BAIT

CHIP

ATCHIP, CARBOXYL TERMINUS OF HSC70-INTERACTING PROTEIN, AT3G07370
E3 ubiquitin-protein ligase CHIP
GO Process (4)
GO Function (2)
GO Component (1)
Arabidopsis thaliana (Columbia)
PREY

RCN1

ATB BETA BETA, EER1, ENHANCED ETHYLENE RESPONSE 1, F2J7.19, F2J7_19, PHOSPHOPROTEIN PHOSPHATASE 2A REGULATORY SUBUNIT A, REGA, ROOTS CURL IN NPA, SERINE/THREONINE PROTEIN PHOSPHATASE TYPE 2A REGULATORY SUBUNIT A, AT1G25490
serine/threonine-protein phosphatase 2A regulatory subunit A alpha isoform
Arabidopsis thaliana (Columbia)

Biochemical Activity (Ubiquitination)

An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation.

Publication

AtCHIP functions as an E3 ubiquitin ligase of protein phosphatase 2A subunits and alters plant response to abscisic acid treatment.

Luo J, Shen G, Yan J, He C, Zhang H

CHIP proteins are E3 ubiquitin ligases that promote degradation of Hsp70 and Hsp90 substrate proteins through the 26S proteasome in animal systems. A CHIP-like protein in Arabidopsis, AtCHIP, also has E3 ubiquitin ligase activity and has important roles to play under conditions of abiotic stress. In an effort to study the mode of action of AtCHIP in plant cells, proteins ... [more]

Plant J. May. 01, 2006; 46(4);649-57 [Pubmed: 16640601]

Throughput

  • Low Throughput

Curated By

  • BioGRID