BAG4

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

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
Gene location (Human)
Chr.Chromosome 8 (human)[1]
Band8p11.23Start38,176,533 bp[1]
End38,213,301 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

9530

67384

Ensembl

ENSG00000156735

ENSMUSG00000037316

UniProt

O95429

Q8CI61

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: 25.76 – 25.79 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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

  1. GRCh38: Ensembl release 89: ENSG00000156735 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000037316 - Ensembl, 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. 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. Jiang Y, Woronicz JD, Liu W, Goeddel DV (Feb 1999). "Prevention of constitutive TNF receptor 1 signaling by silencer of death domains". Science. 283 (5401): 543–6. doi:10.1126/science.283.5401.543. PMID 9915703.
  7. "Entrez Gene: BAG4 BCL2-associated athanogene 4".
  8. Lau PP, Chan L (Dec 2003). "Involvement of a chaperone regulator, Bcl2-associated athanogene-4, in apolipoprotein B mRNA editing". J. Biol. Chem. 278 (52): 52988–96. doi:10.1074/jbc.M310153200. PMID 14559896.
  9. Miki K, Eddy EM (Apr 2002). "Tumor necrosis factor receptor 1 is an ATPase regulated by silencer of death domain". Mol. Cell. Biol. 22 (8): 2536–43. doi:10.1128/MCB.22.8.2536-2543.2002. PMC 133739. PMID 11909948.

Further reading


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