Q3UTH8
SS
Gene name |
Arhgef9 (Kiaa0424) |
Protein name |
Rho guanine nucleotide exchange factor 9 |
Names |
Collybistin, Rac/Cdc42 guanine nucleotide exchange factor 9 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:236915 |
EC number |
|
Protein Class |
|
Descriptions
Arhgef9 is a guanine nucleotide exchange factor (GEF). In the absence of the mutated APC, SH3 domain binds the Rac-binding site on DH domain, and therefore, the guanine nucleotide exchange activity is autoinhibited.
Autoinhibitory domains (AIDs)
Target domain |
103-287 (DH domain) |
Relief mechanism |
Partner binding |
Assay |
|
Accessory elements
No accessory elements
References
- Hamann MJ et al. (2007) "Asef2 functions as a Cdc42 exchange factor and is stimulated by the release of an autoinhibitory module from a concealed C-terminal activation element", Molecular and cellular biology, 27, 1380-93
- Murayama K et al. (2007) "Crystal structure of the rac activator, Asef, reveals its autoinhibitory mechanism", The Journal of biological chemistry, 282, 4238-4242
- Harvey K et al. (2004) "The GDP-GTP exchange factor collybistin: an essential determinant of neuronal gephyrin clustering", The Journal of neuroscience : the official journal of the Society for Neuroscience, 24, 5816-26
- Mitin N et al. (2007) "Release of autoinhibition of ASEF by APC leads to CDC42 activation and tumor suppression", Nature structural & molecular biology, 14, 814-23
- Ravala SK et al. (2020) "The first DEP domain of the RhoGEF P-Rex1 autoinhibits activity and contributes to membrane binding", The Journal of biological chemistry, 295, 12635-12647
Autoinhibited structure
Activated structure
1 structures for Q3UTH8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q3UTH8-F1 | Predicted | AlphaFoldDB |
1 variants for Q3UTH8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs31860546 | 60 | S>C | No | Ensembl |
No associated diseases with Q3UTH8
7 GO annotations of cellular component
| Name | Definition |
|---|---|
| cell cortex | The region of a cell that lies just beneath the plasma membrane and often, but not always, contains a network of actin filaments and associated proteins. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| GABA-ergic synapse | A synapse that uses GABA as a neurotransmitter. These synapses are typically inhibitory. |
| glycinergic synapse | A synapse that uses glycine as a neurotransmitter. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
| postsynaptic density | An electron dense network of proteins within and adjacent to the postsynaptic membrane of an asymmetric, neuron-neuron synapse. Its major components include neurotransmitter receptors and the proteins that spatially and functionally organize them such as anchoring and scaffolding molecules, signaling enzymes and cytoskeletal components. |
| postsynaptic specialization | A network of proteins within and adjacent to the postsynaptic membrane. Its major components include neurotransmitter receptors and the proteins that spatially and functionally organize them such as anchoring and scaffolding molecules, signaling enzymes and cytoskeletal components. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| guanyl-nucleotide exchange factor activity | Stimulates the exchange of GDP to GTP on a signaling GTPase, changing its conformation to its active form. Guanine nucleotide exchange factors (GEFs) act by stimulating the release of guanosine diphosphate (GDP) to allow binding of guanosine triphosphate (GTP), which is more abundant in the cell under normal cellular physiological conditions. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| receptor clustering | The receptor metabolic process that results in grouping of a set of receptors at a cellular location, often to amplify the sensitivity of a signaling response. |
| regulation of postsynaptic specialization assembly | Any process that modulates the frequency, rate or extent of postsynaptic specialization assembly, the aggregation, arrangement and bonding together of a set of components to form a postsynaptic specialization. |
| small GTPase mediated signal transduction | The series of molecular signals in which a small monomeric GTPase relays a signal. |
12 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q58DL7 | ARHGEF9 | Rho guanine nucleotide exchange factor 9 | Bos taurus (Bovine) | SS |
| Q70Z35 | PREX2 | Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 2 protein | Homo sapiens (Human) | SS |
| Q6XZF7 | DNMBP | Dynamin-binding protein | Homo sapiens (Human) | PR |
| Q9NR80 | ARHGEF4 | Rho guanine nucleotide exchange factor 4 | Homo sapiens (Human) | EV |
| A1IGU5 | ARHGEF37 | Rho guanine nucleotide exchange factor 37 | Homo sapiens (Human) | PR |
| Q8TCU6 | PREX1 | Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein | Homo sapiens (Human) | EV |
| Q96N96 | SPATA13 | Spermatogenesis-associated protein 13 | Homo sapiens (Human) | EV |
| O43307 | ARHGEF9 | Rho guanine nucleotide exchange factor 9 | Homo sapiens (Human) | SS |
| Q3LAC4 | Prex2 | Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 2 protein | Mus musculus (Mouse) | SS |
| Q69ZK0 | Prex1 | Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein | Mus musculus (Mouse) | SS |
| Q5DU57 | Spata13 | Spermatogenesis-associated protein 13 | Mus musculus (Mouse) | SS |
| Q7TNR9 | Arhgef4 | Rho guanine nucleotide exchange factor 4 | Mus musculus (Mouse) | EV |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MYDLITGDSI | VSAEAVWDHV | TMANRELAFK | AGDVIKVLDA | SNKDWWWGQI | DDEEGWFPAS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| FVRLWVNQED | GVEEGPSDVQ | NGHLDPNSDC | LCLGRPLQNR | DQMRANVINE | IMSTERHYIK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| HLKDICEGYL | KQCRKRRDMF | SDEQLKVIFG | NIEDIYRFQM | GFVRDLEKQY | NNDDPHLSEI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GPCFLEHQDG | FWIYSEYCNN | HLDACMELSK | LMKDSRYQHF | FEACRLLQQM | IDIAIDGFLL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| TPVQKICKYP | LQLAELLKYT | AQDHSDYRYV | AAALAVMRNV | TQQINERKRR | LENIDKIAQW |
| 310 | 320 | 330 | 340 | 350 | 360 |
| QASVLDWEGE | DILDRSSELI | YTGEMAWIYQ | PYGRNQQRVF | FLFDHQMVLC | KKDLIRRDIL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| YYKGRIDMDK | YEVIDIEDGR | DDDFNVSMKN | AFKLHNKETE | EVHLFFAKKL | EEKIRWLRAF |
| 430 | 440 | 450 | 460 | 470 | 480 |
| REERKMVQED | EKIGFEISEN | QKRQAAMTVR | KASKQKGVNS | ARSVPPSYPP | PQDPLNQGQY |
| 490 | 500 | 510 | |||
| LVPDGIAQSQ | VFEFTEPKRS | QSPFWQNFSR | LTPFKK |