Bag6
entrez
224727
canonical
uniprot
Q9Z1R2
canonical
ensembl
ENSMUSG00000024392
resolver
ensp
ENSMUSP00000025250
resolver
ensp
ENSMUSP00000129324
resolver
ensp
ENSMUSP00000134628
resolver
ensp
ENSMUSP00000236598
resolver
ensp
ENSMUSP00000236599
resolver
ensp
ENSMUSP00000236600
resolver
ensp
ENSMUSP00000236603
resolver
ensp
ENSMUSP00000236605
resolver
ensp
ENSMUSP00000236606
resolver
ensp
ENSMUSP00000236609
resolver
ensp
ENSMUSP00000236615
resolver
ensp
ENSMUSP00000236617
resolver
ensp
ENSMUSP00000236618
resolver
ensp
ENSMUSP00000236619
resolver
ensp
ENSMUSP00000236621
resolver
ensp
ENSMUSP00000236623
resolver
ensp
ENSMUSP00000236624
resolver
ensp
ENSMUSP00000236629
resolver
ensp
ENSMUSP00000236631
resolver
ensp
ENSMUSP00000236637
resolver
ensp
ENSMUSP00000236638
resolver
ensp
ENSMUSP00000236644
resolver
ensp
ENSMUSP00000236645
resolver
ensp
ENSMUSP00000236648
resolver
ensp
ENSMUSP00000236649
resolver
ensp
ENSMUSP00000236651
resolver
ensp
ENSMUSP00000236652
resolver
ensp
ENSMUSP00000236653
resolver
ensp
ENSMUSP00000236654
resolver
ensp
ENSMUSP00000236656
resolver
ensp
ENSMUSP00000236657
resolver
ensp
ENSMUSP00000236658
resolver
ensp
ENSMUSP00000236660
resolver
ensp
ENSMUSP00000341721
resolver
ensp
ENSMUSP00000341722
resolver
ensp
ENSMUSP00000341729
resolver
enst
ENSMUST00000025250
resolver
enst
ENSMUST00000166426
resolver
enst
ENSMUST00000173550
resolver
genesymbol
Bag6
resolver
genesymbol_syn
Bat3
resolver
uniprot
F7AUS8
resolver
uniprot
G3UZT6
resolver
uniprot
Q3UF95
resolver
uniprot
Q8SNA3
resolver
uniprot_entry
BAG6_MOUSE
resolver
uniprot_entry
F7AUS8_MOUSE
resolver
uniprot_entry
G3UZT6_MOUSE
resolver
uniprot_entry
Q3UF95_MOUSE
resolver
uniprot_sec
Q8SNA3
resolver
amino_acid_sequence
MEPSDSASTAMEEPDSLEVLVKTLDSQTRTFIVGAQMNVKEFKEHIAASVSIPSEKQRLIYQGRVLQDDKKLQEYNVGGKVIHLVERAPPQTQLPSGASSGTGSASATHGGAPLPGTRGPGASVHDRNANSYVMVGTFNLPSDGSAVDVHINMEQAPIQSEPRVRLVMAQHMIRDIQTLLSRMECRGGTQAQASQPPPQTPQTVASETVALNSQTSEPVESEAPPREPMESEEMEERPPTQTPELAPSGPAPAGPAPAGPAPAPETNAPNHPSPAEHVEVLQELQRLQRRLQPFLQRYCEVLGAAATTDYNNNHEGREEDQRLINLVGESLRLLGNTFVALSDLRCNLACAPPRHLHVVRPMSHYTTPMVLQQAAIPIQINVGTTVTMTGNGARPPPAPGAEAATPGSAQATSLPPSSTTVDSSTEGAPPPGPAPPPASSHPRVIRISHQSVEPVVMMHMNIQDSGAQPGGVPSAPTGPLGPPGHGQTLGQQVPGFPTAPTRVVIARPTPPQARPSHPGGPPVSGALQGAGLGTNTSLAQMVSGLVGQLLMQPVLVAQGTPGMAQAQAQAQAQAQAQAQAPAPAPAPAPAPATASASAGTTNTATTAGPAPGGPAQPPPPQPSAADLQFSQLLGNLLGPAGPGAGGPGMASPTITVAMPGVPAFLQGMTDFLQASQTAPPPPPPPPPPPPAPEQQSTPPPGSPSGGTASPGGLGPESLPPEFFTSVVQGVLSSLLGSLGARAGSSESIAAFIQRLSGSSNIFEPGADGALGFFGALLSLLCQNFSMVDVVMLLHGHFQPLQRLQPQLRSFFHQHYLGGQEPTPSNIRMATHTLITGLEEYVRESFSLVQVQPGVDIIRTNLEFLQEQFNSIAAHVLHCTDSGFGARLLELCNQGLFECLALNLHCLGGQQMELAAVINGRIRRMSRGVNPSLVSWLTTMMGLRLQVVLEHMPVGPDAILRYVRRVGDPPQTLPEEPMEVQGAERTSPEPQRENASPAPGTTAEEAMSRGPPPAPEGGSRDEQDGASADAEPWAAAVPPEWVPIIQQDIQSQRKVKPQPPLSDAYLSGMPAKRRKTMQGEGPQLLLSEAVSRAAKAAGARPLTSPESLSRDLEAPEVQESYRQQLRSDIQKRLQEDPNYSPQRFPNAHRAFADDP
uniprot
proteins
function
FUNCTION: ATP-independent molecular chaperone preventing the aggregation of misfolded and hydrophobic patches-containing proteins (PubMed:18056262, PubMed:18678708, PubMed:20713601). Functions as part of a cytosolic protein quality control complex, the BAG6/BAT3 complex, which maintains these client proteins in a soluble state and participates in their proper delivery to the endoplasmic reticulum or alternatively can promote their sorting to the proteasome where they undergo degradation (PubMed:20713601). The BAG6/BAT3 complex is involved in the post-translational delivery of tail-anchored/type II transmembrane proteins to the endoplasmic reticulum membrane. Recruited to ribosomes, it interacts with the transmembrane region of newly synthesized tail-anchored proteins and together with SGTA and ASNA1 mediates their delivery to the endoplasmic reticulum. Client proteins that cannot be properly delivered to the endoplasmic reticulum are ubiquitinated by RNF126, an E3 ubiquitin-protein ligase associated with BAG6 and are sorted to the proteasome. SGTA which prevents the recruitment of RNF126 to BAG6 may negatively regulate the ubiquitination and the proteasomal degradation of client proteins. Similarly, the BAG6/BAT3 complex also functions as a sorting platform for proteins of the secretory pathway that are mislocalized to the cytosol either delivering them to the proteasome for degradation or to the endoplasmic reticulum. The BAG6/BAT3 complex also 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. It maintains these retrotranslocated proteins in an unfolded yet soluble state condition in the cytosol to ensure their proper delivery to the proteasome (By similarity). BAG6 is also required for selective ubiquitin-mediated degradation of defective nascent chain polypeptides by the proteasome. In this context, it may participate in the production of antigenic peptides and play a role in antigen presentation in immune response (PubMed:20713601). BAG6 is also involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation. BAG6 may ensure the proper degradation of these proteins and thereby protects the endoplasmic reticulum from protein overload upon stress (By similarity). By inhibiting the polyubiquitination and subsequent proteasomal degradation of HSPA2 it may also play a role in the assembly of the synaptonemal complex during spermatogenesis (PubMed:18678708). Also positively regulates apoptosis by interacting with and stabilizing the proapoptotic factor AIFM1 (PubMed:18056262). By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway (By similarity). {ECO:0000250|UniProtKB:P46379, ECO:0000269|PubMed:18056262, ECO:0000269|PubMed:18678708, ECO:0000269|PubMed:20713601}.; 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). {ECO:0000250|UniProtKB:P46379}.; FUNCTION: Released extracellularly via exosomes, it is a ligand of the natural killer/NK cells receptor NCR3 and stimulates NK cells cytotoxicity. It may thereby trigger NK cells cytotoxicity against neighboring tumor cells and immature myeloid dendritic cells (DC). {ECO:0000250|UniProtKB:P46379}.; FUNCTION: May mediate ricin-induced apoptosis. {ECO:0000250|UniProtKB:P46379}.
uniprot
proteins
mass_dalton
121037
uniprot
proteins
post_translational_modification
PTM: Ricin can induce a cleavage by the caspase CASP3. The released C-terminal peptide induces apoptosis. {ECO:0000250|UniProtKB:P46379}.
uniprot
proteins
pubmed
14656967
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16287848
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
17403783
uniprot
proteins
pubmed
18056262
uniprot
proteins
pubmed
18678708
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
20713601
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
24160817
uniprot
proteins
pubmed
26337389
uniprot
proteins
pubmed
26876100
uniprot
proteins
sequence_length
1154
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18056262}. Nucleus {ECO:0000250|UniProtKB:P46379}. Secreted, extracellular exosome {ECO:0000250|UniProtKB:P46379}. Note=Normally localized in cytosol and nucleus, it can also be released extracellularly, in exosomes, by tumor and myeloid dendritic cells. {ECO:0000250|UniProtKB:P46379}.
uniprot
proteins