SVIL: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''Supervillin''' is a [[protein]] that in humans is encoded by the ''SVIL'' [[gene]].<ref name="pmid9382871">{{cite journal | vauthors = 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 = The Journal of Cell Biology | volume = 139 | issue = 5 | pages = 1255–69 | date = Dec 1997 | pmid = 9382871 | pmc = 2140202 | doi = 10.1083/jcb.139.5.1255 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: SVIL supervillin| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6840| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Supervillin
| HGNCid = 11480
| Symbol = SVIL
| AltSymbols =; DKFZp686A17191
| OMIM = 604126
| ECnumber = 
| Homologene = 25090
| MGIid = 2147319
| GeneAtlas_image1 = PBB_GE_SVIL_202565_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_SVIL_202566_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0051015 |text = actin filament binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0015629 |text = actin cytoskeleton}} {{GNF_GO|id=GO:0043034 |text = costamere}}
| Process = {{GNF_GO|id=GO:0007010 |text = cytoskeleton organization and biogenesis}} {{GNF_GO|id=GO:0007519 |text = striated muscle development}} {{GNF_GO|id=GO:0051016 |text = barbed-end actin filament capping}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 6840
    | Hs_Ensembl = ENSG00000197321
    | Hs_RefseqProtein = NP_003165
    | Hs_RefseqmRNA = NM_003174
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 10
    | Hs_GenLoc_start = 29786273
    | Hs_GenLoc_end = 30064739
    | Hs_Uniprot = O95425
    | Mm_EntrezGene = 225115
    | Mm_Ensembl = ENSMUSG00000024236
    | Mm_RefseqmRNA = NM_153153
    | Mm_RefseqProtein = NP_694793
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 18
    | Mm_GenLoc_start = 5046574
    | Mm_GenLoc_end = 5119288
    | Mm_Uniprot = Q3TTX5
  }}
}}
'''Supervillin''', also known as '''SVIL''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SVIL supervillin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6840| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
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.<ref>{{cite journal | vauthors = Ghoshdastider U, Popp D, Burtnick LD, Robinson RC | title = The expanding superfamily of gelsolin homology domain proteins | journal = Cytoskeleton | volume = 70 | issue = 11 | pages = 775–95 | date = Nov 2013 | pmid = 24155256 | doi = 10.1002/cm.21149 }}</ref> 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.<ref name="entrez" />
{{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.<ref name="entrez">{{cite web | title = Entrez Gene: SVIL supervillin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6840| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
SVIL has been shown to [[Protein-protein interaction|interact]] with [[Androgen receptor]].<ref name=pmid11792840>{{cite journal | vauthors = Ting HJ, Yeh S, Nishimura K, Chang C | title = Supervillin associates with androgen receptor and modulates its transcriptional activity | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 99 | issue = 2 | pages = 661–6 | date = Jan 2002 | pmid = 11792840 | pmc = 117362 | doi = 10.1073/pnas.022469899 | bibcode = 2002PNAS...99..661T }}</ref>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Pope RK, Pestonjamasp KN, Smith KP, Wulfkuhle JD, Strassel CP, Lawrence JB, Luna EJ | title = Cloning, characterization, and chromosomal localization of human superillin (SVIL) | journal = Genomics | volume = 52 | issue = 3 | pages = 342–51 | date = Sep 1998 | pmid = 9867483 | doi = 10.1006/geno.1998.5466 }}
| citations =
* {{cite journal | vauthors = Wulfkuhle JD, Donina IE, Stark NH, Pope RK, Pestonjamasp KN, Niswonger ML, Luna EJ | title = Domain analysis of supervillin, an F-actin bundling plasma membrane protein with functional nuclear localization signals | journal = Journal of Cell Science | volume = 112 ( Pt 13) | issue = 13 | pages = 2125–36 | date = Jul 1999 | pmid = 10362542 | doi =  }}
*{{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 | vauthors = Kim M, Jiang LH, Wilson HL, North RA, Surprenant A | title = Proteomic and functional evidence for a P2X7 receptor signalling complex | journal = The EMBO Journal | volume = 20 | issue = 22 | pages = 6347–58 | date = Nov 2001 | pmid = 11707406 | pmc = 125721 | doi = 10.1093/emboj/20.22.6347 }}
*{{cite journal  | author=Pope RK, Pestonjamasp KN, Smith KP, ''et al.'' |title=Cloning, characterization, and chromosomal localization of human supervillin (SVIL). |journal=Genomics |volume=52 |issue= 3 |pages= 342-51 |year= 1998 |pmid= 9867483 |doi= }}
* {{cite journal | vauthors = Ting HJ, Yeh S, Nishimura K, Chang C | title = Supervillin associates with androgen receptor and modulates its transcriptional activity | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 99 | issue = 2 | pages = 661–6 | date = Jan 2002 | pmid = 11792840 | pmc = 117362 | doi = 10.1073/pnas.022469899 | bibcode = 2002PNAS...99..661T }}
*{{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 | vauthors = Oh SW, Pope RK, Smith KP, Crowley JL, Nebl T, Lawrence JB, Luna EJ | title = Archvillin, a muscle-specific isoform of supervillin, is an early expressed component of the costameric membrane skeleton | journal = Journal of Cell Science | volume = 116 | issue = Pt 11 | pages = 2261–75 | date = Jun 2003 | pmid = 12711699 | doi = 10.1242/jcs.00422 }}
*{{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 | vauthors = Chen Y, Takizawa N, Crowley JL, Oh SW, Gatto CL, Kambara T, Sato O, Li XD, Ikebe M, Luna EJ | title = F-actin and myosin II binding domains in supervillin | journal = The Journal of Biological Chemistry | volume = 278 | issue = 46 | pages = 46094–106 | date = Nov 2003 | pmid = 12917436 | doi = 10.1074/jbc.M305311200 }}
*{{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 | vauthors = Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP | title = Large-scale characterization of HeLa cell nuclear phosphoproteins | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 101 | issue = 33 | pages = 12130–5 | date = Aug 2004 | pmid = 15302935 | pmc = 514446 | doi = 10.1073/pnas.0404720101 | bibcode = 2004PNAS..10112130B }}
*{{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 | vauthors = Jin J, Smith FD, Stark C, Wells CD, Fawcett JP, Kulkarni S, Metalnikov P, O'Donnell P, Taylor P, Taylor L, Zougman A, Woodgett JR, Langeberg LK, Scott JD, Pawson T | title = Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization | journal = Current Biology | volume = 14 | issue = 16 | pages = 1436–50 | date = Aug 2004 | pmid = 15324660 | doi = 10.1016/j.cub.2004.07.051 }}
*{{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 | vauthors = Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M | title = Global, in vivo, and site-specific phosphorylation dynamics in signaling networks | journal = Cell | volume = 127 | issue = 3 | pages = 635–48 | date = Nov 2006 | pmid = 17081983 | doi = 10.1016/j.cell.2006.09.026 }}
*{{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 }}
}}
{{refend}}
{{refend}}


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Latest revision as of 07:20, 11 September 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Supervillin is a protein that in humans is encoded by the SVIL gene.[1][2]

Function

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.[3] 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.[2]

Interactions

SVIL has been shown to interact with Androgen receptor.[4]

References

  1. ↑ Pestonjamasp KN, Pope RK, Wulfkuhle JD, Luna EJ (Dec 1997). "Supervillin (p205): A novel membrane-associated, F-actin-binding protein in the villin/gelsolin superfamily". The Journal of Cell Biology. 139 (5): 1255–69. doi:10.1083/jcb.139.5.1255. PMC 2140202. PMID 9382871.
  2. ↑ 2.0 2.1 "Entrez Gene: SVIL supervillin".
  3. ↑ Ghoshdastider U, Popp D, Burtnick LD, Robinson RC (Nov 2013). "The expanding superfamily of gelsolin homology domain proteins". Cytoskeleton. 70 (11): 775–95. doi:10.1002/cm.21149. PMID 24155256.
  4. ↑ Ting HJ, Yeh S, Nishimura K, Chang C (Jan 2002). "Supervillin associates with androgen receptor and modulates its transcriptional activity". Proceedings of the National Academy of Sciences of the United States of America. 99 (2): 661–6. Bibcode:2002PNAS...99..661T. doi:10.1073/pnas.022469899. PMC 117362. PMID 11792840.

Further reading


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