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Ligand S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine

Basic Ligand Information

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Roles as Enzyme Ligand

In Vivo Substrate in Enzyme-catalyzed Reactions (2 results)

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Show Natural Substrate (2 entries)

EC NUMBER

PROVEN IN VIVO REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.3.2.27

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine

737038, 735611, 735865, 736504, 736600, 736844, 736894

-

2.3.2.27

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [SDIRIP1 protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[SDIRIP1 protein]-L-lysine

736992

-

2.3.2.27

2 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

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

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-

Substrate in Enzyme-catalyzed Reactions (18 results)

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Show Substrate (18 entries)

EC NUMBER

REACTION

REACTION DIAGRAM

LITERATURE

ENZYME 3D STRUCTURE

2.3.2.26

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [caspase-8]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[caspase-8]-L-lysine

733626

-

2.3.2.26

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [ING2]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[ING2]-L-lysine

733856

-

2.3.2.26

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [Sav]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[Sav]-L-lysine

735028

-

2.3.2.26

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [Spry2]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[Spry2]-L-lysine

734163

-

2.3.2.26

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [ubiquitin]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[ubiquitin]-L-lysine

715650

-

2.3.2.27

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [ABI5]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[ABI5]-L-lysine

734217

-

2.3.2.27

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine

737038, 735611, 735865, 736504, 736600, 736844, 736894, 736990

-

2.3.2.27

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [ACS4]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[ACS4]-L-lysine

734954

-

2.3.2.27

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [ACS7]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[ACS7]-L-lysine

734954

-

2.3.2.27

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [bHLH065]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[bHLH065]-L-lysine

734386

-

2.3.2.27

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [BNip1]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[BNip1]-L-lysine

733637

-

2.3.2.27

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [GRP1]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[GRP1]-L-lysine

734386

-

2.3.2.27

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [HCI1]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[HCI1]-L-lysine

734386

-

2.3.2.27

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [histone H2A]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[histone H2A]-L-lysine

733721

-

2.3.2.27

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [PGLU1]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[PGLU1]-L-lysine

734386

-

2.3.2.27

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [Ring1b]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[Ring1b]-L-lysine

733721

-

2.3.2.27

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [SDIRIP1 protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[SDIRIP1 protein]-L-lysine

736992

-

2.3.2.27

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [TIP4.1]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[TIP4.1]-L-lysine

734931

-

2.3.2.26

5 entries

2.3.2.27

13 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

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

-

-

Enzyme Kinetic Parameters

References & Links

Literature References (20)

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Show Reference (20 entries)

BRENDA REFERENCE ID

PUBMED ID

TITLE

YEAR

AUTHORS

JOURNAL

VOLUME

PAGES

715650

20980253

Biochemical and structural studies of a HECT-like ubiquitin ligase from Escherichia coli O157:H7

2011

Lin, D.Y.; Diao, J.; Zhou, D.; Chen, J.

J. Biol. Chem.

286

441-449

733626

24287696

The HECTD3 E3 ubiquitin ligase facilitates cancer cell survival by promoting K63-linked polyubiquitination of caspase-8

2013

Li, Y.; Kong, Y.; Zhou, Z.; Chen, H.; Wang, Z.; Hsieh, Y.C.; Zhao, D.; Zhi, X.; Huang, J.; Zhang, J.; Li, H.; Chen, C.

Cell Death Dis.

4

e935

733637

23896122

A novel RING finger E3 ligase RNF186 regulate ER stress-mediated apoptosis through interaction with BNip1

2013

Wang, P.; Wu, Y.; Li, Y.; Zheng, J.; Tang, J.

Cell. Signal.

25

2320-2333

733721

16710298

Structure and E3-ligase activity of the Ring-Ring complex of polycomb proteins Bmi1 and Ring1b

2006

Buchwald, G.; van der Stoop, P.; Weichenrieder, O.; Perrakis, A.; van Lohuizen, M.; Sixma, T.K.

EMBO J.

25

2465-2474

733856

20621832

HECT ubiquitin ligase Smurf1 targets the tumor suppressor ING2 for ubiquitination and degradation

2010

Nie, J.; Liu, L.; Wu, M.; Xing, G.; He, S.; Yin, Y.; Tian, C.; He, F.; Zhang, L.

FEBS Lett.

584

3005-3012

734163

19864419

HECT domain-containing E3 ubiquitin ligase Nedd4 interacts with and ubiquitinates Sprouty2

2010

Edwin, F.; Anderson, K.; Patel, T.B.

J. Biol. Chem.

285

255-264

734217

23720747

Cytoplasmic degradation of the Arabidopsis transcription factor abscisic acid insensitive 5 is mediated by the RING-type E3 ligase KEEP ON GOING

2013

Liu, H.; Stone, S.L.

J. Biol. Chem.

288

20267-20279

734386

23698632

The rice RING finger E3 ligase, OsHCI1, drives nuclear export of multiple substrate proteins and its heterogeneous overexpression enhances acquired thermotolerance

2013

Lim, S.D.; Cho, H.Y.; Park, Y.C.; Ham, D.J.; Lee, J.K.; Jang, C.S.

J. Exp. Bot.

64

2899-2914

734931

24664473

Positive regulation of rice RING E3 ligase OsHIR1 in arsenic and cadmium uptakes

2014

Lim, S.D.; Hwang, J.G.; Han, A.R.; Park, Y.C.; Lee, C.; Ok, Y.S.; Jang, C.S.

Plant Mol. Biol.

85

365-379

734954

20511490

Arabidopsis RING E3 ligase XBAT32 regulates lateral root production through its role in ethylene biosynthesis

2010

Prasad, M.E.; Schofield, A.; Lyzenga, W.; Liu, H.; Stone, S.L.

Plant Physiol.

153

1587-1596

735028

26125558

Hippo stabilises its adaptor Salvador by antagonising the HECT ubiquitin ligase Herc4

2015

Aerne, B.L.; Gailite, I.; Sims, D.; Tapon, N.

PLoS ONE

10

e0131113

735611

26086094

Arabidopsis RING E3 ubiquitin ligase AtATL80 is negatively involved inphosphate mobilization and cold stress response in sufficient phosphate growth conditions

2015

Suh, J.Y.; Kim, W.T.

Biochem. Biophys. Res. Commun.

463

793-799

735865

26556605

Wheat germ-based protein libraries for the functional characterisation of the Arabidopsis E2 ubiquitin conjugating enzymes and the RING-type E3 ubiquitin ligase enzymes

2015

Ramadan, A.; Nemoto, K.; Seki, M.; Shinozaki, K.; Takeda, H.; Takahashi, H.; Sawasaki, T.

BMC Plant Biol.

15

275

736504

26631732

Interaction between RING1 (R1) and the ubiquitin-like (UBL) domains is critical for the regulation of parkin activity

2016

Ham, S.J.; Lee, S.Y.; Song, S.; Chung, J.R.; Choi, S.; Chung, J.

J. Biol. Chem.

291

1803-1816

736600

25913143

Arabidopsis C3HC4-RING finger E3 ubiquitin ligase AtAIRP4 positively regulates stress-responsive abscisic acid signaling

2016

Yang, L.; Liu, Q.; Liu, Z.; Yang, H.; Wang, J.; Li, X.; Yang, Y.

J. Integr. Plant Biol.

58

67-80

736844

-

OsRFPH2-10, a RING-H2 finger E3 ubiquitin ligase, is involved in rice antiviral defense in the early stages of rice dwarf virus infection

2014

Liu, L.; Jin, L.; Huang, X.; Geng, Y.; Li, F.; Qin, Q.; Wang, R.; Ji, S.; Zhao, S.; Xie, Q.; Wei, C.; Xie, C.; Ding, B.; Li, Y.

Mol. Plant

7

1057-1060

736894

23905547

The Chinese wild grapevine (Vitis pseudoreticulata) E3 ubiquitin ligase Erysiphe necator-induced RING finger protein 1 (EIRP1) activates plant defense responses by inducing proteolysis of the VpWRKY11 transcription factor

2013

Yu, Y.; Xu, W.; Wang, J.; Wang, L.; Yao, W.; Yang, Y.; Xu, Y.; Ma, F.; Du, Y.; Wang, Y.

New Phytol.

200

834-846

736990

24838976

The RING-finger E3 ubiquitin ligase COP1 SUPPRESSOR1 negatively regulates COP1 abundance in maintaining COP1 homeostasis in dark-grown Arabidopsis S´seedlings

2014

Xu, D.; Lin, F.; Jiang, Y.; Huang, X.; Li, J.; Ling, J.; Hettiarachchi, C.; Tellgren-Roth, C.; Holm, M.; Deng, X.W.

Plant Cell

26

1981-1991

736992

25616872

The RING finger ubiquitin E3 ligase SDIR1 targets SDIR1-INTERACTING PROTEIN1 for degradation to modulate the salt stress response and ABA signaling in Arabidopsis

2015

Zhang, H.; Cui, F.; Wu, Y.; Lou, L.; Liu, L.; Tian, M.; Ning, Y.; Shu, K.; Tang, S.; Xie, Q.

Plant Cell

27

214-227

737038

26564152

The RING finger ubiquitin E3 ligase OsHTAS enhances heat tolerance by promoting H2O2-induced stomatal closure in rice

2016

Liu, J.; Zhang, C.; Wei, C.; Liu, X.; Wang, M.; Yu, F.; Xie, Q.; Tu, J.

Plant Physiol.

170

429-443

Links to other databases for S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine

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