Translation machinery-associated protein 7 (TMA7)
The protein contains 64 amino acids for an estimated molecular weight of 7066 Da.
No function (updated: Oct. 10, 2018)
Protein identification was indicated in the following studies:
- 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.
- 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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No binding partner found
The reference OMIM entry for this protein is 615808
Translation machinery-associated 7, s. cerevisiae, homolog of; tma7
Hspc016
CLONING
Dermal papilla cells are mesenchymal cells located at the bottom of hair follicles. In culture, they initially resemble fibroblasts, but then aggregate into clumps of overlapping cells with growth. Using suppression subtractive hybridization to identify genes expressed only in aggregating normal human dermal papilla cells in culture, followed by 5-prime and 3-prime RACE, Song et al. (2005) cloned TMA7, which they called HSPC016. The deduced protein contains 64 amino acids. Northern blot and RT-PCR analyses confirmed high HSPC016 expression in aggregative dermal papilla cells. EST database analysis revealed widespread HSPC016 expression, with highest expression in posterior tongue, anterior rhombomeres, skin, bone marrow, first pharyngeal arch, and several tumors. Song et al. (2005) identified orthologs of HSPC016 in Drosophila, C. elegans, yeast, fungi, and higher plants. Using Western blot analysis, Song et al. (2012) determined that recombinant human HSPC016 had an apparent molecular mass of 7.2 kD.GENE FUNCTION
Early-passage normal human dermal papilla cells tend to aggregate, but they lose the ability to aggregate at high passage numbers. Using small interfering RNA, Song et al. (2012) found that knockdown of HSPC016 reduced the ability of early-passage dermal papilla cells to aggregate and caused morphologic changes, including a switch from oval shape to fusiform. In contrast, addition of recombinant human HSPC016 to the culture medium increased the ability of late-passage dermal papilla cells to aggregate.GENE STRUCTURE
Song et al. (2005) determined that the TMA7 gene contains 4 exons.MAPPING
Song et al. (2005) reported that the TMA7 gene maps to chromosome 3p21.31. ... More on the omim web site
Feb. 23, 2019: Protein entry updated
Automatic update: model status changed
Oct. 20, 2018: Protein entry updated
Automatic update: OMIM entry 615808 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).