SEPT2

Septin 2

Rendering based on PDB 2QA5.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols SEPT2 ; DIFF6; NEDD-5; NEDD5; Pnutl3; hNedd5
External IDs OMIM: 601506 MGI: 97298 HomoloGene: 3243 GeneCards: SEPT2 Gene
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez 4735 18000
Ensembl ENSG00000168385 ENSMUSG00000026276
UniProt Q15019 P42208
RefSeq (mRNA) NM_001008491 NM_001159717
RefSeq (protein) NP_001008491 NP_001153189
Location (UCSC) Chr 2:
241.32 – 241.35 Mb
Chr 1:
93.48 – 93.51 Mb
PubMed search

Septin 2, also known as SEPT2, is a protein which in humans is encoded by the SEPT2 gene.[1][2]

Function

SEPT2 can hetero-oligomerize with SEPT6 and SEPT7 to form filaments.[3] SEPT2 interacted with SEPT6 through its C-terminal coiled-coil domain.[3] 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.[4]

Interactions

SEPT2 has been shown to interact with:

References

  1. "Entrez Gene: SEPT2 septin 2".
  2. 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". Cytogenet. Cell Genet. 73 (3): 224–7. doi:10.1159/000134343. PMID 8697812.
  3. 1 2 Low C, Macara IG (October 2006). "Structural analysis of septin 2, 6, and 7 complexes". J. Biol. Chem. 281 (41): 30697–706. doi:10.1074/jbc.M605179200. PMID 16914550.
  4. 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.
  5. 1 2 3 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.
  6. 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 (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
  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. "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3: 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

Further reading

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