XB-FEAT-969276: Difference between revisions

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=bag3=  
=bag3=  
This is the community wiki page for the gene ''bag3'' please feel free to add any information that is relevant to this gene that is not already captured elsewhere in Xenbase
This is the community wiki page for the gene ''bag3'' please feel free to add any information that is relevant to this gene that is not already captured elsewhere in Xenbase.
 
=nomenclature changes=
10.18.2019
 
Human name has changed for Entrez Gene: 9531. From BCL2 associated athanogene 3 to BAG cochaperone 3
 
=NCBI Summary for human BAG3=
BAG proteins compete with Hip for binding to the Hsc70/Hsp70 ATPase domain and promote substrate release. All the BAG proteins have an approximately 45-amino acid BAG domain near the C terminus but differ markedly in their N-terminal regions. The protein encoded by this gene contains a WW domain in the N-terminal region and a BAG domain in the C-terminal region. The BAG domains of BAG1, BAG2, and BAG3 interact specifically with the Hsc70 ATPase domain in vitro and in mammalian cells. All 3 proteins bind with high affinity to the ATPase domain of Hsc70 and inhibit its chaperone activity in a Hip-repressible manner. [provided by RefSeq, Jul 2008]

Latest revision as of 11:01, 28 October 2019

bag3

This is the community wiki page for the gene bag3 please feel free to add any information that is relevant to this gene that is not already captured elsewhere in Xenbase.

nomenclature changes

10.18.2019

Human name has changed for Entrez Gene: 9531. From BCL2 associated athanogene 3 to BAG cochaperone 3

NCBI Summary for human BAG3

BAG proteins compete with Hip for binding to the Hsc70/Hsp70 ATPase domain and promote substrate release. All the BAG proteins have an approximately 45-amino acid BAG domain near the C terminus but differ markedly in their N-terminal regions. The protein encoded by this gene contains a WW domain in the N-terminal region and a BAG domain in the C-terminal region. The BAG domains of BAG1, BAG2, and BAG3 interact specifically with the Hsc70 ATPase domain in vitro and in mammalian cells. All 3 proteins bind with high affinity to the ATPase domain of Hsc70 and inhibit its chaperone activity in a Hip-repressible manner. [provided by RefSeq, Jul 2008]