BAG4

Protein-coding gene in the species Homo sapiens From Wikipedia, the free encyclopedia

BAG family molecular chaperone regulator 4 is a protein that in humans is encoded by the BAG4 gene.[5][6][7]

PDBOrtholog search: PDBe RCSB
AliasesBAG4, BAG-4, SODD, BCL2 associated athanogene 4, BAG cochaperone 4
Quick facts Available structures, PDB ...
BAG4
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesBAG4, BAG-4, SODD, BCL2 associated athanogene 4, BAG cochaperone 4
External IDsOMIM: 603884; MGI: 1914634; HomoloGene: 31270; GeneCards: BAG4; OMA:BAG4 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_004874
NM_001204878

NM_026121

RefSeq (protein)

NP_001191807
NP_004865

NP_080397

Location (UCSC)Chr 8: 38.18 – 38.21 MbChr 8: 26.25 – 26.28 Mb
PubMed search[3][4]
Wikidata
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Function

The protein encoded by this gene is a member of the BAG1-related protein family. BAG1 is an anti-apoptotic protein that functions through interactions with a variety of cell apoptosis and growth related proteins including BCL-2, Raf-protein kinase, steroid hormone receptors, growth factor receptors and members of the heat shock protein 70 kDa family. This protein contains a BAG domain near the C-terminus, which could bind and inhibit the chaperone activity of Hsc70/Hsp70. This protein was found to be associated with the death domain of tumor necrosis factor receptor type 1 (TNF-R1) and death receptor-3 (DR3), and thereby negatively regulates downstream cell death signaling. The regulatory role of this protein in cell death was demonstrated in epithelial cells which undergo apoptosis while integrin mediated matrix contacts are lost.[7]

Interactions

BAG4 has been shown to interact with:

References

Further reading

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