{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kumar S"],"funding":["Science and Engineering Research Board","Council of Scientific and Industrial Research, India","Department of Science and Technology, Ministry of Science and Technology, India"],"pagination":["1521-1555"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9485218"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["9(6)"],"pubmed_abstract":["The carboxy-terminus of Hsp70-interacting protein (CHIP) is a ubiquitin ligase and co-chaperone belonging to Ubox family that plays a crucial role in the maintenance of cellular homeostasis by switching the equilibrium of the folding-refolding mechanism towards the proteasomal or lysosomal degradation pathway. It links molecular chaperones <i>viz</i>. HSC70, HSP70 and HSP90 with ubiquitin proteasome system (UPS), acting as a quality control system. CHIP contains charged domain in between N-terminal tetratricopeptide repeat (TPR) and C-terminal Ubox domain. TPR domain interacts with the aberrant client proteins <i>via</i> chaperones while Ubox domain facilitates the ubiquitin transfer to the client proteins for ubiquitination. Thus, CHIP is a classic molecule that executes ubiquitination fo"],"journal":["Genes & diseases"],"pubmed_title":["Chaperone-assisted E3 ligase CHIP: A double agent in cancer."],"pmcid":["PMC9485218"],"funding_grant_id":["DST/NM/NT/2018/105"],"pubmed_authors":["Basu M","Ghosh MK","Kumar S"],"additional_accession":[]},"is_claimable":false,"name":"Chaperone-assisted E3 ligase CHIP: A double agent in cancer.","description":"The carboxy-terminus of Hsp70-interacting protein (CHIP) is a ubiquitin ligase and co-chaperone belonging to Ubox family that plays a crucial role in the maintenance of cellular homeostasis by switching the equilibrium of the folding-refolding mechanism towards the proteasomal or lysosomal degradation pathway. It links molecular chaperones <i>viz</i>. HSC70, HSP70 and HSP90 with ubiquitin proteasome system (UPS), acting as a quality control system. CHIP contains charged domain in between N-terminal tetratricopeptide repeat (TPR) and C-terminal Ubox domain. TPR domain interacts with the aberrant client proteins <i>via</i> chaperones while Ubox domain facilitates the ubiquitin transfer to the client proteins for ubiquitination. Thus, CHIP is a classic molecule that executes ubiquitination fo","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Nov","modification":"2026-07-14T15:50:07.882Z","creation":"2025-04-05T12:10:51.208Z"},"accession":"S-EPMC9485218","cross_references":{"pubmed":["36157498"],"doi":["10.1016/j.gendis.2021.08.003"]}}