2889:
610:
155:, signaling GTPases act as transducers to regulate the activity of effector proteins. This inactive-active switch is due to conformational changes in the protein distinguishing these two forms, particularly of the "switch" regions that in the active state are able to make protein-protein contacts with partner proteins that alter the function of these effectors.
441:
complex into its component G protein alpha and beta-gamma subunit components. While these activated G protein subunits are now free to activate their effectors, the active receptor is likewise free to activate additional G proteins – this allows catalytic activation and amplification where one receptor may activate many G proteins.
534:
GTPases. Small GTPases generally serve as molecular switches and signal transducers for a wide variety of cellular signaling events, often involving membranes, vesicles or cytoskeleton. According to their primary amino acid sequences and biochemical properties, the many Ras superfamily small GTPases
440:
complex). Upon receptor activation, the activated receptor intracellular domain acts as GEF to release GDP from the G protein complex and to promote binding of GTP in its place. The GTP-bound complex undergoes an activating conformation shift that dissociates it from the receptor and also breaks the
595:
Much of the SIMIBI class of GTPases is activated by dimerization. Named after the signal recognition particle (SRP), MinD, and BioD, the class is involved in protein localization, chromosome partitioning, and membrane transport. Several members of this class, including MinD and Get3, has shifted in
215:
or GEFs. The nucleotide-free GTPase protein quickly rebinds GTP, which is in far excess in healthy cells over GDP, allowing the GTPase to enter the active conformation state and promote its effects on the cell. For many GTPases, activation of GEFs is the primary control mechanism in the stimulation
525:
function as monomers and have a molecular weight of about 21 kilodaltons that consists primarily of the GTPase domain. They are also called small or monomeric guanine nucleotide-binding regulatory proteins, small or monomeric GTP-binding proteins, or small or monomeric G-proteins, and because they
197:
GTPase activity serves as the shutoff mechanism for the signaling roles of GTPases by returning the active, GTP-bound protein to the inactive, GDP-bound state. Most "GTPases" have functional GTPase activity, allowing them to remain active (that is, bound to GTP) only for a short time before
275:
versus other nucleotides is imparted by the base-recognition motif, which has the consensus sequence KXD. The following classification is based on shared features; some examples have mutations in the base-recognition motif that shift their substrate specificity, most commonly to ATP.
216:
of the GTPase signaling functions, although GAPs also play an important role. For heterotrimeric G proteins and many small GTP-binding proteins, GEF activity is stimulated by cell surface receptors in response to signals outside the cell (for heterotrimeric G proteins, the
202:
or GAPs to accelerate their GTPase activity. This further limits the active lifetime of signaling GTPases. Some GTPases have little to no intrinsic GTPase activity, and are entirely dependent on GAP proteins for deactivation (such as the
210:
To become activated, GTPases must bind to GTP. Since mechanisms to convert bound GDP directly into GTP are unknown, the inactive GTPases are induced to release bound GDP by the action of distinct regulatory proteins called
417:. When activated, a heterotrimeric G protein dissociates into activated, GTP-bound alpha subunit and separate beta-gamma subunit, each of which can perform distinct signaling roles. The α and γ subunit are modified by
444:
G protein signaling is terminated by hydrolysis of bound GTP to bound GDP. This can occur through the intrinsic GTPase activity of the α subunit, or be accelerated by separate regulatory proteins that act as
262:
Mutations (such as those that reduce the intrinsic GTP hydrolysis rate) can lock the GTPase in the active state, and such mutations in the small GTPase Ras are particularly common in some forms of cancer.
496:
are likewise composed of many members, increasing heterotrimer structural and functional diversity. Among the target molecules of the specific G proteins are the second messenger-generating enzymes
284:
The TRAFAC class of G domain proteins is named after the prototypical member, the translation factor G proteins. They play roles in translation, signal transduction, and cell motility.
413:. The alpha subunits contain the GTP binding/GTPase domain flanked by long regulatory regions, while the beta and gamma subunits form a stable dimeric complex referred to as the
1685:
163:
Hydrolysis of GTP bound to an (active) G domain-GTPase leads to deactivation of the signaling/timer function of the enzyme. The hydrolysis of the third (γ)
1716:
664:
and related structural proteins also bind and hydrolyze GTP as part of their function to form intracellular tubules, these proteins utilize a distinct
1131:
Parmeggiani, A; Sander, G (1981). "Properties and regulation of the GTPase activities of elongation factors Tu and G, and of initiation factor 2".
555:. While many small GTPases are activated by their GEFs in response to intracellular signals emanating from cell surface receptors (particularly
2550:
1003:
Sasaki, T; Takai, Y (1998). "The Rho Small G Protein Family-Rho GDI System as a
Temporal and Spatial Determinant for Cytoskeletal Control".
559:), regulatory GEFs for many other small GTPases are activated in response to intrinsic cell signals, not cell surface (external) signals.
224:
151:
GTPases are active when bound to GTP and inactive when bound to GDP. In the generalized receptor-transducer-effector signaling model of
1682:
2409:
1974:
1964:
1918:
1993:
1709:
1939:
347:
237:
Inhibition of GDP dissociation by guanine nucleotide dissociation inhibitors (GDIs) slows down accumulation of active GTPase.
1908:
567:
This class is defined by loss of two beta-strands and additional N-terminal strands. Both namesakes of this superfamily,
453:(RGS) family). The speed of the hydrolysis reaction works as an internal clock limiting the length of the signal. Once G
1702:
212:
220:
are themselves GEFs, while for receptor-activated small GTPases their GEFs are distinct from cell surface receptors).
198:
deactivating themselves by converting bound GTP to bound GDP. However, many GTPases also use accessory proteins named
2608:
1176:"Roles of elusive translational GTPases come to light and inform on the process of ribosome biogenesis in bacteria"
450:
2499:
727:
Stouten, PF; Sander, C; Wittinghofer, A; Valencia, A (1993). "How does the switch II region of G-domains work?".
457:
is returned to being GDP bound, the two parts of the heterotrimer re-associate to the original, inactive state.
2494:
307:
2764:
2516:
964:"The protein cofactor necessary for ADP-ribosylation of Gs by cholera toxin is itself a GTP binding protein"
2909:
2564:
2086:
1881:
1809:
1805:
1782:
1742:
1038:
Murugan, AK; Grieco, M; Tsuchida, N (2019). "RAS Mutations in Human
Cancers: Roles in Precision Medicine".
207:
or ARF family of small GTP-binding proteins that are involved in vesicle-mediated transport within cells).
125:
1626:
Nogales E, Downing KH, Amos LA, Löwe J (June 1998). "Tubulin and FtsZ form a distinct family of GTPases".
311:
2486:
692:
649:
217:
2879:
425:
199:
74:
2865:
2852:
2839:
2826:
2813:
2800:
2787:
2749:
2545:
1984:
1755:
1729:
1283:"Genomic characterization of the human heterotrimeric G protein alpha, beta, and gamma subunit genes"
446:
432:. In unstimulated cells, heterotrimeric G proteins are assembled as the GDP bound, inactive trimer (G
184:
2759:
2713:
2656:
2100:
1795:
1760:
1733:
1676:
392:
387:
322:
binding due to the β-EI domain following the GTPase, the most well-known members of the family are
107:
2661:
2470:
2433:
1772:
1694:
548:
204:
621:
about FlhF, which is not involved in the SRP at all but has a similar structure to Ffh and FtsY.
2200:
1840:
697:
556:
33:
2682:
2601:
2330:
2238:
645:
540:
303:
168:
147:, and vesicle-mediated secretion and uptake, through GTPase control of vesicle coat assembly.
96:
41:
2754:
1541:
1450:
414:
315:
92:
8:
2718:
2535:
176:
70:
63:
GTPases function as molecular switches or timers in many fundamental cellular processes.
1545:
1454:
808:
623:
Please expand the section to include this information. Further details may exist on the
2651:
2116:
1651:
1603:
1576:
1474:
1423:
1251:
1224:
1200:
1175:
1156:
1063:
900:
887:
862:
45:
1335:
980:
963:
2914:
1790:
1643:
1608:
1557:
1514:
1466:
1415:
1380:
1339:
1304:
1256:
1205:
1148:
1113:
1067:
1055:
1020:
985:
944:
892:
812:
744:
740:
461:
234:
Acceleration of GDP dissociation by GEFs speeds up the accumulation of active GTPase.
140:
86:
1478:
1427:
1051:
904:
2697:
2692:
2666:
2594:
2180:
2126:
2108:
1655:
1635:
1598:
1588:
1549:
1506:
1458:
1407:
1370:
1331:
1294:
1246:
1236:
1195:
1187:
1160:
1140:
1105:
1047:
1012:
975:
934:
882:
874:
804:
736:
497:
484:
protein families contains multiple members, such that the mammals have 16 distinct
429:
52:
1672:
1510:
1281:
Hurowitz EH, Melnyk JM, Chen YJ, Kouros-Mehr H, Simon MI, Shizuya H (April 2000).
2744:
2728:
2641:
2527:
2416:
2230:
1930:
1750:
1689:
544:
531:
501:
410:
397:
367:
1398:
Pierce, KL; Premont, RT; Lefkowitz, RJ (2002). "Seven-transmembrane receptors".
2893:
2782:
2723:
1850:
1593:
675:
from a superclass other than the G-domain-containing one. Examples include the
665:
339:
187:) via a pentacoordinate transition state and is dependent on the presence of a
152:
144:
119:
2903:
2687:
2646:
2394:
2004:
1299:
1282:
536:
527:
421:
to increase their association with the inner leaflet of the plasma membrane.
133:
115:
1553:
1462:
795:
Gilman, AG (1987). "G proteins: transducers of receptor-generated signals".
2636:
2379:
2352:
2281:
2274:
2257:
2252:
2226:
1612:
1518:
1470:
1419:
1384:
1375:
1358:
1308:
1260:
1241:
1209:
1117:
1109:
1059:
1016:
939:
922:
676:
522:
517:
418:
359:
240:
Acceleration of GTP hydrolysis by GAPs reduces the amount of active GTPase.
1647:
1561:
1343:
1152:
1024:
989:
948:
896:
816:
748:
2860:
2795:
2631:
2475:
1091:
624:
552:
505:
111:
1639:
1532:
Hall, A (1990). "The cellular functions of small GTP-binding proteins".
526:
have significant homology with the first-identified such protein, named
2460:
2149:
1497:
Takai, Y; Sasaki, T; Matozaki, T (2001). "Small GTP-binding proteins".
1144:
878:
297:
37:
30:
1191:
2834:
2808:
2166:
1725:
428:, coupling receptor activation to downstream signaling effectors and
293:
188:
164:
82:
23:
1094:"Classification and evolution of P-loop GTPases and related ATPases"
1093:
2888:
1411:
535:
are further divided into five subfamilies with distinct functions:
464:
of the α unit and by their functional targets into four families: G
319:
100:
1724:
259:
that cannot be hydrolyzed can lock the GTPase in its active state.
2571:
2540:
2318:
2313:
2072:
2062:
2037:
2032:
1767:
726:
702:
661:
584:
572:
272:
129:
1577:"ATPase and GTPase Tangos Drive Intracellular Protein Transport"
1225:"Phylogenetic distribution of translational GTPases in bacteria"
609:
395:
complexes are composed of three distinct protein subunits named
2847:
2617:
2448:
2067:
2057:
2027:
2022:
2017:
2012:
1969:
1959:
1954:
1949:
1944:
1913:
1901:
1896:
1891:
1886:
1874:
1869:
1864:
1813:
672:
568:
73:
in response to activation of cell surface receptors, including
48:
26:
2821:
2504:
2443:
2426:
2421:
2269:
2247:
2213:
2208:
2193:
2171:
2159:
2154:
2144:
2139:
2134:
1859:
1835:
1441:
Neves, SR; Ram, PT; Iyengar, R (2002). "G protein pathways".
1322:
Clapham DE, Neer EJ (1997). "G protein beta gamma subunits".
1280:
1092:
Leipe D.D.; Wolf Y.I.; Koonin E.V. & Aravind, L. (2002).
680:
668:
that is unrelated to the G domain used by signaling GTPases.
363:
331:
327:
323:
230:
The amount of active GTPase can be changed in several ways:
78:
2509:
2465:
2453:
2438:
2404:
2399:
2384:
2367:
2362:
2357:
2345:
2340:
2335:
2325:
2301:
2296:
2291:
2286:
2188:
343:
335:
44:. The GTP binding and hydrolysis takes place in the highly
2586:
1223:
Margus, Tõnu; Remm, Maido; Tenson, Tanel (December 2007).
863:"Nobel Lecture: Signal transduction: Evolution of an idea"
373:
The superfamily also includes the Bms1 family from yeast.
2559:
2555:
191:
679:
proteins of its own superclass and McrB protein of the
1625:
1397:
227:
or GDIs that stabilize the inactive, GDP-bound state.
2877:
1037:
424:
Heterotrimeric G proteins act as the transducers of
223:
Some GTPases also bind to accessory proteins called
1496:
1359:"Regulation of G proteins by covalent modification"
1005:
671:There are also GTP-hydrolyzing proteins that use a
460:The heterotrimeric G proteins can be classified by
1130:
287:
2901:
1222:
923:"Mammalian RGS proteins: barbarians at the gate"
354:(bacterial selenocysteinyl-tRNA EF-Tu paralog),
1492:
1490:
1488:
1440:
1276:
1274:
1272:
1270:
1087:
1085:
1083:
1081:
1079:
1077:
856:
854:
852:
850:
848:
846:
790:
788:
786:
784:
782:
780:
778:
306:factor family GTPases play important roles in
271:In most GTPases, the specificity for the base
2602:
1710:
1173:
916:
914:
844:
842:
840:
838:
836:
834:
832:
830:
828:
826:
776:
774:
772:
770:
768:
766:
764:
762:
760:
758:
722:
720:
718:
562:
1568:
1485:
1434:
1391:
1350:
1324:Annual Review of Pharmacology and Toxicology
1267:
1167:
920:
587:as a prototype for large monomeric GTPases.
381:
1619:
1525:
1356:
1321:
1315:
1074:
1031:
1002:
2609:
2595:
1717:
1703:
1124:
996:
961:
955:
911:
823:
755:
715:
225:guanine nucleotide dissociation inhibitors
1675:at the U.S. National Library of Medicine
1602:
1592:
1374:
1298:
1250:
1240:
1199:
979:
938:
886:
596:substrate specificity to become ATPases.
362:resistance by ribosomal protection), and
599:
860:
376:
2902:
794:
2590:
1698:
1400:Nature Reviews Molecular Cell Biology
370:protein similar to release factors).
1574:
1531:
603:
1133:Molecular and Cellular Biochemistry
809:10.1146/annurev.bi.56.070187.003151
266:
213:guanine nucleotide exchange factors
13:
66:Examples of these roles include:
14:
2926:
1666:
1336:10.1146/annurev.pharmtox.37.1.167
648:factors and the role of GTP, see
2887:
655:
608:
578:
511:
451:Regulator of G protein signaling
1216:
1174:Gibbs, MR; Fredrick, K (2018).
1052:10.1016/j.semcancer.2019.06.007
968:Journal of Biological Chemistry
927:Journal of Biological Chemistry
921:Berman, DM; Gilman, AG (1998).
590:
530:, they are also referred to as
449:(GAPs), such as members of the
279:
1581:Trends in Biochemical Sciences
1357:Chen, CA; Manning, DR (2001).
288:Translation factor superfamily
1:
1511:10.1152/physrev.2001.81.1.153
981:10.1016/S0021-9258(19)57489-0
962:Kahn, RA; Gilman, AG (1986).
797:Annual Review of Biochemistry
708:
741:10.1016/0014-5793(93)81644-f
318:. Sharing a similar mode of
158:
58:
34:guanosine triphosphate (GTP)
7:
2616:
2487:Protein-synthesizing GTPase
693:G protein-coupled receptors
686:
650:signal recognition particle
575:, have shifted to use ATP.
426:G protein-coupled receptors
218:G protein-coupled receptors
42:guanosine diphosphate (GDP)
10:
2931:
1594:10.1016/j.tibs.2016.08.012
1575:Shan, SO (December 2016).
1040:Seminars in Cancer Biology
563:Myosin-kinesin superfamily
515:
447:GTPase-activating proteins
385:
291:
200:GTPase-activating proteins
2773:
2765:Michaelis–Menten kinetics
2737:
2706:
2675:
2624:
2546:Guanylate-binding protein
2525:
2484:
2224:
2098:
2085:
2050:
2002:
1983:
1929:
1849:
1828:
1821:
1804:
1781:
1741:
1730:acid anhydride hydrolases
382:Heterotrimeric G proteins
185:nucleophilic substitution
2657:Diffusion-limited enzyme
2101:Heterotrimeric G protein
1796:Phosphoadenylylsulfatase
1677:Medical Subject Headings
393:Heterotrimeric G protein
388:Heterotrimeric G protein
342:. Other members include
77:such as those mediating
55:common to many GTPases.
1773:Thiamine-triphosphatase
1554:10.1126/science.2116664
1463:10.1126/science.1071550
557:growth factor receptors
480:family. Each of these G
205:ADP-ribosylation factor
75:transmembrane receptors
1376:10.1038/sj.onc.1204185
1300:10.1093/dnares/7.2.111
1242:10.1186/1471-2164-8-15
1180:Molecular Microbiology
1110:10.1006/jmbi.2001.5378
1017:10.1006/bbrc.1998.8253
940:10.1074/jbc.273.3.1269
698:Growth factor receptor
619:is missing information
298:EF-Tu § Evolution
22:are a large family of
2750:Eadie–Hofstee diagram
2683:Allosteric regulation
2528:Polymerization motors
2239:Rho family of GTPases
1499:Physiological Reviews
600:Translocation factors
504:, as well as various
488:-subunit genes. The G
294:EF-G § Evolution
169:guanosine diphosphate
2760:Lineweaver–Burk plot
644:For a discussion of
377:Ras-like superfamily
316:protein biosynthesis
93:Protein biosynthesis
2910:Signal transduction
2536:dynamin superfamily
1683:MBInfo - RhoGTPases
1640:10.1038/nsb0698-451
1546:1990Sci...249..635H
1455:2002Sci...296.1636N
1449:(5573): 1636–1639.
861:Rodbell, M (1995).
314:and termination of
302:Multiple classical
177:inorganic phosphate
106:Regulation of cell
71:Signal transduction
2719:Enzyme superfamily
2652:Enzyme promiscuity
1688:2013-03-31 at the
1145:10.1007/BF02357085
879:10.1007/bf01207453
867:Bioscience Reports
543:("Ras-homology"),
415:beta-gamma complex
2875:
2874:
2584:
2583:
2580:
2579:
2081:
2080:
2046:
2045:
1791:Adenylylsulfatase
1628:Nat. Struct. Biol
1587:(12): 1050–1060.
1540:(4969): 635–640.
1369:(13): 1643–1652.
1192:10.1111/mmi.13895
974:(17): 7906–7911.
642:
641:
462:sequence homology
430:second messengers
253:β,γ-methylene-GTP
183:2 mechanism (see
179:, occurs by the S
167:of GTP to create
29:that bind to the
2922:
2892:
2891:
2883:
2755:Hanes–Woolf plot
2698:Enzyme activator
2693:Enzyme inhibitor
2667:Enzyme catalysis
2611:
2604:
2597:
2588:
2587:
2096:
2095:
1826:
1825:
1819:
1818:
1719:
1712:
1705:
1696:
1695:
1660:
1659:
1623:
1617:
1616:
1606:
1596:
1572:
1566:
1565:
1529:
1523:
1522:
1494:
1483:
1482:
1438:
1432:
1431:
1395:
1389:
1388:
1378:
1354:
1348:
1347:
1319:
1313:
1312:
1302:
1278:
1265:
1264:
1254:
1244:
1220:
1214:
1213:
1203:
1171:
1165:
1164:
1128:
1122:
1121:
1089:
1072:
1071:
1035:
1029:
1028:
1000:
994:
993:
983:
959:
953:
952:
942:
933:(3): 1269–1272.
918:
909:
908:
890:
858:
821:
820:
792:
753:
752:
724:
637:
634:
628:
612:
604:
498:adenylyl cyclase
267:G domain GTPases
16:Class of enzymes
2930:
2929:
2925:
2924:
2923:
2921:
2920:
2919:
2900:
2899:
2898:
2886:
2878:
2876:
2871:
2783:Oxidoreductases
2769:
2745:Enzyme kinetics
2733:
2729:List of enzymes
2702:
2671:
2642:Catalytic triad
2620:
2615:
2585:
2576:
2521:
2480:
2231:Ras superfamily
2220:
2204:
2184:
2130:
2120:
2112:
2077:
2042:
1998:
1979:
1925:
1882:Plasma membrane
1845:
1800:
1777:
1751:Pyrophosphatase
1737:
1723:
1690:Wayback Machine
1669:
1664:
1663:
1624:
1620:
1573:
1569:
1530:
1526:
1495:
1486:
1439:
1435:
1396:
1392:
1355:
1351:
1320:
1316:
1279:
1268:
1221:
1217:
1172:
1168:
1129:
1125:
1090:
1075:
1036:
1032:
1001:
997:
960:
956:
919:
912:
859:
824:
793:
756:
725:
716:
711:
689:
658:
638:
632:
629:
622:
613:
602:
593:
581:
565:
532:Ras superfamily
520:
514:
502:phospholipase C
495:
491:
487:
483:
479:
475:
471:
467:
456:
439:
435:
390:
384:
379:
368:ribosome rescue
340:release factors
300:
290:
282:
269:
182:
174:
161:
108:differentiation
61:
17:
12:
11:
5:
2928:
2918:
2917:
2912:
2897:
2896:
2873:
2872:
2870:
2869:
2856:
2843:
2830:
2817:
2804:
2791:
2777:
2775:
2771:
2770:
2768:
2767:
2762:
2757:
2752:
2747:
2741:
2739:
2735:
2734:
2732:
2731:
2726:
2721:
2716:
2710:
2708:
2707:Classification
2704:
2703:
2701:
2700:
2695:
2690:
2685:
2679:
2677:
2673:
2672:
2670:
2669:
2664:
2659:
2654:
2649:
2644:
2639:
2634:
2628:
2626:
2622:
2621:
2614:
2613:
2606:
2599:
2591:
2582:
2581:
2578:
2577:
2575:
2574:
2569:
2568:
2567:
2562:
2553:
2548:
2543:
2532:
2530:
2523:
2522:
2520:
2519:
2514:
2513:
2512:
2507:
2502:
2491:
2489:
2482:
2481:
2479:
2478:
2473:
2468:
2463:
2458:
2457:
2456:
2451:
2446:
2441:
2431:
2430:
2429:
2424:
2414:
2413:
2412:
2407:
2402:
2390:
2389:
2388:
2387:
2382:
2372:
2371:
2370:
2365:
2360:
2350:
2349:
2348:
2343:
2338:
2328:
2323:
2322:
2321:
2316:
2306:
2305:
2304:
2299:
2294:
2289:
2279:
2278:
2277:
2272:
2262:
2261:
2260:
2255:
2250:
2235:
2233:
2222:
2221:
2219:
2218:
2217:
2216:
2211:
2202:
2198:
2197:
2196:
2191:
2182:
2178:
2177:
2176:
2175:
2174:
2164:
2163:
2162:
2157:
2147:
2142:
2137:
2128:
2124:
2123:
2122:
2118:
2110:
2105:
2103:
2093:
2083:
2082:
2079:
2078:
2076:
2075:
2070:
2065:
2060:
2054:
2052:
2048:
2047:
2044:
2043:
2041:
2040:
2035:
2030:
2025:
2020:
2015:
2009:
2007:
2000:
1999:
1997:
1996:
1990:
1988:
1981:
1980:
1978:
1977:
1972:
1967:
1962:
1957:
1952:
1947:
1942:
1936:
1934:
1927:
1926:
1924:
1923:
1922:
1921:
1916:
1906:
1905:
1904:
1899:
1894:
1889:
1879:
1878:
1877:
1872:
1867:
1856:
1854:
1847:
1846:
1844:
1843:
1838:
1832:
1830:
1829:Cu++ (3.6.3.4)
1823:
1816:
1802:
1801:
1799:
1798:
1793:
1787:
1785:
1779:
1778:
1776:
1775:
1770:
1765:
1764:
1763:
1758:
1747:
1745:
1739:
1738:
1722:
1721:
1714:
1707:
1699:
1693:
1692:
1680:
1668:
1667:External links
1665:
1662:
1661:
1618:
1567:
1524:
1505:(1): 153–208.
1484:
1433:
1412:10.1038/nrm908
1406:(9): 639–650.
1390:
1349:
1314:
1266:
1215:
1186:(4): 445–454.
1166:
1139:(3): 129–158.
1123:
1073:
1030:
1011:(3): 641–645.
995:
954:
910:
873:(3): 117–133.
822:
754:
713:
712:
710:
707:
706:
705:
700:
695:
688:
685:
666:tubulin domain
657:
654:
640:
639:
616:
614:
607:
601:
598:
592:
589:
580:
577:
564:
561:
516:Main article:
513:
510:
493:
489:
485:
481:
477:
473:
469:
465:
454:
437:
433:
386:Main article:
383:
380:
378:
375:
338:, and class 2
289:
286:
281:
278:
268:
265:
264:
263:
260:
241:
238:
235:
180:
172:
160:
157:
153:Martin Rodbell
149:
148:
137:
123:
104:
90:
60:
57:
53:protein domain
51:"G domain", a
15:
9:
6:
4:
3:
2:
2927:
2916:
2913:
2911:
2908:
2907:
2905:
2895:
2890:
2885:
2884:
2881:
2867:
2863:
2862:
2857:
2854:
2850:
2849:
2844:
2841:
2837:
2836:
2831:
2828:
2824:
2823:
2818:
2815:
2811:
2810:
2805:
2802:
2798:
2797:
2792:
2789:
2785:
2784:
2779:
2778:
2776:
2772:
2766:
2763:
2761:
2758:
2756:
2753:
2751:
2748:
2746:
2743:
2742:
2740:
2736:
2730:
2727:
2725:
2724:Enzyme family
2722:
2720:
2717:
2715:
2712:
2711:
2709:
2705:
2699:
2696:
2694:
2691:
2689:
2688:Cooperativity
2686:
2684:
2681:
2680:
2678:
2674:
2668:
2665:
2663:
2660:
2658:
2655:
2653:
2650:
2648:
2647:Oxyanion hole
2645:
2643:
2640:
2638:
2635:
2633:
2630:
2629:
2627:
2623:
2619:
2612:
2607:
2605:
2600:
2598:
2593:
2592:
2589:
2573:
2570:
2566:
2563:
2561:
2557:
2554:
2552:
2549:
2547:
2544:
2542:
2539:
2538:
2537:
2534:
2533:
2531:
2529:
2524:
2518:
2515:
2511:
2508:
2506:
2503:
2501:
2498:
2497:
2496:
2493:
2492:
2490:
2488:
2483:
2477:
2474:
2472:
2469:
2467:
2464:
2462:
2459:
2455:
2452:
2450:
2447:
2445:
2442:
2440:
2437:
2436:
2435:
2432:
2428:
2425:
2423:
2420:
2419:
2418:
2415:
2411:
2408:
2406:
2403:
2401:
2398:
2397:
2396:
2392:
2391:
2386:
2383:
2381:
2378:
2377:
2376:
2373:
2369:
2366:
2364:
2361:
2359:
2356:
2355:
2354:
2351:
2347:
2344:
2342:
2339:
2337:
2334:
2333:
2332:
2329:
2327:
2324:
2320:
2317:
2315:
2312:
2311:
2310:
2307:
2303:
2300:
2298:
2295:
2293:
2290:
2288:
2285:
2284:
2283:
2280:
2276:
2273:
2271:
2268:
2267:
2266:
2263:
2259:
2256:
2254:
2251:
2249:
2246:
2245:
2244:
2240:
2237:
2236:
2234:
2232:
2228:
2223:
2215:
2212:
2210:
2207:
2206:
2205:
2199:
2195:
2192:
2190:
2187:
2186:
2185:
2179:
2173:
2170:
2169:
2168:
2165:
2161:
2158:
2156:
2153:
2152:
2151:
2148:
2146:
2143:
2141:
2138:
2136:
2133:
2132:
2131:
2125:
2121:
2115:
2114:
2113:
2107:
2106:
2104:
2102:
2097:
2094:
2092:
2088:
2084:
2074:
2071:
2069:
2066:
2064:
2061:
2059:
2056:
2055:
2053:
2049:
2039:
2036:
2034:
2031:
2029:
2026:
2024:
2021:
2019:
2016:
2014:
2011:
2010:
2008:
2006:
2005:P-type ATPase
2001:
1995:
1992:
1991:
1989:
1986:
1982:
1976:
1973:
1971:
1968:
1966:
1963:
1961:
1958:
1956:
1953:
1951:
1948:
1946:
1943:
1941:
1938:
1937:
1935:
1932:
1928:
1920:
1917:
1915:
1912:
1911:
1910:
1907:
1903:
1900:
1898:
1895:
1893:
1890:
1888:
1885:
1884:
1883:
1880:
1876:
1873:
1871:
1868:
1866:
1863:
1862:
1861:
1858:
1857:
1855:
1852:
1848:
1842:
1839:
1837:
1834:
1833:
1831:
1827:
1824:
1820:
1817:
1815:
1811:
1807:
1803:
1797:
1794:
1792:
1789:
1788:
1786:
1784:
1780:
1774:
1771:
1769:
1766:
1762:
1759:
1757:
1754:
1753:
1752:
1749:
1748:
1746:
1744:
1740:
1735:
1731:
1727:
1720:
1715:
1713:
1708:
1706:
1701:
1700:
1697:
1691:
1687:
1684:
1681:
1678:
1674:
1671:
1670:
1657:
1653:
1649:
1645:
1641:
1637:
1633:
1629:
1622:
1614:
1610:
1605:
1600:
1595:
1590:
1586:
1582:
1578:
1571:
1563:
1559:
1555:
1551:
1547:
1543:
1539:
1535:
1528:
1520:
1516:
1512:
1508:
1504:
1500:
1493:
1491:
1489:
1480:
1476:
1472:
1468:
1464:
1460:
1456:
1452:
1448:
1444:
1437:
1429:
1425:
1421:
1417:
1413:
1409:
1405:
1401:
1394:
1386:
1382:
1377:
1372:
1368:
1364:
1360:
1353:
1345:
1341:
1337:
1333:
1329:
1325:
1318:
1310:
1306:
1301:
1296:
1293:(2): 111–20.
1292:
1288:
1284:
1277:
1275:
1273:
1271:
1262:
1258:
1253:
1248:
1243:
1238:
1234:
1230:
1226:
1219:
1211:
1207:
1202:
1197:
1193:
1189:
1185:
1181:
1177:
1170:
1162:
1158:
1154:
1150:
1146:
1142:
1138:
1134:
1127:
1119:
1115:
1111:
1107:
1103:
1099:
1095:
1088:
1086:
1084:
1082:
1080:
1078:
1069:
1065:
1061:
1057:
1053:
1049:
1045:
1041:
1034:
1026:
1022:
1018:
1014:
1010:
1006:
999:
991:
987:
982:
977:
973:
969:
965:
958:
950:
946:
941:
936:
932:
928:
924:
917:
915:
906:
902:
898:
894:
889:
884:
880:
876:
872:
868:
864:
857:
855:
853:
851:
849:
847:
845:
843:
841:
839:
837:
835:
833:
831:
829:
827:
818:
814:
810:
806:
802:
798:
791:
789:
787:
785:
783:
781:
779:
777:
775:
773:
771:
769:
767:
765:
763:
761:
759:
750:
746:
742:
738:
734:
730:
723:
721:
719:
714:
704:
701:
699:
696:
694:
691:
690:
684:
682:
678:
674:
669:
667:
663:
656:Other GTPases
653:
651:
647:
646:Translocation
636:
626:
620:
617:This section
615:
611:
606:
605:
597:
588:
586:
579:Large GTPases
576:
574:
570:
560:
558:
554:
550:
546:
542:
538:
533:
529:
524:
523:Small GTPases
519:
512:Small GTPases
509:
507:
503:
499:
463:
458:
452:
448:
442:
431:
427:
422:
420:
419:lipid anchors
416:
412:
408:
404:
400:
399:
394:
389:
374:
371:
369:
365:
361:
357:
353:
349:
345:
341:
337:
333:
329:
325:
321:
317:
313:
309:
305:
299:
295:
285:
277:
274:
261:
258:
257:β,γ-imino-GTP
254:
250:
246:
245:GTP analogues
242:
239:
236:
233:
232:
231:
228:
226:
221:
219:
214:
208:
206:
201:
195:
193:
190:
186:
178:
170:
166:
156:
154:
146:
142:
139:Transport of
138:
135:
131:
127:
126:Translocation
124:
121:
117:
113:
112:proliferation
109:
105:
102:
98:
94:
91:
88:
84:
80:
76:
72:
69:
68:
67:
64:
56:
54:
50:
47:
43:
39:
35:
32:
28:
25:
21:
2861:Translocases
2858:
2845:
2832:
2819:
2806:
2796:Transferases
2793:
2780:
2637:Binding site
2374:
2308:
2264:
2242:
2227:Small GTPase
2090:
1841:Wilson/ATP7B
1836:Menkes/ATP7A
1634:(6): 451–8.
1631:
1627:
1621:
1584:
1580:
1570:
1537:
1533:
1527:
1502:
1498:
1446:
1442:
1436:
1403:
1399:
1393:
1366:
1362:
1352:
1327:
1323:
1317:
1290:
1287:DNA Research
1286:
1232:
1229:BMC Genomics
1228:
1218:
1183:
1179:
1169:
1136:
1132:
1126:
1104:(1): 41–72.
1101:
1098:J. Mol. Biol
1097:
1043:
1039:
1033:
1008:
1004:
998:
971:
967:
957:
930:
926:
870:
866:
800:
796:
732:
729:FEBS Letters
728:
683:superclass.
670:
659:
643:
633:October 2021
630:
618:
594:
591:SIMIBI class
582:
566:
521:
518:Small GTPase
506:ion channels
476:family and G
459:
443:
423:
406:
402:
396:
391:
372:
366:(eukaryotic
360:tetracycline
355:
351:
301:
283:
280:TRAFAC class
270:
256:
252:
248:
244:
229:
222:
209:
196:
162:
150:
65:
62:
19:
18:
2632:Active site
2551:Mitofusin-1
2526:3.6.5.5-6:
2495:Prokaryotic
1330:: 167–203.
803:: 615–649.
304:translation
243:Artificial
171:(GDP) and P
143:within the
97:translation
2904:Categories
2835:Isomerases
2809:Hydrolases
2676:Regulation
2517:Eukaryotic
2150:Transducin
1987:(3.6.3.10)
1726:Hydrolases
735:(1): 1–6.
709:References
312:elongation
308:initiation
292:See also:
31:nucleotide
2714:EC number
2485:3.6.5.3:
2225:3.6.5.2:
2167:Gustducin
2099:3.6.5.1:
1933:(3.6.3.9)
1853:(3.6.3.8)
1756:Inorganic
1235:(1): 15.
1068:195761467
1046:: 23–35.
625:talk page
472:family, G
468:family, G
189:magnesium
165:phosphate
159:Mechanism
134:membranes
99:) at the
59:Functions
46:conserved
38:hydrolyze
24:hydrolase
2915:EC 3.6.5
2738:Kinetics
2662:Cofactor
2625:Activity
1761:Thiamine
1686:Archived
1613:27658684
1519:11152757
1479:20136388
1471:12040175
1428:23659116
1420:12209124
1385:11313912
1363:Oncogene
1309:10819326
1261:17214893
1210:29235176
1118:11916378
1060:31255772
905:11025853
687:See also
411:subunits
405:(β) and
350:(TypA),
346:(LepA),
320:ribosome
141:vesicles
132:through
130:proteins
120:movement
116:division
101:ribosome
95:(a.k.a.
2894:Biology
2848:Ligases
2618:Enzymes
2572:Tubulin
2541:Dynamin
2393:other:
2073:Katanin
2063:Kinesin
2038:ATP13A3
2033:ATP13A2
1768:Apyrase
1656:5945125
1648:9628483
1604:5627767
1562:2116664
1542:Bibcode
1534:Science
1451:Bibcode
1443:Science
1344:9131251
1252:1780047
1201:5796857
1161:1388090
1153:6113539
1025:9588168
990:3086320
949:9430654
897:7579038
888:1519115
817:3113327
749:8462668
703:Septins
662:tubulin
652:(SRP).
585:dynamin
573:kinesin
273:guanine
249:GTP-γ-S
27:enzymes
20:GTPases
2880:Portal
2822:Lyases
2449:ARL13B
2309:RhoBTB
2203:α12/13
2091:GTPase
2068:Myosin
2058:Dynein
2028:ATP12A
2023:ATP11B
2018:ATP10A
2013:ATP8B1
2003:Other
1975:ATP1B4
1970:ATP1B3
1965:ATP1B2
1960:ATP1B1
1955:ATP1A4
1950:ATP1A3
1945:ATP1A2
1940:ATP1A1
1931:Na+/K+
1919:ATP2C2
1914:ATP2C1
1902:ATP2B4
1897:ATP2B3
1892:ATP2B2
1887:ATP2B1
1875:ATP2A3
1870:ATP2A2
1865:ATP2A1
1814:ATPase
1679:(MeSH)
1673:GTPase
1654:
1646:
1611:
1601:
1560:
1517:
1477:
1469:
1426:
1418:
1383:
1342:
1307:
1259:
1249:
1208:
1198:
1159:
1151:
1116:
1066:
1058:
1023:
988:
947:
903:
895:
885:
815:
747:
673:P-loop
660:While
569:myosin
436:-GDP-G
296:, and
255:, and
87:vision
49:P-loop
40:it to
2774:Types
2505:EF-Tu
2444:SAR1B
2427:RAB27
2422:RAB23
2375:RhoDF
2265:RhoUV
2248:CDC42
2243:Cdc42
2229:>
2214:GNA13
2209:GNA12
2194:GNA11
2183:αq/11
2172:GNAT3
2160:GNAT2
2155:GNAT1
2145:GNAI3
2140:GNAI2
2135:GNAI1
2087:3.6.5
2051:3.6.4
1994:ATP4A
1985:H+/K+
1860:SERCA
1822:3.6.3
1806:3.6.3
1783:3.6.2
1743:3.6.1
1652:S2CID
1475:S2CID
1424:S2CID
1157:S2CID
1064:S2CID
901:S2CID
677:NACHT
492:and G
407:gamma
401:(α),
398:alpha
364:HBS1L
328:EF-Tu
324:EF-1A
247:like
83:smell
79:taste
2866:list
2859:EC7
2853:list
2846:EC6
2840:list
2833:EC5
2827:list
2820:EC4
2814:list
2807:EC3
2801:list
2794:EC2
2788:list
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