Overview
| Uniprot ID | Q99933 |
|---|
| Protein Name | BAG family molecular chaperone regulator 1 |
|---|
| Gene Name | BAG1 |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 221 |
RVMLIGKKNSPQEEV |
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)
Protein Sequence
10
MAQRGGARRP
20
RGDRERLGSR
30
LRALRPGREP
40
RQSEPPAQRG
50
PPPSGRPPAR
60
STASGHDRPT
70
RGAAAGARRP
80
RMKKKTRRRS
90
TRSEELTRSE
100
ELTLSEEATW
110
SEEATQSEEA
120
TQGEEMNRSQ
130
EVTRDEESTR
140
SEEVTREEMA
150
AAGLTVTVTH
160
SNEKHDLHVT
170
SQQGSSEPVV
180
QDLAQVVEEV
190
IGVPQSFQKL
200
IFKGKSLKEM
210
ETPLSALGIQ
220
DGCRVMLIGK
230
KNSPQEEVEL
240
KKLKHLEKSV
250
EKIADQLEEL
260
NKELTGIQQG
270
FLPKDLQAEA
280
LCKLDRRVKA
290
TIEQFMKILE
300
EIDTLILPEN
310
FKDSRLKRKG
320
LVKKVQAFLA
330
ECDTVEQNIC
340
QETERLQSTN
FALAE
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0005829 |
cytosol |
| Cellular Component |
GO:0016020 |
membrane |
| Cellular Component |
GO:0005654 |
nucleoplasm |
| Cellular Component |
GO:0005634 |
nucleus |
| Molecular Function |
GO:0000774 |
adenyl-nucleotide exchange factor activity |
| Molecular Function |
GO:0051087 |
protein-folding chaperone binding |
| Molecular Function |
GO:0031625 |
ubiquitin protein ligase binding |
| Biological Process |
GO:0006915 |
apoptotic process |
| Biological Process |
GO:0007166 |
cell surface receptor signaling pathway |
| Biological Process |
GO:0043066 |
negative regulation of apoptotic process |
| Biological Process |
GO:0034393 |
positive regulation of smooth muscle cell apoptotic process |
| Biological Process |
GO:0006457 |
protein folding |
| Biological Process |
GO:0050821 |
protein stabilization |
Reference
[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.