CHIP, active

Background Information:

CHIP is an E3 ubiquitin ligase and co-chaperone that plays a central role in cellular protein quality control. By interacting with molecular chaperones such as HSC70, HSP70, and HSP90, CHIP monitors the folding state of proteins and determines their fate. When proteins are misfolded or damaged, CHIP shifts the balance away from refolding and toward degradation by tagging these chaperone-bound substrates with ubiquitin, thereby directing them to the proteasomal or, in some contexts, lysosomal degradation pathways. Through this coupling of the chaperone machinery to the ubiquitin–proteasome system, CHIP helps maintain cellular proteostasis and overall homeostasis. CHIP has been shown to ubiquitinate and promote degradation of multiple oncogenic proteins (including receptor tyrosine kinases, steroid hormone receptors, and signaling kinases), positioning it as a context-dependent tumor suppressor or regulator of oncogenic stability. In neurodegenerative and protein-misfolding disorders (e.g., Alzheimer’s and Parkinson’s disease) CHIP is of interest because it facilitates the clearance of aggregation-prone proteins such as tau, alpha-synuclein, and polyglutamine-expanded proteins.

Target Class:

Ubiquitination-related

Family:

U-box

Sub Family:

E3 Ligase

Protein Name:

CHIP

Protein Aliases:

Antigen NY-CO-7

Accession Number:

NM_005861.2

UniProt Number:

Q9UNE7

Gene Name:

STUB1

Gene ID:

10273

Gene Aliases:

CHIP; SCA48; UBOX1; SCAR16; HSPABP2; NY-CO-7; SDCCAG7

Target Species:

Human