TSC22 domain family protein 4 (TSC22D4)
The protein contains 395 amino acids for an estimated molecular weight of 41026 Da.
Transcriptional repressor. (updated: April 1, 2015)
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.
- 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.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- 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.
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| Variant | Description |
|---|---|
| a breast cancer sample; somatic mutation |
The reference OMIM entry for this protein is 611914
Tsc22 domain family, member 4; tsc22d4
Tsc22 homologous gene 1; thg1
Tsc22-like
DESCRIPTION
TSC22D4 is a member of the TSC22 domain family of leucine zipper transcriptional regulators (see TSC22D3; 300506) (Kester et al., 1999; Fiorenza et al., 2001).CLONING
By yeast 2-hybrid screening of a mouse brain cDNA library using TSC22D1 (607715) as bait, followed by database analysis, Kester et al. (1999) cloned human and mouse TSC22D4, which they called THG1. The deduced 395-amino acid human protein contains a TSC box and leucine zipper region and has a calculated molecular mass of 41 kD. TSC22D4 shares similarity with TSC22D1, TSC22D3, KIAA0669, and Drosophila 'shortsighted' shs over the TSC box leucine zipper domain. Fiorenza et al. (2001) used differential screening by subtractive hybridization of cDNAs isolated from embryonic day 12.5 wildtype and Lhx3 (LHX4; 602146) mutant mouse pituitaries to clone mouse Tsc22d4, which they called Thg-1pit. The 387-amino acid mouse protein shares 79% amino acid identity with human TSC22D4. Fiorenza et al. (2001) showed that mouse Tsc22d4 expression in the pituitary cell line GH3 was induced in response to TGF-beta (TGFB1; 190180). RT-PCR assays detected Tsc22d4 expression during mouse embryonic development with expression first detected at stage 98.5 followed by a sharp increase during the next 24 hours that coincided with initiation of Lhx3 expression and preceded formation of the pituitary rudiment. A second increase in Tsc22d4 expression at embryonic day 12.5 coincided with development of Rathke's pouch. Tsc22d4 expression was also detected in the entire central nervous system. In contrast, Tsc22d4 expression in Lhx3 mutant mouse embryos showed an absence of pituitary expression of Tsc22d4 although expression in the rest of the brain was no different from wildtype. Fiorenza et al. (2001) concluded that Tsc22d4 is regulated by Lhx3 during pituitary organogenesis.GENE FUNCTION
By yeast 2-hybrid analysis, gel shift assay, and GST pull-down experiments, Kester et al. (1999) confirmed that TSC22D4 interacts with TSC22D1 by forming heterodimers. They demonstrated that TSC22D4 has transcriptional repressor activity. ... More on the omim web site
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 611914 was added.