BAG2

BAG family molecular chaperone regulator 2 is a protein that in humans is encoded by the BAG2 gene.^[5][6]

PDBOrtholog search: PDBe RCSB

AliasesBAG2, BAG-2, dJ417I1.2, BCL2 associated athanogene 2, BAG cochaperone 2

External IDsOMIM: 603882; MGI: 1891254; HomoloGene: 31233; GeneCards: BAG2; OMA:BAG2 - orthologs

Chr.Chromosome 6 (human)^[1]

Quick facts Available structures, PDB ...

BAG2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3CQX, 3D0T
Identifiers
Aliases	BAG2, BAG-2, dJ417I1.2, BCL2 associated athanogene 2, BAG cochaperone 2
External IDs	OMIM: 603882; MGI: 1891254; HomoloGene: 31233; GeneCards: BAG2; OMA:BAG2 - orthologs
Gene location (Human) Chr. Chromosome 6 (human)[1] Band 6p12.1 Start 57,172,326 bp[1] End 57,189,833 bp[1]
Gene location (Mouse) Chr. Chromosome 1 (mouse)[2] Band 1|1 B Start 33,784,565 bp[2] End 33,796,876 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in tail of epididymis right ventricle biceps brachii Skeletal muscle tissue of biceps brachii saphenous vein seminal vesicula smooth muscle tissue thoracic diaphragm muscle layer of sigmoid colon Skeletal muscle tissue of rectus abdominis Top expressed in interventricular septum cardiac muscle tissue of left ventricle yolk sac right ventricle extraocular muscle entorhinal cortex perirhinal cortex temporal muscle digastric muscle lumbar spinal ganglion More reference expression data BioGPS More reference expression data
Gene ontology Molecular function chaperone binding protein binding identical protein binding adenyl-nucleotide exchange factor activity heat shock protein binding ubiquitin protein ligase binding transmembrane transporter binding tau protein binding Cellular component cytosol microtubule axon dendrite chaperone complex dendritic microtubule Biological process regulation of cellular response to heat protein metabolic process protein folding regulation of catalytic activity positive regulation of protein processing negative regulation of protein ubiquitination negative regulation of protein binding positive regulation of proteasomal ubiquitin-dependent protein catabolic process protein stabilization positive regulation of proteasomal protein catabolic process negative regulation of ubiquitin protein ligase activity Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 9532 213539 Ensembl ENSG00000112208 ENSMUSG00000042215 UniProt O95816 Q91YN9 RefSeq (mRNA) NM_004282 NM_145392 RefSeq (protein) NP_004273 NP_663367 Location (UCSC) Chr 6: 57.17 – 57.19 Mb Chr 1: 33.78 – 33.8 Mb PubMed search [3] [4]
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BAG proteins compete with Hip for binding to the Hsc70/Hsp70 ATPase domain and promote substrate release. All the BAG proteins have an approximately 45-amino acid BAG domain near the C terminus but differ markedly in their N-terminal regions. The predicted BAG2 protein contains 211 amino acids. The BAG domains of BAG1, 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.^[6]