SEPT2

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

SEPTIN2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2QA5, 2QAG, 2QNR
Identifiers
Aliases	SEPTIN2, DIFF6, NEDD-5, NEDD5, Pnutl3, hNedd5, septin 2, SEPT2
External IDs	OMIM: 601506 MGI: 97298 HomoloGene: 3243 GeneCards: SEPTIN2
Gene location (Human) Chr. Chromosome 2 (human)[1] Band 2q37.3 Start 241,315,100 bp[1] End 241,354,027 bp[1]
Gene location (Mouse) Chr. Chromosome 1 (mouse)[2] Band 1|1 D Start 93,478,993 bp[2] End 93,509,733 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • nucleotide binding • GTP binding • GO:0001948 protein binding • cadherin binding • identical protein binding • GTPase activity • GO:0032947 molecular adaptor activity Cellular component • cytoplasm • condensed chromosome kinetochore • cell projection • membrane • cell membrane • spindle • septin complex • chromosome • photoreceptor connecting cilium • cell cortex • exocyst • midbody • nucleolus • ciliary membrane • actin cytoskeleton • perinuclear region of cytoplasm • GO:0035085 axoneme • cleavage furrow • chromosome, centromeric region • cytoskeleton • extracellular exosome • cell nucleus • kinetochore • cytosol • sperm annulus • non-motile cilium • cilium • septin ring • microtubule cytoskeleton • motile cilium Biological process • cell division • cell cycle • neuron projection development • spermatogenesis • cell differentiation • smoothened signaling pathway • cilium morphogenesis • cytoskeleton-dependent cytokinesis Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	4735	18000
Ensembl	ENSG00000168385	ENSMUSG00000116048
UniProt	Q15019	P42208
RefSeq (mRNA)	NM_001008491 NM_001008492 NM_001282972 NM_001282973 NM_004404 NM_006155 NM_001321029 NM_001321030 NM_001321031 NM_001321032 NM_001321033 NM_001321034 NM_001321035 NM_001349287 NM_001349288 NM_001349289 NM_001349290 NM_001349291 NM_001349302 NM_001349304 NM_001349305 NM_001349306 NM_001349307 NM_001349308 NM_001349309 NM_001349310 NM_001349311 NM_001349312 NM_001349313 NM_001349314 NM_001349315	NM_001159717 NM_001159718 NM_001159719 NM_010891
RefSeq (protein)	NP_001008491 NP_001008492 NP_001269901 NP_001269902 NP_001307958 NP_001307959 NP_001307960 NP_001307961 NP_001307962 NP_001307963 NP_001307964 NP_004395 NP_006146 NP_001336216 NP_001336217 NP_001336218 NP_001336219 NP_001336220 NP_001336231 NP_001336233 NP_001336234 NP_001336235 NP_001336236 NP_001336237 NP_001336238 NP_001336239 NP_001336240 NP_001336241 NP_001336242 NP_001336243 NP_001336244	NP_001153189 NP_001153190 NP_001153191 NP_035021
Location (UCSC)	Chr 2: 241.32 – 241.35 Mb	Chr 1: 93.48 – 93.51 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

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]

Interactions

SEPT2 has been shown to interact with:

• SEPT6[9][10]
• SEPT7,[9][11] and
• SEPT9.[9]

References

1. GRCh38: Ensembl release 89: ENSG00000168385 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000116048 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
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. doi:10.1159/000134343. PMID 8697812.
7. 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.
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. doi:10.1016/j.cell.2007.06.053. PMC 2085444. PMID 17803907.
9. 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.
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. doi:10.1038/nature04209. PMID 16189514.
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. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

Further reading

• Nagase T, Seki N, Tanaka A, Ishikawa K, Nomura N (August 1995). "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 Research. 2 (4): 167–74, 199–210. doi:10.1093/dnares/2.4.167. PMID 8590280.
• 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.
• Kinoshita M, Kumar S, Mizoguchi A, Ide C, Kinoshita A, Haraguchi T, Hiraoka Y, Noda M (June 1997). "Nedd5, a mammalian septin, is a novel cytoskeletal component interacting with actin-based structures". Genes & Development. 11 (12): 1535–47. doi:10.1101/gad.11.12.1535. PMID 9203580.
• Hsu SC, Hazuka CD, Roth R, Foletti DL, Heuser J, Scheller RH (June 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, Tomimoto H, Akiguchi I, Kumar S, Noda M, Kimura J (November 1998). "Identification of septins in neurofibrillary tangles in Alzheimer's disease". The American Journal of Pathology. 153 (5): 1551–60. doi:10.1016/S0002-9440(10)65743-4. PMC 1853406. PMID 9811347.
• "Toward a complete human genome sequence". Genome Research. 8 (11): 1097–108. November 1998. doi:10.1101/gr.8.11.1097. PMID 9847074.
• Beites CL, Xie H, Bowser R, Trimble WS (May 1999). "The septin CDCrel-1 binds syntaxin and inhibits exocytosis". Nature Neuroscience. 2 (5): 434–9. doi:10.1038/8100. PMID 10321247.
• Hoja MR, Wahlestedt C, Höög C (August 2000). "A visual intracellular classification strategy for uncharacterized human proteins". Experimental Cell Research. 259 (1): 239–46. doi:10.1006/excr.2000.4948. PMID 10942595.
• Sakai K, Kurimoto M, Tsugu A, Hubbard SL, Trimble WS, Rutka JT (May 2002). "Expression of Nedd5, a mammalian septin, in human brain tumors". Journal of Neuro-Oncology. 57 (3): 169–77. doi:10.1023/A:1015721801075. PMID 12125979.
• 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.
• Sheffield PJ, Oliver CJ, Kremer BE, Sheng S, Shao Z, Macara IG (January 2003). "Borg/septin interactions and the assembly of mammalian septin heterodimers, trimers, and filaments". The Journal of Biological Chemistry. 278 (5): 3483–8. doi:10.1074/jbc.M209701200. PMID 12446710.
• Vega IE, Hsu SC (January 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:10.1097/00001756-200301200-00006. PMID 12544826.
• Koshelev YA, Kiselev SL, Georgiev GP (2004). "Interaction of the S100A4 (Mts1) protein with septins Sept2, Sept6, and Sept7 in vitro". Doklady Biochemistry and Biophysics. 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 Communications in Mass Spectrometry. 18 (10): 1123–30. doi:10.1002/rcm.1453. PMID 15150837.
• Nagata K, Asano T, Nozawa Y, Inagaki M (December 2004). "Biochemical and cell biological analyses of a mammalian septin complex, Sept7/9b/11". The Journal of Biological Chemistry. 279 (53): 55895–904. doi:10.1074/jbc.M406153200. PMID 15485874.
• Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ (January 2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nature Biotechnology. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455.
• Andersen JS, Lam YW, Leung AK, Ong SE, Lyon CE, Lamond AI, Mann M (January 2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413.
• Spiliotis ET, Kinoshita M, Nelson WJ (March 2005). "A mitotic septin scaffold required for Mammalian chromosome congression and segregation". Science. 307 (5716): 1781–5. doi:10.1126/science.1106823. PMC 3368603. PMID 15774761.