CTSW (gene)
From Wikipedia, the free encyclopedia
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Cathepsin W
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| Identifiers | |||||||||||
| Symbol(s) | CTSW; LYPN | ||||||||||
| External IDs | OMIM: 602364 MGI: 1338045 HomoloGene: 37471 | ||||||||||
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| RNA expression pattern | |||||||||||
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| Orthologs | |||||||||||
| Human | Mouse | ||||||||||
| Entrez | 1521 | 13041 | |||||||||
| Ensembl | ENSG00000172543 | ENSMUSG00000024910 | |||||||||
| Uniprot | P56202 | Q8C2M0 | |||||||||
| Refseq | NM_001335 (mRNA) NP_001326 (protein) |
NM_009985 (mRNA) NP_034115 (protein) |
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| Location | Chr 11: 65.4 - 65.41 Mb | Chr 19: 5.47 - 5.47 Mb | |||||||||
| Pubmed search | [1] | [2] | |||||||||
Cathepsin W, also known as CTSW, is a human gene.[1]
The protein encoded by this gene, a member of the peptidase C1 family, is a cysteine proteinase that may have a specific function in the mechanism or regulation of T-cell cytolytic activity. The encoded protein is found associated with the membrane inside the endoplasmic reticulum of natural killer and cytotoxic T-cells. Expression of this gene is up-regulated by interleukin-2.[1]
[edit] References
[edit] Further reading
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:. PMID 15489334.
- Meinhardt C, Peitz U, Treiber G, et al. (2004). "Identification of a novel isoform predominantly expressed in gastric tissue and a triple-base pair polymorphism of the cathepsin W gene.". Biochem. Biophys. Res. Commun. 321 (4): 975–80. doi:. PMID 15358123.
- Zhang Z, Henzel WJ (2005). "Signal peptide prediction based on analysis of experimentally verified cleavage sites.". Protein Sci. 13 (10): 2819–24. doi:. PMID 15340161.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:. PMID 12477932.
- Buhling F, Kellner U, Guenther D, et al. (2003). "Characterization of novel anti-cathepsin W antibodies and cellular distribution of cathepsin W in the gastrointestinal tract.". Biol. Chem. 383 (7-8): 1285–9. PMID 12437118.
- Wex T, Bühling F, Wex H, et al. (2001). "Human cathepsin W, a cysteine protease predominantly expressed in NK cells, is mainly localized in the endoplasmic reticulum.". J. Immunol. 167 (4): 2172–8. PMID 11490002.
- Wex T, Levy B, Wex H, Brömme D (2000). "Human cathepsins W and F form a new subgroup of cathepsins that is evolutionary separated from the cathepsin B- and L-like cysteine proteases.". Adv. Exp. Med. Biol. 477: 271–80. PMID 10849754.
- Brinkworth RI, Tort JF, Brindley PJ, Dalton JP (2000). "Phylogenetic relationships and theoretical model of human cathepsin W (lymphopain), a cysteine proteinase from cytotoxic T lymphocytes.". Int. J. Biochem. Cell Biol. 32 (3): 373–84. PMID 10716634.
- Wex T, Levy B, Wex H, Brömme D (1999). "Human cathepsins F and W: A new subgroup of cathepsins.". Biochem. Biophys. Res. Commun. 259 (2): 401–7. doi:. PMID 10362521.
- Brown J, Matutes E, Singleton A, et al. (1998). "Lymphopain, a cytotoxic T and natural killer cell-associated cysteine proteinase.". Leukemia 12 (11): 1771–81. PMID 9823953.
- Wex T, Levy B, Smeekens SP, et al. (1998). "Genomic structure, chromosomal localization, and expression of human cathepsin W.". Biochem. Biophys. Res. Commun. 248 (2): 255–61. doi:. PMID 9675123.
- Linnevers C, Smeekens SP, Brömme D (1997). "Human cathepsin W, a putative cysteine protease predominantly expressed in CD8+ T-lymphocytes.". FEBS Lett. 405 (3): 253–9. PMID 9108299.
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