BAG4

BCL2-associated athanogene 4

PDB rendering based on 1m62.

Available structures
PDB	1M62, 1M7K

Identifiers

Symbols

BAG4; BAG-4; DKFZp586O2022; SODD

External IDs

OMIM: 603884 MGI: 1914634 HomoloGene: 31270 GeneCards: BAG4 Gene

Gene Ontology
Molecular function	• receptor signaling protein activity
Cellular component	• nucleus • nucleolus • cytoplasm
Biological process	• protein folding • apoptosis • anti-apoptosis
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 8:
38.03 – 38.07 Mb

Chr 8:
26.88 – 26.9 Mb

PubMed search

[1]

[2]

BAG family molecular chaperone regulator 4 is a protein that in humans is encoded by the BAG4 gene.^[1]^[2]^[3]

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.^[3]

Interactions

BAG4 has been shown to interact with HSPA8,^[4] TNFRSF1A^[2]^[4] and APOBEC1.^[5]

References

^ 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.
^ ^a ^b 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.
^ ^a ^b "Entrez Gene: BAG4 BCL2-associated athanogene 4". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9530.
^ ^a ^b Miki, Kiyoshi; Eddy Edward M (Apr. 2002). "Tumor Necrosis Factor Receptor 1 Is an ATPase Regulated by Silencer of Death Domain". Mol. Cell. Biol. (United States) 22 (8): 2536–43. doi:10.1128/MCB.22.8.2536-2543.2002. ISSN 0270-7306. PMC 133739. PMID 11909948. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=133739.
^ Lau, Paul P; Chan Lawrence (Dec. 2003). "Involvement of a chaperone regulator, Bcl2-associated athanogene-4, in apolipoprotein B mRNA editing". J. Biol. Chem. (United States) 278 (52): 52988–96. doi:10.1074/jbc.M310153200. ISSN 0021-9258. PMID 14559896.

Riley BM, Schultz RE, Cooper ME et al. (2007). "A Genome-Wide Linkage Scan for Cleft Lip and Cleft Palate Identifies a Novel Locus on 8p11-23". Am. J. Med. Genet. A 143 (8): 846–52. doi:10.1002/ajmg.a.31673. PMC 2570349. PMID 17366557. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2570349.
Yang ZQ, Streicher KL, Ray ME et al. (2007). "Multiple interacting oncogenes on the 8p11-p12 amplicon in human breast cancer". Cancer Res. 66 (24): 11632–43. doi:10.1158/0008-5472.CAN-06-2946. PMID 17178857.
Gerhard DS, Wagner L, Feingold EA et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
Lau PP, Chan L (2004). "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.
Al-Lamki RS, Wang J, Thiru S et al. (2003). "Expression of Silencer of Death Domains and Death-Receptor-3 in Normal Human Kidney and in Rejecting Renal Transplants". Am. J. Pathol. 163 (2): 401–11. doi:10.1016/S0002-9440(10)63670-X. PMC 1868232. PMID 12875962. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1868232.
Eichholtz-Wirth H, Fritz E, Wolz L (2003). "Overexpression of the 'silencer of death domain', SODD/BAG-4, modulates both TNFR1- and CD95-dependent cell death pathways". Cancer Lett. 194 (1): 81–9. doi:10.1016/S0304-3835(03)00009-0. PMID 12706861.
Strausberg RL, Feingold EA, Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
Briknarová K, Takayama S, Homma S et al. (2002). "BAG4/SODD protein contains a short BAG domain". J. Biol. Chem. 277 (34): 31172–8. doi:10.1074/jbc.M202792200. PMID 12058034.
Eichholtz-Wirth H, Sagan D (2002). "Altered signaling of TNFalpha-TNFR1 and SODD/BAG4 is responsible for radioresistance in human HT-R15 cells". Anticancer Res. 22 (1A): 235–40. PMID 12017295.
Antoku K, Maser RS, Scully WJ et al. (2001). "Isolation of Bcl-2 binding proteins that exhibit homology with BAG-1 and suppressor of death domains protein". Biochem. Biophys. Res. Commun. 286 (5): 1003–10. doi:10.1006/bbrc.2001.5512. PMID 11527400.
Frisch SM (2000). "Evidence for a function of death-receptor-related, death-domain-containing proteins in anoikis". Curr. Biol. 9 (18): 1047–9. doi:10.1016/S0960-9822(99)80455-2. PMID 10508612.

PDB gallery

1m62: Solution structure of the BAG domain from BAG4/SODD

1m7k: Solution Structure of the SODD BAG Domain

BAG4

Interactions

References

Further reading