Q5U464
SS
Gene name |
Asap3 (Ddefl1) |
Protein name |
Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 3 |
Names |
Development and differentiation-enhancing factor-like 1 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:230837 |
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 |
304-391 (PH domain);425-547 (Arf GAP domain) |
Relief mechanism |
Partner binding |
Assay |
|
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q5U464
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5U464-F1 | Predicted | AlphaFoldDB |
52 variants for Q5U464
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3388720294 | 41 | R>W | No | EVA | |
| rs3388727786 | 52 | L>I | No | EVA | |
| rs3388710124 | 54 | R>K | No | EVA | |
| rs3388710097 | 86 | S>N | No | EVA | |
| rs3388718236 | 87 | H>D | No | EVA | |
| rs3388724621 | 107 | R>* | No | EVA | |
| rs3388722527 | 108 | E>K | No | EVA | |
| rs3388718189 | 129 | D>E | No | EVA | |
| rs3388715787 | 139 | G>R | No | EVA | |
| rs3388720678 | 211 | F>I | No | EVA | |
| rs3388722598 | 215 | L>I | No | EVA | |
| rs3388724565 | 300 | Q>* | No | EVA | |
| rs3388710108 | 352 | Q>H | No | EVA | |
| rs3388722604 | 353 | V>M | No | EVA | |
| rs27638036 | 439 | R>H | No | EVA | |
| rs3388717063 | 440 | C>W | No | EVA | |
| rs3388720292 | 444 | G>E | No | EVA | |
| rs3388715778 | 481 | T>S | No | EVA | |
| rs3394953414 | 483 | D>G | No | EVA | |
| rs3394881835 | 488 | S>* | No | EVA | |
| rs3388724573 | 490 | L>P | No | EVA | |
| rs3543084256 | 513 | G>S | No | EVA | |
| rs3388706628 | 518 | S>F | No | EVA | |
| rs3388714230 | 527 | R>K | No | EVA | |
| rs3388727753 | 543 | S>P | No | EVA | |
| rs3388710158 | 547 | P>S | No | EVA | |
| rs3388722091 | 618 | A>V | No | EVA | |
| rs3388717054 | 653 | A>D | No | EVA | |
| rs3395049859 | 683 | F>C | No | EVA | |
| rs3388717018 | 691 | W>* | No | EVA | |
| rs3388724611 | 692 | G>E | No | EVA | |
| rs3388718179 | 720 | C>* | No | EVA | |
| rs32650437 | 724 | V>G | No | EVA | |
| rs27638012 | 744 | T>A | No | EVA | |
| rs3388717064 | 751 | S>R | No | EVA | |
| rs3388714238 | 753 | P>T | No | EVA | |
| rs3388714200 | 756 | P>T | No | EVA | |
| rs3388720689 | 779 | L>F | No | EVA | |
| rs3412959477 | 783 | R>K | No | EVA | |
| rs3388710172 | 787 | P>S | No | EVA | |
| rs3388706673 | 791 | E>V | No | EVA | |
| rs3388723442 | 792 | N>I | No | EVA | |
| rs3388717076 | 816 | P>A | No | EVA | |
| rs3388717076 | 816 | P>S | No | EVA | |
| rs27637997 | 826 | S>P | No | EVA | |
| rs27637996 | 828 | S>G | No | EVA | |
| rs212351553 | 840 | S>P | No | EVA | |
| rs3388720706 | 846 | P>H | No | EVA | |
| rs3388722550 | 878 | R>S | No | EVA | |
| rs3388720363 | 881 | P>L | No | EVA | |
| rs3388714178 | 888 | D>E | No | EVA | |
| rs3388724453 | 894 | V>F | No | EVA |
No associated diseases with Q5U464
5 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. |
| 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). |
| intracellular membrane-bounded organelle | Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane. |
| nucleoplasm | That part of the nuclear content other than the chromosomes or the nucleolus. |
| ruffle | Projection at the leading edge of a crawling cell; the protrusions are supported by a microfilament meshwork. |
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. |
| metal ion binding | Binding to a metal ion. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| cell migration | The controlled self-propelled movement of a cell from one site to a destination guided by molecular cues. |
| positive regulation of GTPase activity | Any process that activates or increases the activity of a GTPase. |
| regulation of stress fiber assembly | Any process that modulates the frequency, rate or extent of the assembly of a stress fiber, a bundle of microfilaments and other proteins found in fibroblasts. |
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 |
| Q9ULH1 | ASAP1 | Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 | Homo sapiens (Human) | EV |
| 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 |
| 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 |
| Q9QWY8 | Asap1 | Arf-GAP with SH3 domain, ANK repeat and PH domain-containing protein 1 | 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 |
| MPEQLSVAEF | LAVTAEDLSS | PAGAAAFAAK | MPRCRGAALA | REEALEGDQA | ILQRIKKAVR |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AIHSSGLGHV | ETEEHYREAV | EALGNSHLSQ | NSHELSTGFL | NLAVFTREVA | ALFKNLVQNL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NNIVSFPLDS | LMKGHLRDGR | HDSKKHLEKA | WKDYESKVAK | LEKERDRARF | PGGSHGVMSQ |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DTQRERRVFQ | LHMCEYLVKA | GESQVKQGPD | FLQSLIKFFH | AQHNFFQDGW | KAAQSLSPFI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DKLAASVHGL | RQAQEEELHK | LTQLRDSLRG | MLHLESREDH | PNRKNSGGGY | SIHQHQGNKQ |
| 310 | 320 | 330 | 340 | 350 | 360 |
| FGTEKVGFLY | KKSDGIRRVW | QKRKCGVKYG | CLTISHSMIN | RPPVKLPLLT | CQVRPNPEEK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| RCFDLVTHNR | TYHFHAEDEQ | ECEAWVSVLQ | NSKDEALSNA | FHGEPSGGQW | SWGTRLDTEP |
| 430 | 440 | 450 | 460 | 470 | 480 |
| HDLTNMLVAE | VKSRPGNDRC | CDCGAADPTW | LSTNLGVLTC | IQCSGVHREL | GVRFSRIQSL |
| 490 | 500 | 510 | 520 | 530 | 540 |
| TLDLLGPSEL | LLALNIGNSH | FNEVMEAHLP | SHGSPKPSAE | SDMSSRRNYI | VAKYVEHKFA |
| 550 | 560 | 570 | 580 | 590 | 600 |
| RHSTPDPQKL | RTAICSRDLL | SVLEAFANGQ | DFGQLLPGPD | GQAPGELALH | LAIRVASHAS |
| 610 | 620 | 630 | 640 | 650 | 660 |
| LPIVDFLIQN | GGHLDAKAAD | GNTALHCAAL | HGQLDCLKLL | LRGRAPVGAV | NDAGETALDI |
| 670 | 680 | 690 | 700 | 710 | 720 |
| ARNRQHKECE | ELLEQAQAGT | LAFPLHMDYH | WGHSMEHGFD | SEEEEEEEKH | CPSKPPAQAC |
| 730 | 740 | 750 | 760 | 770 | 780 |
| WGSVRLDISN | KTYETVATPG | PATTQSQSED | SPPPLPIKNS | SRTIVLGRAG | HCSGDRSDLP |
| 790 | 800 | 810 | 820 | 830 | 840 |
| SLRSESPEAL | ENRSSPASSS | SSLTSSVEPG | GLSQAPSSPE | EGLQESASIS | RPGLASGTTS |
| 850 | 860 | 870 | 880 | 890 | 900 |
| AEVYLPVKFS | SESTRSYRRG | GRSLEDSPSA | RQPLCSRRHI | PVGLVEGDGS | KIGVLPDSLQ |
| LLHD |