Q09116
PR
Gene name |
spn2 (SPAC821.06) |
Protein name |
Septin homolog spn2 |
Names |
|
Species |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
KEGG Pathway |
spo:SPAC821.06 |
EC number |
|
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q09116
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q09116-F1 | Predicted | AlphaFoldDB |
2 variants for Q09116
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| I_990265_G_A | 6 | A>T | No | Jeffares_SNPs | |
| I_990564_T_C | 70 | Y>H | No | Jeffares_SNPs |
No associated diseases with Q09116
1 regional properties for Q09116
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Septin-type guanine nucleotide-binding (G) domain | 29 - 305 | IPR030379 |
Functions
13 GO annotations of cellular component
| Name | Definition |
|---|---|
| cell division site | The eventual plane of cell division (also known as cell cleavage or cytokinesis) in a dividing cell. In Eukaryotes, the cleavage apparatus, composed of septin structures and the actomyosin contractile ring, forms along this plane, and the mitotic, or meiotic, spindle is aligned perpendicular to the division plane. In bacteria, the cell division site is generally located at mid-cell and is the site at which the cytoskeletal structure, the Z-ring, assembles. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| mating projection septin ring | A septin ring, i.e. a ring-shaped structure composed of septins and septin-associated proteins, located at the neck of a shmoo (mating projection). The septin ring in the neck of a shmoo may act as a barrier to localize mating factors in the shmoo tip. |
| medial cortex septin ring | A ring-shaped structure that forms at the medial cortex of a symmetrically dividing cell at the onset of cytokinesis; composed of members of the conserved family of filament forming proteins called septins as well as septin-associated proteins. |
| meiotic septin complex | A heterooligomeric septin complex that acts during meiotic cell division. |
| membrane | A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it. |
| microtubule cytoskeleton | The part of the cytoskeleton (the internal framework of a cell) composed of microtubules and associated proteins. |
| mitotic actomyosin contractile ring, proximal layer | The region of the mitotic actomyosin ring adjacent to the plasma membrane where membrane bound scaffolds are located. |
| mitotic septin complex | A heterooligomeric septin complex that acts during mitotic cell division. |
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
| prospore septin ring | A tight ring-shaped structure that forms in the division plane at the site of cytokinesis in a prospore; composed of septins as well as septin-associated proteins. |
| septin complex | A protein complex containing septins. Typically, these complexes contain multiple septins and are oligomeric. |
| septin ring | A tight ring-shaped structure that forms in the division plane at the site of cytokinesis; composed of members of the conserved family of filament-forming proteins called septins as well as septin-associated proteins. This type of septin structure is observed at the bud neck of budding fungal cells, at the site of cell division in animal cells, at the junction between the mother cell and a pseudohyphal projection, and also within hyphae of filamentous fungi at sites where a septum will form. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| GTP binding | Binding to GTP, guanosine triphosphate. |
| GTPase activity | Catalysis of the reaction: GTP + H2O = GDP + H+ + phosphate. |
| molecular adaptor activity | The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way. |
| phosphatidylinositol-4-phosphate binding | Binding to phosphatidylinositol-4-phosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 4' position. |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| cytoskeleton-dependent cytokinesis | A cytokinesis that involves the function of a set of proteins that are part of the microfilament or microtubule cytoskeleton. |
| mitotic cytokinesis | A cell cycle process that results in the division of the cytoplasm of a cell after mitosis, resulting in the separation of the original cell into two daughter cells. |
| protein localization | Any process in which a protein is transported to, or maintained in, a specific location. |
| septin ring assembly | The aggregation, arrangement and bonding together of septins and associated proteins to form an organized structure resembling a ring at the cell cortex. |
| spore membrane bending pathway | The process in which a bending force is generated in the prospore membrane to form the characteristic curved shape of the prospore. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MEVPSAVTLN | NYVGFDSITS | QINRKLIRRG | FQFNVMVVGP | SGSGKSTLIN | TLFSAHLMDS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KGRLDYQAPY | RQTTEIHVTS | QVVRENRVQL | QLNLIDTPGY | GDQINNDKCW | EPIIKYIRDQ |
| 130 | 140 | 150 | 160 | 170 | 180 |
| HSSYLRRELN | SHREKRLQDT | RVHCCLFFIR | PTGHSLRPID | IAVLKRLTEV | VNVVPVIAKS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DSLTLEERAA | FKQQIREEFV | KHDINLYPYD | SDDADEEEIN | LNAAVRNLIP | FAVVGSEKAI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| IVDGRPIRGR | QNRWGVVNVD | DENHCEFVFL | RNFLMRTHLQ | DLIETTSYYH | YEKFRFKQLS |
| 310 | 320 | 330 | |||
| SLKEQSSLAT | RMGSPAPVYP | SEPHLHTATA | Q |