ST5 (gene)

Suppression of tumorigenicity 5, also known as ST5, is a human gene.cite web | title = Entrez Gene: ST5 suppression of tumorigenicity 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6764| accessdate = ]

PBB_Summary
section_title =
summary_text = This gene was identified by its ability to suppress the tumorigenicity of Hela cells in nude mice. The protein encoded by this gene contains a C-terminal region that shares similarity with the Rab 3 family of small GTP binding proteins. This protein preferentially binds to the SH3 domain of c-Abl kinase, and acts as a regulator of MAPK1/ERK2 kinase, which may contribute to its ability to reduce the tumorigenic phenotype in cells. Three alternatively spliced transcript variants of this gene encoding distinct isoforms are identified.cite web | title = Entrez Gene: ST5 suppression of tumorigenicity 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6764| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Lichy JH, Modi WS, Seuanez HN, Howley PM |title=Identification of a human chromosome 11 gene which is differentially regulated in tumorigenic and nontumorigenic somatic cell hybrids of HeLa cells. |journal=Cell Growth Differ. |volume=3 |issue= 8 |pages= 541–8 |year= 1992 |pmid= 1390339 |doi=
*cite journal | author=Lichy JH, Majidi M, Elbaum J, Tsai MM |title=Differential expression of the human ST5 gene in HeLa-fibroblast hybrid cell lines mediated by YY1: evidence that YY1 plays a part in tumor suppression. |journal=Nucleic Acids Res. |volume=24 |issue= 23 |pages= 4700–8 |year= 1997 |pmid= 8972856 |doi=
*cite journal | author=Majidi M, Hubbs AE, Lichy JH |title=Activation of extracellular signal-regulated kinase 2 by a novel Abl-binding protein, ST5. |journal=J. Biol. Chem. |volume=273 |issue= 26 |pages= 16608–14 |year= 1998 |pmid= 9632734 |doi=
*cite journal | author=Hubbs AE, Majidi M, Lichy JH |title=Expression of an isoform of the novel signal transduction protein ST5 is linked to cell morphology. |journal=Oncogene |volume=18 |issue= 15 |pages= 2519–25 |year= 1999 |pmid= 10229203 |doi= 10.1038/sj.onc.1202554
*cite journal | author=Majidi M, Gutkind JS, Lichy JH |title=Deletion of the COOH terminus converts the ST5 p70 protein from an inhibitor of RAS signaling to an activator with transforming activity in NIH-3T3 cells. |journal=J. Biol. Chem. |volume=275 |issue= 9 |pages= 6560–5 |year= 2000 |pmid= 10692462 |doi=
*cite journal | author=Amid C, Bahr A, Mujica A, "et al." |title=Comparative genomic sequencing reveals a strikingly similar architecture of a conserved syntenic region on human chromosome 11p15.3 (including gene ST5) and mouse chromosome 7. |journal=Cytogenet. Cell Genet. |volume=93 |issue= 3-4 |pages= 284–90 |year= 2001 |pmid= 11528127 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |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
*cite journal | author=Colland F, Jacq X, Trouplin V, "et al." |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
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |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
*cite journal | author=Benzinger A, Muster N, Koch HB, "et al." |title=Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer. |journal=Mol. Cell Proteomics |volume=4 |issue= 6 |pages= 785–95 |year= 2005 |pmid= 15778465 |doi= 10.1074/mcp.M500021-MCP200
*cite journal | author=Olsen JV, Blagoev B, Gnad F, "et al." |title=Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. |journal=Cell |volume=127 |issue= 3 |pages= 635–48 |year= 2006 |pmid= 17081983 |doi= 10.1016/j.cell.2006.09.026

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