Q9QWY8
SS
Gene name |
Asap1 (Ddef1, Kiaa1249, Shag1) |
Protein name |
Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 |
Names |
130 kDa phosphatidylinositol 4,5-bisphosphate-dependent ARF1 GTPase-activating protein , ADP-ribosylation factor-directed GTPase-activating protein 1 , ARF GTPase-activating protein 1 , Development and differentiation-enhancing factor 1 , DEF-1 , Differentiation-enhancing factor 1 , PIP2-dependent ARF1 GAP |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:13196 |
EC number |
|
Protein Class |
|
Descriptions
ASAP1 is an Arf GTPase-activating protein (GAP) that functions on membrane surfaces to catalyze the hydrolysis of GTP bound to Arf. ASAP1 has a BAR domain which functions as membrane curvature sensors or as inducers of membrane curvature. The BAR domain influences GAP activity by binding to the PH domain and/or Arf GAP domain. The deletion of the entire BAR domain or the N-terminal extension increased GAP activity.
Autoinhibitory domains (AIDs)
Target domain |
341-428 (PH domain);454-577 (Arf GAP domain) |
Relief mechanism |
Partner binding |
Assay |
|
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
4 structures for Q9QWY8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 5C6R | X-ray | 180 A | A/B | 325-451 | PDB |
| 5C79 | X-ray | 160 A | A/B | 325-451 | PDB |
| 8HLO | X-ray | 117 A | A | 1087-1147 | PDB |
| AF-Q9QWY8-F1 | Predicted | AlphaFoldDB |
53 variants for Q9QWY8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3389326146 | 7 | R>W | No | EVA | |
| rs3389284649 | 70 | A>V | No | EVA | |
| rs3389284609 | 171 | K>N | No | EVA | |
| rs3389365320 | 227 | E>D | No | EVA | |
| rs3389372034 | 233 | G>S | No | EVA | |
| rs3389353321 | 237 | L>M | No | EVA | |
| rs3389357808 | 257 | T>M | No | EVA | |
| rs3389365352 | 294 | K>E | No | EVA | |
| rs3389353252 | 299 | L>P | No | EVA | |
| rs3389357511 | 305 | G>D | No | EVA | |
| rs3389378686 | 311 | S>T | No | EVA | |
| rs3389326201 | 353 | I>T | No | EVA | |
| rs3389333011 | 402 | L>M | No | EVA | |
| rs3389284626 | 411 | F>I | No | EVA | |
| rs3389378715 | 412 | Q>* | No | EVA | |
| rs3389370051 | 477 | P>S | No | EVA | |
| rs3389357833 | 497 | R>S | No | EVA | |
| rs3389365110 | 498 | E>* | No | EVA | |
| rs3389314179 | 504 | S>A | No | EVA | |
| rs3389284620 | 516 | T>N | No | EVA | |
| rs3389369978 | 549 | S>G | No | EVA | |
| rs3389359281 | 559 | T>I | No | EVA | |
| rs1135344679 | 572 | C>R | No | EVA | |
| rs3389369958 | 620 | L>I | No | EVA | |
| rs3406212339 | 650 | S>F | No | EVA | |
| rs3406531453 | 654 | T>P | No | EVA | |
| rs3406531480 | 656 | L>P | No | EVA | |
| rs3389314193 | 678 | V>M | No | EVA | |
| rs3389370015 | 713 | N>T | No | EVA | |
| rs108530409 | 761 | S>L | No | EVA | |
| rs3389365332 | 774 | P>S | No | EVA | |
| rs3389365168 | 780 | L>H | No | EVA | |
| rs225084524 | 818 | T>S | No | EVA | |
| rs1132610060 | 821 | P>T | No | EVA | |
| rs1133870606 | 825 | P>A | No | EVA | |
| rs3389314190 | 827 | G>S | No | EVA | |
| rs3389372000 | 844 | P>S | No | EVA | |
| rs32149275 | 879 | L>S | No | EVA | |
| rs3389314187 | 883 | K>R | No | EVA | |
| rs3389343348 | 899 | S>F | No | EVA | |
| rs3389365171 | 901 | K>R | No | EVA | |
| rs3389314203 | 932 | T>I | No | EVA | |
| rs3389359283 | 1009 | P>L | No | EVA | |
| rs3389372059 | 1012 | Q>* | No | EVA | |
| rs3389369995 | 1044 | L>Q | No | EVA | |
| rs3389365336 | 1047 | N>I | No | EVA | |
| rs3389357858 | 1052 | D>N | No | EVA | |
| rs3389333012 | 1056 | K>N | No | EVA | |
| rs3389359258 | 1087 | V>M | No | EVA | |
| rs3389378672 | 1093 | I>V | No | EVA | |
| rs3406273978 | 1102 | D>V | No | EVA | |
| rs3389365146 | 1122 | W>* | No | EVA | |
| rs3389357544 | 1126 | H>R | No | EVA |
No associated diseases with Q9QWY8
7 regional properties for Q9QWY8
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | FERM domain | 5 - 295 | IPR000299 |
| domain | Ezrin/radixin/moesin, C-terminal | 502 - 577 | IPR011259 |
| domain | FERM, N-terminal | 9 - 70 | IPR018979 |
| domain | FERM, C-terminal PH-like domain | 210 - 299 | IPR018980 |
| conserved_site | FERM conserved site | 58 - 88 | IPR019747-1 |
| conserved_site | FERM conserved site | 176 - 205 | IPR019747-2 |
| domain | FERM central domain | 91 - 206 | IPR019748 |
6 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. |
| dendritic spine | A small, membranous protrusion from a dendrite that forms a postsynaptic compartment, typically receiving input from a single presynapse. They function as partially isolated biochemical and an electrical compartments. Spine morphology is variable:they can be thin, stubby, mushroom, or branched, with a continuum of intermediate morphologies. They typically terminate in a bulb shape, linked to the dendritic shaft by a restriction. Spine remodeling is though to be involved in synaptic plasticity. |
| glutamatergic synapse | A synapse that uses glutamate as a neurotransmitter. |
| Golgi membrane | The lipid bilayer surrounding any of the compartments of the Golgi apparatus. |
| podosome | An actin-rich adhesion structure characterized by formation upon cell substrate contact and localization at the substrate-attached part of the cell, contain an F-actin-rich core surrounded by a ring structure containing proteins such as vinculin and talin, and have a diameter of 0.5 mm. |
| trans-Golgi network membrane | The lipid bilayer surrounding any of the compartments that make up the trans-Golgi network. |
5 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. |
| metal ion binding | Binding to a metal ion. |
| phosphatidylinositol-3,4,5-trisphosphate binding | Binding to phosphatidylinositol-3,4,5-trisphosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 3', 4' and 5' positions. |
| phosphatidylinositol-4,5-bisphosphate binding | Binding to phosphatidylinositol-4,5-bisphosphate, a derivative of phosphatidylinositol in which the inositol ring is phosphorylated at the 4' and 5' positions. |
| phosphatidylserine binding | Binding to phosphatidylserine, a class of glycophospholipids in which a phosphatidyl group is esterified to the hydroxyl group of L-serine. |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| cilium assembly | The assembly of a cilium, a specialized eukaryotic organelle that consists of a filiform extrusion of the cell surface. Each cilium is bounded by an extrusion of the cytoplasmic membrane, and contains a regular longitudinal array of microtubules, anchored basally in a centriole. |
| negative regulation of dendritic spine development | Any process that decreases the rate, frequency, or extent of dendritic spine development, the process whose specific outcome is the progression of the dendritic spine over time, from its formation to the mature structure. |
| positive regulation of membrane tubulation | Any process that activates or increases the frequency, rate or extent of membrane tubulation. |
| protein localization to cilium | A process in which a protein is transported to, or maintained in, a location within a cilium. |
| regulation of postsynapse organization | Any process that modulates the physical form of a postsynapse. |
15 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| A5PK26 | ACAP1 | Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1 | Bos taurus (Bovine) | SS |
| O97902 | ASAP1 | Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 | Bos taurus (Bovine) | SS |
| A1Z7A6 | Asap | ArfGAP with SH3 domain, ANK repeat and PH domain-containing protein | Drosophila melanogaster (Fruit fly) | SS |
| Q15027 | ACAP1 | Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1 | Homo sapiens (Human) | EV |
| Q15057 | ACAP2 | Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2 | Homo sapiens (Human) | PR |
| O43150 | ASAP2 | Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2 | Homo sapiens (Human) | SS |
| Q8TDY4 | ASAP3 | Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 3 | Homo sapiens (Human) | SS |
| Q9ULH1 | ASAP1 | Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 | Homo sapiens (Human) | EV |
| Q8K2H4 | Acap1 | Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1 | Mus musculus (Mouse) | SS |
| Q6ZQK5 | Acap2 | Arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 2 | Mus musculus (Mouse) | PR |
| Q7SIG6 | Asap2 | Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 2 | Mus musculus (Mouse) | SS |
| Q5U464 | Asap3 | Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 3 | Mus musculus (Mouse) | SS |
| Q1AAU6 | Asap1 | Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 | Rattus norvegicus (Rat) | SS |
| Q9C6C3 | AGD2 | ADP-ribosylation factor GTPase-activating protein AGD2 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| Q9SMX5 | AGD4 | ADP-ribosylation factor GTPase-activating protein AGD4 | Arabidopsis thaliana (Mouse-ear cress) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MRSSASRLSS | FSSRDSLWNR | MPDQISVSEF | IAETTEDYNS | PTTSSFTTRL | HNCRNTVTLL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EEALDQDRTA | LQKVKKSVKA | IYNSGQDHVQ | NEENYAQVLD | KFGSNFLSRD | NPDLGTAFVK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| FSTLTKELST | LLKNLLQGLS | HNVIFTLDSL | LKGDLKGVKG | DLKKPFDKAW | KDYETKFTKI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EKEKREHAKQ | HGMIRTEITG | AEIAEEMEKE | RRLFQLQMCE | YLIKVNEIKT | KKGVDLLQNL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| IKYYHAQCNF | FQDGLKTADK | LKQYIEKLAA | DLYNIKQTQD | EEKKQLTALR | DLIKSSLQLD |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PKEVGGLYVA | SRANSSRRDS | QSRQGGYSMH | QLQGNKEYGS | EKKGFLLKKS | DGIRKVWQRR |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KCAVKNGILT | ISHATSNRQP | AKLNLLTCQV | KPNAEDKKSF | DLISHNRTYH | FQAEDEQDYI |
| 430 | 440 | 450 | 460 | 470 | 480 |
| AWISVLTNSK | EEALTMAFRG | EQSTGENSLE | DLTKAIIEDV | QRLPGNDICC | DCGSSEPTWL |
| 490 | 500 | 510 | 520 | 530 | 540 |
| STNLGILTCI | ECSGIHREMG | VHISRIQSLE | LDKLGTSELL | LAKNVGNNSF | NDIMEANLPS |
| 550 | 560 | 570 | 580 | 590 | 600 |
| PSPKPTPSSD | MTVRKEYITA | KYVDHRFSRK | TCASSSAKLN | ELLEAIKSRD | LLALIQVYAE |
| 610 | 620 | 630 | 640 | 650 | 660 |
| GVELMEPLLE | PGQELGETAL | HLAVRTADQT | SLHLVDFLVQ | NCGNLDKQTS | VGNTVLHYCS |
| 670 | 680 | 690 | 700 | 710 | 720 |
| MYGKPECLKL | LLRSKPTVDI | VNQNGETALD | IAKRLKATQC | EDLLSQAKSG | KFNPHVHVEY |
| 730 | 740 | 750 | 760 | 770 | 780 |
| EWNLRQDEMD | ESDDDLDDKP | SPIKKERSPR | PQSFCHSSSI | SPQDKLALPG | FSTPRDKQRL |
| 790 | 800 | 810 | 820 | 830 | 840 |
| SYGAFTNQIF | ASTSTDLPTS | PTSEAPPLPP | RNAGKGPTGP | PSTLPLGTQT | SSGSSTLSKK |
| 850 | 860 | 870 | 880 | 890 | 900 |
| RPPPPPPGHK | RTLSDPPSPL | PHGPPNKGAI | PWGNDVGPLS | SSKTANKFEG | LSQQASTSSA |
| 910 | 920 | 930 | 940 | 950 | 960 |
| KTALGPRVLP | KLPQKVALRK | TETSHHLSLD | RTNIPPETFQ | KSSQLTELPQ | KPPLGELPPK |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| PVELAPKPQV | GELPPKPGEL | PPKPQLGDLP | PKPQLSDLPP | KPQMKDLPPK | PQLGDLLAKS |
| 1030 | 1040 | 1050 | 1060 | 1070 | 1080 |
| QAGDVSAKVQ | PPSEVTQRSH | TGDLSPNVQS | RDAIQKQASE | DSNDLTPTLP | ETPVPLPRKI |
| 1090 | 1100 | 1110 | 1120 | 1130 | 1140 |
| NTGKNKVRRV | KTIYDCQADN | DDELTFIEGE | VIIVTGEEDQ | EWWIGHIEGQ | PERKGVFPVS |
| FVHILSD |