BAG1
entrez
573
canonical
uniprot
Q99933
canonical
ensembl
ENSG00000107262
resolver
ensp
ENSP00000369026
resolver
ensp
ENSP00000489189
resolver
genesymbol
BAG1
resolver
genesymbol_syn
HAP
resolver
hgnc
HGNC:937
resolver
uniprot
A0A0S2Z3K4
resolver
uniprot
O75315
resolver
uniprot
Q14414
resolver
uniprot
Q53H32
resolver
uniprot
Q5VZE8
resolver
uniprot
Q5VZE9
resolver
uniprot
Q5VZF0
resolver
uniprot
Q96TG2
resolver
uniprot
Q9Y2V4
resolver
uniprot_entry
A0A0S2Z3K4_HUMAN
resolver
uniprot_entry
BAG1_HUMAN
resolver
uniprot_sec
O75315
resolver
uniprot_sec
Q14414
resolver
uniprot_sec
Q53H32
resolver
uniprot_sec
Q5VZE8
resolver
uniprot_sec
Q5VZE9
resolver
uniprot_sec
Q5VZF0
resolver
uniprot_sec
Q96TG2
resolver
uniprot_sec
Q9Y2V4
resolver
amino_acid_sequence
MAQRGGARRPRGDRERLGSRLRALRPGREPRQSEPPAQRGPPPSGRPPARSTASGHDRPTRGAAAGARRPRMKKKTRRRSTRSEELTRSEELTLSEEATWSEEATQSEEATQGEEMNRSQEVTRDEESTRSEEVTREEMAAAGLTVTVTHSNEKHDLHVTSQQGSSEPVVQDLAQVVEEVIGVPQSFQKLIFKGKSLKEMETPLSALGIQDGCRVMLIGKKNSPQEEVELKKLKHLEKSVEKIADQLEELNKELTGIQQGFLPKDLQAEALCKLDRRVKATIEQFMKILEEIDTLILPENFKDSRLKRKGLVKKVQAFLAECDTVEQNICQETERLQSTNFALAE
uniprot
proteins
function
FUNCTION: Co-chaperone for HSP70 and HSC70 chaperone proteins. Acts as a nucleotide-exchange factor (NEF) promoting the release of ADP from the HSP70 and HSC70 proteins thereby triggering client/substrate protein release. Nucleotide release is mediated via its binding to the nucleotide-binding domain (NBD) of HSPA8/HSC70 where as the substrate release is mediated via its binding to the substrate-binding domain (SBD) of HSPA8/HSC70 (PubMed:24318877, PubMed:27474739, PubMed:9873016). Inhibits the pro-apoptotic function of PPP1R15A, and has anti-apoptotic activity (PubMed:12724406). Markedly increases the anti-cell death function of BCL2 induced by various stimuli (PubMed:9305631). Involved in the STUB1-mediated proteasomal degradation of ESR1 in response to age-related circulating estradiol (17-beta-estradiol/E2) decline, thereby promotes neuronal apoptosis in response to ischemic reperfusion injury (By similarity). {ECO:0000250|UniProtKB:B0K019, ECO:0000269|PubMed:12724406, ECO:0000269|PubMed:24318877, ECO:0000269|PubMed:27474739, ECO:0000269|PubMed:9305631, ECO:0000269|PubMed:9873016}.
uniprot
proteins
mass_dalton
38779
uniprot
proteins
mutagenesis
MUTAGEN 308..309; /note="RK->AA: Significant loss of interaction with HSPA8."; /evidence="ECO:0000269|PubMed:27474739
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated; mediated by SIAH1 or SIAH2 and leading to its subsequent proteasomal degradation. {ECO:0000305}.
uniprot
proteins
pubmed
10477749
uniprot
proteins
pubmed
11222862
uniprot
proteins
pubmed
12724406
uniprot
proteins
pubmed
15164053
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15986447
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
24318877
uniprot
proteins
pubmed
27474739
uniprot
proteins
pubmed
8524784
uniprot
proteins
pubmed
8812483
uniprot
proteins
pubmed
9305631
uniprot
proteins
pubmed
9396724
uniprot
proteins
pubmed
9582267
uniprot
proteins
pubmed
9679980
uniprot
proteins
pubmed
9873016
uniprot
proteins
sequence_length
345
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 1]: Nucleus. Cytoplasm. Note=Isoform 1 localizes predominantly to the nucleus.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Nucleus. Note=Isoform 2 localizes to the cytoplasm and shuttles into the nucleus in response to heat shock.; SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm. Nucleus. Note=Isoform 4 localizes predominantly to the cytoplasm. The cellular background in which it is expressed can influence whether it resides primarily in the cytoplasm or is also found in the nucleus. In the presence of BCL2, localizes to intracellular membranes (what appears to be the nuclear envelope and perinuclear membranes) as well as punctate cytosolic structures suggestive of mitochondria.
uniprot
proteins