BAG6
entrez
7917
canonical
uniprot
P46379
canonical
ensembl
ENSG00000096155
resolver
ensembl
ENSG00000204463
resolver
ensembl
ENSG00000227761
resolver
ensembl
ENSG00000228760
resolver
ensembl
ENSG00000229524
resolver
ensembl
ENSG00000233348
resolver
ensembl
ENSG00000234651
resolver
ensp
ENSP00000211379
resolver
ensp
ENSP00000354875
resolver
ensp
ENSP00000365131
resolver
ensp
ENSP00000365143
resolver
ensp
ENSP00000402856
resolver
ensp
ENSP00000502941
resolver
ensp
ENSP00000558869
resolver
ensp
ENSP00000558870
resolver
ensp
ENSP00000558871
resolver
ensp
ENSP00000558872
resolver
ensp
ENSP00000558873
resolver
ensp
ENSP00000558874
resolver
ensp
ENSP00000558878
resolver
ensp
ENSP00000558880
resolver
ensp
ENSP00000558882
resolver
ensp
ENSP00000558883
resolver
ensp
ENSP00000558884
resolver
ensp
ENSP00000558891
resolver
ensp
ENSP00000558896
resolver
ensp
ENSP00000558897
resolver
ensp
ENSP00000558901
resolver
ensp
ENSP00000558902
resolver
ensp
ENSP00000558903
resolver
ensp
ENSP00000558904
resolver
ensp
ENSP00000558906
resolver
ensp
ENSP00000558907
resolver
ensp
ENSP00000558910
resolver
ensp
ENSP00000558916
resolver
ensp
ENSP00000558917
resolver
ensp
ENSP00000558923
resolver
ensp
ENSP00000558924
resolver
ensp
ENSP00000558926
resolver
ensp
ENSP00000558927
resolver
ensp
ENSP00000592037
resolver
ensp
ENSP00000592039
resolver
ensp
ENSP00000592041
resolver
ensp
ENSP00000592043
resolver
ensp
ENSP00000630857
resolver
ensp
ENSP00000630859
resolver
ensp
ENSP00000630862
resolver
ensp
ENSP00000630863
resolver
ensp
ENSP00000630864
resolver
enst
ENST00000375964
resolver
genesymbol
BAG6
resolver
genesymbol_syn
BAT3
resolver
genesymbol_syn
G3
resolver
hgnc
HGNC:13919
resolver
uniprot
A0A7P0MQS5
resolver
uniprot
A2ADJ7
resolver
uniprot
A3KQ42
resolver
uniprot
A3KQ44
resolver
uniprot
A6NGY6
resolver
uniprot
A6PWF7
resolver
uniprot
B0UX84
resolver
uniprot
B4DZ12
resolver
uniprot
B4E3V4
resolver
uniprot
E7EMZ4
resolver
uniprot
F8VXY4
resolver
uniprot
O95874
resolver
uniprot
Q5HYL9
resolver
uniprot
Q5SQ35
resolver
uniprot
Q5SQ36
resolver
uniprot
Q5SQ37
resolver
uniprot
Q5SQ41
resolver
uniprot
Q5SRP8
resolver
uniprot
Q5SRP9
resolver
uniprot
Q5STC1
resolver
uniprot
Q5STX1
resolver
uniprot
Q5STX3
resolver
uniprot
Q96SA6
resolver
uniprot
Q9BCN4
resolver
uniprot_entry
A0A7P0MQS5_HUMAN
resolver
uniprot_entry
BAG6_HUMAN
resolver
uniprot_sec
A2ADJ7
resolver
uniprot_sec
A3KQ42
resolver
uniprot_sec
A3KQ44
resolver
uniprot_sec
A6NGY6
resolver
uniprot_sec
A6PWF7
resolver
uniprot_sec
B0UX84
resolver
uniprot_sec
B4DZ12
resolver
uniprot_sec
B4E3V4
resolver
uniprot_sec
E7EMZ4
resolver
uniprot_sec
F8VXY4
resolver
uniprot_sec
O95874
resolver
uniprot_sec
Q5HYL9
resolver
uniprot_sec
Q5SQ35
resolver
uniprot_sec
Q5SQ36
resolver
uniprot_sec
Q5SQ37
resolver
uniprot_sec
Q5SQ41
resolver
uniprot_sec
Q5SRP8
resolver
uniprot_sec
Q5SRP9
resolver
uniprot_sec
Q5STC1
resolver
uniprot_sec
Q5STX1
resolver
uniprot_sec
Q5STX3
resolver
uniprot_sec
Q96SA6
resolver
uniprot_sec
Q9BCN4
resolver
amino_acid_sequence
MEPNDSTSTAVEEPDSLEVLVKTLDSQTRTFIVGAQMNVKEFKEHIAASVSIPSEKQRLIYQGRVLQDDKKLQEYNVGGKVIHLVERAPPQTHLPSGASSGTGSASATHGGGSPPGTRGPGASVHDRNANSYVMVGTFNLPSDGSAVDVHINMEQAPIQSEPRVRLVMAQHMIRDIQTLLSRMETLPYLQCRGGPQPQHSQPPPQPPAVTPEPVALSSQTSEPVESEAPPREPMEAEEVEERAPAQNPELTPGPAPAGPTPAPETNAPNHPSPAEYVEVLQELQRLESRLQPFLQRYYEVLGAAATTDYNNNHEGREEDQRLINLVGESLRLLGNTFVALSDLRCNLACTPPRHLHVVRPMSHYTTPMVLQQAAIPIQINVGTTVTMTGNGTRPPPTPNAEAPPPGPGQASSVAPSSTNVESSAEGAPPPGPAPPPATSHPRVIRISHQSVEPVVMMHMNIQDSGTQPGGVPSAPTGPLGPPGHGQTLGQQVPGFPTAPTRVVIARPTPPQARPSHPGGPPVSGTLQGAGLGTNASLAQMVSGLVGQLLMQPVLVAQGTPGMAPPPAPATASASAGTTNTATTAGPAPGGPAQPPPTPQPSMADLQFSQLLGNLLGPAGPGAGGSGVASPTITVAMPGVPAFLQGMTDFLQATQTAPPPPPPPPPPPPAPEQQTMPPPGSPSGGAGSPGGLGLESLSPEFFTSVVQGVLSSLLGSLGARAGSSESIAAFIQRLSGSSNIFEPGADGALGFFGALLSLLCQNFSMVDVVMLLHGHFQPLQRLQPQLRSFFHQHYLGGQEPTPSNIRMATHTLITGLEEYVRESFSLVQVQPGVDIIRTNLEFLQEQFNSIAAHVLHCTDSGFGARLLELCNQGLFECLALNLHCLGGQQMELAAVINGRIRRMSRGVNPSLVSWLTTMMGLRLQVVLEHMPVGPDAILRYVRRVGDPPQPLPEEPMEVQGAERASPEPQRENASPAPGTTAEEAMSRGPPPAPEGGSRDEQDGASAETEPWAAAVPPEWVPIIQQDIQSQRKVKPQPPLSDAYLSGMPAKRRKTMQGEGPQLLLSEAVSRAAKAAGARPLTSPESLSRDLEAPEVQESYRQQLRSDIQKRLQEDPNYSPQRFPNAQRAFADDP
uniprot
proteins
function
FUNCTION: ATP-independent molecular chaperone preventing the aggregation of misfolded and hydrophobic patches-containing proteins (PubMed:21636303). 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:20516149, PubMed:21636303, PubMed:21743475, PubMed:28104892). 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 (PubMed:20516149, PubMed:20676083, PubMed:25535373, PubMed:28104892). 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 (PubMed:24981174, PubMed:27193484, PubMed:28104892). SGTA which prevents the recruitment of RNF126 to BAG6 may negatively regulate the ubiquitination and the proteasomal degradation of client proteins (PubMed:23129660, PubMed:25179605, PubMed:27193484). 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 (PubMed:21743475). 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 (PubMed:21636303). 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 (By similarity). 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 (PubMed:26565908). 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 (By similarity). Also positively regulates apoptosis by interacting with and stabilizing the proapoptotic factor AIFM1 (By similarity). By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway (PubMed:26692333). {ECO:0000250|UniProtKB:Q9Z1R2, ECO:0000269|PubMed:20516149, ECO:0000269|PubMed:20676083, ECO:0000269|PubMed:21636303, ECO:0000269|PubMed:21743475, ECO:0000269|PubMed:23129660, ECO:0000269|PubMed:24981174, ECO:0000269|PubMed:25179605, ECO:0000269|PubMed:26565908, ECO:0000269|PubMed:26692333, ECO:0000269|PubMed:27193484, ECO:0000269|PubMed:28104892}.; 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 (PubMed:17403783). When nuclear, may also act as a component of some chromatin regulator complex that regulates histone 3 'Lys-4' dimethylation (H3K4me2) (PubMed:18765639). {ECO:0000269|PubMed:17403783, ECO:0000269|PubMed:18765639}.; 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:0000269|PubMed:18055229, ECO:0000269|PubMed:18852879}.; FUNCTION: Mediates ricin-induced apoptosis. {ECO:0000269|PubMed:14960581}.
uniprot
proteins
mass_dalton
119409
uniprot
proteins
mutagenesis
MUTAGEN 1001; /note="D->A: Abolishes cleavage by the caspase CASP3."; /evidence="ECO:0000269|PubMed:14960581"; MUTAGEN 1010; /note="W->A: Decreases interaction with GET4. Localizes in the nucleus and cytoplasm. Decreases interaction with GET4, localizes in the nucleus and increases GET4 ubiquitination; when associated with A-1042."; /evidence="ECO:0000269|PubMed:29042515"; MUTAGEN 1018; /note="W->A: Decreases interaction with GET4. Localizes in the nucleus. Decreases interaction with GET4, localizes in the nucleus and increases GET4 ubiquitination; when associated with A-1042."; /evidence="ECO:0000269|PubMed:29042515"; MUTAGEN 1030..1031; /note="RK->SL: No effect on interaction with GET4 and KPNA2."; /evidence="ECO:0000269|PubMed:29042515"; MUTAGEN 1042; /note="Y->A: Decreases interaction with GET4. Localizes in the nucleus. Decreases interaction with GET4, localizes in the nucleus and increases GET4 ubiquitination; when associated with A-1010 or A-1018."; /evidence="ECO:0000269|PubMed:29042515"; MUTAGEN 1049..1050; /note="KR->SL: No effect on interaction with GET4. Inhibits interaction with KPNA2."; /evidence="ECO:0000269|PubMed:29042515"; MUTAGEN 1067; /note="V->R: No effect on interaction with UBL4A. No effect on interaction with UBL4A; when associated with A-1078. Abolishes on interaction with UBL4A; when associated with R-1085."; /evidence="ECO:0000269|PubMed:25713138"; MUTAGEN 1078; /note="P->A: No effect on interaction with UBL4A. No effect on interaction with UBL4A; when associated with R-1067 or R-1085."; /evidence="ECO:0000269|PubMed:25713138"; MUTAGEN 1085; /note="L->R: No effect on interaction with UBL4A. No effect on interaction with UBL4A; when associated with R-1078. Abolishes on interaction with UBL4A; when associated with R-1067."; /evidence="ECO:0000269|PubMed:25713138"; MUTAGEN 1088; /note="D->H: No effect on interaction with UBL4A."; /evidence="ECO:0000269|PubMed:25713138
uniprot
proteins
post_translational_modification
PTM: Ricin can induce a cleavage by the caspase CASP3. The released C-terminal peptide induces apoptosis. {ECO:0000269|PubMed:14960581}.; PTM: (Microbial infection) In case of infection by L.pneumophila, ubiquitinated by the SCF(LegU1) complex. {ECO:0000269|PubMed:20547746}.
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
14656967
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14960581
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17403783
uniprot
proteins
pubmed
17924679
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18055229
uniprot
proteins
pubmed
18088087
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18765639
uniprot
proteins
pubmed
18852879
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20516149
uniprot
proteins
pubmed
20547746
uniprot
proteins
pubmed
20676083
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
2156268
uniprot
proteins
pubmed
21636303
uniprot
proteins
pubmed
21743475
uniprot
proteins
pubmed
23129660
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24160817
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24424410
uniprot
proteins
pubmed
24981174
uniprot
proteins
pubmed
25179605
uniprot
proteins
pubmed
25535373
uniprot
proteins
pubmed
25713138
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26337389
uniprot
proteins
pubmed
26565908
uniprot
proteins
pubmed
26692333
uniprot
proteins
pubmed
27113755
uniprot
proteins
pubmed
27193484
uniprot
proteins
pubmed
28104892
uniprot
proteins
pubmed
29042515
uniprot
proteins
pubmed
34887561
uniprot
proteins
pubmed
40105103
uniprot
proteins
sequence_length
1132
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17403783, ECO:0000269|PubMed:20676083, ECO:0000269|PubMed:21636303, ECO:0000269|PubMed:29042515}. Nucleus {ECO:0000269|PubMed:14960581, ECO:0000269|PubMed:17403783, ECO:0000269|PubMed:21636303, ECO:0000269|PubMed:29042515}. Secreted, extracellular exosome {ECO:0000269|PubMed:18055229, ECO:0000269|PubMed:18852879}. Note=Normally localized in cytosol and nucleus, it can also be released extracellularly, in exosomes, by tumor and myeloid dendritic cells (PubMed:18055229, PubMed:18852879). Cytoplasmic retention is due to interaction with GET4 (PubMed:29042515). {ECO:0000269|PubMed:18055229, ECO:0000269|PubMed:18852879, ECO:0000269|PubMed:29042515}.
uniprot
proteins