Q5ZMW5
PR
Gene name |
ARHGAP26 (GRAF) |
Protein name |
Rho GTPase-activating protein 26 |
Names |
GTPase regulator associated with focal adhesion kinase, Rho-type GTPase-activating protein 26 |
Species |
Gallus gallus (Chicken) |
KEGG Pathway |
gga:396113 |
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
2 structures for Q5ZMW5
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1F7C | X-ray | 240 A | A | 353-583 | PDB |
| AF-Q5ZMW5-F1 | Predicted | AlphaFoldDB |
16 variants for Q5ZMW5
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs734339583 | 94 | L>P | No | Ensembl | |
| rs738766777 | 105 | I>S | No | Ensembl | |
| rs314486361 | 151 | L>W | No | Ensembl | |
| rs736611578 | 166 | Q>R | No | Ensembl | |
| rs740184679 | 301 | V>G | No | Ensembl | |
| rs735041052 | 355 | E>G | No | Ensembl | |
| rs738309451 | 362 | E>G | No | Ensembl | |
| rs736378380 | 377 | N>K | No | Ensembl | |
| rs732969710 | 388 | I>V | No | Ensembl | |
| rs735006951 | 420 | V>G | No | Ensembl | |
| rs741194258 | 480 | E>K | No | Ensembl | |
| rs735465419 | 577 | S>L | No | Ensembl | |
| rs314023159 | 607 | A>T | No | Ensembl | |
| rs731861174 | 616 | R>Q | No | Ensembl | |
| rs1058644446 | 718 | D>N | No | Ensembl | |
| rs736097700 | 752 | I>L | No | Ensembl |
No associated diseases with Q5ZMW5
6 regional properties for Q5ZMW5
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Rho GTPase-activating protein domain | 383 - 568 | IPR000198 |
| domain | SH3 domain | 702 - 760 | IPR001452 |
| domain | Pleckstrin homology domain | 265 - 371 | IPR001849 |
| domain | BAR domain | 6 - 249 | IPR004148 |
| domain | GRAF, SH3 domain | 705 - 760 | IPR035481 |
| domain | GRAF, PH domain | 267 - 371 | IPR047225 |
Functions
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| cytoskeleton | A cellular structure that forms the internal framework of eukaryotic and prokaryotic cells. The cytoskeleton includes intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles. |
| focal adhesion | A cell-substrate junction that anchors the cell to the extracellular matrix and that forms a point of termination of actin filaments. In insects focal adhesion has also been referred to as hemi-adherens junction (HAJ). |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| GTPase activator activity | Binds to and increases the activity of a GTPase, an enzyme that catalyzes the hydrolysis of GTP. |
| phospholipid binding | Binding to a phospholipid, a class of lipids containing phosphoric acid as a mono- or diester. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| actin cytoskeleton organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments and their associated proteins. |
| regulation of small GTPase mediated signal transduction | Any process that modulates the frequency, rate or extent of small GTPase mediated signal transduction. |
| signal transduction | The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell. |
9 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q7YQL6 | OPHN1 | Oligophrenin-1 | Pan troglodytes (Chimpanzee) | PR |
| A6NI28 | ARHGAP42 | Rho GTPase-activating protein 42 | Homo sapiens (Human) | PR |
| O60890 | OPHN1 | Oligophrenin-1 | Homo sapiens (Human) | PR |
| Q9UNA1 | ARHGAP26 | Rho GTPase-activating protein 26 | Homo sapiens (Human) | PR |
| Q99J31 | Ophn1 | Oligophrenin-1 | Mus musculus (Mouse) | PR |
| B2RQE8 | Arhgap42 | Rho GTPase-activating protein 42 | Mus musculus (Mouse) | PR |
| Q6ZQ82 | Arhgap26 | Rho GTPase-activating protein 26 | Mus musculus (Mouse) | PR |
| P0CAX5 | Ophn1 | Oligophrenin-1 | Rattus norvegicus (Rat) | PR |
| B5DFQ4 | arhgap26 | Rho GTPase-activating protein 26 | Xenopus tropicalis (Western clawed frog) (Silurana tropicalis) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MGLPALEFSE | CCLDSPQFRE | RLRSHEAELE | KTNKFIKELI | KDGKSLIAAL | KNLSSAKRKF |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ADSLNEFKFR | CIGDAETDDE | ICIAKSLQEF | ATVLRNLEDE | RMRMIENASE | VLITPLEKFR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KEQIGAAKDA | KKKYDKETEK | YCGVLEKHLN | LSSKKKESQL | QEADSQVDLV | RQHFYEVSLE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| YVFKVQEVQE | RKMFEFVEPL | LAFLQGLFTF | YHHGYELAKD | FSDFKTELTI | SIQNTRNRFE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| GTRSEVESLM | KKMKENPHEH | KNISPYTMEG | YLYVQEKRHF | GTSWVKHYCT | YQRESKRITM |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VPFDQKSGGK | GGEDEAVILK | SCTRRKTDSI | EKRFCFDVEA | VDRPGVITMQ | ALSEEDRRLW |
| 370 | 380 | 390 | 400 | 410 | 420 |
| MEAMDGREPV | YNSNKDNQSE | GTAQLDSIGF | SIIKKCIHAV | ETRGINEQGL | YRIVGVNSRV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| QKLLSILMDP | KTATETETEI | CAEWEIKTIT | SALKTYLRML | PGPLMMYQFQ | RSFIKAAKLE |
| 490 | 500 | 510 | 520 | 530 | 540 |
| NQESRVSEIH | SLVHRLPEKN | RQMLHLLMNH | LAKVADNHKQ | NLMTVANLGV | VFGPTLLRPQ |
| 550 | 560 | 570 | 580 | 590 | 600 |
| EETVAAIMDI | KFQNIVIEIL | IENHEKIFNT | VPETPPSNSQ | LLLSRKKSTD | SKPPSCSERP |
| 610 | 620 | 630 | 640 | 650 | 660 |
| LTLFHTAQPN | EKQESRNSII | NSSLESVISS | NANSFLNSNS | APQSNLNSSD | LELEVIKPNR |
| 670 | 680 | 690 | 700 | 710 | 720 |
| PNSLPQNPSP | TSPLSPSWPM | FSAPSSPMPT | SSTSSDSSPI | SSPLRKARAL | YACKAEHDSE |
| 730 | 740 | 750 | |||
| LSFTAGTVFD | NVHPSQEPGW | LEGTLNGKTG | LIPENYVEFL |