# BAG3

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Protein-coding gene in the species Homo sapiens

BAG3 Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1UK5 Identifiers Aliases BAG3, BAG-3, BIS, CAIR-1, MFM6, BCL2 associated athanogene 3, BAG cochaperone 3 External IDs OMIM: 603883; MGI: 1352493; HomoloGene: 3162; GeneCards: BAG3; OMA:BAG3 - orthologs Gene location (Human) Chr. Chromosome 10 (human)[1] Band 10q26.11 Start 119,651,380 bp[1] End 119,677,819 bp[1] Gene location (Mouse) Chr. Chromosome 7 (mouse)[2] Band 7|7 F3 Start 128,125,340 bp[2] End 128,148,705 bp[2] RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in gastrocnemius muscle Skeletal muscle tissue of rectus abdominis body of tongue glutes muscle of thigh quadriceps femoris muscle vastus lateralis muscle tibialis anterior muscle triceps brachii muscle vena cava Top expressed in cardiac muscle tissue of left ventricle gastrula muscle of thigh ankle plantaris muscle interventricular septum right ventricle soleus muscle extraocular muscle digastric muscle More reference expression data BioGPS More reference expression data Gene ontology Molecular function chaperone binding protein binding adenyl-nucleotide exchange factor activity cadherin binding protein-containing complex binding Cellular component cytosol plasma membrane Z discdkac neuron projection nucleus cytoplasm Biological process negative regulation of striated muscle cell apoptotic process protein stabilization negative regulation of apoptotic process cellular response to mechanical stimulus brain development protein folding spinal cord development extrinsic apoptotic signaling pathway in absence of ligand regulation of cellular response to heat extrinsic apoptotic signaling pathway via death domain receptors apoptotic process regulation of catalytic activity cellular response to heat positive regulation of protein export from nucleus negative regulation of transcription from RNA polymerase II promoter in response to stress positive regulation of protein import into nucleus Sources:Amigo / QuickGO Orthologs Species Human Mouse Entrez 9531 29810 Ensembl ENSG00000151929 ENSMUSG00000030847 UniProt O95817 Q9JLV1 RefSeq (mRNA) NM_004281 NM_013863 RefSeq (protein) NP_004272 NP_038891 Location (UCSC) Chr 10: 119.65 – 119.68 Mb Chr 7: 128.13 – 128.15 Mb PubMed search [3] [4] Wikidata View/Edit Human View/Edit Mouse

**BAG family molecular chaperone regulator 3** is a [protein](/source/Protein) that in humans is encoded by the *BAG3* [gene](/source/Gene). BAG3 is involved in [chaperone-assisted selective autophagy](/source/Chaperone-assisted_selective_autophagy).[5][6][7][8][9]

## Function

BAG proteins compete with [Hip-1](/source/Hip-1) for binding to the [Hsc70](/source/Hsc70)/[Hsp70](/source/Hsp70) [ATPase](/source/ATPase) domain and promote substrate release. All the BAG proteins have an approximately 45-amino acid [BAG domain](/source/BAG_domain) near the [C terminus](/source/C_terminus) but differ markedly in their [N-terminal](/source/N-terminal) regions. The protein encoded by this gene contains a [WW domain](/source/WW_domain) in the N-terminal region and a BAG domain in the C-terminal region. The BAG domains of [BAG1](/source/BAG1), [BAG2](/source/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.[7]

## Clinical significance

BAG gene has been implicated in age related neurodegenerative diseases such as [Alzheimer](/source/Alzheimer)'s. It has been demonstrated that BAG1 and BAG3 regulate the proteasomal and lysosomal protein elimination pathways, respectively.[10][11] It has also been shown to be a cause of familial [dilated cardiomyopathy](/source/Dilated_cardiomyopathy).[12] That BAG3 mutations are responsible for familial dilated cardiomyopathy is confirmed by another study describing 6 new molecular variants (2 missense and 4 premature Stops ). Moreover, the same publication reported that BAG3 polymorphisms are also associated with sporadic forms of the disease together with HSPB7 locus.[13]

In muscle cells, BAG3 cooperates with the molecular chaperones Hsc70 and [HspB8](/source/HSPB8) to induce the degradation of mechanically damaged cytoskeleton components in lysosomes. This process is called [chaperone-assisted selective autophagy](/source/Chaperone-assisted_selective_autophagy) and is essential for maintaining muscle activity in flies, mice and men.[8]

BAG3 is able to stimulate the expression of [cytoskeleton](/source/Cytoskeleton) proteins in response to mechanical tension by activating the [transcription](/source/Transcription_(genetics)) regulators [YAP1](/source/YAP1) and [WWTR1](/source/WWTR1).[9] BAG3 balances protein synthesis and protein degradation under mechanical stress.

## Interactions

PLCG1 has been shown to [interact](/source/Protein-protein_interaction) with:

- [FGFR1](/source/FGFR1),[14]

- [CD117](/source/CD117),[15][16]

- [CD31](/source/CD31),[17]

- [Cbl gene](/source/Cbl_gene)[18][19]

- [CISH](/source/CISH_(gene))[20]

- [Epidermal growth factor receptor](/source/Epidermal_growth_factor_receptor),[18][21]

- [Eukaryotic translation elongation factor 1 alpha 1](/source/Eukaryotic_translation_elongation_factor_1_alpha_1),[22]

- [FLT1](/source/FLT1),[23]

- [GAB1](/source/GAB1),[24][25]

- [GIT1](/source/GIT1),[26]

- [Grb2](/source/Grb2),[27][28][29]

- [HER2/neu](/source/HER2%2Fneu),[30][31]

- [IRS2](/source/IRS2),[32]

- [ITK](/source/ITK_(gene)),[33][34]

- [KHDRBS1](/source/KHDRBS1),[35][36][37]

- [Linker of activated T cells](/source/Linker_of_activated_T_cells),[38][39][40]

- [Lymphocyte cytosolic protein 2](/source/Lymphocyte_cytosolic_protein_2),[41]

- [PDGFRA](/source/PDGFRA),[42]

- [PLD2](/source/PLD2),[43]

- [RHOA](/source/RHOA),[44]

- [SOS1](/source/SOS1),[29][45]

- [TUB](/source/TUB_(gene)),[46]

- [TrkA](/source/TrkA),[47][48][49][50]

- [TrkB](/source/TrkB),[49][51]

- [VAV1](/source/VAV1),[52] and

- [Wiskott-Aldrich syndrome protein](/source/Wiskott-Aldrich_syndrome_protein).[53][54]

## References

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## Further reading

- Maruyama K, Sugano S (Jan 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". *Gene*. **138** (1–2): 171–4. [doi](/source/Doi_(identifier)):[10.1016/0378-1119(94)90802-8](https://doi.org/10.1016%2F0378-1119%2894%2990802-8). [PMID](/source/PMID_(identifier)) [8125298](https://pubmed.ncbi.nlm.nih.gov/8125298).

- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (Oct 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". *Gene*. **200** (1–2): 149–56. [doi](/source/Doi_(identifier)):[10.1016/S0378-1119(97)00411-3](https://doi.org/10.1016%2FS0378-1119%2897%2900411-3). [PMID](/source/PMID_(identifier)) [9373149](https://pubmed.ncbi.nlm.nih.gov/9373149).

- Lee JH, Takahashi T, Yasuhara N, Inazawa J, Kamada S, Tsujimoto Y (Nov 1999). ["Bis, a Bcl-2-binding protein that synergizes with Bcl-2 in preventing cell death"](https://doi.org/10.1038%2Fsj.onc.1203043). *Oncogene*. **18** (46): 6183–90. [doi](/source/Doi_(identifier)):[10.1038/sj.onc.1203043](https://doi.org/10.1038%2Fsj.onc.1203043). [PMID](/source/PMID_(identifier)) [10597216](https://pubmed.ncbi.nlm.nih.gov/10597216).

- Doong H, Price J, Kim YS, Gasbarre C, Probst J, Liotta LA, Blanchette J, Rizzo K, Kohn E (Sep 2000). ["CAIR-1/BAG-3 forms an EGF-regulated ternary complex with phospholipase C-gamma and Hsp70/Hsc70"](https://doi.org/10.1038%2Fsj.onc.1203797). *Oncogene*. **19** (38): 4385–95. [doi](/source/Doi_(identifier)):[10.1038/sj.onc.1203797](https://doi.org/10.1038%2Fsj.onc.1203797). [PMID](/source/PMID_(identifier)) [10980614](https://pubmed.ncbi.nlm.nih.gov/10980614).

- Liao Q, Ozawa F, Friess H, Zimmermann A, Takayama S, Reed JC, Kleeff J, Büchler MW (Aug 2001). ["The anti-apoptotic protein BAG-3 is overexpressed in pancreatic cancer and induced by heat stress in pancreatic cancer cell lines"](https://doi.org/10.1016%2FS0014-5793%2801%2902728-4). *FEBS Letters*. **503** (2–3): 151–7. [doi](/source/Doi_(identifier)):[10.1016/S0014-5793(01)02728-4](https://doi.org/10.1016%2FS0014-5793%2801%2902728-4). [PMID](/source/PMID_(identifier)) [11513873](https://pubmed.ncbi.nlm.nih.gov/11513873). [S2CID](/source/S2CID_(identifier)) [10672504](https://api.semanticscholar.org/CorpusID:10672504).

- Antoku K, Maser RS, Scully WJ, Delach SM, Johnson DE (Sep 2001). "Isolation of Bcl-2 binding proteins that exhibit homology with BAG-1 and suppressor of death domains protein". *Biochemical and Biophysical Research Communications*. **286** (5): 1003–10. [doi](/source/Doi_(identifier)):[10.1006/bbrc.2001.5512](https://doi.org/10.1006%2Fbbrc.2001.5512). [PMID](/source/PMID_(identifier)) [11527400](https://pubmed.ncbi.nlm.nih.gov/11527400).

- Suzuki H, Fukunishi Y, Kagawa I, Saito R, Oda H, Endo T, Kondo S, Bono H, Okazaki Y, Hayashizaki Y (Oct 2001). ["Protein-protein interaction panel using mouse full-length cDNAs"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC311163). *Genome Research*. **11** (10): 1758–65. [doi](/source/Doi_(identifier)):[10.1101/gr.180101](https://doi.org/10.1101%2Fgr.180101). [PMC](/source/PMC_(identifier)) [311163](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC311163). [PMID](/source/PMID_(identifier)) [11591653](https://pubmed.ncbi.nlm.nih.gov/11591653).

- Romano MF, Festa M, Pagliuca G, Lerose R, Bisogni R, Chiurazzi F, Storti G, Volpe S, Venuta S, Turco MC, Leone A (Mar 2003). ["BAG3 protein controls B-chronic lymphocytic leukaemia cell apoptosis"](https://doi.org/10.1038%2Fsj.cdd.4401167). *Cell Death and Differentiation*. **10** (3): 383–5. [doi](/source/Doi_(identifier)):[10.1038/sj.cdd.4401167](https://doi.org/10.1038%2Fsj.cdd.4401167). [PMID](/source/PMID_(identifier)) [12700638](https://pubmed.ncbi.nlm.nih.gov/12700638).

- Pagliuca MG, Lerose R, Cigliano S, Leone A (Apr 2003). ["Regulation by heavy metals and temperature of the human BAG-3 gene, a modulator of Hsp70 activity"](https://doi.org/10.1016%2FS0014-5793%2803%2900274-6). *FEBS Letters*. **541** (1–3): 11–5. [doi](/source/Doi_(identifier)):[10.1016/S0014-5793(03)00274-6](https://doi.org/10.1016%2FS0014-5793%2803%2900274-6). [PMID](/source/PMID_(identifier)) [12706811](https://pubmed.ncbi.nlm.nih.gov/12706811). [S2CID](/source/S2CID_(identifier)) [33081500](https://api.semanticscholar.org/CorpusID:33081500).

- Doong H, Rizzo K, Fang S, Kulpa V, Weissman AM, Kohn EC (Aug 2003). ["CAIR-1/BAG-3 abrogates heat shock protein-70 chaperone complex-mediated protein degradation: accumulation of poly-ubiquitinated Hsp90 client proteins"](https://doi.org/10.1074%2Fjbc.M209682200). *The Journal of Biological Chemistry*. **278** (31): 28490–500. [doi](/source/Doi_(identifier)):[10.1074/jbc.M209682200](https://doi.org/10.1074%2Fjbc.M209682200). [PMID](/source/PMID_(identifier)) [12750378](https://pubmed.ncbi.nlm.nih.gov/12750378).

- Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villén J, Li J, Cohn MA, Cantley LC, Gygi SP (Aug 2004). ["Large-scale characterization of HeLa cell nuclear phosphoproteins"](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC514446). *Proceedings of the National Academy of Sciences of the United States of America*. **101** (33): 12130–5. [Bibcode](/source/Bibcode_(identifier)):[2004PNAS..10112130B](https://ui.adsabs.harvard.edu/abs/2004PNAS..10112130B). [doi](/source/Doi_(identifier)):[10.1073/pnas.0404720101](https://doi.org/10.1073%2Fpnas.0404720101). [PMC](/source/PMC_(identifier)) [514446](https://www.ncbi.nlm.nih.gov/pmc/articles/PMC514446). [PMID](/source/PMID_(identifier)) [15302935](https://pubmed.ncbi.nlm.nih.gov/15302935).

- Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ (Jan 2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". *Nature Biotechnology*. **23** (1): 94–101. [doi](/source/Doi_(identifier)):[10.1038/nbt1046](https://doi.org/10.1038%2Fnbt1046). [PMID](/source/PMID_(identifier)) [15592455](https://pubmed.ncbi.nlm.nih.gov/15592455). [S2CID](/source/S2CID_(identifier)) [7200157](https://api.semanticscholar.org/CorpusID:7200157).

- Tao WA, Wollscheid B, O'Brien R, Eng JK, Li XJ, Bodenmiller B, Watts JD, Hood L, Aebersold R (Aug 2005). "Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry". *Nature Methods*. **2** (8): 591–8. [doi](/source/Doi_(identifier)):[10.1038/nmeth776](https://doi.org/10.1038%2Fnmeth776). [PMID](/source/PMID_(identifier)) [16094384](https://pubmed.ncbi.nlm.nih.gov/16094384). [S2CID](/source/S2CID_(identifier)) [20475874](https://api.semanticscholar.org/CorpusID:20475874).

- Seo YJ, Jeon MH, Lee JH, Lee YJ, Youn HJ, Ko JH, Lee JH (Dec 2005). ["Bis induces growth inhibition and differentiation of HL-60 cells via up-regulation of p27"](https://doi.org/10.1038%2Femm.2005.76). *Experimental & Molecular Medicine*. **37** (6): 624–30. [doi](/source/Doi_(identifier)):[10.1038/emm.2005.76](https://doi.org/10.1038%2Femm.2005.76). [PMID](/source/PMID_(identifier)) [16391524](https://pubmed.ncbi.nlm.nih.gov/16391524).

- Kassis JN, Guancial EA, Doong H, Virador V, Kohn EC (Sep 2006). ["CAIR-1/BAG-3 modulates cell adhesion and migration by downregulating activity of focal adhesion proteins"](https://zenodo.org/record/1259459). *Experimental Cell Research*. **312** (15): 2962–71. [doi](/source/Doi_(identifier)):[10.1016/j.yexcr.2006.05.023](https://doi.org/10.1016%2Fj.yexcr.2006.05.023). [PMID](/source/PMID_(identifier)) [16859681](https://pubmed.ncbi.nlm.nih.gov/16859681).

- Beausoleil SA, Villén J, Gerber SA, Rush J, Gygi SP (Oct 2006). "A probability-based approach for high-throughput protein phosphorylation analysis and site localization". *Nature Biotechnology*. **24** (10): 1285–92. [doi](/source/Doi_(identifier)):[10.1038/nbt1240](https://doi.org/10.1038%2Fnbt1240). [PMID](/source/PMID_(identifier)) [16964243](https://pubmed.ncbi.nlm.nih.gov/16964243). [S2CID](/source/S2CID_(identifier)) [14294292](https://api.semanticscholar.org/CorpusID:14294292).

## External links

- [GeneReviews/NIH/NCBI/UW entry on Myofibrillar Myopathy](https://www.ncbi.nlm.nih.gov/books/NBK1499/)

- Human [*BAG3*](https://genome.ucsc.edu/cgi-bin/hgTracks?db=hg38&singleSearch=knownCanonical&position=BAG3) genome location and [*BAG3*](https://genome.ucsc.edu/cgi-bin/hgGene?db=hg38&hgg_type=knownGene&hgg_gene=BAG3) gene details page in the [UCSC Genome Browser](/source/UCSC_Genome_Browser).

- Overview of all the structural information available in the [PDB](/source/Protein_Data_Bank) for [UniProt](/source/UniProt): *[Q9JLV1](https://www.ebi.ac.uk/pdbe/pdbe-kb/proteins/Q9JLV1)* (Mouse BAG family molecular chaperone regulator 3) at the [PDBe-KB](/source/PDBe-KB).

v t e PDB gallery 1uk5: Solution structure of the Murine BAG domain of Bcl2-associated athanogene 3

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Adapted from the Wikipedia article [BAG3](https://en.wikipedia.org/wiki/BAG3) by Wikipedia contributors ([contributor history](https://en.wikipedia.org/wiki/BAG3?action=history)). Available under [Creative Commons Attribution-ShareAlike 4.0 International](https://creativecommons.org/licenses/by-sa/4.0/). Changes may have been made.