ST13
Template:PBB Hsc70-interacting protein also known as suppression of tumorigenicity 13 (ST13) is a protein that in humans is encoded by the ST13 gene.[1][2][3]
Function
The protein encoded by this gene is an adaptor protein that mediates the association of the heat shock proteins HSP70 and HSP90. This protein has been shown to be involved in the assembly process of glucocorticoid receptor, which requires the assistance of multiple molecular chaperones. The expression of this gene is reported to be downregulated in colorectal carcinoma tissue suggesting that is a candidate tumor suppressor gene.[3]
References
- ^ Zhang Y, Cai X, Schlegelberger B, Zheng S (Mar 1999). "Assignment1 of human putative tumor suppressor genes ST13 (alias SNC6) and ST14 (alias SNC19) to human chromosome bands 22q13 and 11q24→q25 by in situ hybridization". Cytogenet Cell Genet. 83 (1–2): 56–7. doi:10.1159/000015125. PMID 9925927.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Prapapanich V, Chen S, Nair SC, Rimerman RA, Smith DF (Oct 1996). "Molecular cloning of human p48, a transient component of progesterone receptor complexes and an Hsp70-binding protein". Mol Endocrinol. 10 (4): 420–31. doi:10.1210/me.10.4.420. PMID 8721986.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ a b "Entrez Gene: ST13 suppression of tumorigenicity 13 (colon carcinoma) (Hsp70 interacting protein)".
Further reading
- Prapapanich V, Chen S, Toran EJ, et al. (1996). "Mutational analysis of the hsp70-interacting protein Hip". Mol. Cell. Biol. 16 (11): 6200–7. PMC 231623. PMID 8887650.
- Cao J, Cai X, Zheng L, et al. (1997). "Characterization of colorectal-cancer-related cDNA clones obtained by subtractive hybridization screening". J. Cancer Res. Clin. Oncol. 123 (8): 447–51. doi:10.1007/BF01372549. PMID 9292708.
- Mo Y, Zheng S, Shen D (1998). "[Differential expression of HSU17714 gene in colorectal cancer and normal colonic mucosa]". Zhonghua Zhong Liu Za Zhi. 18 (4): 241–3. PMID 9387309.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - Johnson BD, Schumacher RJ, Ross ED, Toft DO (1998). "Hop modulates Hsp70/Hsp90 interactions in protein folding". J. Biol. Chem. 273 (6): 3679–86. doi:10.1074/jbc.273.6.3679. PMID 9452498.
{{cite journal}}: CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link) - Zheng S, Cai X, Cao J, et al. (1998). "Screening and identification of down-regulated genes in colorectal carcinoma by subtractive hybridization: a method to identify putative tumor suppressor genes". Chin. Med. J. 110 (7): 543–7. PMID 9594214.
- Chen S, Smith DF (1999). "Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery". J. Biol. Chem. 273 (52): 35194–200. doi:10.1074/jbc.273.52.35194. PMID 9857057.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - Scanlan MJ, Gordan JD, Williamson B, et al. (1999). "Antigens recognized by autologous antibody in patients with renal-cell carcinoma". Int. J. Cancer. 83 (4): 456–64. doi:10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5. PMID 10508479.
- Dunham I, Shimizu N, Roe BA, et al. (1999). "The DNA sequence of human chromosome 22". Nature. 402 (6761): 489–95. doi:10.1038/990031. PMID 10591208.
- Morishima Y, Kanelakis KC, Silverstein AM, et al. (2000). "The Hsp organizer protein hop enhances the rate of but is not essential for glucocorticoid receptor folding by the multiprotein Hsp90-based chaperone system". J. Biol. Chem. 275 (10): 6894–900. doi:10.1074/jbc.275.10.6894. PMID 10702249.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - Rajapandi T, Greene LE, Eisenberg E (2000). "The molecular chaperones Hsp90 and Hsc70 are both necessary and sufficient to activate hormone binding by glucocorticoid receptor". J. Biol. Chem. 275 (29): 22597–604. doi:10.1074/jbc.M002035200. PMID 10781595.
{{cite journal}}: CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link) - Agarraberes FA, Dice JF (2002). "A molecular chaperone complex at the lysosomal membrane is required for protein translocation". J. Cell. Sci. 114 (Pt 13): 2491–9. PMID 11559757.
- Velten M, Gomez-Vrielynck N, Chaffotte A, Ladjimi MM (2002). "Domain structure of the HSC70 cochaperone, HIP". J. Biol. Chem. 277 (1): 259–66. doi:10.1074/jbc.M106881200. PMID 11687574.
{{cite journal}}: CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link) - Fan GH, Yang W, Sai J, Richmond A (2002). "Hsc/Hsp70 interacting protein (hip) associates with CXCR2 and regulates the receptor signaling and trafficking". J. Biol. Chem. 277 (8): 6590–7. doi:10.1074/jbc.M110588200. PMC 2665275. PMID 11751889.
{{cite journal}}: CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link) - 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:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Nelson GM, Prapapanich V, Carrigan PE, et al. (2005). "The heat shock protein 70 cochaperone hip enhances functional maturation of glucocorticoid receptor". Mol. Endocrinol. 18 (7): 1620–30. doi:10.1210/me.2004-0054. PMID 15071092.
- Colland F, Jacq X, Trouplin V, et al. (2004). "Functional proteomics mapping of a human signaling pathway". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMC 442148. PMID 15231748.
- Collins JE, Wright CL, Edwards CA, et al. (2005). "A genome annotation-driven approach to cloning the human ORFeome". Genome Biol. 5 (10): R84. doi:10.1186/gb-2004-5-10-r84. PMC 545604. PMID 15461802.
{{cite journal}}: CS1 maint: unflagged free DOI (link) - 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:10.1101/gr.2596504. PMC 528928. PMID 15489334.
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