Q58DL7
SS
Gene name |
ARHGEF9 |
Protein name |
Rho guanine nucleotide exchange factor 9 |
Names |
Collybistin , Rac/Cdc42 guanine nucleotide exchange factor 9 |
Species |
Bos taurus (Bovine) |
KEGG Pathway |
bta:537718 |
EC number |
|
Protein Class |
|
Descriptions
The Rac-specific guanine nucleotide exchange factor (GEF) Asef is activated by binding to the tumor suppressor adenoma- tous polyposis coli mutant, which is found in sporadic and familial colorectal tumors. This activated Asef is involved in the migration of colorectal tumor cells. The GEFs for Rho family GTPases contain the Dbl homology (DH) domain and the pleckstrin homology (PH) domain. When Asef is in the resting state, the GEF activity of the DH-PH module is intramolecularly inhibited by its Src homology 3 (SH3) domain. Binding of the armadillo repeats of APC to a core APC-binding (CAB) motif within ASEF positioned adjacent to the SH3 domain relieves autoinhibition.
Autoinhibitory domains (AIDs)
Target domain |
148-332 (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
- 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
Autoinhibited structure
Activated structure
1 structures for Q58DL7
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q58DL7-F1 | Predicted | AlphaFoldDB |
No variants for Q58DL7
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q58DL7 | |||||
No associated diseases with Q58DL7
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| 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. |
| 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. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| 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. |
12 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| 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 |
| Q5DU57 | Spata13 | Spermatogenesis-associated protein 13 | Mus musculus (Mouse) | SS |
| Q3LAC4 | Prex2 | Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 2 protein | Mus musculus (Mouse) | SS |
| Q7TNR9 | Arhgef4 | Rho guanine nucleotide exchange factor 4 | Mus musculus (Mouse) | EV |
| Q69ZK0 | Prex1 | Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein | Mus musculus (Mouse) | SS |
| Q3UTH8 | Arhgef9 | Rho guanine nucleotide exchange factor 9 | Mus musculus (Mouse) | SS |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MELDQVGWRR | SRKLCTDNLD | QGSKTLETCK | NIGGYFKPQG | PGTEHINELI | TGDSIVSAEA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VWDHVTMANR | ELAFKAGDVI | KVLDASNKDW | WWGQIDDEEG | WFPASFVRLW | VNQEDGVEEG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| PSDVQNGHLD | PNSDCLCLGR | PLQNRDQMRA | NVINEIMSTE | RHYIKHLKDI | CEGYLKQCRK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RRDMFSDEQL | KVIFGNIEDI | YRFQMGFVRD | LEKQYNNDDP | HLSEIGPCFL | EHQDGFWIYS |
| 250 | 260 | 270 | 280 | 290 | 300 |
| EYCNNHLDAC | MELSKLMKDS | RYQHFFEACR | LLQQMIDIAI | DGFLLTPVQK | ICKYPLQLAE |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LLKYTAQDHS | DYRYVAAALA | VMRNVTQQIN | ERKRRLENID | KIAQWQASVL | DWEGEDILDR |
| 370 | 380 | 390 | 400 | 410 | 420 |
| SSELIYTGEM | AWIYQPYGRN | QQRVFFLFDH | QMVLCKKDLI | RRDILYYKGR | IDMDKYEVVD |
| 430 | 440 | 450 | 460 | 470 | 480 |
| IEDGRDDDFN | VSMKNAFKLH | NKETEEIHLF | FAKKLEEKIR | WLRAFREERK | MVQEDEKIGF |
| 490 | 500 | 510 | 520 | 530 | 540 |
| EISENQKRQA | AMTVRKVSKQ | KGVNSARSVP | PSYPPPQDPL | NQGQYLVPDG | IAQSQVFEFT |
| 550 | 560 | ||||
| EPKRSQSPFW | QNFSRLTPFK | K |