Family

Molecular chaperone regulator BAG-1 (IPR017093)

Short name: BAG-1

Overlapping homologous superfamilies

None.

Family relationships

Description

This group represents a molecular chaperone regulator BAG-1 [PMID: 9873016]. BAG-1 contains a BAG domain that is formed by two antiparallel helices, while the third helix is extended away and stabilized by crystal-packing interactions [PMID: 15333932].

BAG-family proteins contain a single BAG domain, except for human BAG-5 which has four BAG repeats. The BAG domain is a conserved region located at the C terminus of the BAG-family proteins that binds the ATPase domain of Hsc70/Hsp70. BAG family proteins regulate chaperone protein activities through their interaction with Hsc70/Hsp70 [PMID: 12406544].

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0051087 chaperone binding

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PIRSF
PANTHER