Literature summary for 2.3.2.B8 extracted from

Zhu, K.; Shan, Z.; Chen, X.; Cai, Y.; Cui, L.; Yao, W.; Wang, Z.; Shi, P.; Tian, C.; Lou, J.; Xie, Y.; Wen, W.
Allosteric auto-inhibition and activation of the Nedd4 family E3 ligase Itch (2017), EMBO Rep., 18, 1618-1630 .

Search for more literature for 2.3.2.B8

Crystallization (Commentary)

Crystallization (Comment)	Organism
the WW domains proceeding the catalytic HECT domain play an inhibitory role by binding directly to HECT. The WW2 domain and a following linker allosterically lock HECT in an inactive state inhibiting E2-E3 transthiolation. Binding of the Ndfip1 adaptor or JNK1-mediated phosphorylation relieves the auto-inhibition of Itch in a WW2-dependent manner	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q96J02	-	-
Mus musculus	Q8C863	-	-

Synonyms

Synonyms	Comment	Organism
E3 ubiquitin-protein ligase Itchy homolog	-	Mus musculus
E3 ubiquitin-protein ligase Itchy homolog	-	Homo sapiens
Itch	-	Mus musculus
Itch	-	Homo sapiens

General Information

General Information	Comment	Organism
physiological function	itch ligase activities are controlled via autoinhibition. Aberrant activation of Itch leads to migration defects of cortical neurons during development	Mus musculus

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)