BAIT
SHD
AtHsp90-7, AtHsp90.7, HEAT SHOCK PROTEIN 90-7, HEAT SHOCK PROTEIN 90.7, HSP90.7, SHEPHERD, T22A6.20, T22A6_20, AT4G24190
HSP90-like protein GRP94
GO Process (8)
GO Function (1)
GO Component (10)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Arabidopsis thaliana (Columbia)
PREY
SMT2
COTYLEDON VASCULAR PATTERN 1, CVP1, F14O10.7, F14O10_7, FRILL1, FRL1, sterol methyltransferase 2, AT1G20330
24-methylenesterol C-methyltransferase 2
GO Process (5)
GO Function (1)
GO Component (2)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Arabidopsis thaliana (Columbia)
Two-hybrid
Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.
Publication
A highly charged region in the middle domain of plant endoplasmic reticulum (ER)-localized heat-shock protein 90 is required for resistance to tunicamycin or high calcium-induced ER stresses.
Heat-shock protein 90 (HSP90) is a highly conserved molecular chaperone that is involved in modulating a multitude of cellular processes under both physiological and stress conditions. In Arabidopsis, there are seven HSP90 isoforms (HSP90.1-HSP90.7) that are localized in the cytoplasm/nucleus, mitochondrion, chloroplast, and endoplasmic reticulum (ER) where protein folding actively takes place. In this study, we analysed the sequence of ... [more]
J. Exp. Bot. Jan. 01, 2015; 66(1);113-24 [Pubmed: 25297550]
Throughput
- Low Throughput
Curated By
- BioGRID