D
IPR049548

E3 ubiquitin-protein ligase Sina-like, RING finger

InterPro entry
Short nameSina-like_RING
domain relationships

Description

This is the RING finger domain of Sina and its homologues from animals, such as Siah-1/2 and plants, such as SINAT3 from Arabidopsis
[3]
. Sina (seven in absentia) was first identified in Drosophila and is essential for the determination of the R7 pathway in photoreceptor cell development. It consists of a RING zinc finger at the N-terminal, followed by two zinc finger (C2H2 type) domains and a C-terminal TRAF-like domain (
IPR018121
)
[2, 1]
. This domain carries the E3 ubiquitin ligase activity of these proteins.

References

1.Elucidation of the substrate binding site of Siah ubiquitin ligase. House CM, Hancock NC, Moller A, Cromer BA, Fedorov V, Bowtell DD, Parker MW, Polekhina G. Structure 14, 695-701, (2006). View articlePMID: 16615911

2.Two high-resolution structures of the human E3 ubiquitin ligase Siah1. Rimsa V, Eadsforth TC, Hunter WN. Acta Crystallogr Sect F Struct Biol Cryst Commun 69, 1339-43, (2013). PMID: 24316825

3.SINAT E3 Ubiquitin Ligases Mediate FREE1 and VPS23A Degradation to Modulate Abscisic Acid Signaling. Xia FN, Zeng B, Liu HS, Qi H, Xie LJ, Yu LJ, Chen QF, Li JF, Chen YQ, Jiang L, Xiao S. Plant Cell 32, 3290-3310, (2020). PMID: 32753431

Cross References

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