Q9QZR6
PR
Gene name |
Septin9 |
Protein name |
Septin-9 |
Names |
Eighth septin, Eseptin, Septin-like protein, SLP |
Species |
Rattus norvegicus (Rat) |
KEGG Pathway |
rno:83788 |
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 Q9QZR6
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9QZR6-F1 | Predicted | AlphaFoldDB |
No variants for Q9QZR6
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9QZR6 | |||||
No associated diseases with Q9QZR6
1 regional properties for Q9QZR6
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Aminoacyl-tRNA synthetase, class I, conserved site | 42 - 52 | IPR001412 |
Functions
9 GO annotations of cellular component
| Name | Definition |
|---|---|
| axoneme | The bundle of microtubules and associated proteins that forms the core of cilia (also called flagella) in eukaryotic cells and is responsible for their movements. |
| 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. |
| microtubule | Any of the long, generally straight, hollow tubes of internal diameter 12-15 nm and external diameter 24 nm found in a wide variety of eukaryotic cells; each consists (usually) of 13 protofilaments of polymeric tubulin, staggered in such a manner that the tubulin monomers are arranged in a helical pattern on the microtubular surface, and with the alpha/beta axes of the tubulin subunits parallel to the long axis of the tubule; exist in equilibrium with pool of tubulin monomers and can be rapidly assembled or disassembled in response to physiological stimuli; concerned with force generation, e.g. in the spindle. |
| microtubule cytoskeleton | The part of the cytoskeleton (the internal framework of a cell) composed of microtubules and associated proteins. |
| non-motile cilium | A cilium which may have a variable array of axonemal microtubules but does not contain molecular motors. |
| perinuclear region of cytoplasm | Cytoplasm situated near, or occurring around, the nucleus. |
| 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. |
| stress fiber | A contractile actin filament bundle that consists of short actin filaments with alternating polarity, cross-linked by alpha-actinin and possibly other actin bundling proteins, and with myosin present in a periodic distribution along the fiber. |
3 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. |
3 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. |
| positive regulation of non-motile cilium assembly | Any process that activates or increases the frequency, rate or extent of non-motile cilium assembly. |
| protein localization | Any process in which a protein is transported to, or maintained in, a specific location. |
11 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P25342 | CDC10 | Cell division control protein 10 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | PR |
| Q08DM7 | SEPTIN3 | Neuronal-specific septin-3 | Bos taurus (Bovine) | PR |
| Q9UH03 | SEPTIN3 | Neuronal-specific septin-3 | Homo sapiens (Human) | PR |
| Q9UHD8 | SEPTIN9 | Septin-9 | Homo sapiens (Human) | PR |
| Q9Z1S5 | Septin3 | Neuronal-specific septin-3 | Mus musculus (Mouse) | PR |
| Q80UG5 | Septin9 | Septin-9 | Mus musculus (Mouse) | PR |
| Q9WU34 | Septin3 | Neuronal-specific septin-3 | Rattus norvegicus (Rat) | PR |
| Q9WVC0 | Septin7 | Septin-7 | Rattus norvegicus (Rat) | PR |
| B3GNI6 | Septin11 | Septin-11 | Rattus norvegicus (Rat) | PR |
| B0BNF1 | Septin8 | Septin-8 | Rattus norvegicus (Rat) | PR |
| A2BGU8 | septin3 | Neuronal-specific septin-3 | Danio rerio (Zebrafish) (Brachydanio rerio) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MERDRITALK | RSFEVEEIEP | PNSTPPRRVQ | TPLLRATVAS | SSQKFQDLGV | KNSEPAARLV |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DTLSQRSPKP | SLRRVDLAGA | KAPEPMSRRT | ELSIDISSKQ | VESTASTPGP | SRFGLKRAEV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LGHKTPEPVP | RRTEITIVKP | QESGLRRVET | PASKAPEGSA | MPVTDAAPKR | VEIQVPKPAE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| APNCPLPPQT | LENSEAPMSQ | LQSRLEPRPP | VTEVPYRNQE | DSEVAPSCVV | DMADNPRDAM |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LKQAPVSRNE | KAPVDFGYVG | IDSILEQMRR | KAMKQGFEFN | IMVVGQSGLG | KSTLINTLFK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SKISRKSVQP | ISEERIPKTI | EIKSITHDIE | EKGVRMKLTV | IDTPGFGDHI | NNENCWQPIM |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KFINDQYEKY | LQEEVNINRK | KRIPDTRVHC | CLYFIPATGH | SLRPLDIEFM | KRLSKVVNIV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| PVIAKADTLT | LEERVYFKQR | ITSDLLSNGI | DVYPQKEFDE | AEDRLVNEKF | REMIPFAVVG |
| 490 | 500 | 510 | 520 | 530 | 540 |
| SDHEYQVNGK | RILGRKTKWG | TIEVENTTHC | EFAYLRDLLI | RTHMQNIKDI | TSNIHFEAYR |
| 550 | 560 | ||||
| VKRLNEGNSA | MANGIEKEPE | TQEM |