View source for ST13

{{about|the gene and protein|the Star Trek 13 film|Star Trek Beyond|the ST13 postcode|ST postcode area}}
{{Infobox_gene}}
'''Hsc70-interacting protein''' also known as '''suppression of tumorigenicity 13''' (ST13) is a [[protein]] that in humans is encoded by the ''ST13'' [[gene]].<ref name="pmid9925927">{{cite journal | vauthors = Zhang Y, Cai X, Schlegelberger B, Zheng S | title = 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 | journal = Cytogenet Cell Genet | volume = 83 | issue = 1–2 | pages = 56–7 |date=Mar 1999 | pmid = 9925927 | doi =10.1159/000015125  | s2cid = 37163219 }}</ref><ref name="pmid8721986">{{cite journal | vauthors = Prapapanich V, Chen S, Nair SC, Rimerman RA, Smith DF | title = Molecular cloning of human p48, a transient component of progesterone receptor complexes and an Hsp70-binding protein | journal = Mol Endocrinol | volume = 10 | issue = 4 | pages = 420–31 |date=Oct 1996 | doi = 10.1210/mend.10.4.8721986 | pmid = 8721986 | doi-access = free }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ST13 suppression of tumorigenicity 13 (colon carcinoma) (Hsp70 interacting protein)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6767}}</ref>
== Function ==
The protein encoded by this gene is an [[Signal transducing adaptor protein|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]].<ref name="entrez"/>
==References==
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==Further reading==
{{refbegin | 2}}
*{{cite journal   |vauthors=Prapapanich V, Chen S, Toran EJ, etal |title=Mutational analysis of the hsp70-interacting protein Hip |journal=Mol. Cell. Biol. |volume=16 |issue= 11 |pages= 6200–7 |year= 1996 |pmid= 8887650 |doi=  10.1128/MCB.16.11.6200| pmc=231623  }}
*{{cite journal   |vauthors=Cao J, Cai X, Zheng L, etal |title=Characterization of colorectal-cancer-related cDNA clones obtained by subtractive hybridization screening |journal=J. Cancer Res. Clin. Oncol. |volume=123 |issue= 8 |pages= 447–51 |year= 1997 |pmid= 9292708 |doi=10.1007/BF01372549  |s2cid=42097617 }}
*{{cite journal  | vauthors=Mo Y, Zheng S, Shen D |title=[Differential expression of HSU17714 gene in colorectal cancer and normal colonic mucosa] |journal=Zhonghua Zhong Liu Za Zhi |volume=18 |issue= 4 |pages= 241–3 |year= 1998 |pmid= 9387309 }}
*{{cite journal  | vauthors=Johnson BD, Schumacher RJ, Ross ED, Toft DO |title=Hop modulates Hsp70/Hsp90 interactions in protein folding |journal=J. Biol. Chem. |volume=273 |issue= 6 |pages= 3679–86 |year= 1998 |pmid= 9452498 |doi=10.1074/jbc.273.6.3679  |doi-access=free }}
*{{cite journal   |vauthors=Zheng S, Cai X, Cao J, etal |title=Screening and identification of down-regulated genes in colorectal carcinoma by subtractive hybridization: a method to identify putative tumor suppressor genes |journal=Chin. Med. J. |volume=110 |issue= 7 |pages= 543–7 |year= 1998 |pmid= 9594214 }}
*{{cite journal  | vauthors=Chen S, Smith DF |title=Hop as an adaptor in the heat shock protein 70 (Hsp70) and hsp90 chaperone machinery |journal=J. Biol. Chem. |volume=273 |issue= 52 |pages= 35194–200 |year= 1999 |pmid= 9857057 |doi=10.1074/jbc.273.52.35194  |doi-access=free }}
*{{cite journal   |vauthors=Scanlan MJ, Gordan JD, Williamson B, etal |title=Antigens recognized by autologous antibody in patients with renal-cell carcinoma |journal=Int. J. Cancer |volume=83 |issue= 4 |pages= 456–64 |year= 1999 |pmid= 10508479 |doi=10.1002/(SICI)1097-0215(19991112)83:4<456::AID-IJC4>3.0.CO;2-5  |s2cid=21839750 |doi-access= }}
*{{cite journal   |vauthors=Dunham I, Shimizu N, Roe BA, etal |title=The DNA sequence of human chromosome 22 |journal=Nature |volume=402 |issue= 6761 |pages= 489–95 |year= 1999 |pmid= 10591208 |doi= 10.1038/990031 |bibcode=1999Natur.402..489D |doi-access= free }}
*{{cite journal   |vauthors=Morishima Y, Kanelakis KC, Silverstein AM, etal |title=The Hsp organizer protein hop enhances the rate of but is not essential for glucocorticoid receptor folding by the multiprotein Hsp90-based chaperone system |journal=J. Biol. Chem. |volume=275 |issue= 10 |pages= 6894–900 |year= 2000 |pmid= 10702249 |doi=10.1074/jbc.275.10.6894  |doi-access=free }}
*{{cite journal  | vauthors=Rajapandi T, Greene LE, Eisenberg E |title=The molecular chaperones Hsp90 and Hsc70 are both necessary and sufficient to activate hormone binding by glucocorticoid receptor |journal=J. Biol. Chem. |volume=275 |issue= 29 |pages= 22597–604 |year= 2000 |pmid= 10781595 |doi= 10.1074/jbc.M002035200 |doi-access= free }}
*{{cite journal  | vauthors=Agarraberes FA, Dice JF |title=A molecular chaperone complex at the lysosomal membrane is required for protein translocation |journal=J. Cell Sci. |volume=114 |issue= Pt 13 |pages= 2491–9 |year= 2002 |doi=10.1242/jcs.114.13.2491 |pmid= 11559757 }}
*{{cite journal  | vauthors=Velten M, Gomez-Vrielynck N, Chaffotte A, Ladjimi MM |title=Domain structure of the HSC70 cochaperone, HIP |journal=J. Biol. Chem. |volume=277 |issue= 1 |pages= 259–66 |year= 2002 |pmid= 11687574 |doi= 10.1074/jbc.M106881200 |doi-access= free }}
*{{cite journal  | vauthors=Fan GH, Yang W, Sai J, Richmond A |title=Hsc/Hsp70 interacting protein (hip) associates with CXCR2 and regulates the receptor signaling and trafficking |journal=J. Biol. Chem. |volume=277 |issue= 8 |pages= 6590–7 |year= 2002 |pmid= 11751889 |doi= 10.1074/jbc.M110588200  | pmc=2665275 |doi-access=free }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241 |bibcode=2002PNAS...9916899M |doi-access=free }}
*{{cite journal   |vauthors=Nelson GM, Prapapanich V, Carrigan PE, etal |title=The heat shock protein 70 cochaperone hip enhances functional maturation of glucocorticoid receptor |journal=Mol. Endocrinol. |volume=18 |issue= 7 |pages= 1620–30 |year= 2005 |pmid= 15071092 |doi= 10.1210/me.2004-0054 |doi-access= free }}
*{{cite journal   |vauthors=Colland F, Jacq X, Trouplin V, etal |title=Functional proteomics mapping of a human signaling pathway |journal=Genome Res. |volume=14 |issue= 7 |pages= 1324–32 |year= 2004 |pmid= 15231748 |doi= 10.1101/gr.2334104  | pmc=442148 }}
*{{cite journal   |vauthors=Collins JE, Wright CL, Edwards CA, etal |title=A genome annotation-driven approach to cloning the human ORFeome |journal=Genome Biol. |volume=5 |issue= 10 |pages= R84 |year= 2005 |pmid= 15461802 |doi= 10.1186/gb-2004-5-10-r84  | pmc=545604 |doi-access=free }}
*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504  | pmc=528928 }}
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[[Category:Co-chaperones]]