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Ligand S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine

Basic Ligand Information

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (4 results)

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Show Natural Substrate (4 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.3.2.23

S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine

734357, 737299, 736181, 737253, 735453, 758713, 759030, 759535, 758749, 759768, 759820, 758741, 758765, 760168, 759600, 760224, 759492, 758642, 759478, 759764, 736063, 725526, 759124

-

2.3.2.25

S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N-terminal-amino acid = [E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[acceptor protein]

759030, 759630, 758638, 759848, 759122

-

2.3.2.25

S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [huntingtin]-N-terminal-amino acid = [E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[huntingtin]

759848

-

2.3.2.25

S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [NLRP1B]-N-terminal-amino acid = [E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[NLRP1B]

759122

-

2.3.2.25

3 entries

In Vivo Product in Enzyme-catalyzed Reactions (1 result)

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Show Natural Product (1 entry)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

6.2.1.45

ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine

0

-

Substrate in Enzyme-catalyzed Reactions (26 results)

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Show Substrate (26 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.3.2.23

S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine

734357, 737299, 736181, 737253, 735453, 758713, 759030, 759535, 758749, 759768, 759820, 758741, 758765, 760168, 759600, 760224, 759492, 758642, 759478, 759764, 736063, 725526, 759124

-

2.3.2.24

S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-L-lysine

734117

-

2.3.2.24

S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + N6-(ubiquitin)n-[E2 enzyme CDC34]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + N6-(ubiquitin)(n+1)-[E2 enzyme CDC34]-L-lysine

734679

-

2.3.2.24

S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + N6-(ubiquitin)n-[histone H2A]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + N6-(ubiquitin)(n+1)-[histone H2A]-L-lysine

734838

-

2.3.2.24

S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + S-(ubiquitin)n-Ube2g2-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-(ubiquitin)(n+1)-Ube2g2-L-cysteine

733857

-

2.3.2.24

S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + S-(ubiquitin)n-Ube2K-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-(ubiquitin)(n+1)-Ube2K-L-cysteine

733857

-

2.3.2.24

S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + UbcH10-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-monoubiquitinyl-UbcH10-L-cysteine

733857

-

2.3.2.24

S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + Ube2g2-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-monoubiquitinyl-Ube2g2-L-cysteine

733857

-

2.3.2.24

S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + Ube2K-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-monoubiquitinyl-Ube2K-L-cysteine

733857

-

2.3.2.24

S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [cytochrome c]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[cytochrome c]-L-lysine lysine

734117

-

2.3.2.24

S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 enzyme CDC34]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[E2 enzyme CDC34]-L-lysine

734679

-

2.3.2.24

S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [histone H1]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[histone H1]-L-lysine

734119

-

2.3.2.24

S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [histone H2A]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[histone H2A]-L-lysine

734117, 734838, 734119

-

2.3.2.24

S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [histone H2B]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[histone H2B]-L-lysine

734679, 734119

-

2.3.2.24

S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [histone H2B]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[histone H2B]-L-lysine lysine

734117

-

2.3.2.24

S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [histone H3]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[histone H3]-L-lysine

734119

-

2.3.2.24

S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [histone H4]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + N6-monoubiquitinyl-[histone H4]-L-lysine

734119

-

2.3.2.25

S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [acceptor protein]-N-terminal-amino acid = [E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[acceptor protein]

759030, 759630, 758638, 759848, 759122

-

2.3.2.25

S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [alpha-synuclein]-N-terminal-amino acid = [E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[alpha-synuclein]

759630

-

2.3.2.25

S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [huntingtin]-N-terminal-amino acid = [E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[huntingtin]

759848

-

2.3.2.25

S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [NLRP1B]-N-terminal-amino acid = [E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[NLRP1B]

759122

-

2.3.2.25

S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [NLRP1B]-N-terminal-leucine248 = [E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[NLRP1B]

759122

-

2.3.2.25

S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [Rnf4]-N-terminal-amino acid = [E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[Rnf4]

758638

-

2.3.2.25

S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [SUMO-2]-N-terminal-amino acid = [E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[SUMO-2]

733291

-

2.3.2.25

S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [tau tetra-repeat domain]-N-terminal-Lys18 = [E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[tau tetra-repeat domain]

759630

-

2.3.2.25

S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [Ube2W]-N-terminal-amino acid = [E1 ubiquitin-activating enzyme]-L-cysteine + N-terminal-ubiquitinyl-[Ube2W]

733291

-

2.3.2.24

16 entries

2.3.2.25

9 entries

Product in Enzyme-catalyzed Reactions (1 result)

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Show Product (1 entry)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

6.2.1.45

ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine

0

-

Enzyme Kinetic Parameters

K_M Value (1 result)

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Show KM Value (1 entry)

EC NUMBER

KM VALUE [MM]

KM VALUE MAXIMUM [MM]

COMMENTARY

LITERATURE

2.3.2.23

1

-

about, pH 7.5, temperature not specified in the publication

759768

References & Links

Literature References (33)

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Show Reference (33 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

725526

23696636

The ubiquitin-conjugating enzyme (E2) Ube2w ubiquitinates the N terminus of substrates

2013

Scaglione, K.M.; Basrur, V.; Ashraf, N.S.; Konen, J.R.; Elenitoba-Johnson, K.S.; Todi, S.V.; Paulson, H.L.

J. Biol. Chem.

288

18784-18788

733291

23560854

Ube2W conjugates ubiquitin to alpha-amino groups of protein N-termini

2013

Tatham, M.H.; Plechanovova, A.; Jaffray, E.G.; Salmen, H.; Hay, R.T.

Biochem. J.

453

137-145

733857

22079664

Assembly of different length of polyubiquitins on the catalytic cysteine of E2 enzymes without E3 ligase; a novel application of non-reduced/reduced 2-dimensional electrophoresis

2011

Shin, D.Y.; Lee, H.; Park, E.S.; Yoo, Y.J.

FEBS Lett.

585

3959-3963

734117

2981864

Functional heterogeneity of ubiquitin carrier proteins

1985

Pickart, C.M.; Rose, I.A.

J. Biol. Chem.

260

1573-1581

734119

2843516

Functional diversity among putative E2 isozymes in the mechanism of ubiquitin-histone ligation

1988

Haas, A.L.; Bright, P.M.; Jackson, V.E.

J. Biol. Chem.

263

13268-13275

734357

24928900

A specific subset of E2 ubiquitin-conjugating enzymes regulate Parkin activation and mitophagy differently

2014

Fiesel, F.; Moussaud-Lamodiere, E.; Ando, M.; Springer, W.

J. Cell Sci.

127

3488-3504

734679

7862115

Novel CDC34 (UBC3) ubiquitin-conjugating enzyme mutants obtained by charge-to-alanine scanning mutagenesis

1995

Pitluk, Z.W.; McDonough, M.; Sangan, P.; Gonda, D.K.

Mol. Cell. Biol.

15

1210-1219

734838

15480785

Molecular cloning and characterization of cDNA encoding a ubiquitin-conjugating enzyme from Clonorchis sinensis

2004

Song, L.; Chen, S.; Yu, X.; Wu, Z.; Xu, J.; Yang, G.; Zheng, N.; Hu, X.; Guo, L.; Dai, J.; Xu, J.; Ji, C.; Gu, S.; Ying, K.

Parasitol. Res.

94

227-232

735453

23918348

Serine/threonine kinases and E2-ubiquitin conjugating enzymes in Planctomycetes: unexpected findings

2013

Arcas, A.; Cases, I.; Rojas, A.

Antonie van Leeuwenhoek

104

509-520

736063

26283706

Spectrin's chimeric E2/E3 enzymatic activity

2015

Goodman, S.; Petrofes Chapa, R.; Zimmer, W.

Exp. Biol. Med.

240

1039-1049

736181

26927519

A newly discovered ubiquitin-conjugating enzyme E2 correlated with the cryogenic autolysis of Volvariella volvacea

2016

Gong, M.; Wang, H.; Chen, M.; Bao, D.; Zhu, Q.; Tan, Q.

Gene

583

58-63

737253

26525192

Biochemical and structural characterization of a novel ubiquitin-conjugating enzyme E2 from Agrocybe aegeria reveals Ube2w family-specific properties

2015

Qi, C.; Li, D.F.; Feng, L.; Hou, Y.; Sun, H.; Wang, D.C.; Liu, W.

Sci. Rep.

5

16056

737299

26135843

Cellular Ubc2/Rad6 E2 ubiquitin-conjugating enzyme facilitates tombusvirus replication in yeast and plants

2015

Imura, Y.; Molho, M.; Chuang, C.; Nagy, P.D.

Virology

484

265-275

758638

31710394

UBE2W down-regulation promotes cell apoptosis and correlates with hypospermatogenesis

2020

Lei, B.; Xie, L.; Zhang, S.; Lv, D.; Shu, F.; Deng, Y.

Andrologia

52

e13474

758642

27038327

Insights into the allosteric inhibition of the SUMO E2 enzyme Ubc9

2016

Hewitt, W.M.; Lountos, G.T.; Zlotkowski, K.; Dahlhauser, S.D.; Saunders, L.B.; Needle, D.; Tropea, J.E.; Zhan, C.; Wei, G.; Ma, B.; Nussinov, R.; Waugh, D.S.; Schneekloth, J.S.

Angew. Chem. Int. Ed. Engl.

55

5703-5707

758713

30658189

Differential use of E2 ubiquitin conjugating enzymes for regulated degradation of the rate-limiting enzymes HMGCR and SQLE in cholesterol biosynthesis

2019

Tan, J.M.E.; Cook, E.C.L.; van den Berg, M.; Scheij, S.; Zelcer, N.; Loregger, A.

Atherosclerosis

281

137-142

758741

26718580

DNA damage-induced foci of E2 ubiquitin-conjugating enzyme are detectable upon co-transfection with an interacting E3 ubiquitin ligase

2016

Wang, D.; Tian, Y.; Wei, D.; Jing, Y.; Niu, H.; Xie, K.; Song, Y.

Biochem. Genet.

54

147-157

758749

27729585

Mechanism and disease association of E2-conjugating enzymes lessons from UBE2T and UBE2L3

2016

Alpi, A.F.; Chaugule, V.; Walden, H.

Biochem. J.

473

3401-3419

758765

30449727

Ubiquitin-conjugating enzyme E2 B regulates the ubiquitination of O6-methylguanine-DNA methyltransferase and BCNU sensitivity in human nasopharyngeal carcinoma cells

2018

Hsu, S.H.; Chen, S.H.; Kuo, C.C.; Chang, J.Y.

Biochem. Pharmacol.

158

327-338

759030

27002219

E2 enzymes more than just middle men

2016

Stewart, M.D.; Ritterhoff, T.; Klevit, R.E.; Brzovic, P.S.

Cell Res.

26

423-440

759122

31268597

The N-end rule ubiquitin ligase UBR2 mediates NLRP1B inflammasome activation by anthrax lethal toxin

2019

Xu, H.; Shi, J.; Gao, H.; Liu, Y.; Yang, Z.; Shao, F.; Dong, N.

EMBO J.

38

e101996

759124

31523916

The ubiquitin E2 enzyme UBE2QL1 mediates lysophagy

2019

Mizushima, N.

EMBO Rep.

20

e49104

759478

26555268

Structure of UBE2Z enzyme provides functional insight into specificity in the FAT10 protein conjugation machinery

2016

Schelpe, J.; Monte, D.; Dewitte, F.; Sixma, T.; Rucktooa, P.

J. Biol. Chem.

291

630-639

759492

29414787

Ubiquitin-conjugating enzyme E2 D1 (Ube2D1) mediates lysine-independent ubiquitination of the E3 ubiquitin ligase March-I

2018

Lei, L.; Bandola-Simon, J.; Roche, P.A.

J. Biol. Chem.

293

3904-3912

759535

28743740

Multiple E2 ubiquitin-conjugating enzymes regulate human cytomegalovirus US2-mediated immunoreceptor downregulation

2017

van de Weijer, M.L.; Schuren, A.B.C.; van den Boomen, D.J.H.; Mulder, A.; Claas, F.H.J.; Lehner, P.J.; Lebbink, R.J.; Wiertz, E.J.H.J.

J. Cell Sci.

130

2883-2892

759600

28437106

Allosteric targeting of the Fanconi anemia ubiquitin-conjugating enzyme Ube2T by fragment screening

2017

Morreale, F.E.; Bortoluzzi, A.; Chaugule, V.K.; Arkinson, C.; Walden, H.; Ciulli, A.

J. Med. Chem.

60

4093-4098

759630

31518613

N-terminal ubiquitination of amyloidogenic proteins triggers removal of their oligomers by the proteasome holoenzyme

2020

Ye, Y.; Klenerman, D.; Finley, D.

J. Mol. Biol.

432

585-596

759764

27570074

Posttranscriptional regulation of glycoprotein quality control in the endoplasmic reticulum is controlled by the E2 Ub-conjugating enzyme UBC6e

2016

Hagiwara, M.; Ling, J.; Koenig, P.A.; Ploegh, H.L.

Mol. Cell

63

753-767

759768

27044868

Mechanism of lysine 48 selectivity during polyubiquitin chain formation by the Ube2R1/2 ubiquitin-conjugating enzyme

2016

Hill, S.; Harrison, J.S.; Lewis, S.M.; Kuhlman, B.; Kleiger, G.

Mol. Cell. Biol.

36

1720-1732

759820

31341161

Structural insights into E1 recognition and the ubiquitin-conjugating activity of the E2 enzyme Cdc34

2019

Williams, K.M.; Qie, S.; Atkison, J.H.; Salazar-Arango, S.; Alan Diehl, J.; Olsen, S.K.

Nat. Commun.

10

3296

759848

28986324

The ubiquitin conjugating enzyme Ube2W regulates solubility of the Huntingtons disease protein, huntingtin

2018

Wang, B.; Zeng, L.; Merillat, S.A.; Fischer, S.; Ochaba, J.; Thompson, L.M.; Barmada, S.J.; Scaglione, K.M.; Paulson, H.L.

Neurobiol. Dis.

109

127-136

760168

29725124

Active site gate dynamics modulate the catalytic activity of the ubiquitination enzyme E2-25K

2018

Rout, M.K.; Lee, B.L.; Lin, A.; Xiao, W.; Spyracopoulos, L.

Sci. Rep.

8

7002

760224

27020591

Ubiquitin-conjugating enzyme E2T is an independent prognostic factor and promotes gastric cancer progression

2016

Yu, H.; Xiang, P.; Pan, Q.; Huang, Y.; Xie, N.; Zhu, W.

Tumour Biol.

37

11723-11732

Links to other databases for S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine

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Show Links (1 entry)