Q8BYW1
Gene name |
Arhgap25 (Kiaa0053) |
Protein name |
Rho GTPase-activating protein 25 |
Names |
Rho-type GTPase-activating protein 25 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:232201 |
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 Q8BYW1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q8BYW1-F1 | Predicted | AlphaFoldDB |
32 variants for Q8BYW1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3388848995 | 91 | Y>F | No | EVA | |
| rs3388807663 | 111 | V>I | No | EVA | |
| rs3388821935 | 160 | Q>L | No | EVA | |
| rs3388840538 | 176 | L>M | No | EVA | |
| rs3388842369 | 225 | R>K | No | EVA | |
| rs3388842444 | 267 | E>K | No | EVA | |
| rs3388844945 | 307 | K>N | No | EVA | |
| rs3388828042 | 310 | V>M | No | EVA | |
| rs3388848970 | 327 | E>D | No | EVA | |
| rs3388824550 | 329 | P>L | No | EVA | |
| rs3388844972 | 341 | R>* | No | EVA | |
| rs261049976 | 351 | E>D | No | EVA | |
| rs3388807673 | 375 | P>S | No | EVA | |
| rs3397031799 | 388 | D>Y | No | EVA | |
| rs3388836761 | 393 | R>M | No | EVA | |
| rs3388849031 | 407 | T>I | No | EVA | |
| rs3388821919 | 412 | P>A | No | EVA | |
| rs3388821919 | 412 | P>S | No | EVA | |
| rs3397004789 | 420 | E>D | No | EVA | |
| rs3397008085 | 421 | D>Y | No | EVA | |
| rs3388838439 | 458 | T>I | No | EVA | |
| rs3388842861 | 463 | L>M | No | EVA | |
| rs3388838449 | 477 | A>S | No | EVA | |
| rs3388846711 | 502 | T>I | No | EVA | |
| rs3388836674 | 578 | N>E* | No | EVA | |
| rs3388836730 | 580 | E>G | No | EVA | |
| rs3388842441 | 614 | V>L | No | EVA | |
| rs3388844930 | 635 | F>Y | No | EVA | |
| rs3388807678 | 637 | K>SDG* | No | EVA | |
| rs3388840960 | 639 | M>K | No | EVA | |
| rs3388840536 | 639 | M>L | No | EVA | |
| rs3388838462 | 648 | P>S | No | EVA |
No associated diseases with Q8BYW1
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| phagocytic cup | An invagination of the cell membrane formed by an actin dependent process during phagocytosis. Following internalization it is converted into a phagosome. |
1 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. |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| actin filament 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. Includes processes that control the spatial distribution of actin filaments, such as organizing filaments into meshworks, bundles, or other structures, as by cross-linking. |
| activation of GTPase activity | Any process that initiates the activity of an inactive GTPase through the replacement of GDP by GTP. |
| negative regulation of small GTPase mediated signal transduction | Any process that stops, prevents, or reduces the frequency, rate or extent of small GTPase mediated signal transduction. |
| phagocytosis, engulfment | The internalization of bacteria, immune complexes and other particulate matter or of an apoptotic cell by phagocytosis, including the membrane and cytoskeletal processes required, which involves one of three mechanisms: zippering of pseudopods around a target via repeated receptor-ligand interactions, sinking of the target directly into plasma membrane of the phagocytosing cell, or induced uptake via an enhanced membrane ruffling of the phagocytosing cell similar to macropinocytosis. |
| 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. |
7 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q9VDS5 | RhoGAP92B | Rho GTPase-activating protein 92B | Drosophila melanogaster (Fruit fly) | PR |
| Q9Y3L3 | SH3BP1 | SH3 domain-binding protein 1 | Homo sapiens (Human) | PR |
| P32019 | INPP5B | Type II inositol 1,4,5-trisphosphate 5-phosphatase | Homo sapiens (Human) | PR |
| Q8K2H3 | Fam13b | Protein FAM13B | Mus musculus (Mouse) | PR |
| P55194 | Sh3bp1 | SH3 domain-binding protein 1 | Mus musculus (Mouse) | PR |
| Q8K337 | Inpp5b | Type II inositol 1,4,5-trisphosphate 5-phosphatase | Mus musculus (Mouse) | PR |
| Q3TBD2 | Arhgap45 | Rho GTPase-activating protein 45 | Mus musculus (Mouse) | SS |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSLKLPRNWD | FNLKAEASKI | ARSRSVMTGE | QMAAFHPPTT | PNPLERPIKV | GWLKKQRSIV |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KNWQQRYFVL | RAQQLYYYKD | EEDSKPQGCM | YLPGSTVKEI | ATNPEEAGKF | VFEVIPASSD |
| 130 | 140 | 150 | 160 | 170 | 180 |
| QNRIGQDSYV | LMASSQVEME | EWVKFLRRVA | GTPSGAVFGQ | RLDETVAYEQ | KFGPHLVPIL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VEKCAEFILE | HGVSEEGIFR | LPGQDNLVKQ | LRDAFDAGER | PSFDRDTDVH | TVASLLKLYL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RDLPEPVVPW | SQYEGFLLCG | QLMNADEAKA | QQELVKQLST | LPRDNYNLLS | YICRFLHEIQ |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LNCAVNKMSV | DNLATVIGVN | LIRSKVEDPA | VIMRGTPQIQ | RVMTMMIRDH | EVLFPKSKDA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| PISPPAQKND | AKKAPVPRSS | VGWDATEDPP | LSRTDSFSNT | ASSPDATSPT | GPLPSDQHQE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| DSGKAPRENP | GDWKMQSRKR | TQTLPNRKCF | LTSAFQGTTS | SKLEIFKNEF | WSPSSEAKAG |
| 490 | 500 | 510 | 520 | 530 | 540 |
| EGHRRTMSQD | LRHLSNDQRT | STYDNVPTSP | QSQGNPAGAL | SPPASDSKRD | ALVSTDSEME |
| 550 | 560 | 570 | 580 | 590 | 600 |
| AGSKNSGEDD | LDSLQRTVQS | LQKEIETQKQ | VYEEQIKNLE | KENYDVWAKV | VRLNEELERE |
| 610 | 620 | 630 | 640 | ||
| RKKFAALEIS | LRNVERSRED | VEKRNRVLEE | EVKEFVKSME | KPKTKTDP |