2018)
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.
- 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.
This protein is annotated as membranous in Gene Ontology, is annotated as membranous in UniProt, is predicted to be membranous by TOPCONS.
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No binding partner found
Biological Process
Regulation of cytokine production
Regulation of immune response
T cell receptor signaling pathway
The reference OMIM entry for this protein is 111620
Radin blood group antigen; rd
Blood group--radin antigen
A number sign (#) is used with this entry because of evidence that the Radin antigen (Rd) belongs to the Scianna blood group system (111750) and is determined by a specific change in the gene encoding erythroblast membrane-associated protein (ERMAP; 609017).
DESCRIPTION
Radin is a rare red cell antigen discovered by Rausen et al. (1967) in 5 families with varying ethnic backgrounds. It has been shown to cause mild to moderate hemolytic disease of the newborn in some cases. The Radin antigen is determined by a polymorphism in the ERMAP gene (609017.0003) and thus is a member of the blood group Scianna (Wagner et al., 2003). Radin has alternatively been labeled Sc4 to reflect this relationship. Harvey et al. (1983) estimated the frequency of the Radin antigen among Europeans to be 0.04% to 0.66% with the highest frequencies occurring among Swedes and Danes.MAPPING
Lewis and Kaita (1979) found linkage of Rd with Rh (lod score of 3.89 at a recombination fraction of 0.10). This suggested that Radin might be part of the Scianna system, since the latter locus is on 1p in the region of Rh. Lewis et al. (1980) presented evidence that the Radin blood group antigen is governed by a locus called Rd, which is located between PGM1 (171900) and alpha-fucosidase--Rh, and is either very closely linked to or identical with Sc. Hilden et al. (1985) found linkage of Rd to chromosome 1 in 9 of 11 families studied.MOLECULAR GENETICS
Wagner et al. (2003) demonstrated heterozygosity for a pro60-to-ala allele in the ERMAP gene (609017.0003) in an Rd+ proband. ... More on the omim web site
June 30, 2020: Protein entry updated
Automatic update: OMIM entry 111620 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).