BAG family molecular chaperone regulator 2 is a protein that in humans is encoded by the BAG2 gene.[5][6]

BAG2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesBAG2, BAG-2, dJ417I1.2, BCL2 associated athanogene 2, BAG cochaperone 2
External IDsOMIM: 603882; MGI: 1891254; HomoloGene: 31233; GeneCards: BAG2; OMA:BAG2 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_004282

NM_145392

RefSeq (protein)

NP_004273

NP_663367

Location (UCSC)Chr 6: 57.17 – 57.19 MbChr 1: 33.78 – 33.8 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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 predicted BAG2 protein contains 211 amino acids. 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.[6]

Interactions

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BAG2 has been shown to interact with HSPA8.[5]

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000112208Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000042215Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b Takayama S, Xie Z, Reed JC (Feb 1999). "An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone regulators". J Biol Chem. 274 (2): 781–6. doi:10.1074/jbc.274.2.781. PMID 9873016.
  6. ^ a b "Entrez Gene: BAG2 BCL2-associated athanogene 2".
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Further reading

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