P42208 · SEPT2_MOUSE
- ProteinSeptin-2
- GeneSeptin2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids361 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Filament-forming cytoskeletal GTPase. Forms a filamentous structure with SEPTIN12, SEPTIN6, SEPTIN2 and probably SEPTIN4 at the sperm annulus which is required for the structural integrity and motility of the sperm tail during postmeiotic differentiation (By similarity).
Required for normal organization of the actin cytoskeleton. Plays a role in the biogenesis of polarized columnar-shaped epithelium by maintaining polyglutamylated microtubules, thus facilitating efficient vesicle transport, and by impeding MAP4 binding to tubulin. Required for the progression through mitosis. Forms a scaffold at the midplane of the mitotic splindle required to maintain CENPE localization at kinetochores and consequently chromosome congression. During anaphase, may be required for chromosome segregation and spindle elongation. Plays a role in ciliogenesis and collective cell movements (By similarity).
In cilia, required for the integrity of the diffusion barrier at the base of the primary cilium that prevents diffusion of transmembrane proteins between the cilia and plasma membranes: probably acts by regulating the assembly of the tectonic-like complex (also named B9 complex) by localizing TMEM231 protein
Required for normal organization of the actin cytoskeleton. Plays a role in the biogenesis of polarized columnar-shaped epithelium by maintaining polyglutamylated microtubules, thus facilitating efficient vesicle transport, and by impeding MAP4 binding to tubulin. Required for the progression through mitosis. Forms a scaffold at the midplane of the mitotic splindle required to maintain CENPE localization at kinetochores and consequently chromosome congression. During anaphase, may be required for chromosome segregation and spindle elongation. Plays a role in ciliogenesis and collective cell movements (By similarity).
In cilia, required for the integrity of the diffusion barrier at the base of the primary cilium that prevents diffusion of transmembrane proteins between the cilia and plasma membranes: probably acts by regulating the assembly of the tectonic-like complex (also named B9 complex) by localizing TMEM231 protein
Miscellaneous
Coordinated expression with SEPTIN6 and SEPTIN7.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 44-52 | GTP (UniProtKB | ChEBI) | |||
Binding site | 78 | GTP (UniProtKB | ChEBI) | |||
Binding site | 104 | GTP (UniProtKB | ChEBI) | |||
Site | 156 | Important for dimerization | |||
Binding site | 183-186 | GTP (UniProtKB | ChEBI) | |||
Binding site | 241 | GTP (UniProtKB | ChEBI) | |||
Binding site | 256 | GTP (UniProtKB | ChEBI) | |||
Binding site | 258 | GTP (UniProtKB | ChEBI) | |||
GO annotations
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSeptin-2
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP42208
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: In metaphase cells, localized within the microtubule spindle. At the metaphase plate, in close apposition to the kinetochores of the congressed chromosomes. In cells undergoing cytokinesis, localized to the midbody, the ingressing cleavage furrow, and the central spindle (By similarity).
In interphase and postmitotic cells, localized to fibrous or granular structures, depending on the growth state of the cell. Localizes at the base of the cilia near the morphological distinction between the cilia and plasma membranes. Found in the sperm annulus
In interphase and postmitotic cells, localized to fibrous or granular structures, depending on the growth state of the cell. Localizes at the base of the cilia near the morphological distinction between the cilia and plasma membranes. Found in the sperm annulus
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Mutagenesis | 46 | Loss of GTP-binding. | |||
Mutagenesis | 47 | Loss of GTP-binding activity. | |||
Mutagenesis | 51 | Loss of GTP-binding activity. | |||
Mutagenesis | 78 | Reduces affinity for GTP 20-fold. | |||
Mutagenesis | 125 | Loss of GTP-binding activity. | |||
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 11 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000173516 | 1-361 | Septin-2 | ||
Modified residue | 17 | Phosphotyrosine | |||
Modified residue | 190 | N6-acetyllysine | |||
Modified residue | 211 | Phosphotyrosine | |||
Modified residue | 218 | Phosphoserine | |||
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Tissue specificity
Widely expressed.
Developmental stage
Expressed at 17 dpc in the brain with levels remaining relatively stable up to adulthood (at protein level).
Gene expression databases
Interaction
Subunit
Septins polymerize into heterooligomeric protein complexes that form filaments, and associate with cellular membranes, actin filaments and microtubules (By similarity).
GTPase activity is required for filament formation (By similarity).
Septin filaments are assembled from asymmetrical heterotrimers, composed of SEPTIN2, SEPTIN6 and SEPTIN7 that associate head-to-head to form a hexameric unit (By similarity).
Interaction between SEPTIN2 and SEPTIN7 seems indirect (By similarity).
Interacts also with SEPTIN9 and SEPTIN5 (PubMed:11739749).
Interaction with SEPTIN4 not detected (PubMed:11739749).
Component of a septin core octameric complex consisting of SEPTIN12, SEPTIN7, SEPTIN6 and SEPTIN2 or SEPTIN4 in the order 12-7-6-2-2-6-7-12 or 12-7-6-4-4-6-7-12 and located in the sperm annulus (By similarity).
Interacts with MAP4 (By similarity).
Interacts with DZIP1L (By similarity).
GTPase activity is required for filament formation (By similarity).
Septin filaments are assembled from asymmetrical heterotrimers, composed of SEPTIN2, SEPTIN6 and SEPTIN7 that associate head-to-head to form a hexameric unit (By similarity).
Interaction between SEPTIN2 and SEPTIN7 seems indirect (By similarity).
Interacts also with SEPTIN9 and SEPTIN5 (PubMed:11739749).
Interaction with SEPTIN4 not detected (PubMed:11739749).
Component of a septin core octameric complex consisting of SEPTIN12, SEPTIN7, SEPTIN6 and SEPTIN2 or SEPTIN4 in the order 12-7-6-2-2-6-7-12 or 12-7-6-4-4-6-7-12 and located in the sperm annulus (By similarity).
Interacts with MAP4 (By similarity).
Interacts with DZIP1L (By similarity).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 34-306 | Septin-type G | |||
Region | 44-51 | G1 motif | |||
Region | 101-104 | G3 motif | |||
Region | 182-185 | G4 motif | |||
Region | 260-270 | Important for dimerization | |||
Sequence similarities
Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. Septin GTPase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length361
- Mass (Da)41,526
- Last updated1996-02-01 v2
- MD5 ChecksumFADC449AA9E21C3EED0AD8B486F7298F
Computationally mapped potential isoform sequences
There are 9 potential isoforms mapped to this entry
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D49382 EMBL· GenBank· DDBJ | BAA08380.1 EMBL· GenBank· DDBJ | mRNA | ||
AK028072 EMBL· GenBank· DDBJ | BAC25737.1 EMBL· GenBank· DDBJ | mRNA | ||
AK146616 EMBL· GenBank· DDBJ | BAE27305.1 EMBL· GenBank· DDBJ | mRNA | ||
AK151591 EMBL· GenBank· DDBJ | BAE30531.1 EMBL· GenBank· DDBJ | mRNA | ||
AK171331 EMBL· GenBank· DDBJ | BAE42396.1 EMBL· GenBank· DDBJ | mRNA | ||
CH466520 EMBL· GenBank· DDBJ | EDL39946.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH466520 EMBL· GenBank· DDBJ | EDL39948.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC138636 EMBL· GenBank· DDBJ | AAI38637.1 EMBL· GenBank· DDBJ | mRNA | ||
BC138637 EMBL· GenBank· DDBJ | AAI38638.1 EMBL· GenBank· DDBJ | mRNA |