599:
468:
events much in the same way as the single ubiquitylation mechanism, using instead a lysine residue from a ubiquitin molecule currently attached to substrate protein to attack the C-terminus of a new ubiquitin molecule. For example, a common 4-ubiquitin tag, linked through the lysine at position 48 (K48) recruits the tagged protein to the proteasome, and subsequent degradation. However, all seven of the ubiquitin lysine residues (K6, K11, K27, K29, K33, K48, and K63), as well as the N-terminal methionine are used in chains in vivo.
460:
4053:
358:
451:-F-box protein complex). SCF complexes consist of four proteins: Rbx1, Cul1, Skp1, which are invariant among SCF complexes, and an F-box protein, which varies. Around 70 human F-box proteins have been identified. F-box proteins contain an F-box, which binds the rest of the SCF complex, and a substrate binding domain, which gives the E3 its substrate specificity.
40:
341:. However, many other types of linkages are possible and alter a protein's activity, interactions, or localization. Ubiquitination by E3 ligases regulates diverse areas such as cell trafficking, DNA repair, and signaling and is of profound importance in cell biology. E3 ligases are also key players in cell cycle control, mediating the degradation of
845:, causing increased transcription of MDM2 mRNA. Several proteomics-based experimental techniques are available for identifying E3 ubiquitin ligase-substrate pairs, such as proximity-dependent biotin identification (BioID), ubiquitin ligase-substrate trapping, and tandem ubiquitin-binding entities (TUBEs).
467:
Ubiquitin signaling relies on the diversity of ubiquitin tags for the specificity of its message. A protein can be tagged with a single ubiquitin molecule (monoubiquitylation), or variety of different chains of ubiquitin molecules (polyubiquitylation). E3 ubiquitin ligases catalyze polyubiquitination
336:
residue, which is part of the target protein. E3 ligases interact with both the target protein and the E2 enzyme, and so impart substrate specificity to the E2. Commonly, E3s polyubiquitinate their substrate with Lys48-linked chains of ubiquitin, targeting the substrate for destruction by the
494:
either for degradation (K48 polyubiquitin chain), or for nuclear export (monoubiquitylation). These events occur in a concentration dependent fashion, suggesting that modulating E3 ligase concentration is a cellular regulatory strategy for controlling protein homeostasis and localization.
324:, recognizes a protein substrate, and assists or directly catalyzes the transfer of ubiquitin from the E2 to the protein substrate. In simple and more general terms, the ligase enables movement of ubiquitin from a ubiquitin carrier to another protein (the substrate) by some mechanism. The
434:
Humans have an estimated 500-1000 E3 ligases, which impart substrate specificity onto the E1 and E2. The E3 ligases are classified into four families: HECT, RING-finger, U-box, and PHD-finger. The RING-finger E3 ligases are the largest family and contain ligases such as the
421:
type ligases transfer ubiquitin directly from E2 to the substrate. The final step in the first ubiquitylation event is an attack from the target protein lysine amine group, which will remove the cysteine, and form a stable isopeptide bond. One notable exception to this is
412:
Ub-S-E1 complex. The energy from ATP and diphosphate hydrolysis drives the formation of this reactive thioester, and subsequent steps are thermoneutral. Next, a transthiolation reaction occurs, in which an E2 cysteine residue attacks and replaces the E1.
602:
A phosphorylated degron (green) is stabilized by hydrogen bonding (yellow) between oxygen atoms of its phosphate (red) and side chains of the SCFubiquitin ligase (blue). The relevant part of the ubiquitin ligase is shown in gray. PDB entry
2332:
de
Martino M, Taus C, Wessely IS, Lucca I, Hofbauer SL, Haitel A, Shariat SF, Klatte T (February 2015). "The T309G murine double minute 2 gene polymorphism is an independent prognostic factor for patients with renal cell carcinoma".
821:
E3 ubiquitin ligases regulate homeostasis, cell cycle, and DNA repair pathways, and as a result, a number of these proteins are involved in a variety of cancers, including famously MDM2,
2078:
Jaakkola P, Mole DR, Tian YM, Wilson MI, Gielbert J, Gaskell SJ, von
Kriegsheim A, Hebestreit HF, Mukherji M, Schofield CJ, Maxwell PH, Pugh CW, Ratcliffe PJ (April 2001).
722:
In addition to recognizing amino acids, ubiquitin ligases can also detect unusual features on substrates that serve as signals for their destruction. For example, San1 (
210:
2602:
3406:
1311:"Genome-wide and functional annotation of human E3 ubiquitin ligases identifies MULAN, a mitochondrial E3 that regulates the organelle's dynamics and signaling"
404:
The ubiquitylation reaction proceeds in three or four steps depending on the mechanism of action of the E3 ubiquitin ligase. In the conserved first step, an E1
2855:
747:
546:, different N-terminal amino acids (or N-degrons) are recognized to a different extent by their appropriate ubiquitin ligase (N-recognin), influencing the
2368:
Tang T, Song X, Yang Z, Huang L, Wang W, Tan H (November 2014). "Association between murine double minute 2 T309G polymorphism and risk of liver cancer".
519:, and from other (ubiquitination-inactive) forms of the same protein. This can be achieved by different mechanisms, most of which involve recognition of
813:
interaction. TRF1 cannot be ubiquinated while telomere bound, likely because the same TRF1 domain that binds to its E3 ligase also binds to telomeres.
723:
2413:"Using proteomics to identify ubiquitin ligase-substrate pairs: how novel methods may unveil therapeutic targets for neurodegenerative diseases"
3455:
1703:
Li M, Brooks CL, Wu-Baer F, Chen D, Baer R, Gu W (December 2003). "Mono- versus polyubiquitination: differential control of p53 fate by Mdm2".
627:
residue. In this case, the ubiquitin ligase exclusively recognizes the phosphorylated version of the substrate due to stabilization within the
279:
267:
3265:
229:
3636:
2595:
1847:
Sriram SM, Kim BY, Kwon YT (October 2011). "The N-end rule pathway: emerging functions and molecular principles of substrate recognition".
3607:
3481:
417:
type E3 ligases will have one more transthiolation reaction to transfer the ubiquitin molecule onto the E3, whereas the much more common
3520:
676:
4078:
3712:
3154:
3149:
3124:
3114:
3109:
3099:
961:
957:
953:
3170:
3104:
2588:
1143:
1100:
999:
991:
222:
2549:
3660:
3401:
3200:
2035:
Reinhardt HC, Yaffe MB (September 2013). "Phospho-Ser/Thr-binding domains: navigating the cell cycle and DNA damage response".
1124:
939:
1429:
173:
3626:
877:
An F-box domain (as in the SCF complex) binds the ubiquitinated substrate. (e.g., Cdc 4, which binds the target protein
672:
17:
3448:
3418:
826:
3772:
1945:
346:
3727:
476:
426:
protein, which appears to be ubiquitylated using its N-terminal amine, thus forming a peptide bond with ubiquitin.
349:
proteins. The human genome encodes over 600 putative E3 ligases, allowing for tremendous diversity in substrates.
3732:
2611:
608:
167:
3722:
3616:
2811:
2231:"RINGs of good and evil: RING finger ubiquitin ligases at the crossroads of tumour suppression and oncogenesis"
149:
1946:"Recognition of substrate degrons by E3 ubiquitin ligases and modulation by small-molecule mimicry strategies"
515:. The ligases must simultaneously distinguish their protein substrate from thousands of other proteins in the
3928:
3739:
3565:
3441:
2505:"SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box"
2080:"Targeting of HIF-alpha to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation"
1309:
Li W, Bengtson MH, Ulbrich A, Matsuda A, Reddy VA, Orth A, Chanda SK, Batalov S, Joazeiro CA (January 2008).
154:
1668:
Bonifacino JS, Traub LM (2003). "Signals for sorting of transmembrane proteins to endosomes and lysosomes".
3024:
1171:
899:
370:
317:
2969:
1166:
366:
234:
874:
ene) domain binds the E2 conjugase and might be found to mediate enzymatic activity in the E2-E3 complex
385:
and transfers it to an E2 enzyme. The E2 enzyme interacts with a specific E3 partner and transfers the
142:
4043:
3707:
3702:
3675:
3585:
3560:
3545:
3505:
909:
436:
382:
77:
4029:
4016:
4003:
3990:
3977:
3964:
3951:
3913:
3697:
3621:
3580:
3540:
3530:
3525:
3510:
3490:
2562:
1583:
Vijay-Kumar S, Bugg CE, Cook WJ (April 1987). "Structure of ubiquitin refined at 1.8 A resolution".
463:
Ubiquitin with lysine residues (red), N-terminal methionine (blue), and C-terminal glycine (yellow).
3923:
3877:
3820:
3590:
3515:
3500:
3472:
2909:
2572:
2566:
842:
483:. C-Cbl monoubiquitylates EGFR, signaling for its internalization and trafficking to the lysosome.
398:
170:
60:
94:
44:
E3 ubiquitin ligase Cbl (blue) in complex with E2 (cyan) and substrate peptide (green). PDB entry
3825:
3570:
3550:
3535:
3495:
3234:
841:(amongst others) to deregulate MDM2 concentrations by increasing its promoter’s affinity for the
696:
675:(VHL) protein (substrate recognition part of a specific E3 ligase), for instance, recognizes the
486:
Monoubiquitination also can regulate cytosolic protein localization. For example, the E3 ligase
3687:
3595:
3575:
3555:
3275:
1625:
Behrends C, Harper JW (May 2011). "Constructing and decoding unconventional ubiquitin chains".
374:
3846:
3765:
3717:
3433:
2656:
1681:
762:
and SCF. These recognition domains have small hydrophobic pockets allowing them to bind high-
504:
786:
on the substrate. In this case, the 3D motif can allow the substrate to directly relate its
598:
3918:
3645:
2091:
1712:
1322:
834:
807:
535:
130:
1907:
1776:
1287:
8:
3882:
2619:
1763:
Zheng N, Shabek N (June 2017). "Ubiquitin
Ligases: Structure, Function, and Regulation".
699:
response to hypoxia. Another example of small molecule control of protein degradation is
291:
106:
72:
2437:
2412:
2095:
1716:
1491:
Nakayama KI, Nakayama K (May 2006). "Ubiquitin ligases: cell-cycle control and cancer".
1326:
65:
3815:
2633:
2450:
2393:
2309:
2282:
2255:
2230:
2206:
2179:
2160:
2117:
2060:
2012:
1987:
1916:
1891:
1872:
1824:
1799:
1736:
1650:
1516:
1394:
1369:
1345:
1310:
1216:
1192:"Structural basis for autoinhibition and phosphorylation-dependent activation of c-Cbl"
1191:
929:
855:
418:
272:
2521:
2504:
1560:
1535:
1463:
1446:
710:
ubiquitin ligase) increasing the affinity of TIR1 for its substrates (transcriptional
185:
2935:
2546:
2526:
2485:
2442:
2385:
2350:
2314:
2260:
2211:
2152:
2109:
2052:
2017:
1968:
1921:
1864:
1829:
1780:
1728:
1685:
1642:
1600:
1596:
1565:
1508:
1468:
1425:
1399:
1350:
1291:
1256:
1252:
1221:
688:
161:
2454:
2397:
2164:
2121:
1876:
1740:
1654:
1520:
3861:
3856:
3830:
3758:
2899:
2516:
2477:
2432:
2424:
2377:
2342:
2304:
2294:
2250:
2242:
2201:
2191:
2144:
2099:
2044:
2007:
1999:
1960:
1911:
1903:
1856:
1819:
1811:
1772:
1720:
1677:
1634:
1592:
1555:
1547:
1500:
1458:
1389:
1381:
1340:
1330:
1283:
1248:
1211:
1203:
783:
503:
Ubiquitin ligases are the final, and potentially the most important determinant of
2064:
651:
residues to the phosphate, as shown in the figure to the right. In absence of the
408:
residue attacks the ATP-activated C-terminal glycine on ubiquitin, resulting in a
365:
The ubiquitin ligase is referred to as an E3, and operates in conjunction with an
296:
284:
4073:
3908:
3892:
3805:
2624:
2580:
2553:
1335:
1138:
739:
727:
612:
394:
329:
1534:
Jin J, Cardozo T, Lovering RC, Elledge SJ, Pagano M, Harper JW (November 2004).
189:
4057:
3946:
3887:
3692:
2948:
2943:
2428:
830:
735:
692:
516:
475:
pathways. For example, phosphorylation of the
Tyrosine at position 1045 in the
205:
2381:
1964:
888:, which is involved in the transfer of ubiquitin from the E2 to the substrate.
4067:
3851:
3810:
2196:
2135:
Shabek N, Zheng N (April 2014). "Plant ubiquitin ligases as signaling hubs".
755:
700:
644:
636:
567:
180:
2104:
2079:
2003:
1724:
46:
3800:
3304:
3286:
2503:
Bai C, Sen P, Hofmann K, Ma L, Goebl M, Harper JW, Elledge SJ (July 1996).
2489:
2446:
2389:
2354:
2318:
2299:
2264:
2215:
2156:
2113:
2056:
2021:
1972:
1925:
1868:
1833:
1784:
1732:
1689:
1646:
1569:
1512:
1472:
1403:
1354:
1295:
1225:
838:
743:
684:
628:
373:. There is one major E1 enzyme, shared by all ubiquitin ligases, that uses
2530:
2346:
1604:
1260:
695:
and thus operates in the cell at higher concentrations which can initiate
4024:
3959:
3795:
3380:
3248:
1274:
Teixeira LK, Reed SI (2013). "Ubiquitin ligases and cell cycle control".
1190:
Dou H, Buetow L, Hock A, Sibbet GJ, Vousden KH, Huang DT (January 2012).
885:
787:
759:
707:
640:
472:
440:
414:
2575:
1551:
1447:"Proteasome-mediated degradation of p21 via N-terminal ubiquitinylation"
1422:
Posttranslational
Modification of Proteins: Expanding Nature's Inventory
118:
3210:
2638:
2180:"Sugar-Recognizing Ubiquitin Ligases: Action Mechanisms and Physiology"
1385:
810:
583:
571:
563:
543:
539:
524:
480:
397:, is, in general, responsible for targeting ubiquitination to specific
338:
2481:
2148:
1988:"Expanding the ubiquitin code through post-translational modification"
1638:
1445:
Bloom J, Amador V, Bartolini F, DeMartino G, Pagano M (October 2003).
1207:
3998:
3972:
2958:
2904:
1800:"Diversity of degradation signals in the ubiquitin-proteasome system"
1161:
791:
711:
652:
624:
559:
547:
508:
409:
386:
378:
325:
321:
2246:
2048:
1860:
1815:
1504:
706:
in plants. Auxin binds to TIR1 (the substrate recognition domain of
459:
4052:
3238:
2871:
2863:
2411:
Rayner SL, Morsch M, Molloy MP, Shi B, Chung R, Lee A (July 2019).
1370:"HECT and RING finger families of E3 ubiquitin ligases at a glance"
799:
668:
648:
616:
575:
551:
405:
1536:"Systematic analysis and nomenclature of mammalian F-box proteins"
586:) are recognized preferentially and thus considered destabilizing
2989:
2876:
2836:
2767:
2762:
2757:
2752:
2747:
2702:
763:
680:
579:
512:
390:
357:
342:
328:, once it reaches its destination, ends up being attached by an
313:
137:
4011:
3781:
3655:
3468:
3464:
3205:
3180:
3175:
3165:
3129:
3119:
3094:
3079:
3074:
3069:
3064:
3059:
3054:
3049:
3044:
3009:
2994:
2841:
2806:
2791:
2786:
2781:
2742:
2737:
2732:
2727:
2722:
2717:
2712:
2707:
2697:
2692:
2687:
2682:
2677:
1083:
1078:
1068:
1064:
1049:
1027:
1017:
965:
779:
767:
664:
620:
587:
555:
520:
448:
333:
217:
113:
101:
89:
3463:
658:
3985:
3665:
3396:
3386:
3376:
3361:
3343:
3338:
3333:
3328:
3260:
3220:
3185:
3159:
3144:
3139:
3134:
3089:
3084:
3039:
3034:
3029:
2999:
2984:
2881:
2850:
2831:
2826:
2821:
2816:
2801:
2796:
2776:
2672:
2665:
2661:
2651:
2646:
1444:
1114:
1109:
1105:
1096:
1092:
1088:
1073:
1044:
1040:
1036:
1032:
1022:
1013:
1004:
995:
987:
983:
979:
974:
970:
948:
943:
822:
803:
802:
length), which is recognized by its corresponding E3 ligase (
795:
731:
703:
632:
3680:
3670:
3411:
3391:
3371:
3366:
3316:
3299:
3255:
3243:
3225:
3215:
3014:
3004:
2979:
2974:
2919:
2914:
1156:
1133:
1129:
1119:
1059:
1054:
1008:
934:
925:
921:
915:
904:
878:
751:
643:
ubiquitin ligase, stabilizes a phosphorylated substrate by
487:
444:
125:
3750:
2331:
1533:
1239:
Hershko A, Ciechanover A (1998). "The ubiquitin system".
491:
479:(EGFR) can recruit the RING type E3 ligase c-Cbl, via an
423:
1308:
2468:
Ardley HC, Robinson PA (2005). "E3 ubiquitin ligases".
1367:
691:, on the other hand, HIF-a is not hydroxylated, evades
590:
since they allow faster degradation of their proteins.
471:
Monoubiquitination has been linked to membrane protein
39:
2557:
2177:
2077:
1368:
Metzger MB, Hristova VA, Weissman AM (February 2012).
679:(HIF-α) only under normal oxygen conditions, when its
4041:
2410:
1889:
829:. For example, a mutation of MDM2 has been found in
738:, which allows it to bind to hydrophobic domains of
607:
A degron can be converted into its active form by a
1702:
1582:
1189:
2610:
1238:
892:
550:of the protein. For instance, positively charged (
2367:
2228:
1797:
782:, the E3 ligase can in some cases also recognize
4065:
2283:"Role of E3 ubiquitin ligases in gastric cancer"
1490:
454:
2502:
2178:Yoshida Y, Mizushima T, Tanaka K (2019-02-19).
1667:
527:sequences or chemical motifs on the substrate.
361:Schematic diagram of the ubiquitylation system.
2467:
2034:
1890:Tasaki T, Sriram SM, Park KS, Kwon YT (2012).
1624:
750:pathway, on the other hand, are recognized by
717:
3766:
3449:
2596:
1846:
714:: Aux/IAA), and promoting their degradation.
1985:
1273:
429:
2547:Quips article describing E3 Ligase function
2134:
1943:
1762:
1620:
1618:
1616:
1614:
1183:
659:Oxygen and small molecule dependent degrons
3773:
3759:
3456:
3442:
2603:
2589:
1798:Ravid T, Hochstrasser M (September 2008).
1486:
1484:
1482:
38:
2565:at the U.S. National Library of Medicine
2520:
2436:
2308:
2298:
2254:
2205:
2195:
2137:Nature Structural & Molecular Biology
2103:
2011:
1915:
1823:
1627:Nature Structural & Molecular Biology
1559:
1462:
1393:
1344:
1334:
1215:
1196:Nature Structural & Molecular Biology
794:. This relation can be demonstrated with
2229:Lipkowitz S, Weissman AM (August 2011).
1682:10.1146/annurev.biochem.72.121801.161800
1611:
655:, residues of FBW7 repel the substrate.
597:
538:can lead to exposure of residues at the
498:
458:
356:
352:
2280:
1479:
1415:
1413:
14:
4066:
2276:
2274:
671:can influence degron recognition. The
3754:
3521:D-alanine—poly(phosphoribitol) ligase
3437:
2584:
2037:Nature Reviews Molecular Cell Biology
1986:Herhaus L, Dikic I (September 2015).
1953:Current Opinion in Structural Biology
1939:
1937:
1935:
1908:10.1146/annurev-biochem-051710-093308
1849:Nature Reviews Molecular Cell Biology
1804:Nature Reviews Molecular Cell Biology
1777:10.1146/annurev-biochem-060815-014922
1758:
1756:
1754:
1752:
1750:
1419:
1288:10.1146/annurev-biochem-060410-105307
2417:Cellular and Molecular Life Sciences
1410:
816:
773:
2271:
24:
3661:Von Hippel–Lindau tumor suppressor
3419:Prokaryotic ubiquitin-like protein
1932:
1747:
827:Von Hippel-Lindau tumor suppressor
742:. Misfolded or excess unassembled
25:
4090:
2540:
2287:World Journal of Gastroenterology
639:substrate recognition unit of an
593:
347:cyclin dependent kinase inhibitor
4051:
3627:Long-chain-fatty-acid—CoA ligase
2281:Hou YC, Deng JY (January 2015).
1253:10.1146/annurev.biochem.67.1.425
477:Epidermal Growth Factor Receptor
4079:Post-translational modification
2496:
2461:
2404:
2361:
2325:
2222:
2171:
2128:
2071:
2028:
1979:
1944:Lucas X, Ciulli A (June 2017).
1883:
1840:
1791:
1696:
1661:
1576:
893:Individual E3 ubiquitin ligases
609:post-translational modification
542:of a protein. According to the
371:E2 ubiquitin-conjugating enzyme
3723:Carbamoyl phosphate synthetase
3617:Succinyl coenzyme A synthetase
2949:Mitochondrial targeting signal
2612:Posttranslational modification
1527:
1438:
1361:
1302:
1267:
1232:
677:hypoxia-inducible factor alpha
367:E1 ubiquitin-activating enzyme
13:
1:
2522:10.1016/S0092-8674(00)80098-7
1896:Annual Review of Biochemistry
1765:Annual Review of Biochemistry
1670:Annual Review of Biochemistry
1464:10.1016/S0092-8674(03)00755-4
1276:Annual Review of Biochemistry
1241:Annual Review of Biochemistry
1177:
734:, has a disordered substrate
455:Mono- and poly-ubiquitylation
3025:Ubiquitin-conjugating enzyme
1597:10.1016/0022-2836(87)90679-6
1585:Journal of Molecular Biology
1336:10.1371/journal.pone.0001487
1172:Ubiquitin-conjugating enzyme
530:
318:ubiquitin-conjugating enzyme
7:
3780:
3313:E2 SUMO-conjugating enzyme
2970:Ubiquitin-activating enzyme
1420:Walsh, Christopher (2006).
1167:Ubiquitin-activating enzyme
1150:
848:
718:Misfolded and sugar degrons
10:
4095:
3708:Holocarboxylase synthetase
3703:Argininosuccinate synthase
3676:Anaphase-promoting complex
3296:E1 SUMO-activating enzyme
2429:10.1007/s00018-019-03082-9
1424:. Englewood, CO: Roberts.
910:Anaphase-promoting complex
437:anaphase-promoting complex
393:. The E3, which may be a
320:that has been loaded with
3937:
3929:Michaelis–Menten kinetics
3901:
3870:
3839:
3788:
3740:Glutamate–cysteine ligase
3698:Adenylosuccinate synthase
3635:
3606:
3491:Aminoacyl tRNA synthetase
3480:
3354:
3285:
3274:
2957:
2934:
2892:
2632:
2618:
2563:Ubiquitin-Protein+Ligases
2382:10.1007/s13277-014-2432-9
1965:10.1016/j.sbi.2016.12.015
881:; Grr1, which binds Cln).
430:Ubiquitin ligase families
290:
278:
266:
258:
253:
248:
228:
216:
204:
199:
195:
179:
160:
148:
136:
124:
112:
100:
88:
83:
71:
59:
54:
37:
32:
3821:Diffusion-limited enzyme
2910:Survival of motor neuron
2567:Medical Subject Headings
2197:10.3389/fphys.2019.00104
1892:"The N-end rule pathway"
843:Sp1 transcription factor
33:Ubiquitin—protein ligase
3276:Ubiquitin-like proteins
3235:Deubiquitinating enzyme
2184:Frontiers in Physiology
2105:10.1126/science.1059796
2004:10.15252/embr.201540891
1725:10.1126/science.1091362
1540:Genes & Development
1374:Journal of Cell Science
3688:Glutathione synthetase
2470:Essays in Biochemistry
2300:10.3748/wjg.v21.i3.786
2235:Nature Reviews. Cancer
1493:Nature Reviews. Cancer
778:In addition to linear
604:
464:
362:
3914:Eadie–Hofstee diagram
3847:Allosteric regulation
3718:Asparagine synthetase
3622:Acetyl—CoA synthetase
2347:10.1089/dna.2014.2653
601:
499:Substrate recognition
462:
395:multi-protein complex
360:
353:Ubiquitination system
3924:Lineweaver–Burk plot
3646:Glutamine synthetase
2335:DNA and Cell Biology
835:renal cell carcinoma
798:(regulator of human
754:and Fbs2, mammalian
536:Proteolytic cleavage
316:that recruits an E2
2634:Heat shock proteins
2096:2001Sci...292..468J
1717:2003Sci...302.1972L
1552:10.1101/gad.1255304
1327:2008PLoSO...3.1487L
730:quality control in
310:E3 ubiquitin ligase
18:E3 Ubiquitin ligase
3883:Enzyme superfamily
3816:Enzyme promiscuity
2552:2012-11-30 at the
1386:10.1242/jcs.091777
740:misfolded proteins
605:
465:
419:RING finger domain
363:
4039:
4038:
3748:
3747:
3639:: Carbon-Nitrogen
3431:
3430:
3427:
3426:
2936:Protein targeting
2930:
2929:
2482:10.1042/EB0410015
2423:(13): 2499–2510.
2149:10.1038/nsmb.2804
1639:10.1038/nsmb.2066
1431:978-0-9747077-3-0
1208:10.1038/nsmb.2231
924:/ BC-box/ eloBC/
817:Disease relevance
784:structural motifs
774:Structural motifs
673:von Hippel-Lindau
523:: specific short
302:
301:
244:
243:
240:
239:
143:metabolic pathway
16:(Redirected from
4086:
4056:
4055:
4047:
3919:Hanes–Woolf plot
3862:Enzyme activator
3857:Enzyme inhibitor
3831:Enzyme catalysis
3775:
3768:
3761:
3752:
3751:
3651:Ubiquitin ligase
3458:
3451:
3444:
3435:
3434:
3283:
3282:
3196:Ubiquitin ligase
2962:(ubiquitylation)
2900:Alpha crystallin
2630:
2629:
2605:
2598:
2591:
2582:
2581:
2535:
2534:
2524:
2500:
2494:
2493:
2465:
2459:
2458:
2440:
2408:
2402:
2401:
2365:
2359:
2358:
2329:
2323:
2322:
2312:
2302:
2278:
2269:
2268:
2258:
2226:
2220:
2219:
2209:
2199:
2175:
2169:
2168:
2132:
2126:
2125:
2107:
2090:(5516): 468–72.
2075:
2069:
2068:
2032:
2026:
2025:
2015:
1983:
1977:
1976:
1950:
1941:
1930:
1929:
1919:
1887:
1881:
1880:
1844:
1838:
1837:
1827:
1795:
1789:
1788:
1760:
1745:
1744:
1711:(5652): 1972–5.
1700:
1694:
1693:
1665:
1659:
1658:
1622:
1609:
1608:
1580:
1574:
1573:
1563:
1531:
1525:
1524:
1488:
1477:
1476:
1466:
1442:
1436:
1435:
1417:
1408:
1407:
1397:
1365:
1359:
1358:
1348:
1338:
1306:
1300:
1299:
1271:
1265:
1264:
1236:
1230:
1229:
1219:
1187:
724:Sir antagonist 1
663:The presence of
645:hydrogen binding
308:(also called an
306:ubiquitin ligase
262:Ubiquitin ligase
249:Ubiquitin ligase
246:
245:
197:
196:
49:
42:
30:
29:
21:
4094:
4093:
4089:
4088:
4087:
4085:
4084:
4083:
4064:
4063:
4062:
4050:
4042:
4040:
4035:
3947:Oxidoreductases
3933:
3909:Enzyme kinetics
3897:
3893:List of enzymes
3866:
3835:
3806:Catalytic triad
3784:
3779:
3749:
3744:
3631:
3610:: Carbon-Sulfur
3602:
3484:: Carbon-Oxygen
3476:
3467:: CO CS and CN
3462:
3432:
3423:
3350:
3325:E3 SUMO ligase
3289:
3278:
3270:
2961:
2953:
2926:
2888:
2867:
2859:
2637:
2625:protein folding
2623:
2614:
2609:
2554:Wayback Machine
2543:
2538:
2501:
2497:
2466:
2462:
2409:
2405:
2376:(11): 11353–7.
2366:
2362:
2330:
2326:
2279:
2272:
2247:10.1038/nrc3120
2227:
2223:
2176:
2172:
2133:
2129:
2076:
2072:
2049:10.1038/nrm3640
2033:
2029:
1984:
1980:
1948:
1942:
1933:
1888:
1884:
1861:10.1038/nrm3217
1845:
1841:
1816:10.1038/nrm2468
1796:
1792:
1761:
1748:
1701:
1697:
1666:
1662:
1623:
1612:
1581:
1577:
1546:(21): 2573–80.
1532:
1528:
1505:10.1038/nrc1881
1489:
1480:
1443:
1439:
1432:
1418:
1411:
1380:(Pt 3): 531–7.
1366:
1362:
1307:
1303:
1272:
1268:
1237:
1233:
1188:
1184:
1180:
1153:
1148:
895:
851:
819:
776:
728:nuclear protein
720:
697:transcriptional
667:or other small
661:
631:. For example,
613:phosphorylation
596:
533:
507:specificity in
501:
457:
432:
355:
330:isopeptide bond
268:OPM superfamily
50:
45:
28:
23:
22:
15:
12:
11:
5:
4092:
4082:
4081:
4076:
4061:
4060:
4037:
4036:
4034:
4033:
4020:
4007:
3994:
3981:
3968:
3955:
3941:
3939:
3935:
3934:
3932:
3931:
3926:
3921:
3916:
3911:
3905:
3903:
3899:
3898:
3896:
3895:
3890:
3885:
3880:
3874:
3872:
3871:Classification
3868:
3867:
3865:
3864:
3859:
3854:
3849:
3843:
3841:
3837:
3836:
3834:
3833:
3828:
3823:
3818:
3813:
3808:
3803:
3798:
3792:
3790:
3786:
3785:
3778:
3777:
3770:
3763:
3755:
3746:
3745:
3743:
3742:
3737:
3736:
3735:
3730:
3720:
3715:
3710:
3705:
3700:
3695:
3693:CTP synthetase
3690:
3685:
3684:
3683:
3678:
3673:
3668:
3663:
3658:
3648:
3642:
3640:
3633:
3632:
3630:
3629:
3624:
3619:
3613:
3611:
3604:
3603:
3601:
3600:
3599:
3598:
3593:
3588:
3583:
3578:
3573:
3568:
3563:
3558:
3553:
3548:
3543:
3538:
3533:
3528:
3523:
3518:
3513:
3508:
3503:
3498:
3487:
3485:
3478:
3477:
3461:
3460:
3453:
3446:
3438:
3429:
3428:
3425:
3424:
3422:
3421:
3415:
3414:
3409:
3404:
3399:
3394:
3389:
3384:
3374:
3369:
3364:
3358:
3356:
3352:
3351:
3349:
3348:
3347:
3346:
3341:
3336:
3331:
3322:
3321:
3320:
3319:
3310:
3309:
3308:
3307:
3302:
3293:
3291:
3280:
3272:
3271:
3269:
3268:
3263:
3258:
3252:
3251:
3246:
3241:
3231:
3230:
3229:
3228:
3223:
3218:
3213:
3208:
3203:
3191:
3190:
3189:
3188:
3183:
3178:
3173:
3168:
3163:
3157:
3152:
3147:
3142:
3137:
3132:
3127:
3122:
3117:
3112:
3107:
3102:
3097:
3092:
3087:
3082:
3077:
3072:
3067:
3062:
3057:
3052:
3047:
3042:
3037:
3032:
3020:
3019:
3018:
3017:
3012:
3007:
3002:
2997:
2992:
2987:
2982:
2977:
2965:
2963:
2955:
2954:
2952:
2951:
2946:
2944:Signal peptide
2940:
2938:
2932:
2931:
2928:
2927:
2925:
2924:
2923:
2922:
2917:
2907:
2902:
2896:
2894:
2890:
2889:
2887:
2886:
2885:
2884:
2879:
2874:
2869:
2865:
2861:
2857:
2847:
2846:
2845:
2844:
2839:
2834:
2829:
2824:
2819:
2814:
2809:
2804:
2799:
2794:
2789:
2784:
2773:
2772:
2771:
2770:
2765:
2760:
2755:
2750:
2745:
2740:
2735:
2730:
2725:
2720:
2715:
2710:
2705:
2700:
2695:
2690:
2685:
2680:
2669:
2668:
2659:
2654:
2649:
2643:
2641:
2627:
2616:
2615:
2608:
2607:
2600:
2593:
2585:
2579:
2578:
2570:
2560:
2542:
2541:External links
2539:
2537:
2536:
2495:
2460:
2403:
2370:Tumour Biology
2360:
2324:
2270:
2221:
2170:
2127:
2070:
2027:
1998:(9): 1071–83.
1978:
1931:
1882:
1855:(11): 735–47.
1839:
1790:
1771:(1): 129–157.
1746:
1695:
1660:
1610:
1575:
1526:
1478:
1437:
1430:
1409:
1360:
1301:
1266:
1231:
1181:
1179:
1176:
1175:
1174:
1169:
1164:
1159:
1152:
1149:
1147:
1146:
1141:
1136:
1127:
1122:
1117:
1112:
1103:
1086:
1081:
1076:
1071:
1062:
1057:
1052:
1047:
1030:
1025:
1020:
1011:
1002:
977:
968:
951:
946:
937:
932:
919:
913:
907:
902:
896:
894:
891:
890:
889:
882:
875:
850:
847:
831:stomach cancer
818:
815:
808:intermolecular
792:ubiquitination
775:
772:
758:of E3 ligases
756:F-box proteins
736:binding domain
719:
716:
693:ubiquitination
660:
657:
595:
594:Phosphodegrons
592:
532:
529:
509:ubiquitination
500:
497:
490:ubiquitylates
456:
453:
439:(APC) and the
431:
428:
389:to the target
354:
351:
300:
299:
294:
288:
287:
282:
276:
275:
270:
264:
263:
260:
256:
255:
251:
250:
242:
241:
238:
237:
232:
226:
225:
220:
214:
213:
208:
202:
201:
193:
192:
183:
177:
176:
165:
158:
157:
152:
146:
145:
140:
134:
133:
128:
122:
121:
116:
110:
109:
104:
98:
97:
92:
86:
85:
81:
80:
75:
69:
68:
63:
57:
56:
52:
51:
43:
35:
34:
26:
9:
6:
4:
3:
2:
4091:
4080:
4077:
4075:
4072:
4071:
4069:
4059:
4054:
4049:
4048:
4045:
4031:
4027:
4026:
4021:
4018:
4014:
4013:
4008:
4005:
4001:
4000:
3995:
3992:
3988:
3987:
3982:
3979:
3975:
3974:
3969:
3966:
3962:
3961:
3956:
3953:
3949:
3948:
3943:
3942:
3940:
3936:
3930:
3927:
3925:
3922:
3920:
3917:
3915:
3912:
3910:
3907:
3906:
3904:
3900:
3894:
3891:
3889:
3888:Enzyme family
3886:
3884:
3881:
3879:
3876:
3875:
3873:
3869:
3863:
3860:
3858:
3855:
3853:
3852:Cooperativity
3850:
3848:
3845:
3844:
3842:
3838:
3832:
3829:
3827:
3824:
3822:
3819:
3817:
3814:
3812:
3811:Oxyanion hole
3809:
3807:
3804:
3802:
3799:
3797:
3794:
3793:
3791:
3787:
3783:
3776:
3771:
3769:
3764:
3762:
3757:
3756:
3753:
3741:
3738:
3734:
3731:
3729:
3726:
3725:
3724:
3721:
3719:
3716:
3714:
3711:
3709:
3706:
3704:
3701:
3699:
3696:
3694:
3691:
3689:
3686:
3682:
3679:
3677:
3674:
3672:
3669:
3667:
3664:
3662:
3659:
3657:
3654:
3653:
3652:
3649:
3647:
3644:
3643:
3641:
3638:
3634:
3628:
3625:
3623:
3620:
3618:
3615:
3614:
3612:
3609:
3605:
3597:
3594:
3592:
3589:
3587:
3584:
3582:
3579:
3577:
3574:
3572:
3569:
3567:
3566:Phenylalanine
3564:
3562:
3559:
3557:
3554:
3552:
3549:
3547:
3544:
3542:
3539:
3537:
3534:
3532:
3529:
3527:
3524:
3522:
3519:
3517:
3514:
3512:
3509:
3507:
3504:
3502:
3499:
3497:
3494:
3493:
3492:
3489:
3488:
3486:
3483:
3479:
3474:
3470:
3466:
3459:
3454:
3452:
3447:
3445:
3440:
3439:
3436:
3420:
3417:
3416:
3413:
3410:
3408:
3405:
3403:
3400:
3398:
3395:
3393:
3390:
3388:
3385:
3382:
3378:
3375:
3373:
3370:
3368:
3365:
3363:
3360:
3359:
3357:
3353:
3345:
3342:
3340:
3337:
3335:
3332:
3330:
3327:
3326:
3324:
3323:
3318:
3315:
3314:
3312:
3311:
3306:
3303:
3301:
3298:
3297:
3295:
3294:
3292:
3290:(SUMOylation)
3288:
3284:
3281:
3277:
3273:
3267:
3264:
3262:
3259:
3257:
3254:
3253:
3250:
3247:
3245:
3242:
3240:
3236:
3233:
3232:
3227:
3224:
3222:
3219:
3217:
3214:
3212:
3209:
3207:
3204:
3202:
3199:
3198:
3197:
3193:
3192:
3187:
3184:
3182:
3179:
3177:
3174:
3172:
3169:
3167:
3164:
3161:
3158:
3156:
3153:
3151:
3148:
3146:
3143:
3141:
3138:
3136:
3133:
3131:
3128:
3126:
3123:
3121:
3118:
3116:
3113:
3111:
3108:
3106:
3103:
3101:
3098:
3096:
3093:
3091:
3088:
3086:
3083:
3081:
3078:
3076:
3073:
3071:
3068:
3066:
3063:
3061:
3058:
3056:
3053:
3051:
3048:
3046:
3043:
3041:
3038:
3036:
3033:
3031:
3028:
3027:
3026:
3022:
3021:
3016:
3013:
3011:
3008:
3006:
3003:
3001:
2998:
2996:
2993:
2991:
2988:
2986:
2983:
2981:
2978:
2976:
2973:
2972:
2971:
2967:
2966:
2964:
2960:
2956:
2950:
2947:
2945:
2942:
2941:
2939:
2937:
2933:
2921:
2918:
2916:
2913:
2912:
2911:
2908:
2906:
2903:
2901:
2898:
2897:
2895:
2891:
2883:
2880:
2878:
2875:
2873:
2870:
2868:
2862:
2860:
2854:
2853:
2852:
2849:
2848:
2843:
2840:
2838:
2835:
2833:
2830:
2828:
2825:
2823:
2820:
2818:
2815:
2813:
2810:
2808:
2805:
2803:
2800:
2798:
2795:
2793:
2790:
2788:
2785:
2783:
2780:
2779:
2778:
2775:
2774:
2769:
2766:
2764:
2761:
2759:
2756:
2754:
2751:
2749:
2746:
2744:
2741:
2739:
2736:
2734:
2731:
2729:
2726:
2724:
2721:
2719:
2716:
2714:
2711:
2709:
2706:
2704:
2701:
2699:
2696:
2694:
2691:
2689:
2686:
2684:
2681:
2679:
2676:
2675:
2674:
2671:
2670:
2667:
2663:
2660:
2658:
2655:
2653:
2650:
2648:
2645:
2644:
2642:
2640:
2635:
2631:
2628:
2626:
2621:
2617:
2613:
2606:
2601:
2599:
2594:
2592:
2587:
2586:
2583:
2577:
2574:
2571:
2568:
2564:
2561:
2559:
2555:
2551:
2548:
2545:
2544:
2532:
2528:
2523:
2518:
2515:(2): 263–74.
2514:
2510:
2506:
2499:
2491:
2487:
2483:
2479:
2475:
2471:
2464:
2456:
2452:
2448:
2444:
2439:
2434:
2430:
2426:
2422:
2418:
2414:
2407:
2399:
2395:
2391:
2387:
2383:
2379:
2375:
2371:
2364:
2356:
2352:
2348:
2344:
2341:(2): 107–12.
2340:
2336:
2328:
2320:
2316:
2311:
2306:
2301:
2296:
2293:(3): 786–93.
2292:
2288:
2284:
2277:
2275:
2266:
2262:
2257:
2252:
2248:
2244:
2241:(9): 629–43.
2240:
2236:
2232:
2225:
2217:
2213:
2208:
2203:
2198:
2193:
2189:
2185:
2181:
2174:
2166:
2162:
2158:
2154:
2150:
2146:
2142:
2138:
2131:
2123:
2119:
2115:
2111:
2106:
2101:
2097:
2093:
2089:
2085:
2081:
2074:
2066:
2062:
2058:
2054:
2050:
2046:
2043:(9): 563–80.
2042:
2038:
2031:
2023:
2019:
2014:
2009:
2005:
2001:
1997:
1993:
1989:
1982:
1974:
1970:
1966:
1962:
1958:
1954:
1947:
1940:
1938:
1936:
1927:
1923:
1918:
1913:
1909:
1905:
1901:
1897:
1893:
1886:
1878:
1874:
1870:
1866:
1862:
1858:
1854:
1850:
1843:
1835:
1831:
1826:
1821:
1817:
1813:
1810:(9): 679–90.
1809:
1805:
1801:
1794:
1786:
1782:
1778:
1774:
1770:
1766:
1759:
1757:
1755:
1753:
1751:
1742:
1738:
1734:
1730:
1726:
1722:
1718:
1714:
1710:
1706:
1699:
1691:
1687:
1683:
1679:
1675:
1671:
1664:
1656:
1652:
1648:
1644:
1640:
1636:
1632:
1628:
1621:
1619:
1617:
1615:
1606:
1602:
1598:
1594:
1591:(3): 531–44.
1590:
1586:
1579:
1571:
1567:
1562:
1557:
1553:
1549:
1545:
1541:
1537:
1530:
1522:
1518:
1514:
1510:
1506:
1502:
1499:(5): 369–81.
1498:
1494:
1487:
1485:
1483:
1474:
1470:
1465:
1460:
1456:
1452:
1448:
1441:
1433:
1427:
1423:
1416:
1414:
1405:
1401:
1396:
1391:
1387:
1383:
1379:
1375:
1371:
1364:
1356:
1352:
1347:
1342:
1337:
1332:
1328:
1324:
1320:
1316:
1312:
1305:
1297:
1293:
1289:
1285:
1281:
1277:
1270:
1262:
1258:
1254:
1250:
1246:
1242:
1235:
1227:
1223:
1218:
1213:
1209:
1205:
1202:(2): 184–92.
1201:
1197:
1193:
1186:
1182:
1173:
1170:
1168:
1165:
1163:
1160:
1158:
1155:
1154:
1145:
1142:
1140:
1137:
1135:
1131:
1128:
1126:
1123:
1121:
1118:
1116:
1113:
1111:
1107:
1104:
1102:
1098:
1094:
1090:
1087:
1085:
1082:
1080:
1077:
1075:
1072:
1070:
1066:
1063:
1061:
1058:
1056:
1053:
1051:
1048:
1046:
1042:
1038:
1034:
1031:
1029:
1026:
1024:
1021:
1019:
1015:
1012:
1010:
1006:
1003:
1001:
997:
993:
989:
985:
981:
978:
976:
972:
969:
967:
963:
959:
955:
952:
950:
947:
945:
941:
938:
936:
933:
931:
927:
923:
920:
917:
914:
911:
908:
906:
903:
901:
898:
897:
887:
883:
880:
876:
873:
869:
865:
861:
857:
853:
852:
846:
844:
840:
836:
832:
828:
824:
814:
812:
809:
805:
801:
797:
793:
789:
785:
781:
771:
769:
765:
761:
757:
753:
749:
745:
744:glycoproteins
741:
737:
733:
729:
725:
715:
713:
709:
705:
702:
698:
694:
690:
686:
682:
678:
674:
670:
666:
656:
654:
650:
646:
642:
638:
634:
630:
626:
622:
618:
614:
610:
600:
591:
589:
585:
581:
577:
573:
569:
566:amino acids (
565:
561:
557:
553:
549:
545:
541:
537:
528:
526:
522:
518:
514:
510:
506:
496:
493:
489:
484:
482:
478:
474:
469:
461:
452:
450:
446:
442:
438:
427:
425:
420:
416:
411:
407:
402:
400:
396:
392:
388:
384:
380:
376:
372:
368:
359:
350:
348:
345:, as well as
344:
340:
335:
331:
327:
323:
319:
315:
311:
307:
298:
295:
293:
289:
286:
283:
281:
277:
274:
271:
269:
265:
261:
257:
252:
247:
236:
233:
231:
227:
224:
221:
219:
215:
212:
209:
207:
203:
198:
194:
191:
187:
184:
182:
181:Gene Ontology
178:
175:
172:
169:
166:
163:
159:
156:
153:
151:
147:
144:
141:
139:
135:
132:
129:
127:
123:
120:
119:NiceZyme view
117:
115:
111:
108:
105:
103:
99:
96:
93:
91:
87:
82:
79:
76:
74:
70:
67:
64:
62:
58:
53:
48:
41:
36:
31:
19:
4025:Translocases
4022:
4009:
3996:
3983:
3970:
3960:Transferases
3957:
3944:
3801:Binding site
3713:GMP synthase
3650:
3287:SUMO protein
3195:
2512:
2508:
2498:
2473:
2469:
2463:
2420:
2416:
2406:
2373:
2369:
2363:
2338:
2334:
2327:
2290:
2286:
2238:
2234:
2224:
2187:
2183:
2173:
2143:(4): 293–6.
2140:
2136:
2130:
2087:
2083:
2073:
2040:
2036:
2030:
1995:
1992:EMBO Reports
1991:
1981:
1956:
1952:
1899:
1895:
1885:
1852:
1848:
1842:
1807:
1803:
1793:
1768:
1764:
1708:
1704:
1698:
1673:
1669:
1663:
1633:(5): 520–8.
1630:
1626:
1588:
1584:
1578:
1543:
1539:
1529:
1496:
1492:
1457:(1): 71–82.
1454:
1450:
1440:
1421:
1377:
1373:
1363:
1321:(1): e1487.
1318:
1314:
1304:
1279:
1275:
1269:
1244:
1240:
1234:
1199:
1195:
1185:
871:
867:
863:
859:
839:liver cancer
820:
796:TRF1 protein
790:function to
777:
721:
701:phytohormone
685:hydroxylated
662:
629:binding site
606:
562:) and bulky
534:
502:
485:
470:
466:
433:
403:
377:to activate
364:
309:
305:
303:
107:BRENDA entry
3796:Active site
3381:neddylation
2647:Hsp10/GroES
2639:Chaperonins
1959:: 101–110.
1676:: 395–447.
1282:: 387–414.
886:HECT domain
866:nteresting
788:biochemical
766:containing
564:hydrophobic
473:endocytosis
441:SCF complex
415:HECT domain
383:conjugation
280:OPM protein
254:Identifiers
95:IntEnz view
78:74812-49-0
55:Identifiers
4068:Categories
3999:Isomerases
3973:Hydrolases
3840:Regulation
3586:Tryptophan
3561:Methionine
3546:Isoleucine
3506:Asparagine
2673:Hsp40/DnaJ
2620:Chaperones
1902:: 261–89.
1247:: 425–79.
1178:References
811:beta sheet
712:repressors
544:N-end rule
540:N-terminus
525:amino acid
481:SH2 domain
401:proteins.
339:proteasome
292:Membranome
164:structures
131:KEGG entry
3878:EC number
3581:Threonine
3541:Histidine
3531:Glutamine
3526:Glutamate
3511:Aspartate
2959:Ubiquitin
2905:Clusterin
2476:: 15–30.
1162:Ubiquitin
806:) via an
669:molecules
653:phosphate
625:threonine
548:half-life
531:N-degrons
505:substrate
410:thioester
399:substrate
387:ubiquitin
379:ubiquitin
326:ubiquitin
322:ubiquitin
84:Databases
3902:Kinetics
3826:Cofactor
3789:Activity
3591:Tyrosine
3516:Cysteine
3501:Arginine
3475:6.1-6.3)
3239:Ataxin 3
2576:6.3.2.19
2550:Archived
2490:16250895
2455:85527795
2447:30919022
2438:11105231
2398:16385927
2390:25119589
2355:25415135
2319:25624711
2265:21863050
2216:30837888
2165:41227590
2157:24699076
2122:20914281
2114:11292861
2057:23969844
2022:26268526
1973:28130986
1926:22524314
1877:10555455
1869:22016057
1834:18698327
1785:28375744
1741:43124248
1733:14671306
1690:12651740
1655:19237120
1647:21540891
1570:15520277
1521:19594293
1513:16633365
1473:14532004
1404:22389392
1355:18213395
1315:PLOS ONE
1296:23495935
1226:22266821
1151:See also
849:Examples
800:telomere
687:. Under
649:arginine
617:tyrosine
611:such as
513:proteins
406:cysteine
235:proteins
223:articles
211:articles
168:RCSB PDB
66:2.3.2.27
4058:Biology
4012:Ligases
3782:Enzymes
3571:Proline
3551:Leucine
3536:Glycine
3496:Alanine
3469:ligases
3465:Enzymes
3162:(CDC34)
2531:8706131
2310:4299330
2256:3542975
2207:6389600
2190:: 104.
2092:Bibcode
2084:Science
2013:4576978
1917:3610525
1825:2606094
1713:Bibcode
1705:Science
1605:3041007
1395:3381717
1346:2198940
1323:Bibcode
1261:9759494
1217:3880865
780:degrons
768:glycans
764:mannose
746:of the
689:hypoxia
681:proline
588:degrons
521:degrons
391:protein
369:and an
343:cyclins
314:protein
312:) is a
190:QuickGO
155:profile
138:MetaCyc
73:CAS no.
27:Protein
4074:EC 6.3
4044:Portal
3986:Lyases
3656:Cullin
3596:Valine
3576:Serine
3556:Lysine
3206:Cullin
2569:(MeSH)
2529:
2488:
2453:
2445:
2435:
2396:
2388:
2353:
2317:
2307:
2263:
2253:
2214:
2204:
2163:
2155:
2120:
2112:
2065:149598
2063:
2055:
2020:
2010:
1971:
1924:
1914:
1875:
1867:
1832:
1822:
1783:
1739:
1731:
1688:
1653:
1645:
1603:
1568:
1561:525538
1558:
1519:
1511:
1471:
1428:
1402:
1392:
1353:
1343:
1294:
1259:
1224:
1214:
1139:Parkin
1084:TRIP12
1079:TOPORS
1069:SMURF2
1065:SMURF1
1050:RANBP2
1028:PRPF19
1018:NEDD4L
966:HECTD4
962:HECTD3
958:HECTD2
954:HECTD1
935:LNXp80
918:(EDD1)
862:eally
837:, and
825:, and
665:oxygen
635:, the
621:serine
449:Cullin
334:lysine
259:Symbol
218:PubMed
200:Search
186:AmiGO
174:PDBsum
114:ExPASy
102:BRENDA
90:IntEnz
61:EC no.
3938:Types
3666:UBE3A
3397:ATG12
3387:FAT10
3377:NEDD8
3362:ISG15
3355:Other
3344:PIAS4
3339:PIAS3
3334:PIAS2
3329:PIAS1
3279:(UBL)
3261:BIRC6
3221:FANCL
2893:Other
2882:TRAP1
2851:Hsp90
2777:Hsp70
2666:GroEL
2662:HSP60
2657:Hsp47
2652:Hsp27
2451:S2CID
2394:S2CID
2161:S2CID
2118:S2CID
2061:S2CID
1949:(PDF)
1873:S2CID
1737:S2CID
1651:S2CID
1517:S2CID
1144:MKRN1
1115:UBOX5
1110:UBE4B
1106:UBE4A
1101:UBE3D
1097:UBE3C
1093:UBE3B
1089:UBE3A
1074:STUB1
1045:PIAS4
1041:PIAS3
1037:PIAS2
1033:PIAS1
1023:PPIL2
1014:NEDD4
1005:HUWE1
1000:HERC6
996:HERC5
992:HERC4
988:HERC3
984:HERC2
980:HERC1
975:HECW2
971:HECW1
949:HACE1
944:CBLL1
912:(APC)
823:BRCA1
804:FBXO4
732:yeast
726:), a
704:auxin
637:F-box
615:of a
332:to a
150:PRIAM
4030:list
4023:EC7
4017:list
4010:EC6
4004:list
3997:EC5
3991:list
3984:EC4
3978:list
3971:EC3
3965:list
3958:EC2
3952:list
3945:EC1
3681:UBR1
3671:Mdm2
3412:UBL5
3402:FUB1
3392:ATG8
3372:UFM1
3367:URM1
3317:UBC9
3305:SAE2
3300:SAE1
3266:UFC1
3256:ATG3
3249:CYLD
3244:USP6
3226:UBR1
3216:MDM2
3015:SAE1
3010:NAE1
3005:ATG7
3000:UBA7
2995:UBA6
2990:UBA5
2985:UBA3
2980:UBA2
2975:UBA1
2920:SMN2
2915:SMN1
2558:PDBe
2527:PMID
2509:Cell
2486:PMID
2443:PMID
2386:PMID
2351:PMID
2315:PMID
2261:PMID
2212:PMID
2153:PMID
2110:PMID
2053:PMID
2018:PMID
1969:PMID
1922:PMID
1865:PMID
1830:PMID
1781:PMID
1729:PMID
1686:PMID
1643:PMID
1601:PMID
1566:PMID
1509:PMID
1469:PMID
1451:Cell
1426:ISBN
1400:PMID
1351:PMID
1292:PMID
1257:PMID
1222:PMID
1157:ERAD
1134:WWP2
1130:WWP1
1120:UBR5
1060:RBX1
1055:RNF4
1009:ITCH
940:CBX4
930:RING
926:CUL5
922:SOCS
916:UBR5
905:mdm2
879:Sic1
856:RING
752:Fbs1
748:ERAD
647:its
633:FBW7
603:2ovr
517:cell
488:MDM2
445:Skp1
381:for
285:4v6p
230:NCBI
171:PDBe
126:KEGG
47:4a4c
3637:6.3
3608:6.2
3482:6.1
3407:MUB
3211:CBL
3201:VHL
3194:E3
3023:E2
2968:E1
2837:12A
2768:C19
2763:C14
2758:C13
2753:C11
2748:C10
2703:B11
2556:at
2517:doi
2478:doi
2433:PMC
2425:doi
2378:doi
2343:doi
2305:PMC
2295:doi
2251:PMC
2243:doi
2202:PMC
2192:doi
2145:doi
2100:doi
2088:292
2045:doi
2008:PMC
2000:doi
1961:doi
1912:PMC
1904:doi
1857:doi
1820:PMC
1812:doi
1773:doi
1721:doi
1709:302
1678:doi
1635:doi
1593:doi
1589:194
1556:PMC
1548:doi
1501:doi
1459:doi
1455:115
1390:PMC
1382:doi
1378:125
1341:PMC
1331:doi
1284:doi
1249:doi
1212:PMC
1204:doi
1125:VHL
900:E3A
870:ew
760:SCF
708:SCF
683:is
641:SCF
623:or
584:Ile
580:Leu
576:Tyr
572:Trp
568:Phe
560:His
556:Lys
552:Arg
511:of
492:p53
424:p21
375:ATP
297:240
273:471
206:PMC
162:PDB
4070::
3733:II
3473:EC
3237::
3181:V2
3176:V1
3166:R2
3160:R1
3155:Q2
3150:Q1
3130:L6
3125:L4
3120:L3
3115:L2
3110:L1
3100:J2
3095:J1
3080:G2
3075:G1
3070:E3
3065:E2
3060:E1
3055:D3
3050:D2
3045:D1
2877:ER
2842:14
2807:4L
2792:1L
2787:1B
2782:1A
2743:C7
2738:C6
2733:C5
2728:C3
2723:C1
2718:B9
2713:B6
2708:B4
2698:B2
2693:B1
2688:A3
2683:A2
2678:A1
2573:EC
2525:.
2513:86
2511:.
2507:.
2484:.
2474:41
2472:.
2449:.
2441:.
2431:.
2421:76
2419:.
2415:.
2392:.
2384:.
2374:35
2372:.
2349:.
2339:34
2337:.
2313:.
2303:.
2291:21
2289:.
2285:.
2273:^
2259:.
2249:.
2239:11
2237:.
2233:.
2210:.
2200:.
2188:10
2186:.
2182:.
2159:.
2151:.
2141:21
2139:.
2116:.
2108:.
2098:.
2086:.
2082:.
2059:.
2051:.
2041:14
2039:.
2016:.
2006:.
1996:16
1994:.
1990:.
1967:.
1957:44
1955:.
1951:.
1934:^
1920:.
1910:.
1900:81
1898:.
1894:.
1871:.
1863:.
1853:12
1851:.
1828:.
1818:.
1806:.
1802:.
1779:.
1769:86
1767:.
1749:^
1735:.
1727:.
1719:.
1707:.
1684:.
1674:72
1672:.
1649:.
1641:.
1631:18
1629:.
1613:^
1599:.
1587:.
1564:.
1554:.
1544:18
1542:.
1538:.
1515:.
1507:.
1495:.
1481:^
1467:.
1453:.
1449:.
1412:^
1398:.
1388:.
1376:.
1372:.
1349:.
1339:.
1329:.
1317:.
1313:.
1290:.
1280:82
1278:.
1255:.
1245:67
1243:.
1220:.
1210:.
1200:19
1198:.
1194:.
1132:,
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