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Gene Review

SEPT1  -  septin 1

Homo sapiens

Synonyms: DIFF6, LARP, PNUTL3, Peanut-like protein 3, SEP1, ...
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Disease relevance of SEPT1


High impact information on SEPT1


Biological context of SEPT1


Anatomical context of SEPT1

  • Unlike lower eukaryotic cells, the physiological significance of mammalian septin complexes is largely unknown [12].
  • One of these clones, DIFF6, is derived from an RNA whose expression level is higher in several cell lines producing high amounts of MEL-14-reactive gp90, and absent or present at lower levels in several cell lines expressing low levels of this glycoprotein [13].
  • Overproduction of Mid2p depolarizes cell growth and affects the organization of both the septin and actin cytoskeletons [14].
  • This model cannot, however, explain the GTP-biochemistry of heteromeric septin complexes from cytosol [15].
  • These results strongly suggest that septin filaments may interact not only with actin filaments but also with microtubule networks and that GTPase activity of MSF-A is not indispensable to incorporation of MSF-A into septin filaments [16].

Associations of SEPT1 with chemical compounds

  • Parkin functions as a ubiquitin protein ligase in the degradation of several proteins, including the neuron-specific septin CDCrel-1 [17].
  • Moreover, Rab35 is involved in the intercellular bridge localization of two molecules essential for the postfurrowing steps of cytokinesis: the phosphatidylinositol 4,5-bis phosphate (PIP2) lipid and the septin SEPT2 [18].
  • Studies have shown that septin 1 with site-directed mutations of five serine residues (Ser19, Ser206, Ser307, Ser312 and Ser315) has a much lower degree of aggregation and better structural homogeneity and that the mutations cause only slight perturbations in the secondary structure of septin 1 [19].

Regulatory relationships of SEPT1


Other interactions of SEPT1

  • It is shown that SEPT13 and the other known human septins are expressed in all tissue types but some show high expression in lymphoid (SEPT1, 6, 9, and 12) or brain tissues (SEPT2, 3, 4, 5, 7, 8, and 11) [11].
  • These results suggest that AF17q25 and hCDCrel might define a new septin family particularly involved in the pathogenesis of 11q23-associated leukemia [1].
  • A novel septin, SEPT13, has been identified and is shown to be related to SEPT7 [11].
  • Mass spectroscopic analysis of proteins coprecipitating with Sept6 identified the microtubule-associated protein MAP4 as a septin binding partner [9].
  • The novel human platelet septin SEPT8 is an interaction partner of SEPT4 [20].

Analytical, diagnostic and therapeutic context of SEPT1


  1. AF17q25, a putative septin family gene, fuses the MLL gene in acute myeloid leukemia with t(11;17)(q23;q25). Taki, T., Ohnishi, H., Shinohara, K., Sako, M., Bessho, F., Yanagisawa, M., Hayashi, Y. Cancer Res. (1999) [Pubmed]
  2. Analysis of mammalian septin expression in human malignant brain tumors. Kim, D.S., Hubbard, S.L., Peraud, A., Salhia, B., Sakai, K., Rutka, J.T. Neoplasia (2004) [Pubmed]
  3. Sint1, a common integration site in SL3-3-induced T-cell lymphomas, harbors a putative proto-oncogene with homology to the septin gene family. Sørensen, A.B., Lund, A.H., Ethelberg, S., Copeland, N.G., Jenkins, N.A., Pedersen, F.S. J. Virol. (2000) [Pubmed]
  4. FLJ10849, a septin family gene, fuses MLL in a novel leukemia cell line CNLBC1 derived from chronic neutrophilic leukemia in transformation with t(4;11)(q21;q23). Kojima, K., Sakai, I., Hasegawa, A., Niiya, H., Azuma, T., Matsuo, Y., Fujii, N., Tanimoto, M., Fujita, S. Leukemia (2004) [Pubmed]
  5. The septin CDCrel-1 binds syntaxin and inhibits exocytosis. Beites, C.L., Xie, H., Bowser, R., Trimble, W.S. Nat. Neurosci. (1999) [Pubmed]
  6. Lipopolysaccharide (LPS)-binding protein is carried on lipoproteins and acts as a cofactor in the neutralization of LPS. Wurfel, M.M., Kunitake, S.T., Lichenstein, H., Kane, J.P., Wright, S.D. J. Exp. Med. (1994) [Pubmed]
  7. Septin: a factor in plasma that opsonizes lipopolysaccharide-bearing particles for recognition by CD14 on phagocytes. Wright, S.D., Ramos, R.A., Patel, M., Miller, D.S. J. Exp. Med. (1992) [Pubmed]
  8. A novel mitochondrial septin-like protein, ARTS, mediates apoptosis dependent on its P-loop motif. Larisch, S., Yi, Y., Lotan, R., Kerner, H., Eimerl, S., Tony Parks, W., Gottfried, Y., Birkey Reffey, S., de Caestecker, M.P., Danielpour, D., Book-Melamed, N., Timberg, R., Duckett, C.S., Lechleider, R.J., Steller, H., Orly, J., Kim, S.J., Roberts, A.B. Nat. Cell Biol. (2000) [Pubmed]
  9. Mammalian septins regulate microtubule stability through interaction with the microtubule-binding protein MAP4. Kremer, B.E., Haystead, T., Macara, I.G. Mol. Biol. Cell (2005) [Pubmed]
  10. SEPT2 is a new fusion partner of MLL in acute myeloid leukemia with t(2;11)(q37;q23). Cerveira, N., Correia, C., Bizarro, S., Pinto, C., Lisboa, S., Mariz, J.M., Marques, M., Teixeira, M.R. Oncogene (2006) [Pubmed]
  11. Expression profiling the human septin gene family. Hall, P.A., Jung, K., Hillan, K.J., Russell, S.E. J. Pathol. (2005) [Pubmed]
  12. Biochemical and cell biological analyses of a mammalian septin complex, Sept7/9b/11. Nagata, K., Asano, T., Nozawa, Y., Inagaki, M. J. Biol. Chem. (2004) [Pubmed]
  13. Lymphocyte HEV adhesion variants differ in the expression of multiple gene sequences. Nottenburg, C., Gallatin, W.M., St John, T. Gene (1990) [Pubmed]
  14. An anillin homologue, Mid2p, acts during fission yeast cytokinesis to organize the septin ring and promote cell separation. Tasto, J.J., Morrell, J.L., Gould, K.L. J. Cell Biol. (2003) [Pubmed]
  15. Cytoskeleton: what does GTP do for septins? Mitchison, T.J., Field, C.M. Curr. Biol. (2002) [Pubmed]
  16. Filament formation of MSF-A, a mammalian septin, in human mammary epithelial cells depends on interactions with microtubules. Nagata, K., Kawajiri, A., Matsui, S., Takagishi, M., Shiromizu, T., Saitoh, N., Izawa, I., Kiyono, T., Itoh, T.J., Hotani, H., Inagaki, M. J. Biol. Chem. (2003) [Pubmed]
  17. Dopamine-dependent neurodegeneration in rats induced by viral vector-mediated overexpression of the parkin target protein, CDCrel-1. Dong, Z., Ferger, B., Paterna, J.C., Vogel, D., Furler, S., Osinde, M., Feldon, J., Büeler, H. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  18. Rab35 regulates an endocytic recycling pathway essential for the terminal steps of cytokinesis. Kouranti, I., Sachse, M., Arouche, N., Goud, B., Echard, A. Curr. Biol. (2006) [Pubmed]
  19. Crystallization and preliminary crystallographic studies of human septin 1 with site-directed mutations. Hu, H., Yu, W.B., Li, S.X., Ding, X.M., Yu, L., Bi, R.C. Acta Crystallograph. Sect. F Struct. Biol. Cryst. Commun. (2006) [Pubmed]
  20. The novel human platelet septin SEPT8 is an interaction partner of SEPT4. Bläser, S., Horn, J., Würmell, P., Bauer, H., Strümpell, S., Nurden, P., Pagenstecher, A., Busse, A., Wunderle, D., Hainmann, I., Zieger, B. Thromb. Haemost. (2004) [Pubmed]
  21. Cytoskeletal modification of Rho guanine nucleotide exchange factor activity: identification of a Rho guanine nucleotide exchange factor as a binding partner for Sept9b, a mammalian septin. Nagata, K., Inagaki, M. Oncogene (2005) [Pubmed]
  22. Genomic organization, complex splicing pattern and expression of a human septin gene on chromosome 17q25.3. McIlhatton, M.A., Burrows, J.F., Donaghy, P.G., Chanduloy, S., Johnston, P.G., Russell, S.E. Oncogene (2001) [Pubmed]
  23. Human septin 3 on chromosome 22q13.2 is upregulated by neuronal differentiation. Methner, A., Leypoldt, F., Joost, P., Lewerenz, J. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
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