Literature summary for 2.3.2.26 extracted from

Verdecia, M.A.; Joazeiro, C.A.; Wells, N.J.; Ferrer, J.L.; Bowman, M.E.; Hunter, T.; Noel, J.P.
Conformational flexibility underlies ubiquitin ligation mediated by the WWP1 HECT domain E3 ligase (2003), Mol. Cell, 11, 249-259.

Search for more literature for 2.3.2.26

Cloned(Commentary)

Cloned (Comment)	Organism
-	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure of the HECT domain of human ubiquitin ligase WWP1/AIP5 maintains a two-lobed structure like the HECT domain of the human ubiquitin ligase E6AP. The organization of the two lobes relative one another is different from E6AP due to a rotation about a polypeptide hinge linking the N and C lobes	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q9H0M0	-	-

Synonyms

Synonyms	Comment	Organism
WWP1	-	Homo sapiens

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Release 2023.1 (January 2023)