ID:BAG6_HUMAN DESCRIPTION: RecName: Full=Large proline-rich protein BAG6; AltName: Full=BAG family molecular chaperone regulator 6; AltName: Full=BCL2-associated athanogene 6; Short=BAG-6; Short=BAG6; AltName: Full=HLA-B-associated transcript 3; AltName: Full=Protein G3; AltName: Full=Protein Scythe; FUNCTION: Chaperone that plays a key role in various processes such as apoptosis, insertion of tail-anchored (TA) membrane proteins to the endoplasmic reticulum membrane and regulation of chromatin. Acts in part by regulating stability of proteins and their degradation by the proteasome. Participates in endoplasmic reticulum stress-induced apoptosis via its interaction with AIFM1/AIF by regulating AIFM1/AIF stability and preventing its degradation. Also required during spermatogenesis for synaptonemal complex assembly via its interaction with HSPA2, by inhibiting polyubiquitination and subsequent proteasomal degradation of HSPA2. 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. Key component of the BAG6/BAT3 complex, a cytosolic multiprotein complex involved in the post-translational delivery of tail-anchored (TA) membrane proteins to the endoplasmic reticulum membrane. TA membrane proteins, also named type II transmembrane proteins, contain a single C-terminal transmembrane region. BAG6/BAT3 acts by facilitating TA membrane proteins capture by ASNA1/TRC40: it is recruited to ribosomes synthesizing membrane proteins, interacts with the transmembrane region of newly released TA proteins and transfers them to ASNA1/TRC40 for targeting to the endoplasmic reticulum membrane. FUNCTION: Involved in DNA damage-induced apoptosis: following DNA damage, accumulates in the nucleus and forms a complex with p300/EP300, enhancing p300/EP300-mediated p53/TP53 acetylation leading to increase p53/TP53 transcriptional activity. When nuclear, may also act as a component of some chromatin regulator complex that regulates histone 3 'Lys-4' dimethylation (H3K4me2). FUNCTION: Can be released from tumor and dendritic cells in membrane vesicles or exosomes, and engage NCR3 thereby promoting natural killer cell (NK) activation and cytotoxicity. SUBUNIT: Component of the BAT3 complex, at least composed of BAG6/BAT3, UBL4A and GET3/TRC35. Interacts with AIFM1, CTCFL, HSPA2 and p300/EP300. Interacts with ricin A chain. Interacts with L.pneumophila proteins Lpg2160 and LegU1. Interacts with NCR3. INTERACTION: Q7Z434:MAVS; NbExp=2; IntAct=EBI-347552, EBI-995373; SUBCELLULAR LOCATION: Cytoplasm, cytosol. Nucleus. Note=The C- terminal fragment generated by caspase-3 is cytoplasmic. Also found in extracellular vesicular exosomes in some tumor cells. PTM: Cleavage by caspase-3 releases a C-terminal peptide that plays a role in ricin-induced apoptosis. PTM: In case of infection by L.pneumophila, ubiquitinated by the SCF(LegU1) complex. SIMILARITY: Contains 1 ubiquitin-like domain. SEQUENCE CAUTION: Sequence=AAD18085.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; Sequence=BAB63390.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; Sequence=CAI18318.2; Type=Erroneous gene model prediction;
ModBase Predicted Comparative 3D Structure on P46379
Front
Top
Side
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.
Other Names for This Gene
Press "+" in the title bar above to open this section.
Methods, Credits, and Use Restrictions
Click here
for details on how this gene model was made and data restrictions if any.