NCBI Accession #
NP_566305.1
NCBI GenBank Nucleotide #
NM_111616.3
NCBI Official Full Name
carboxyl terminus of HSC70-interacting protein
NCBI Official Symbol
CHIP
NCBI Official Synonym Symbols
ATCHIP; carboxyl terminus of HSC70-interacting protein; CARBOXYL TERMINUS OF HSC70-INTERACTING PROTEIN
NCBI Protein Information
carboxyl terminus of HSC70-interacting protein
NCBI Summary
Encodes AtCHIP, a new class of E3 ubiquitin ligases with three tetratricopeptide repeats and a U-box domain, structurally similar to the animal CHIP proteins. Plays an important role in plant cellular metabolism under temperature stress conditions. Functions as an E3 ubiquitin ligase of protein phosphatase 2A subunits and alters plant response to abscisic acid treatment. Belongs to one of the 36 carboxylate clamp (CC)-tetratricopeptide repeat (TPR) proteins (Prasad 2010, Pubmed ID: 20856808) with potential to interact with Hsp90/Hsp70 as co-chaperones.
UniProt Synonym Gene Names
AtCHIP
UniProt Protein Name
E3 ubiquitin-protein ligase CHIP
UniProt Synonym Protein Names
Carboxyl terminus of HSC70-interacting protein
UniProt Primary Accession #
Q9SRS9
UniProt Related Accession #
Q9SRS9
UniProt Comments
Has E3 ubiquitin-protein ligase activity and may target misfolded substrates towards proteasomal degradation. Regulates the activity of some serine/threonine-protein phosphatases by E3 ubiquitin-protein ligase activity. Required for responses to biotic and abiotic stresses such as auxin, abscisic acid (ABA), low and high temperature and darkness, probably through the activation of serine/threonine-protein phosphatase and the subsequent modification of the plasma membrane composition. Regulates the chloroplastic Clp proteolytic activity in response to stresses. Ubiquitylates FtsH1, a component of the chloroplast FtsH protease, and affects protein degradation in chloroplasts. Mediates plastid precursor degradation to prevent cytosolic precursor accumulation, together with the molecular chaperone HSC70-4. Mediates ubiquitination of transit peptides and thereby led to their degradation through the ubiquitin-proteasome system.