SEPT7

Septin 7
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2QAG​, 3T5D​, 3TW4​
Identifiers
Symbols	SEPT7 ; CDC10; CDC3; NBLA02942; SEPT7A
External IDs	OMIM: 603151 MGI: 1335094 HomoloGene: 1354 GeneCards: SEPT7 Gene
Gene ontology Molecular function • structural molecule activity • protein binding • GTP binding • identical protein binding Cellular component • condensed chromosome kinetochore • stress fiber • nucleus • nucleolus • cytoplasm • spindle • plasma membrane • axoneme • actin cytoskeleton • microtubule cytoskeleton • apical plasma membrane • midbody • septin complex • cleavage furrow • axon terminus • synapse • extracellular exosome Biological process • cytokinesis • mitotic nuclear division • regulation of embryonic cell shape • protein heterooligomerization • cilium morphogenesis Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	989	235072
Ensembl	ENSG00000122545	ENSMUSG00000001833
UniProt	Q16181	O55131
RefSeq (mRNA)	NM_001011553	NM_001205367
RefSeq (protein)	NP_001011553	NP_001192296
Location (UCSC)	Chr 7: 35.8 – 35.91 Mb	Chr 9: 25.25 – 25.31 Mb
PubMed search

Septin-7 is a protein that in humans is encoded by the SEPT7 gene.^[1][2]

Function

This gene encodes a protein that is highly similar to the CDC10 protein of Saccharomyces cerevisiae. The protein also shares similarity with Diff 6 of Drosophila and with H5 of mouse. Each of these similar proteins, including the yeast CDC10, contains a GTP-binding motif. The yeast CDC10 protein is a structural component of the 10 nm filament which lies inside the cytoplasmic membrane and is essential for cytokinesis. Although the exact function of this gene has not yet been determined, its high similarity to yeast CDC10 and the high conservative nature of eukaryotic cell cycle machinery suggest a similar role to that of its yeast counterpart. Alternative splicing results in two transcript variants encoding different isoforms.^[2]

Interactions

SEPT7 has been shown to interact with SEPT2^[3][4] and SEPT9.^[4]

References

1. Nakatsuru S, Sudo K, Nakamura Y (Aug 1994). "Molecular cloning of a novel human cDNA homologous to CDC10 in Saccharomyces cerevisiae". Biochem Biophys Res Commun 202 (1): 82–7. doi:10.1006/bbrc.1994.1896. PMID 8037772.
2. "Entrez Gene: SEPT7 septin 7".
3. Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D. "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3: 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
4. Surka MC, Tsang CW, Trimble WS (Oct 2002). "The mammalian septin MSF localizes with microtubules and is required for completion of cytokinesis". Mol. Biol. Cell 13 (10): 3532–45. doi:10.1091/mbc.E02-01-0042. PMC 129964. PMID 12388755.

Further reading

• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Hsu SC, Hazuka CD, Roth R, Foletti DL, Heuser J, Scheller RH (1998). "Subunit composition, protein interactions, and structures of the mammalian brain sec6/8 complex and septin filaments". Neuron 20 (6): 1111–22. doi:10.1016/S0896-6273(00)80493-6. PMID 9655500.
• Oegema K, Savoian MS, Mitchison TJ, Field CM (2000). "Functional Analysis of a Human Homologue of the Drosophila Actin Binding Protein Anillin Suggests a Role in Cytokinesis". J. Cell Biol. 150 (3): 539–52. doi:10.1083/jcb.150.3.539. PMC 2175195. PMID 10931866.
• Joberty G, Perlungher RR, Sheffield PJ, Kinoshita M, Noda M, Haystead T, Macara IG (2001). "Borg proteins control septin organization and are negatively regulated by Cdc42". Nat. Cell Biol. 3 (10): 861–6. doi:10.1038/ncb1001-861. PMID 11584266.
• Surka MC, Tsang CW, Trimble WS (2003). "The Mammalian Septin MSF Localizes with Microtubules and Is Required for Completion of Cytokinesis". Mol. Biol. Cell 13 (10): 3532–45. doi:10.1091/mbc.E02-01-0042. PMC 129964. PMID 12388755.
• Koshelev YA, Kiselev SL, Georgiev GP (2004). "Interaction of the S100A4 (Mts1) protein with septins Sept2, Sept6, and Sept7 in vitro". Dokl. Biochem. Biophys. 391: 195–7. doi:10.1023/A:1025149005902. PMID 14531065.
• Suzuki Y, Yamashita R, Shirota M, Sakakibara Y, Chiba J, Mizushima-Sugano J, Nakai K, Sugano S (2004). "Sequence Comparison of Human and Mouse Genes Reveals a Homologous Block Structure in the Promoter Regions". Genome Res. 14 (9): 1711–8. doi:10.1101/gr.2435604. PMC 515316. PMID 15342556.
• Nagata K, Asano T, Nozawa Y, Inagaki M (2005). "Biochemical and cell biological analyses of a mammalian septin complex, Sept7/9b/11". J. Biol. Chem. 279 (53): 55895–904. doi:10.1074/jbc.M406153200. PMID 15485874.
• Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nat. Biotechnol. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455.
• Andersen JS, Lam YW, Leung AK, Ong SE, Lyon CE, Lamond AI, Mann M (2005). "Nucleolar proteome dynamics". Nature 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413.
• Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S (2006). "Diversification of transcriptional modulation: Large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
• Low C, Macara IG (2006). "Structural analysis of septin 2, 6, and 7 complexes". J. Biol. Chem. 281 (41): 30697–706. doi:10.1074/jbc.M605179200. PMID 16914550.
• Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983.
• Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein–protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
• Sirajuddin M, Farkasovsky M, Hauer F, Kühlmann D, Macara IG, Weyand M, Stark H, Wittinghofer A (2007). "Structural insight into filament formation by mammalian septins". Nature 449 (7160): 311–5. doi:10.1038/nature06052. PMID 17637674.
• Kremer BE, Adang LA, Macara IG (2007). "Septins Regulate Actin Organization and Cell Cycle Arrest Through SOCS7-Mediated Nuclear Accumulation of NCK". Cell 130 (5): 837–50. doi:10.1016/j.cell.2007.06.053. PMC 2085444. PMID 17803907.