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- Q4834553 subject Q8802898.
- Q4834553 abstract "In molecular biology, BAG domains are protein domains found in proteins which are modulators of chaperone activity, they bind to HSP70/HSC70 proteins and promote substrate release. The proteins have anti-apoptotic activity and increase the anti-cell death function of BCL-2 induced by various stimuli. BAG-1 binds to the serine/threonine kinase Raf-1 or Hsc70/Hsp70 in a mutually exclusive interaction. BAG-1 promotes cell growth by binding to and stimulating Raf-1 activity. The binding of Hsp70 to BAG-1 diminishes Raf-1 signalling and inhibits subsequent events, such as DNA synthesis, as well as arrests the cell cycle. BAG-1 has been suggested to function as a molecular switch that encourages cells to proliferate in normal conditions but become quiescent under a stressful environment .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. The BAG domain is evolutionarily conserved, and BAG domain containing proteins have been described and/or proven in a variety of organisms including Mus musculus (Mouse), Xenopus spp., Drosophila spp., Bombyx mori (Silk moth), Caenorhabditis elegans, Saccharomyces cerevisiae (Baker's yeast), Schizosaccharomyces pombe (Fission yeast), and Arabidopsis thaliana (Mouse-ear cress).The BAG domain has 110-124 amino acids and is composed of three anti-parallel alpha-helices, each approximately 30-40 amino acids in length. The first and second helices interact with the serine/threonine kinase Raf-1 and the second and third helices are the sites of the BAG domain interaction with the ATPase domain of Hsc70/Hsp70. Binding of the BAG domain to the ATPase domain is mediated by both electrostatic and hydrophobic interactions in BAG-1 and is energy requiring.".
- Q4834553 symbol "BAG".
- Q4834553 thumbnail PDB_1hx1_EBI.jpg?width=300.
- Q4834553 wikiPageWikiLink Q1063.
- Q4834553 wikiPageWikiLink Q11379.
- Q4834553 wikiPageWikiLink Q12119506.
- Q4834553 wikiPageWikiLink Q1342298.
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- Q4834553 wikiPageWikiLink Q14863436.
- Q4834553 wikiPageWikiLink Q14903573.
- Q4834553 wikiPageWikiLink Q158695.
- Q4834553 wikiPageWikiLink Q15978631.
- Q4834553 wikiPageWikiLink Q17837016.
- Q4834553 wikiPageWikiLink Q18034354.
- Q4834553 wikiPageWikiLink Q188941.
- Q4834553 wikiPageWikiLink Q189159.
- Q4834553 wikiPageWikiLink Q210973.
- Q4834553 wikiPageWikiLink Q219567.
- Q4834553 wikiPageWikiLink Q2236682.
- Q4834553 wikiPageWikiLink Q26336.
- Q4834553 wikiPageWikiLink Q283399.
- Q4834553 wikiPageWikiLink Q2902757.
- Q4834553 wikiPageWikiLink Q300033.
- Q4834553 wikiPageWikiLink Q312154.
- Q4834553 wikiPageWikiLink Q3456514.
- Q4834553 wikiPageWikiLink Q419102.
- Q4834553 wikiPageWikiLink Q421851.
- Q4834553 wikiPageWikiLink Q422496.
- Q4834553 wikiPageWikiLink Q4857068.
- Q4834553 wikiPageWikiLink Q4995178.
- Q4834553 wikiPageWikiLink Q6507061.
- Q4834553 wikiPageWikiLink Q719725.
- Q4834553 wikiPageWikiLink Q7239.
- Q4834553 wikiPageWikiLink Q7868.
- Q4834553 wikiPageWikiLink Q8066.
- Q4834553 wikiPageWikiLink Q8802898.
- Q4834553 wikiPageWikiLink Q896177.
- Q4834553 wikiPageWikiLink Q898273.
- Q4834553 wikiPageWikiLink Q91703.
- Q4834553 symbol "BAG".
- Q4834553 type Biomolecule.
- Q4834553 type Protein.
- Q4834553 type Thing.
- Q4834553 type Q206229.
- Q4834553 type Q8054.
- Q4834553 comment "In molecular biology, BAG domains are protein domains found in proteins which are modulators of chaperone activity, they bind to HSP70/HSC70 proteins and promote substrate release. The proteins have anti-apoptotic activity and increase the anti-cell death function of BCL-2 induced by various stimuli. BAG-1 binds to the serine/threonine kinase Raf-1 or Hsc70/Hsp70 in a mutually exclusive interaction. BAG-1 promotes cell growth by binding to and stimulating Raf-1 activity.".
- Q4834553 label "BAG domain".
- Q4834553 depiction PDB_1hx1_EBI.jpg.