Malignant T-cell-amplified sequence 1 (MCTS1)
The protein contains 181 amino acids for an estimated molecular weight of 20555 Da.
Anti-oncogene that plays a role in cell cycle regulation; decreases cell doubling time and anchorage-dependent growth; shortens the duration of G1 transit time and G1/S transition. When constitutively expressed, increases CDK4 and CDK6 kinases activity and CCND1/cyclin D1 protein level, as well as G1 cyclin/CDK complex formation. Involved in translation initiation; promotes recruitment of aminoacetyled initiator tRNA to P site of 40S ribosomes. Can promote release of deacylated tRNA and mRNA from recycled 40S subunits following ABCE1-mediated dissociation of post-termination ribosomal complexes into subunits. Plays a role as translation enhancer; recruits the density-regulated protein/DENR and binds to the cap complex of the 5'-terminus of mRNAs, subsequently altering the mRNA translation profile; up-regulates protein levels of BCL2L2, TFDP1, MRE11, CCND1 and E2F1, while mRNA levels remains constant. Hyperactivates DNA damage signaling pathway; increased gamma-irradiation-induced phosphorylation of histone H2AX, and induces damage foci formation. Increases the overall number of chromosomal abnormalities such as larger chromosomes formation and multiple chromosomal fusions when overexpressed in gamma-irradiated cells. May play a role in promoting lymphoid tumor development: lymphoid cell lines overexpressing MCTS1 exhibit increased growth rates and display increased protection against apoptosis. May contribute to the pathogenesis and progression of breast cancer via promotion (updated: June 2, 2021)
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.
- 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.
This protein is annotated as membranous in Gene Ontology.
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| Variant | Description |
|---|---|
| dbSNP:rs2233110 |
Biological Process
Cell cycle
Cellular response to DNA damage stimulus
Formation of translation preinitiation complex
IRES-dependent translational initiation of linear mRNA
IRES-dependent viral translational initiation
Positive regulation of cell population proliferation
Regulation of growth
Regulation of transcription, DNA-templated
Ribosome disassembly
Transcription, DNA-templated
Translation reinitiation
The reference OMIM entry for this protein is 300587
Malignant t-cell amplified sequence 1; mcts1
Mct1
CLONING
Prosniak et al. (1998) identified MCTS1, which they called MCT1, based on its amplification in a T-cell lymphoma cell line derived from a patient with Sezary syndrome. Using 5-prime RACE, they obtained a full-length MCT1 cDNA. The deduced 181-amino acid protein has a calculated molecular mass of 20 kD. MCT1 has 4 phosphorylation sites and a 58-amino acid C-terminal domain similar to the protein-protein interaction domain of cyclin H (CCNH; 601953). Northern blot analysis detected low ubiquitous expression of an MCT1 transcript smaller than 1 kb.GENE FUNCTION
Prosniak et al. (1998) found that overexpression of MCT1 in mouse fibroblasts increased the cell proliferative rate by decreasing the length of the G1 phase without a reciprocal increase in the S and G2-M phases. Overexpression of MCT1 also supported anchorage-independent growth. Shi et al. (2003) found increased MCT1 protein expression in a panel of T-cell lymphoid cell lines, in non-Hodgkin lymphoma cell lines, and in a subset of primary diffuse large B-cell lymphomas. All transformed follicular lymphomas demonstrated elevated MCT1 protein levels. MCT1 protein was not detected in leukemic cells from patients with chronic lymphocytic leukemia or in any healthy lymphoid tissue examined. Lymphoid cell lines overexpressing MCT1 exhibited increased growth and were protected from serum starvation-induced apoptosis. MCT1-overexpressing cells showed constitutively higher levels of phosphorylated AKT (164730) protein, especially under serum starvation. Schleich et al. (2014) uncovered the noncanonical initiation factors density-regulated protein (DENR; 604550) and MCT1 as the first selective regulators of eukaryotic reinitiation. mRNAs containing upstream open reading frames (ORFs) with strong Kozak sequences selectively required DENR-MCT1 for their proper translation, yielding a novel class of mRNAs that can be coregulated and that is enriched for regulatory proteins such as oncogenic kinases. Schleich et al. (2014) concluded that their data revealed that cells have a theretofore unappreciated translational control system with a key role in supporting proliferation and tissue growth.GENE STRUCTURE
Shi et al. (2003) determined that the MCTS1 promoter is TATA-less, and they identified an enhancer region required for maximum MCTS1 transcription.MAPPING
By FISH, Prosniak et al. (1998) mapped the MCTS1 gene to chromosome Xq22-q24. ... More on the omim web site
July 1, 2021: 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
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 300587 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed