SEPT7

From Wikipedia, the free encyclopedia

Septin 7

Identifiers

SEPT7; CDC10; CDC3; Nbla02942; SEPT7A

External IDs

OMIM: 603151 MGI: 1335094 HomoloGene: 1354

Gene ontology
Molecular Function:	• nucleotide binding • structural molecule activity • protein binding • GTP binding
Cellular Component:	• stress fiber • nucleus • synaptosome
Biological Process:	• cytokinesis • cell cycle • protein heterooligomerization

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001011553 (mRNA)
NP_001011553 (protein)

NM_009859 (mRNA)
NP_033989 (protein)

Location

Chr 7: 35.81 - 35.91 Mb

Chr 9: 25 - 25.06 Mb

Pubmed search

[1]

[2]

Septin 7, also known as SEPT7, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: SEPT7 septin 7.

[edit] Further reading

Nakatsuru S, Sudo K, Nakamura Y (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.
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. PMID 8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. PMID 9373149.
Hsu SC, Hazuka CD, Roth R, et al. (1998). "Subunit composition, protein interactions, and structures of the mammalian brain sec6/8 complex and septin filaments.". Neuron 20 (6): 1111–22. 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. PMID 10931866.
Joberty G, Perlungher RR, Sheffield PJ, et al. (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. PMID 12388755.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
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. PMID 14531065.
Suzuki Y, Yamashita R, Shirota M, et al. (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. 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.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.
Rush J, Moritz A, Lee KA, et al. (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, et al. (2005). "Nucleolar proteome dynamics.". Nature 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413.
Kimura K, Wakamatsu A, Suzuki Y, et al. (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. 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, et al. (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, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry.". Mol. Syst. Biol. 3: 89. doi:10.1038/msb4100134. PMID 17353931.
Sirajuddin M, Farkasovsky M, Hauer F, et al. (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 nuclear accumulation of NCK mediated by SOCS7.". Cell 130 (5): 837–50. doi:10.1016/j.cell.2007.06.053. PMID 17803907.