SEPT6

SEPTIN6
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2QAG
Identifiers
Aliases	SEPTIN6 , SEP2, SEPT2, septin 6, SEPT6
External IDs	OMIM: 300683 MGI: 1888939 HomoloGene: 62617 GeneCards: SEPTIN6
Gene location (Human)
Chr.	X chromosome (human)
End	119,693,370 bp
Gene location (Mouse)
Chr.	X chromosome (mouse)
End	36,255,447 bp
RNA expression pattern
	Top expressed in
	thymus; ; lymph node; ; appendix; ; left adrenal gland; ; blood; ; bone marrow cells; ; spleen; ; endothelial cell; ; sural nerve; ; monocyte;
	Top expressed in
	barrel cortex; ; facial motor nucleus; ; habenula; ; thymus; ; medial geniculate nucleus; ; medial dorsal nucleus; ; substantia nigra; ; motor neuron; ; blood; ; lateral geniculate nucleus;
	More reference expression data
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	nucleotide binding ; GTP binding ; protein binding ; GTPase activity ; molecular adaptor activity ;
Cellular component	cytoplasm ; axon terminus ; spindle ; midbody ; cleavage furrow ; chromosome, centromeric region ; cytoskeleton ; synaptic vesicle ; kinetochore ; chromosome ; septin ring ; septin collar ; septin complex ; sperm annulus ; cell projection ; motile cilium ; cilium ; presynapse ; microtubule cytoskeleton ; septin filament array ;
Biological process	cell cycle ; viral process ; cell division ; spermatogenesis ; cell differentiation ; mitotic cytokinesis ; septin ring assembly ; cilium assembly ; cytoskeleton-dependent cytokinesis ;
	Sources:Amigo / QuickGO
Orthologs
	23157
	56526
	ENSG00000125354
	ENSMUSG00000050379
	Q14141
	Q9R1T4
	NM_015129 ; NM_145799 ; NM_145800 ; NM_145802
NM_001177323 ; NM_001177324 ; NM_001253706 ; NM_019942 ; NM_001359140 ;
	NM_001359141 ; NM_001359142
	NP_055944 ; NP_665798 ; NP_665799 ; NP_665801
NP_001170794 ; NP_001170795 ; NP_001240635 ; NP_064326 ; NP_001346069 ;
	NP_001346070 ; NP_001346071
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated December 01, 2023

Septin-6 is a protein that in humans is encoded by the SEPT6 gene.^[5]^[6]^[7]

Function

This gene is a member of the septin family of GTPases. Members of this family are required for cytokinesis. This gene encodes four transcript variants encoding three distinct isoforms. An additional transcript variant has been identified, but its biological validity has not been determined.^[7]

Clinical significance

One version of pediatric acute myeloid leukemia is the result of a reciprocal translocation between chromosomes 11 and X, with the breakpoint associated with the genes encoding the mixed-lineage leukemia and septin 2 proteins.^[7]

Interactions

SEPT6 has been shown to interact with SEPT2.^[8]^[9]

Related Research Articles

Septins are a group of GTP-binding proteins expressed in all eukaryotic cells except plants. Different septins form protein complexes with each other. These complexes can further assemble into filaments, rings and gauzes. Assembled as such, septins function in cells by localizing other proteins, either by providing a scaffold to which proteins can attach, or by forming a barrier preventing the diffusion of molecules from one compartment of the cell to another, or in the cell cortex as a barrier to the diffusion of membrane-bound proteins.

Histone-lysine N-methyltransferase 2A, also known as acute lymphoblastic leukemia 1 (ALL-1), myeloid/lymphoid or mixed-lineage leukemia1 (MLL1), or zinc finger protein HRX (HRX), is an enzyme that in humans is encoded by the KMT2A gene.

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

Septin-9 is a protein that in humans is encoded by the SEPT9 gene.

Septin-5 is a protein that in humans is encoded by the SEPT5 gene.

Septin-4 is a protein that in humans is encoded by the SEPT4 gene.

Anillin is a conserved protein implicated in cytoskeletal dynamics during cellularization and cytokinesis. The ANLN gene in humans and the scraps gene in Drosophila encode Anillin. In 1989, anillin was first isolated in embryos of Drosophila melanogaster. It was identified as an F-actin binding protein. Six years later, the anillin gene was cloned from cDNA originating from a Drosophila ovary. Staining with anti-anillin antibody showed the anillin localizes to the nucleus during interphase and to the contractile ring during cytokinesis. These observations agree with further research that found anillin in high concentrations near the cleavage furrow coinciding with RhoA, a key regulator of contractile ring formation.

Septin-7 is a protein that in humans is encoded by the SEPT7 gene.

Protein AF-10 is a protein that in humans is encoded by the MLLT10 gene.

Phosphatidylinositol binding clathrin assembly protein, also known as PICALM, is a protein which in humans is encoded by the PICALM gene.

Sialic acid-binding Ig-like lectin 5 is a protein that in humans is encoded by the SIGLEC5 gene. SIGLEC5 has also been designated CD170.

Protein Regulator of cytokinesis 1 (PRC1) is a protein that in humans is encoded by the PRC1 gene and is involved in cytokinesis.

Protein CBFA2T2 is a protein that in humans is encoded by the CBFA2T2 gene.

Protein AF-9 is a protein that in humans is encoded by the MLLT3 gene.

G-protein-signaling modulator 2, also called LGN for its 10 Leucine-Glycine-Asparagine repeats, is a protein that in humans is encoded by the GPSM2 gene.

Protein ENL is a protein that in humans is encoded by the MLLT1 gene.

Septin-11 is a protein that in humans is encoded by the SEPT11 gene.

Myeloid leukemia factor 1 is a protein that in humans is encoded by the MLF1 gene.

Ten-eleven translocation methylcytosine dioxygenase 1 (TET1) is a member of the TET family of enzymes, in humans it is encoded by the TET1 gene. Its function, regulation, and utilizable pathways remain a matter of current research while it seems to be involved in DNA demethylation and therefore gene regulation.

Tet methylcytosine dioxygenase 2 (TET2) is a human gene. It resides at chromosome 4q24, in a region showing recurrent microdeletions and copy-neutral loss of heterozygosity (CN-LOH) in patients with diverse myeloid malignancies.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000125354 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000050379 - 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.
↑ 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.
↑ Xue J, Wang X, Malladi CS, Kinoshita M, Milburn PJ, Lengyel I, Rostas JA, Robinson PJ (April 2000). "Phosphorylation of a new brain-specific septin, G-septin, by cGMP-dependent protein kinase". The Journal of Biological Chemistry. 275 (14): 10047–56. doi: 10.1074/jbc.275.14.10047 . PMID 10744683.
1 2 3 "Entrez Gene: SEPT6 septin 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 (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.
↑ 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.

Kinoshita A, Noda M, Kinoshita M (December 2000). "Differential localization of septins in the mouse brain". The Journal of Comparative Neurology. 428 (2): 223–39. doi:10.1002/1096-9861(20001211)428:2<223::AID-CNE3>3.0.CO;2-M. PMID 11064363. S2CID 13174934.
Ono R, Taki T, Taketani T, Kawaguchi H, Taniwaki M, Okamura T, Kawa K, Hanada R, Kobayashi M, Hayashi Y (January 2002). "SEPTIN6, a human homologue to mouse Septin6, is fused to MLL in infant acute myeloid leukemia with complex chromosomal abnormalities involving 11q23 and Xq24". Cancer Research. 62 (2): 333–7. PMID 11809673.
Slater DJ, Hilgenfeld E, Rappaport EF, Shah N, Meek RG, Williams WR, Lovett BD, Osheroff N, Autar RS, Ried T, Felix CA (July 2002). "MLL-SEPTIN6 fusion recurs in novel translocation of chromosomes 3, X, and 11 in infant acute myelomonocytic leukaemia and in t(X;11) in infant acute myeloid leukaemia, and MLL genomic breakpoint in complex MLL-SEPTIN6 rearrangement is a DNA topoisomerase II cleavage site". Oncogene. 21 (30): 4706–14. doi:10.1038/sj.onc.1205572. PMID 12096348. S2CID 19525801.
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. S2CID 22757290.
Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J (May 2003). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nature Biotechnology. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801. S2CID 23783563.
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.
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.
Kadkol SS, Bruno A, Oh S, Schmidt ML, Lindgren V (July 2006). "MLL-SEPT6 fusion transcript with a novel sequence in an infant with acute myeloid leukemia". Cancer Genetics and Cytogenetics. 168 (2): 162–7. doi:10.1016/j.cancergencyto.2006.02.020. PMID 16843108.
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.
Kim CS, Seol SK, Song OK, Park JH, Jang SK (April 2007). "An RNA-binding protein, hnRNP A1, and a scaffold protein, septin 6, facilitate hepatitis C virus replication". Journal of Virology. 81 (8): 3852–65. doi:10.1128/JVI.01311-06. PMC 1866118 . PMID 17229681.
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.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000125354 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000050379 - 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.

[pmid8590280-5] 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.

[pmid10744683-6] Xue J, Wang X, Malladi CS, Kinoshita M, Milburn PJ, Lengyel I, Rostas JA, Robinson PJ (April 2000). "Phosphorylation of a new brain-specific septin, G-septin, by cGMP-dependent protein kinase". The Journal of Biological Chemistry. 275 (14): 10047–56. doi: 10.1074/jbc.275.14.10047 . PMID 10744683.

[entrez-7] 1 2 3 "Entrez Gene: SEPT6 septin 6".

[pmid16189514-8] 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.

[pmid12388755-9] 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.

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