BAG3 information

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
Gene location (Human)
Chr.	Chromosome 10 (human)
End	119,677,819 bp
Gene location (Mouse)
Chr.	Chromosome 7 (mouse)
End	128,148,705 bp
RNA expression pattern
	Top expressed in
	gastrocnemius muscle; ; body of tongue; ; quadriceps femoris muscle; ; vastus lateralis muscle; ; tibialis anterior muscle; ; triceps brachii muscle; ; vena cava; ; thoracic diaphragm; ; deltoid muscle; ; trachea;
	Top expressed in
	ankle; ; plantaris muscle; ; interventricular septum; ; right ventricle; ; soleus muscle; ; extraocular muscle; ; digastric muscle; ; thoracic diaphragm; ; extensor digitorum longus muscle; ; temporal muscle;
	More reference expression data
	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 disc; 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
	9531
	29810
	ENSG00000151929
	ENSMUSG00000030847
	O95817
	Q9JLV1
	NM_004281
	NM_013863
	NP_004272
	NP_038891
	Wikidata
View/Edit Human	View/Edit Mouse

BAG family molecular chaperone regulator 3 is a protein that in humans is encoded by the BAG3 gene. BAG3 is involved in chaperone-assisted selective autophagy.^[5]^[6]^[7]^[8]^[9]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000151929 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000030847 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Takayama S, Xie Z, Reed JC (Jan 1999). "An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone regulators". The Journal of Biological Chemistry. 274 (2): 781–6. doi:10.1074/jbc.274.2.781. PMID 9873016.
^ Carra S, Seguin SJ, Landry J (Feb 2008). "HspB8 and Bag3: a new chaperone complex targeting misfolded proteins to macroautophagy". Autophagy. 4 (2): 237–9. doi:10.4161/auto.5407. PMID 18094623.
^ "Entrez Gene: BAG3 BCL2-associated athanogene 3".
^ Arndt V, Dick N, Tawo R, Dreiseidler M, Wenzel D, Hesse M, Fürst DO, Saftig P, Saint R, Fleischmann BK, Hoch M, Höhfeld J (Jan 2010). "Chaperone-assisted selective autophagy is essential for muscle maintenance". Current Biology. 20 (2): 143–8. doi:10.1016/j.cub.2009.11.022. PMID 20060297. S2CID 8885338.
^ Ulbricht A, Eppler FJ, Tapia VE, van der Ven PF, Hampe N, Hersch N, Vakeel P, Stadel D, Haas A, Saftig P, Behrends C, Fürst DO, Volkmer R, Hoffmann B, Kolanus W, Höhfeld J (Mar 2013). "Cellular mechanotransduction relies on tension-induced and chaperone-assisted autophagy". Current Biology. 23 (5): 430–5. doi:10.1016/j.cub.2013.01.064. PMID 23434281.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000151929 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000030847 – 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.

[pmid9873016-5] Takayama S, Xie Z, Reed JC (Jan 1999). "An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone regulators". The Journal of Biological Chemistry. 274 (2): 781–6. doi:10.1074/jbc.274.2.781. PMID 9873016.

[pmid18094623-6] Carra S, Seguin SJ, Landry J (Feb 2008). "HspB8 and Bag3: a new chaperone complex targeting misfolded proteins to macroautophagy". Autophagy. 4 (2): 237–9. doi:10.4161/auto.5407. PMID 18094623.

[entrez-7] "Entrez Gene: BAG3 BCL2-associated athanogene 3".

[pmid20060297-8] Arndt V, Dick N, Tawo R, Dreiseidler M, Wenzel D, Hesse M, Fürst DO, Saftig P, Saint R, Fleischmann BK, Hoch M, Höhfeld J (Jan 2010). "Chaperone-assisted selective autophagy is essential for muscle maintenance". Current Biology. 20 (2): 143–8. doi:10.1016/j.cub.2009.11.022. PMID 20060297. S2CID 8885338.

[pmid23434281-9] Ulbricht A, Eppler FJ, Tapia VE, van der Ven PF, Hampe N, Hersch N, Vakeel P, Stadel D, Haas A, Saftig P, Behrends C, Fürst DO, Volkmer R, Hoffmann B, Kolanus W, Höhfeld J (Mar 2013). "Cellular mechanotransduction relies on tension-induced and chaperone-assisted autophagy". Current Biology. 23 (5): 430–5. doi:10.1016/j.cub.2013.01.064. PMID 23434281.

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