SEPT2

Septin 2, also known as SEPT2, is a protein which in humans is encoded by the SEPT2 gene.[4][5]

SEPTIN2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesSEPTIN2, DIFF6, NEDD-5, NEDD5, Pnutl3, hNedd5, septin 2, SEPT2
External IDsOMIM: 601506 MGI: 97298 HomoloGene: 3243 GeneCards: SEPTIN2
Orthologs
SpeciesHumanMouse
Entrez

4735

18000

Ensembl

ENSG00000168385

n/a

UniProt

Q15019

P42208

RefSeq (mRNA)

NM_001159717
NM_001159718
NM_001159719
NM_010891

RefSeq (protein)

NP_001153189
NP_001153190
NP_001153191
NP_035021

Location (UCSC)Chr 2: 241.32 – 241.35 Mbn/a
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse

Function

SEPT2 can hetero-oligomerize with SEPT6 and SEPT7 to form filaments.[6] SEPT2 interacted with SEPT6 through its C-terminal coiled-coil domain.[6] 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 ties regulation of the DNA damage response to the cytoskeleton.[7]

Interactions

SEPT2 has been shown to interact with:

References

  1. GRCh38: Ensembl release 89: ENSG00000168385 - Ensembl, May 2017
  2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Entrez Gene: SEPT2 septin 2".
  5. 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. doi:10.1159/000134343. PMID 8697812.
  6. 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.
  7. 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.
  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.
  9. 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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
  10. 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.

Further reading


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