×

Network disruptions

We have been experiencing disruptions on our local network which has affected the stability of these web pages. We have been working with IT support team to get this fixed as a matter of urgency and apologise for any inconvenience.

CATH Classification

Domain Context

CATH Clusters

Superfamily 2.20.70.10
Functional Family E3 ubiquitin-protein ligase NEDD4

Enzyme Information

2.3.2.26
HECT-type E3 ubiquitin transferase.
based on mapping to UniProt Q96J02
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)- ubiquitinyl-[acceptor protein]-L-lysine.
-!- In the first step the enzyme transfers ubiquitin from the E2 ubiquitin-conjugating enzyme (EC 2.3.2.23) to a cysteine residue in its HECT domain (which is located in the C-terminal region), forming a thioester bond. -!- In a subsequent step the enzyme transfers the ubiquitin to an acceptor protein, resulting in the formation of an isopeptide bond between the C-terminal glycine residue of ubiquitin and the epsilon- amino group of an L-lysine residue of the acceptor protein. -!- Cf. EC 2.3.2.27 and EC 2.3.2.31.

UniProtKB Entries (1)

Q9H3M7
TXNIP_HUMAN
Homo sapiens
Thioredoxin-interacting protein

PDB Structure

PDB 5CQ2
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structural basis for the regulatory role of the PPxY motifs in the thioredoxin-interacting protein TXNIP.
Liu, Y., Lau, J., Li, W., Tempel, W., Li, L., Dong, A., Narula, A., Qin, S., Min, J.
Biochem.J.
CATH-Gene3D is a Global Biodata Core Resource Learn more...