BAT3 an ATP-dependent chaperone protein that functions as part of the BAT3 complex (minimally composed of BAG6, UBL4A and GET3), a cytosolic protein quality control complex. Maintains client proteins in a soluble state and participates to the post-translational delivery of tail-anchored (TA), type II transmembrane proteins to the endoplasmic reticulum membrane. It is recruited to ribosomes synthesizing membrane proteins, interacts with the transmembrane region of newly released TA proteins, and together with SGTA and ASNA1 mediates their delivery to the endoplasmic reticulum membrane. Alternatively, it can promote the sorting of client proteins to the proteasome where they undergo degradation. Plays a role in the endoplasmic reticulum-associated degradation (ERAD), a quality control mechanism that eliminates unwanted proteins of the endoplasmic reticulum through their retrotranslocation to the cytosol and their targeting to the proteasome. Participates in endoplasmic reticulum stress-induced apoptosis via its interaction with AIFM1 by regulating AIFM1 stability and preventing its degradation. Required for selective ubiquitin-mediated degradation of defective nascent chain polypeptides by the proteasome. In this context, may play a role in immuno-proteasomes to generate antigenic peptides via targeted degradation, thereby playing a role in antigen presentation in immune response. Additionally interacts with CTCFL, HSPA2, EP300, NCR3, ricin A chain, and L.pneumophila proteins Lpg2160 and LegU1. 3 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Apoptosis; Cell cycle regulation; Chaperone; Ubiquitin conjugating system
Chromosomal Location of mouse Ortholog: 17 B1|17 18.59 cM
Cellular Component:  BAT3 complex; cytoplasm; cytosol; extracellular exosome; extracellular region; intracellular membrane-bounded organelle; membrane; nucleoplasm; nucleus
Molecular Function:  Hsp70 protein binding; identical protein binding; misfolded protein binding; polyubiquitin modification-dependent protein binding; proteasome binding; protein binding; ribosome binding; signaling receptor binding; ubiquitin protein ligase binding; ubiquitin-specific protease binding
Biological Process:  antigen processing and presentation of peptide antigen via MHC class I; apoptotic process; brain development; cell differentiation; chromatin organization; endoplasmic reticulum stress-induced pre-emptive quality control; ER-associated misfolded protein catabolic process; immune response-activating cell surface receptor signaling pathway; immune system process; internal peptidyl-lysine acetylation; intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; kidney development; lung development; maintenance of unfolded protein involved in ERAD pathway; natural killer cell activation; negative regulation of apoptotic process; negative regulation of proteasomal ubiquitin-dependent protein catabolic process; negative regulation of proteolysis; positive regulation of ERAD pathway; proteasomal protein catabolic process; proteasome-mediated ubiquitin-dependent protein catabolic process; protein stabilization; regulation of apoptotic process; regulation of embryonic development; spermatogenesis; synaptonemal complex assembly; tail-anchored membrane protein insertion into ER membrane; ubiquitin-dependent ERAD pathway; ubiquitin-dependent protein catabolic process
Reference #:  Q9Z1R2 (UniProtKB)
Alt. Names/Synonyms: 2410045D21Rik; AA408914; BAG family molecular chaperone regulator 6; BAG-6; BAG6; Bat; Bat3; BCL2-associated athanogene 6; D17H6S52; D17H6S52E; G3; HLA-B-associated transcript 3; Large proline-rich protein BAG6; Large proline-rich protein BAT3; Protein Scythe; Scyth; Scythe
Gene Symbols: Bag6
Molecular weight: 121,037 Da
Basal Isoelectric point: 5.46  Predict pI for various phosphorylation states
Protein-Specific Antibodies, siRNAs or Recombinant Proteins from Cell Signaling Technology® Total Proteins
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Protein Structure Not Found.

Cross-references to other databases:  AlphaFold  |  STRING  |  BioGPS  |  Pfam  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene