SEPT2

Septin 2

Rendering based on PDB 2QA5.

Available structures
PDB	2QA5, 2QAG, 2QNR

Identifiers

Symbols

SEPT2; DIFF6; KIAA0158; NEDD5; Pnutl3; hNedd5

External IDs

OMIM: 601506 MGI: 97298 HomoloGene: 3243 GeneCards: SEPT2 Gene

Gene Ontology
Molecular function	• nucleotide binding • protein binding • GTP binding • enzyme regulator activity • protein complex scaffold
Cellular component	• exocyst • condensed chromosome kinetochore • nucleus • chromosome • nucleolus • cytoplasm • spindle • plasma membrane • cell cortex • cell surface • actin cytoskeleton • synaptosome • midbody • septin complex • cleavage furrow • cell projection • perinuclear region of cytoplasm
Biological process	• regulation of L-glutamate transport • cell cycle • mitosis • neuron projection development • regulation of protein localization • cell division
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 2:
242.25 – 242.29 Mb

Chr 1:
95.38 – 95.41 Mb

PubMed search

[1]

[2]

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

1 Function
2 Interactions
3 References
4 Further reading

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 SEPT9,^[5] SEPT6^[5]^[6] and SEPT7.^[5]^[7]

References

^ "Entrez Gene: SEPT2 septin 2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4735.
^ 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.
^ ^a ^b 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.
^ 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2085444.
^ ^a ^b ^c Surka, Mark C; Tsang Christopher W, Trimble William S (Oct. 2002). "The mammalian septin MSF localizes with microtubules and is required for completion of cytokinesis". Mol. Biol. Cell (United States) 13 (10): 3532–45. doi:10.1091/mbc.E02-01-0042. ISSN 1059-1524. PMC 129964. PMID 12388755. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=129964.
^ Rual, Jean-François; Venkatesan Kavitha, Hao Tong, Hirozane-Kishikawa Tomoko, Dricot Amélie, Li Ning, Berriz Gabriel F, Gibbons Francis D, Dreze Matija, Ayivi-Guedehoussou Nono, Klitgord Niels, Simon Christophe, Boxem Mike, Milstein Stuart, Rosenberg Jennifer, Goldberg Debra S, Zhang Lan V, Wong Sharyl L, Franklin Giovanni, Li Siming, Albala Joanna S, Lim Janghoo, Fraughton Carlene, Llamosas Estelle, Cevik Sebiha, Bex Camille, Lamesch Philippe, Sikorski Robert S, Vandenhaute Jean, Zoghbi Huda Y, Smolyar Alex, Bosak Stephanie, Sequerra Reynaldo, Doucette-Stamm Lynn, Cusick Michael E, Hill David E, Roth Frederick P, Vidal Marc (Oct. 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature (England) 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
^ Ewing, Rob M; Chu Peter, Elisma Fred, Li Hongyan, Taylor Paul, Climie Shane, McBroom-Cerajewski Linda, Robinson Mark D, O'Connor Liam, Li Michael, Taylor Rod, Dharsee Moyez, Ho Yuen, Heilbut Adrian, Moore Lynda, Zhang Shudong, Ornatsky Olga, Bukhman Yury V, Ethier Martin, Sheng Yinglun, Vasilescu Julian, Abu-Farha Mohamed, Lambert Jean-Philippe, Duewel Henry S, Stewart Ian I, Kuehl Bonnie, Hogue Kelly, Colwill Karen, Gladwish Katharine, Muskat Brenda, Kinach Robert, Adams Sally-Lin, Moran Michael F, Morin Gregg B, Topaloglou Thodoros, Figeys Daniel (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. (England) 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1847948.

Nagase T, Seki N, Tanaka A, et al. (1996). "Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1.". DNA Res. 2 (4): 167–74, 199–210. doi:10.1093/dnares/2.4.167. PMID 8590280.
Mori T, Miura K, Fujiwara T, et al. (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.
Kinoshita M, Kumar S, Mizoguchi A, et al. (1997). "Nedd5, a mammalian septin, is a novel cytoskeletal component interacting with actin-based structures.". Genes Dev. 11 (12): 1535–47. doi:10.1101/gad.11.12.1535. PMID 9203580.
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. doi:10.1016/S0896-6273(00)80493-6. PMID 9655500.
Kinoshita A, Kinoshita M, Akiyama H, et al. (1998). "Identification of septins in neurofibrillary tangles in Alzheimer's disease.". Am. J. Pathol. 153 (5): 1551–60. doi:10.1016/S0002-9440(10)65743-4. PMC 1853406. PMID 9811347. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1853406.
"Toward a complete human genome sequence.". Genome Res. 8 (11): 1097–108. 1999. doi:10.1101/gr.8.11.1097. PMID 9847074.
Beites CL, Xie H, Bowser R, Trimble WS (1999). "The septin CDCrel-1 binds syntaxin and inhibits exocytosis.". Nat. Neurosci. 2 (5): 434–9. doi:10.1038/8100. PMID 10321247.
Hoja MR, Wahlestedt C, Höög C (2000). "A visual intracellular classification strategy for uncharacterized human proteins.". Exp. Cell Res. 259 (1): 239–46. doi:10.1006/excr.2000.4948. PMID 10942595.
Sakai K, Kurimoto M, Tsugu A, et al. (2003). "Expression of Nedd5, a mammalian septin, in human brain tumors.". J. Neurooncol. 57 (3): 169–77. doi:10.1023/A:1015721801075. PMID 12125979.
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. PMC 129964. PMID 12388755. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=129964.
Sheffield PJ, Oliver CJ, Kremer BE, et al. (2003). "Borg/septin interactions and the assembly of mammalian septin heterodimers, trimers, and filaments.". J. Biol. Chem. 278 (5): 3483–8. doi:10.1074/jbc.M209701200. PMID 12446710.
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. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
Vega IE, Hsu SC (2003). "The septin protein Nedd5 associates with both the exocyst complex and microtubules and disruption of its GTPase activity promotes aberrant neurite sprouting in PC12 cells.". Neuroreport 14 (1): 31–7. doi:10.1097/01.wnr.0000050304.92401.50. PMID 12544826.
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. doi:10.1023/A:1025149005902. PMID 14531065.
She YM, Huang YW, Zhang L, Trimble WS (2004). "Septin 2 phosphorylation: theoretical and mass spectrometric evidence for the existence of a single phosphorylation site in vivo.". Rapid Commun. Mass Spectrom. 18 (10): 1123–30. doi:10.1002/rcm.1453. PMID 15150837.
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. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
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.
Spiliotis ET, Kinoshita M, Nelson WJ (2005). "A mitotic septin scaffold required for Mammalian chromosome congression and segregation.". Science 307 (5716): 1781–5. doi:10.1126/science.1106823. PMID 15774761.

SEPT2

Contents

Function

Interactions

References

Further reading