SVIL

SVIL

Supervillin, also known as SVIL, is a human gene.cite web | title = Entrez Gene: SVIL supervillin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6840| accessdate = ]

PBB_Summary
section_title =
summary_text = This gene encodes a bipartite protein with distinct amino- and carboxy-terminal domains. The amino-terminus contains nuclear localization signals and the carboxy-terminus contains numerous consecutive sequences with extensive similarity to proteins in the gelsolin family of actin-binding proteins, which cap, nucleate, and/or sever actin filaments. The gene product is tightly associated with both actin filaments and plasma membranes, suggesting a role as a high-affinity link between the actin cytoskeleton and the membrane. Its function may include recruitment of actin and other cytoskeletal proteins into specialized structures at the plasma membrane and in the nuclei of growing cells. Two transcript variants encoding different isoforms of supervillin have been described.cite web | title = Entrez Gene: SVIL supervillin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6840| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Pestonjamasp KN, Pope RK, Wulfkuhle JD, Luna EJ |title=Supervillin (p205): A novel membrane-associated, F-actin-binding protein in the villin/gelsolin superfamily. |journal=J. Cell Biol. |volume=139 |issue= 5 |pages= 1255–69 |year= 1997 |pmid= 9382871 |doi=
*cite journal | author=Pope RK, Pestonjamasp KN, Smith KP, "et al." |title=Cloning, characterization, and chromosomal localization of human superillin (SVIL). |journal=Genomics |volume=52 |issue= 3 |pages= 342–51 |year= 1998 |pmid= 9867483 |doi=
*cite journal | author=Wulfkuhle JD, Donina IE, Stark NH, "et al." |title=Domain analysis of supervillin, an F-actin bundling plasma membrane protein with functional nuclear localization signals. |journal=J. Cell. Sci. |volume=112 ( Pt 13) |issue= |pages= 2125–36 |year= 1999 |pmid= 10362542 |doi=
*cite journal | author=Kim M, Jiang LH, Wilson HL, "et al." |title=Proteomic and functional evidence for a P2X7 receptor signalling complex. |journal=EMBO J. |volume=20 |issue= 22 |pages= 6347–58 |year= 2002 |pmid= 11707406 |doi= 10.1093/emboj/20.22.6347
*cite journal | author=Ting HJ, Yeh S, Nishimura K, Chang C |title=Supervillin associates with androgen receptor and modulates its transcriptional activity. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 2 |pages= 661–6 |year= 2002 |pmid= 11792840 |doi= 10.1073/pnas.022469899
*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=Oh SW, Pope RK, Smith KP, "et al." |title=Archvillin, a muscle-specific isoform of supervillin, is an early expressed component of the costameric membrane skeleton. |journal=J. Cell. Sci. |volume=116 |issue= Pt 11 |pages= 2261–75 |year= 2004 |pmid= 12711699 |doi= 10.1242/jcs.00422
*cite journal | author=Chen Y, Takizawa N, Crowley JL, "et al." |title=F-actin and myosin II binding domains in supervillin. |journal=J. Biol. Chem. |volume=278 |issue= 46 |pages= 46094–106 |year= 2003 |pmid= 12917436 |doi= 10.1074/jbc.M305311200
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*cite journal | author=Deloukas P, Earthrowl ME, Grafham DV, "et al." |title=The DNA sequence and comparative analysis of human chromosome 10. |journal=Nature |volume=429 |issue= 6990 |pages= 375–81 |year= 2004 |pmid= 15164054 |doi= 10.1038/nature02462
*cite journal | author=Beausoleil SA, Jedrychowski M, Schwartz D, "et al." |title=Large-scale characterization of HeLa cell nuclear phosphoproteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 33 |pages= 12130–5 |year= 2004 |pmid= 15302935 |doi= 10.1073/pnas.0404720101
*cite journal | author=Jin J, Smith FD, Stark C, "et al." |title=Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization. |journal=Curr. Biol. |volume=14 |issue= 16 |pages= 1436–50 |year= 2004 |pmid= 15324660 |doi= 10.1016/j.cub.2004.07.051
*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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