[{"@context":"http:\/\/schema.org\/","@type":"BlogPosting","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/sept6-wikipedia\/#BlogPosting","mainEntityOfPage":"https:\/\/wiki.edu.vn\/en\/wiki24\/sept6-wikipedia\/","headline":"SEPT6 &#8211; Wikipedia","name":"SEPT6 &#8211; Wikipedia","description":"before-content-x4 From Wikipedia, the free encyclopedia after-content-x4 Protein-coding gene in the species Homo sapiens Septin-6 is a protein that in","datePublished":"2015-11-27","dateModified":"2015-11-27","author":{"@type":"Person","@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/#Person","name":"lordneo","url":"https:\/\/wiki.edu.vn\/en\/wiki24\/author\/lordneo\/","image":{"@type":"ImageObject","@id":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","url":"https:\/\/secure.gravatar.com\/avatar\/c9645c498c9701c88b89b8537773dd7c?s=96&d=mm&r=g","height":96,"width":96}},"publisher":{"@type":"Organization","name":"Enzyklop\u00e4die","logo":{"@type":"ImageObject","@id":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","url":"https:\/\/wiki.edu.vn\/wiki4\/wp-content\/uploads\/2023\/08\/download.jpg","width":600,"height":60}},"image":{"@type":"ImageObject","@id":"https:\/\/en.wikipedia.org\/wiki\/Special:CentralAutoLogin\/start?type=1x1","url":"https:\/\/en.wikipedia.org\/wiki\/Special:CentralAutoLogin\/start?type=1x1","height":"1","width":"1"},"url":"https:\/\/wiki.edu.vn\/en\/wiki24\/sept6-wikipedia\/","wordCount":5608,"articleBody":"     (adsbygoogle = window.adsbygoogle || []).push({});before-content-x4From Wikipedia, the free encyclopedia       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4Protein-coding gene in the species Homo sapiensSeptin-6 is a protein that in humans is encoded by the SEPT6 gene.[5][6][7]       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4Table of ContentsFunction[edit]Clinical significance[edit]Interactions[edit]References[edit]Further reading[edit]Function[edit]This gene is a member of the septin family of GTPases. Members of this family are required for cytokinesis. This gene encodes four transcript variants encoding three distinct isoforms. An additional transcript variant has been identified, but its biological validity has not been determined.[7]Clinical significance[edit]One version of pediatric acute myeloid leukemia is the result of a reciprocal translocation between chromosomes 11 and X, with the breakpoint associated with the genes encoding the mixed-lineage leukemia and septin 2 proteins.[7]       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4Interactions[edit]SEPT6 has been shown to interact with SEPT2.[8][9]References[edit]^ a b c GRCh38: Ensembl release 89: ENSG00000125354 &#8211; Ensembl, May 2017^ a b c GRCm38: Ensembl release 89: ENSMUSG00000050379 &#8211; Ensembl, May 2017^ &#8220;Human PubMed Reference:&#8221;. National Center for Biotechnology Information, U.S. National Library of Medicine.^ &#8220;Mouse PubMed Reference:&#8221;. National Center for Biotechnology Information, U.S. National Library of Medicine.^ Nagase T, Seki N, Tanaka A, Ishikawa K, Nomura N (August 1995). &#8220;Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1&#8221;. DNA Research. 2 (4): 167\u201374, 199\u2013210. doi:10.1093\/dnares\/2.4.167. PMID\u00a08590280.^ Xue J, Wang X, Malladi CS, Kinoshita M, Milburn PJ, Lengyel I, Rostas JA, Robinson PJ (April 2000). &#8220;Phosphorylation of a new brain-specific septin, G-septin, by cGMP-dependent protein kinase&#8221;. The Journal of Biological Chemistry. 275 (14): 10047\u201356. doi:10.1074\/jbc.275.14.10047. PMID\u00a010744683.^ a b c &#8220;Entrez Gene: SEPT6 septin 6&#8221;.^ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). &#8220;Towards a proteome-scale map of the human protein-protein interaction network&#8221;. Nature. 437 (7062): 1173\u20138. Bibcode:2005Natur.437.1173R. doi:10.1038\/nature04209. PMID\u00a016189514. S2CID\u00a04427026.^ Surka MC, Tsang CW, Trimble WS (October 2002). &#8220;The mammalian septin MSF localizes with microtubules and is required for completion of cytokinesis&#8221;. Molecular Biology of the Cell. 13 (10): 3532\u201345. doi:10.1091\/mbc.E02-01-0042. PMC\u00a0129964. PMID\u00a012388755.Further reading[edit]Kinoshita A, Noda M, Kinoshita M (December 2000). &#8220;Differential localization of septins in the mouse brain&#8221;. The Journal of Comparative Neurology. 428 (2): 223\u201339. doi:10.1002\/1096-9861(20001211)428:23.0.CO;2-M. PMID\u00a011064363. S2CID\u00a013174934.Ono R, Taki T, Taketani T, Kawaguchi H, Taniwaki M, Okamura T, Kawa K, Hanada R, Kobayashi M, Hayashi Y (January 2002). &#8220;SEPTIN6, a human homologue to mouse Septin6, is fused to MLL in infant acute myeloid leukemia with complex chromosomal abnormalities involving 11q23 and Xq24&#8221;. Cancer Research. 62 (2): 333\u20137. PMID\u00a011809673.Slater DJ, Hilgenfeld E, Rappaport EF, Shah N, Meek RG, Williams WR, Lovett BD, Osheroff N, Autar RS, Ried T, Felix CA (July 2002). &#8220;MLL-SEPTIN6 fusion recurs in novel translocation of chromosomes 3, X, and 11 in infant acute myelomonocytic leukaemia and in t(X;11) in infant acute myeloid leukaemia, and MLL genomic breakpoint in complex MLL-SEPTIN6 rearrangement is a DNA topoisomerase II cleavage site&#8221;. Oncogene. 21 (30): 4706\u201314. doi:10.1038\/sj.onc.1205572. PMID\u00a012096348.Surka MC, Tsang CW, Trimble WS (October 2002). &#8220;The mammalian septin MSF localizes with microtubules and is required for completion of cytokinesis&#8221;. Molecular Biology of the Cell. 13 (10): 3532\u201345. doi:10.1091\/mbc.E02-01-0042. PMC\u00a0129964. PMID\u00a012388755.Sheffield PJ, Oliver CJ, Kremer BE, Sheng S, Shao Z, Macara IG (January 2003). &#8220;Borg\/septin interactions and the assembly of mammalian septin heterodimers, trimers, and filaments&#8221;. The Journal of Biological Chemistry. 278 (5): 3483\u20138. doi:10.1074\/jbc.M209701200. PMID\u00a012446710.Vega IE, Hsu SC (January 2003). &#8220;The septin protein Nedd5 associates with both the exocyst complex and microtubules and disruption of its GTPase activity promotes aberrant neurite sprouting in PC12 cells&#8221;. NeuroReport. 14 (1): 31\u20137. doi:10.1097\/00001756-200301200-00006. PMID\u00a012544826. S2CID\u00a022757290.Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J (May 2003). &#8220;Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides&#8221;. Nature Biotechnology. 21 (5): 566\u20139. doi:10.1038\/nbt810. PMID\u00a012665801. S2CID\u00a023783563.Koshelev YA, Kiselev SL, Georgiev GP (2004). &#8220;Interaction of the S100A4 (Mts1) protein with septins Sept2, Sept6, and Sept7 in vitro&#8221;. Doklady Biochemistry and Biophysics. 391: 195\u20137. doi:10.1023\/A:1025149005902. PMID\u00a014531065. S2CID\u00a026291196.Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). &#8220;Towards a proteome-scale map of the human protein-protein interaction network&#8221;. Nature. 437 (7062): 1173\u20138. Bibcode:2005Natur.437.1173R. doi:10.1038\/nature04209. PMID\u00a016189514. S2CID\u00a04427026.Kadkol SS, Bruno A, Oh S, Schmidt ML, Lindgren V (July 2006). &#8220;MLL-SEPT6 fusion transcript with a novel sequence in an infant with acute myeloid leukemia&#8221;. Cancer Genetics and Cytogenetics. 168 (2): 162\u20137. doi:10.1016\/j.cancergencyto.2006.02.020. PMID\u00a016843108.Low C, Macara IG (October 2006). &#8220;Structural analysis of septin 2, 6, and 7 complexes&#8221;. The Journal of Biological Chemistry. 281 (41): 30697\u2013706. doi:10.1074\/jbc.M605179200. PMID\u00a016914550.Kim CS, Seol SK, Song OK, Park JH, Jang SK (April 2007). &#8220;An RNA-binding protein, hnRNP A1, and a scaffold protein, septin 6, facilitate hepatitis C virus replication&#8221;. Journal of Virology. 81 (8): 3852\u201365. doi:10.1128\/JVI.01311-06. PMC\u00a01866118. PMID\u00a017229681.Sirajuddin M, Farkasovsky M, Hauer F, K\u00fchlmann D, Macara IG, Weyand M, Stark H, Wittinghofer A (September 2007). &#8220;Structural insight into filament formation by mammalian septins&#8221;. Nature. 449 (7160): 311\u20135. Bibcode:2007Natur.449..311S. doi:10.1038\/nature06052. PMID\u00a017637674.Kremer BE, Adang LA, Macara IG (September 2007). &#8220;Septins regulate actin organization and cell-cycle arrest through nuclear accumulation of NCK mediated by SOCS7&#8221;. Cell. 130 (5): 837\u201350. doi:10.1016\/j.cell.2007.06.053. PMC\u00a02085444. PMID\u00a017803907.       (adsbygoogle = window.adsbygoogle || []).push({});after-content-x4"},{"@context":"http:\/\/schema.org\/","@type":"BreadcrumbList","itemListElement":[{"@type":"ListItem","position":1,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/#breadcrumbitem","name":"Enzyklop\u00e4die"}},{"@type":"ListItem","position":2,"item":{"@id":"https:\/\/wiki.edu.vn\/en\/wiki24\/sept6-wikipedia\/#breadcrumbitem","name":"SEPT6 &#8211; Wikipedia"}}]}]