Literature summary for 2.3.2.23 extracted from

McAlpine, J.M.R.B.; Zhu, J.; Pudjihartono, N.; Teyra, J.; Currie, M.J.; Tillett, Z.D.; Dobson, R.C.J.; Sidhu, S.S.; Day, C.L.; Middleton, A.J.
Structural and biophysical characterisation of ubiquitin variants that inhibit the ubiquitin conjugating enzyme Ube2d2 (2024), FEBS J., 291, 5305-5321.

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Protein Variants

Protein Variants	Comment	Organism
S22R	mutation disrupts backside ubiquitin binding	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	generation of ubiquitin variants that inhibit the E2 enzyme. The variants inhibit ubiquitin chain building, and bind to UB2D2 with low micromolar affinity and high specificity. The binding site overlaps with E1 binding, and the variants can have an additional binding site that blocks a critical non-covalent ubiquitin-binding site on the E2 enzyme	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P62837	-	-

Synonyms

Synonyms	Comment	Organism
UBE2D2	-	Homo sapiens

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Release 2026.1 (March 2026)