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Appears in Networks 1

In-Edges 1

p(PFAM:"CHIP_TPR_N") increases complex(a(MESH:"HSP70 Heat-Shock Proteins"), p(FPLX:HSP90), p(HGNC:STUB1)) View Subject | View Object

CHIP has two important domains for his chaperone activity: the amino terminus tetratricopeptide repeat (TPR) domain that links CHIP to Hsp70 and Hsp90 [24] and the carboxyl terminus containing the U-box that is important for the E3 ubiquitin ligase function of CHIP. PubMed:25374103

Out-Edges 3

About

BEL Commons is developed and maintained in an academic capacity by Charles Tapley Hoyt and Daniel Domingo-Fernández at the Fraunhofer SCAI Department of Bioinformatics with support from the IMI project, AETIONOMY. It is built on top of PyBEL, an open source project. Please feel free to contact us here to give us feedback or report any issues. Also, see our Publishing Notes and Data Protection information.

If you find BEL Commons useful in your work, please consider citing: Hoyt, C. T., Domingo-Fernández, D., & Hofmann-Apitius, M. (2018). BEL Commons: an environment for exploration and analysis of networks encoded in Biological Expression Language. Database, 2018(3), 1–11.