SEPT7

Septin-7 is a protein that in humans is encoded by the SEPT7 gene.[5][6]

SEPTIN7
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2QAG, 3T5D, 3TW4
Identifiers
Aliases	SEPTIN7, CDC10, CDC3, NBLA02942, SEPT7A, septin 7, SEPT7
External IDs	OMIM: 603151 MGI: 1335094 HomoloGene: 1354 GeneCards: SEPTIN7
Gene location (Human) Chr. Chromosome 7 (human)[1] Band 7p14.2 Start 35,800,932 bp[1] End 35,907,105 bp[1]
Gene location (Mouse) Chr. Chromosome 9 (mouse)[2] Band 9|9 A4 Start 25,252,439 bp[2] End 25,308,571 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • nucleotide binding • GTP binding • structural molecule activity • GO:0001948 protein binding • identical protein binding • cadherin binding • GTPase activity • GO:0032947 molecular adaptor activity Cellular component • condensed chromosome kinetochore • cytosol • cell projection • spindle • cilium • septin complex • stress fiber • chromosome • midbody • apical plasma membrane • GO:0035085 axoneme • cleavage furrow • chromosome, centromeric region • cytoskeleton • extracellular exosome • cell nucleus • kinetochore • cytoplasm • sperm annulus • non-motile cilium • septin ring • microtubule cytoskeleton • motile cilium Biological process • cilium morphogenesis • protein heterooligomerization • cytokinesis • regulation of embryonic cell shape • cell division • positive regulation of non-motile cilium assembly • cell cycle • spermatogenesis • cell differentiation • negative regulation of cell migration • positive regulation of apoptotic process • cytoskeleton-dependent cytokinesis • negative regulation of G1/S transition of mitotic cell cycle Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	989	235072
Ensembl	ENSG00000122545	ENSMUSG00000001833
UniProt	Q16181	O55131
RefSeq (mRNA)	NM_001011553 NM_001242956 NM_001788 NM_001363715 NM_001375299	NM_001205367 NM_009859 NM_001359736 NM_001359737 NM_001359738
RefSeq (protein)	NP_001011553 NP_001229885 NP_001779 NP_001350644 NP_001362228	NP_001192296 NP_033989 NP_001346665 NP_001346666 NP_001346667
Location (UCSC)	Chr 7: 35.8 – 35.91 Mb	Chr 9: 25.25 – 25.31 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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.[6]

Interactions

SEPT7 has been shown to interact with SEPT2[7][8] and SEPT9.[8]

References

1. GRCh38: Ensembl release 89: ENSG00000122545 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000001833 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Nakatsuru S, Sudo K, Nakamura Y (July 1994). "Molecular cloning of a novel human cDNA homologous to CDC10 in Saccharomyces cerevisiae". Biochemical and Biophysical Research Communications. 202 (1): 82–7. doi:10.1006/bbrc.1994.1896. PMID 8037772.
6. "Entrez Gene: SEPT7 septin 7".
7. 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". Molecular Systems Biology. 3: 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
8. Surka MC, Tsang CW, Trimble WS (October 2002). "The mammalian septin MSF localizes with microtubules and is required for completion of cytokinesis". Molecular Biology of the Cell. 13 (10): 3532–45. doi:10.1091/mbc.E02-01-0042. PMC 129964. PMID 12388755.

Further reading

• Maruyama K, Sugano S (January 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 (October 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 (June 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 (August 2000). "Functional analysis of a human homologue of the Drosophila actin binding protein anillin suggests a role in cytokinesis". The Journal of Cell Biology. 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 (October 2001). "Borg proteins control septin organization and are negatively regulated by Cdc42". Nature Cell Biology. 3 (10): 861–6. doi:10.1038/ncb1001-861. PMID 11584266.
• Surka MC, Tsang CW, Trimble WS (October 2002). "The mammalian septin MSF localizes with microtubules and is required for completion of cytokinesis". Molecular Biology of the 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". Doklady Biochemistry and Biophysics. 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 (September 2004). "Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions". Genome Research. 14 (9): 1711–8. doi:10.1101/gr.2435604. PMC 515316. PMID 15342556.
• Nagata K, Asano T, Nozawa Y, Inagaki M (December 2004). "Biochemical and cell biological analyses of a mammalian septin complex, Sept7/9b/11". The Journal of Biological Chemistry. 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 (January 2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nature Biotechnology. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455.
• Andersen JS, Lam YW, Leung AK, Ong SE, Lyon CE, Lamond AI, Mann M (January 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 (January 2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Research. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
• Low C, Macara IG (October 2006). "Structural analysis of septin 2, 6, and 7 complexes". The Journal of Biological Chemistry. 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 (November 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". Molecular Systems Biology. 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 (September 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 (September 2007). "Septins regulate actin organization and cell-cycle arrest through nuclear accumulation of NCK mediated by SOCS7". Cell. 130 (5): 837–50. doi:10.1016/j.cell.2007.06.053. PMC 2085444. PMID 17803907.