SEPT7

Protein-coding gene in the species Homo sapiens

SEPTIN7

Available structures

PDB

Ortholog search: PDBe RCSB

List of PDB id codes
2QAG, 3T5D, 3TW4

Identifiers

Aliases

SEPTIN7, CDC10, CDC3, NBLA02942, SEPT7A, septin 7, SEPT7

External IDs

OMIM: 603151; MGI: 1335094; HomoloGene: 1354; GeneCards: SEPTIN7; OMA:SEPTIN7 - orthologs

Gene location (Human)

Chr.	Chromosome 7 (human)^[1]

Band	7p14.2	Start	35,800,932 bp^[1]
Band	7p14.2	End	35,907,110 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 9 (mouse)^[2]

Band	9\|9 A4	Start	25,163,735 bp^[2]
Band	9\|9 A4	End	25,219,867 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

corpus callosum

subthalamic nucleus

inferior ganglion of vagus nerve

external globus pallidus

occipital lobe

prefrontal cortex

Achilles tendon

endothelial cell

amygdala

Brodmann area 9

Top expressed in

atrioventricular valve

dermis

prefrontal cortex

left lung lobe

calvaria

optic nerve

nucleus accumbens

belly cord

medial geniculate nucleus

abdominal wall

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	nucleotide binding GTP binding structural molecule activity protein binding identical protein binding cadherin binding GTPase activity molecular adaptor activity
Cellular component	cytosol cell projection spindle cilium septin complex stress fiber chromosome midbody apical plasma membrane axoneme cleavage furrow chromosome, centromeric region cytoskeleton extracellular exosome nucleus kinetochore cytoplasm sperm annulus non-motile cilium septin ring microtubule cytoskeleton motile cilium
Biological process	cilium assembly protein heterooligomerization cytokinesis regulation of embryonic cell shape cell division positive regulation of non-motile cilium assembly cell cycle spermatogenesis cell differentiation negative regulation of cell migration positive regulation of apoptotic process cytoskeleton-dependent cytokinesis negative regulation of G1/S transition of mitotic cell cycle
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


989


235072

Ensembl


ENSG00000122545


ENSMUSG00000001833

UniProt


Q16181


O55131

RefSeq (mRNA)


NM_001011553 NM_001242956 NM_001788 NM_001363715 NM_001375299


NM_001205367 NM_009859 NM_001359736 NM_001359737 NM_001359738

RefSeq (protein)


NP_001011553 NP_001229885 NP_001779 NP_001350644 NP_001362228


NP_001192296 NP_033989 NP_001346665 NP_001346666 NP_001346667

Location (UCSC)

Chr 7: 35.8 – 35.91 Mb

Chr 9: 25.16 – 25.22 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Septin-7 is a protein that in humans is encoded by the SEPT7 gene.^[5]^[6]

Function

This gene encodes a protein that is highly similar to the CDC10 protein of Saccharomyces cerevisiae. The protein also shares similarity with Diff 6 of Drosophila and with H5 of mouse. Each of these similar proteins, including the yeast CDC10, contains a GTP-binding motif. The yeast CDC10 protein is a structural component of the 10 nm filament which lies inside the cytoplasmic membrane and is essential for cytokinesis. Although the exact function of this gene has not yet been determined, its high similarity to yeast CDC10 and the high conservative nature of eukaryotic cell cycle machinery suggest a similar role to that of its yeast counterpart. Alternative splicing results in two transcript variants encoding different isoforms.^[6]

Interactions

SEPT7 has been shown to interact with SEPT2^[7]^[8] and SEPT9.^[8]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000122545 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000001833 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Nakatsuru S, Sudo K, Nakamura Y (July 1994). "Molecular cloning of a novel human cDNA homologous to CDC10 in Saccharomyces cerevisiae". Biochemical and Biophysical Research Communications. 202 (1): 82–7. doi:10.1006/bbrc.1994.1896. PMID 8037772.
^ ^a ^b "Entrez Gene: SEPT7 septin 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 (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.
^ ^a ^b 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.

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Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
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. S2CID 10915358.
Oegema K, Savoian MS, Mitchison TJ, Field CM (August 2000). "Functional analysis of a human homologue of the Drosophila actin binding protein anillin suggests a role in cytokinesis". The Journal of Cell Biology. 150 (3): 539–52. doi:10.1083/jcb.150.3.539. PMC 2175195. PMID 10931866.
Joberty G, Perlungher RR, Sheffield PJ, Kinoshita M, Noda M, Haystead T, Macara IG (October 2001). "Borg proteins control septin organization and are negatively regulated by Cdc42". Nature Cell Biology. 3 (10): 861–6. doi:10.1038/ncb1001-861. PMID 11584266. S2CID 58805.
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.
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. S2CID 26291196.
Suzuki Y, Yamashita R, Shirota M, Sakakibara Y, Chiba J, Mizushima-Sugano J, Nakai K, Sugano S (September 2004). "Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions". Genome Research. 14 (9): 1711–8. doi:10.1101/gr.2435604. PMC 515316. PMID 15342556.
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. S2CID 7200157.
Andersen JS, Lam YW, Leung AK, Ong SE, Lyon CE, Lamond AI, Mann M (January 2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. Bibcode:2005Natur.433...77A. doi:10.1038/nature03207. PMID 15635413. S2CID 4344740.
Kimura K, Wakamatsu A, Suzuki Y, Ota T, Nishikawa T, Yamashita R, Yamamoto J, Sekine M, Tsuritani K, Wakaguri H, Ishii S, Sugiyama T, Saito K, Isono Y, Irie R, Kushida N, Yoneyama T, Otsuka R, Kanda K, Yokoi T, Kondo H, Wagatsuma M, Murakawa K, Ishida S, Ishibashi T, Takahashi-Fujii A, Tanase T, Nagai K, Kikuchi H, Nakai K, Isogai T, Sugano S (January 2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Research. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
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.
Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (November 2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.
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 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
Sirajuddin M, Farkasovsky M, Hauer F, Kühlmann D, Macara IG, Weyand M, Stark H, Wittinghofer A (September 2007). "Structural insight into filament formation by mammalian septins". Nature. 449 (7160): 311–5. Bibcode:2007Natur.449..311S. doi:10.1038/nature06052. PMID 17637674.
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.