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Search results 1 to 33 out of 33 for Sept8

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Type Details Score
Protein Domain
IPR030646 | SEPT8
Type: Family
Description: Septin 8 (SEPT8) belongs to the septin family. It suppresses the interaction between VAMP2 (vesicle-associated membrane protein 2) and synaptophysin through binding to VAMP2. It also forms a complex with syntaxin1A and may participate in the process of the SNARE complex formation and subsequent neurotransmitter release [].Septins were first discovered in budding yeast as a major component of bud neck filaments during cell septation [, ]. Later, its homologues were identified in nearly all eukaryotes, including humans. They are all GTP-binding proteins that are involved in diverse cellular functions, including cell cycle progression, vesicle trafficking, cytokinesis, cell migration, membrane dynamics, and chromosome segregation [, ]. Similar to cytoskeleton components such as actins and tubulins, they can assemble into filaments and bundles. However, unlike actin filaments and microtubules, septin filaments are not polar, similarly to intermediate filaments []. The number of septin genes per organism is variable: S. cerevisiae has seven and humans have 13 (SEPT1-12 and SEPT14; SEPT13 is a pseudogene now called SEPT7P2) []. All septins can form heteromeric complexes, which associate to form higher-order structures, including filaments, rings and cage-like formations [, ].
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Protein
B7ZC46
Organism: Mus musculus/domesticus
Length: 440  
Fragment?: false
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Protein
B1AQY9
Organism: Mus musculus/domesticus
Length: 442  
Fragment?: false
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Protein
E0CYM4
Organism: Mus musculus/domesticus
Length: 51  
Fragment?: true
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Protein
B1AQZ0
Organism: Mus musculus/domesticus
Length: 484  
Fragment?: false
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Publication
19196426 | J:266473
First Author: Ito H
Year: 2009
Journal: J Neurochem
Title: Sept8 controls the binding of vesicle-associated membrane protein 2 to synaptophysin.
Volume: 108
Issue: 4
Pages: 867-80
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Protein
Q8CHH9
Organism: Mus musculus/domesticus
Length: 429  
Fragment?: false
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Publication
773946 | -
First Author: Byers B
Year: 1976
Journal: J Cell Biol
Title: A highly ordered ring of membrane-associated filaments in budding yeast.
Volume: 69
Issue: 3
Pages: 717-21
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Publication
22314400 | -
First Author: Mostowy S
Year: 2012
Journal: Nat Rev Mol Cell Biol
Title: Septins: the fourth component of the cytoskeleton.
Volume: 13
Issue: 3
Pages: 183-94
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Publication
21990096 | -
First Author: Hall PA
Year: 2012
Journal: J Pathol
Title: Mammalian septins: dynamic heteromers with roles in cellular morphogenesis and compartmentalization.
Volume: 226
Issue: 2
Pages: 287-99
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Publication
24469395 | -
First Author: Zhai G
Year: 2014
Journal: Mol Cell Biol
Title: Sept6 is required for ciliogenesis in Kupffer's vesicle, the pronephros, and the neural tube during early embryonic development.
Volume: 34
Issue: 7
Pages: 1310-21
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Publication
4950437 | -
First Author: Hartwell LH
Year: 1971
Journal: Exp Cell Res
Title: Genetic control of the cell division cycle in yeast. IV. Genes controlling bud emergence and cytokinesis.
Volume: 69
Issue: 2
Pages: 265-76
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Publication
27084579 | J:246510
First Author: Kurkinen KM
Year: 2016
Journal: J Cell Sci
Title: SEPT8 modulates β-amyloidogenic processing of APP by affecting the sorting and accumulation of BACE1.
Volume: 129
Issue: 11
Pages: 2224-38
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Protein
Q8CHH9-2
Organism: Mus musculus/domesticus
Length: 430  
Fragment?: false
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Publication
12909369 | -
 
First Author: Bläser S
Year: 2003
Journal: Gene
Title: Isolation of new splice isoforms, characterization and expression analysis of the human septin SEPT8 (KIAA0202).
Volume: 312
Pages: 313-20
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Protein Coding Gene
MGI:894310 | Septin8
Type: protein_coding_gene
Organism: mouse, laboratory
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Allele
Tg(A94G6)1Rub | MGI:3615509
Name: transgene insertion 1, Edward M Rubin
Allele Type: Transgenic
Attribute String: Inserted expressed sequence
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Publication
9149945 | J:40314
First Author: Frazer KA
Year: 1997
Journal: Genome Res
Title: Computational and biological analysis of 680 kb of DNA sequence from the human 5q31 cytokine gene cluster region.
Volume: 7
Issue: 5
Pages: 495-512
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Strain
MGI:3615513 | STOCK Del(11Irf1-D11Mit23)1Rub Tg(A94G6)1Rub/Mmucd
Attribute String: mutant stock, transgenic, targeted mutation, deletion
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Publication
10655497 | J:60187
First Author: Zhu Y
Year: 2000
Journal: Proc Natl Acad Sci U S A
Title: Genomic interval engineering of mice identifies a novel modulator of triglyceride production.
Volume: 97
Issue: 3
Pages: 1137-42
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Genotype
Genotype
Symbol: Del(11Irf1-D11Mit23)1Rub/Del(11Irf1-D11Mit23)1Rub Tg(A94G6)1Rub/?
Background: involves: 129S6/SvEvTac * C57BL/6J
Zygosity: cx
Has Mutant Allele: true
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Publication
10321247 | -
First Author: Beites CL
Year: 1999
Journal: Nat Neurosci
Title: The septin CDCrel-1 binds syntaxin and inhibits exocytosis.
Volume: 2
Issue: 5
Pages: 434-9
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Publication
18385322 | -
First Author: Amin ND
Year: 2008
Journal: J Neurosci
Title: Cyclin-dependent kinase 5 phosphorylation of human septin SEPT5 (hCDCrel-1) modulates exocytosis.
Volume: 28
Issue: 14
Pages: 3631-43
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Publication
17224448 | J:120894
First Author: Taniguchi M
Year: 2007
Journal: J Biol Chem
Title: Phosphorylation of adult type Sept5 (CDCrel-1) by cyclin-dependent kinase 5 inhibits interaction with syntaxin-1.
Volume: 282
Issue: 11
Pages: 7869-76
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Publication
16767699 | -
First Author: Bläser S
Year: 2006
Journal: J Pathol
Title: Human endothelial cell septins: SEPT11 is an interaction partner of SEPT5.
Volume: 210
Issue: 1
Pages: 103-10
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Protein Domain
IPR030647 | SEPT5
Type: Family
Description: Septin 5 (SEPT5) belongs to the septin family. Septin 5, also known as CDCrel-1, is predominantly expressed in the nervous system, co-localises with synaptic vesicles and is involved in exocytosis []. In humans, its role in exocytotic secretion that is modulated by Cdk5 phosphorylation [, ]. SEPT5 interacts with SEPT8 and SEPT11. The complex formed by SEPT5 and SEPT11 is involved in the exocytosis mechanism in human umbilical vein endothelial cells (HUVECs) [].Septins were first discovered in budding yeast as a major component of bud neck filaments during cell septation [, ]. Later, its homologues were identified in nearly all eukaryotes, including humans. They are all GTP-binding proteins that are involved in diverse cellular functions, including cell cycle progression, vesicle trafficking, cytokinesis, cell migration, membrane dynamics, and chromosome segregation [, ]. Similar to cytoskeleton components such as actins and tubulins, they can assemble into filaments and bundles. However, unlike actin filaments and microtubules, septin filaments are not polar, similarly to intermediate filaments []. The number of septin genes per organism is variable: S. cerevisiae has seven and humans have 13 (SEPT1-12 and SEPT14; SEPT13 is a pseudogene now called SEPT7P2) []. All septins can form heteromeric complexes, which associate to form higher-order structures, including filaments, rings and cage-like formations [, ].
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Protein
Q68FM0
Organism: Mus musculus/domesticus
Length: 169  
Fragment?: true
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Protein
Q9Z2Q6
Organism: Mus musculus/domesticus
Length: 369  
Fragment?: false
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Protein
A0A338P729
Organism: Mus musculus/domesticus
Length: 248  
Fragment?: false
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Protein
A0A338P769
Organism: Mus musculus/domesticus
Length: 378  
Fragment?: false
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Protein
Q52KH2
Organism: Mus musculus/domesticus
Length: 268  
Fragment?: true
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Protein
A0A338P6R8
Organism: Mus musculus/domesticus
Length: 365  
Fragment?: false
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Protein
B7ZNM7
Organism: Mus musculus/domesticus
Length: 381  
Fragment?: false
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