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

Basic Ligand Information

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Roles as Enzyme Ligand

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

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Show Natural Substrate (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

735079, 733442, 735013, 735041, 733931, 744655, 733532, 744190, 745863, 745858, 744237, 745952, 733043, 760342, 760825, 734395

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In Vivo Product in Enzyme-catalyzed Reactions (9 results)

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Show Natural Product (9 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

0

-

2.3.2.24

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

0

-

2.3.2.24

[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [AMPKalpha2]-L-lysine48 = [E1 ubiquitin-activating enzyme]-L-cysteine + [AMPKalpha2]-N6-monoubiquitinyl-L-lysine48

0

-

2.3.2.24

[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [BAP1]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + [BAP1]-N6-monoubiquitinyl-L-lysine

0

-

2.3.2.24

[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [BMAL1]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + [BMAL1]-N6-monoubiquitinyl-L-lysine

0

-

2.3.2.24

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

0

-

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]

0

-

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]

0

-

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]

0

-

2.3.2.24

5 entries

2.3.2.25

3 entries

Substrate in Enzyme-catalyzed Reactions (1 result)

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Show Substrate (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

735079, 733442, 735013, 735041, 733931, 744655, 733532, 744190, 745863, 745858, 744237, 745952, 733043, 760342, 760825, 734395

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Product in Enzyme-catalyzed Reactions (36 results)

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Show Product (36 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

0

-

2.3.2.24

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

0

-

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

0

-

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

0

-

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

0

-

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

0

-

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

0

-

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

0

-

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

0

-

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

0

-

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

0

-

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

0

-

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

0

-

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

0

-

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

0

-

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

0

-

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

0

-

2.3.2.24

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

0

-

2.3.2.24

[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [AMPKalpha2]-L-lysine48 = [E1 ubiquitin-activating enzyme]-L-cysteine + [AMPKalpha2 ]-N6-monoubiquitinyl-L-lysine48

0

-

2.3.2.24

[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [AMPKalpha2]-L-lysine48 = [E1 ubiquitin-activating enzyme]-L-cysteine + [AMPKalpha2]-N6-monoubiquitinyl-L-lysine48

0

-

2.3.2.24

[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [BAP1]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + [BAP1]-N6-monoubiquitinyl-L-lysine

0

-

2.3.2.24

[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [BMAL1]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + [BMAL1]-N6-monoubiquitinyl-L-lysine

0

-

2.3.2.24

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

0

-

2.3.2.24

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

0

-

2.3.2.24

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

0

-

2.3.2.24

[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [SMAD6]-L-lysine = [E1 ubiquitin-activating enzyme]-L-cysteine + [SMAD6]-N6-monoubiquitinyl-L-lysine

0

-

2.3.2.24

[E1 ubiquitin-activating enzyme]-S-ubiquitinyl-L-cysteine + [TRAF6]-L-lysine63 = [E1 ubiquitin-activating enzyme]-L-cysteine + [TRAF6]-N6-monoubiquitinyl-L-lysine63

0

-

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]

0

-

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]

0

-

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]

0

-

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]

0

-

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]

0

-

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]

0

-

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]

0

-

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]

0

-

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]

0

-

2.3.2.24

26 entries

2.3.2.25

9 entries

Enzyme Kinetic Parameters

References & Links

Literature References (16)

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Show Reference (16 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

733043

22498829

The ubiquitin-activating enzyme (E1) of the early-branching eukaryote Giardia intestinalis shows unusual proteolytic modifications and play important roles during encystation

2012

Nino, C.A.; Prucca, C.G.; Chaparro, J.; Lujan, H.D.; Wasserman, M.

Acta Trop.

123

39-46

733442

24637489

Construction of a mouse Aos1-Uba2 chimeric SUMO-E1 enzyme, mAU, and its expression in baculovirus-insect cells

2014

Nakayama, T.; Yuasa, E.; Kanemaru, A.; Saito, M.; Saitoh, H.

Bioengineered

5

133-137

733532

25209502

Expression, purification, and crystal structure of N-terminal domains of human ubiquitin-activating enzyme (E1)

2014

Xie, S.T.

Biosci. Biotechnol. Biochem.

78

1542-1549

733931

23154060

Molecular characterization and expression analysis of ubiquitin-activating enzyme E1 gene in Citrus reticulata

2013

Miao, H.X.; Qin, Y.H.; Ye, Z.X.; Hu, G.B.

Gene

513

249-259

734395

-

The role of ginsenosides in inhibiting ubiquitin activating enzyme (E1) activity

2014

Chang, T.; Huang, Y.; Ou, Y.

J. Funct. Foods

7

462-470

735013

25768649

Conjugation of the ubiquitin activating enzyme UBE1 with the ubiquitin-like modifier FAT10 targets it for proteasomal degradation

2015

Bialas, J.; Groettrup, M.; Aichem, A.

PLoS ONE

10

e0120329

735041

22279528

Largazole and its derivatives selectively inhibit ubiquitin activating enzyme (E1)

2012

Ungermannova, D.; Parker, S.J.; Nasveschuk, C.G.; Wang, W.; Quade, B.; Zhang, G.; Kuchta, R.D.; Phillips, A.J.; Liu, X.

PLoS ONE

7

e29208

735079

23382794

Mutation in E1, the ubiquitin activating enzyme, reduces Drosophila lifespan and results in motor impairment

2013

Liu, H.Y.; Pfleger, C.M.

PLoS ONE

8

e32835

744190

26919560

The ubiquitin-activating enzyme E1 as a novel therapeutic target for the treatment of restenosis

2016

Qin, Z.; Cui, B.; Jin, J.; Song, M.; Zhou, B.; Guo, H.; Qian, D.; He, Y.; Huang, L.

Atherosclerosis

247

142-153

744237

27569286

LMO2 blocks the UBA6-USE1 interaction and downstream FAT10ylation by targeting the ubiquitin fold domain of UBA6

2016

Wu, C.; Liu, Y.; Gu, X.; Zhu, T.; Yang, S.; Sun, W.

Biochem. Biophys. Res. Commun.

478

1442-1448

744655

27653677

Trans-binding mechanism of ubiquitin-like protein activation revealed by a UBA5-UFM1 complex

2016

Oweis, W.; Padala, P.; Hassouna, F.; Cohen-Kfir, E.; Gibbs, D.R.; Todd, E.A.; Berndsen, C.E.; Wiener, R.

Cell Rep.

16

3113-3120

745858

27550514

A MUB E2 structure reveals E1 selectivity between cognate ubiquitin E2s in eukaryotes

2016

Lu, X.; Malley, K.R.; Brenner, C.C.; Koroleva, O.; Korolev, S.; Downes, B.P.

Nat. Commun.

7

12580

745863

28134249

Orthogonal ubiquitin transfer identifies ubiquitination substrates under differential control by the two ubiquitin activating enzymes

2017

Liu, X.; Zhao, B.; Sun, L.; Bhuripanyo, K.; Wang, Y.; Bi, Y.; Davuluri, R.; Duong, D.; Nanavati, D.; Yin, J.; Kiyokawa, H.

Nat. Commun.

8

14286

745952

29152096

The non-canonical ubiquitin activating enzyme UBA6 suppresses epithelial-mesenchymal transition of mammary epithelial cells

2017

Liu, X.; Sun, L.; Gursel, D.B.; Cheng, C.; Huang, S.; Rademaker, A.W.; Khan, S.A.; Yin, J.; Kiyokawa, H.

Oncotarget

8

87480-87493

760342

32714456

Changes in expression of interferon-stimulated genes and ubiquitin activating enzyme E1-like in ovine thymus during early pregnancy

2020

Zhang, L.; Zhao, Z.; Wang, Y.; Li, N.; Cao, N.; Yang, L.

Anim. Reprod.

17

e20190134

760825

32583128

Structural and functional characterisation of the domains of ubiquitin-activating enzyme (E1) of Saccharomyces cerevisiae

2020

Prabha, C.

Cell Biochem. Biophys.

78

309-319

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

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Show Links (1 entry)