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Protein SEPT2 PDB 2QA5.png
Available structures
PDB Ortholog search: PDBe RCSB
Aliases SEPT2, DIFF6, NEDD-5, NEDD5, Pnutl3, hNedd5, septin 2
External IDs MGI: 97298 HomoloGene: 3243 GeneCards: SEPT2
Gene location (Human)
Chromosome 2 (human)
Chr. Chromosome 2 (human)[1]
Chromosome 2 (human)
Genomic location for SEPT2
Genomic location for SEPT2
Band No data available Start 241,315,100 bp[1]
End 241,354,027 bp[1]
RNA expression pattern
PBB GE SEPT2 200778 s at fs.png

PBB GE SEPT2 gnf1h09425 s at fs.png
More reference expression data
Species Human Mouse
RefSeq (mRNA)


RefSeq (protein)


Location (UCSC) Chr 2: 241.32 – 241.35 Mb Chr 2: 93.48 – 93.51 Mb
PubMed search [3] [4]
View/Edit Human View/Edit Mouse

Septin 2, also known as SEPT2, is a protein which in humans is encoded by the SEPT2 gene.[5][6]


SEPT2 can hetero-oligomerize with SEPT6 and SEPT7 to form filaments.[7] SEPT2 interacted with SEPT6 through its C-terminal coiled-coil domain.[7] Knockdown of SEPT2, SEPT6, and SEPT7 in causes actin stress fibers to disintegrate and cells to lose polarity. Septins, SOCS7, and NCK1 are part of a signaling pathway that couples regulation of the DNA damage response to the cytoskeleton.[8]


SEPT2 has been shown to interact with:


  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000168385 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000112508 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". 
  4. ^ "Mouse PubMed Reference:". 
  5. ^ "Entrez Gene: SEPT2 septin 2". 
  6. ^ Mori T, Miura K, Fujiwara T, Shin S, Inazawa J, Nakamura Y (1996). "Isolation and mapping of a human gene (DIFF6) homologous to yeast CDC3, CDC10, CDC11, and CDC12, and mouse Diff6". Cytogenetics and Cell Genetics. 73 (3): 224–7. PMID 8697812. doi:10.1159/000134343. 
  7. ^ a b Low C, Macara IG (October 2006). "Structural analysis of septin 2, 6, and 7 complexes". The Journal of Biological Chemistry. 281 (41): 30697–706. PMID 16914550. doi:10.1074/jbc.M605179200. 
  8. ^ 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. PMC 2085444Freely accessible. PMID 17803907. doi:10.1016/j.cell.2007.06.053. 
  9. ^ a b c 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. PMC 129964Freely accessible. PMID 12388755. doi:10.1091/mbc.E02-01-0042. 
  10. ^ 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). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. PMID 16189514. doi:10.1038/nature04209. 
  11. ^ 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". Molecular Systems Biology. 3: 89. PMC 1847948Freely accessible. PMID 17353931. doi:10.1038/msb4100134. 

Further reading[edit]