+ |
BAG1 | up-regulates activity
binding
|
STUB1 |
0.556 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272587 |
|
|
Chlorocebus aethiops |
COS-1 Cell |
pmid |
sentence |
11676916 |
BAG-1 stimulates CHIP-induced degradation of the glucocorticoid hormone receptor (GR). A model for the cooperation of CHIP and BAG-1 in coupling Hsc/Hsp70 to the ubiquitin/proteasome system. CHIP associates with Hsc/Hsp70 via its TPR chaperone adaptor (TPR) and, at the same time, recruits E2 ubiquitin-conjugating enzymes of the Ubc4/5 family to the chaperone complex. BAG-1 binds to Hsp70 via its BAG domain (BAG) and utilizes its ubiquitin-like domain (ubl) for proteasomal association |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
BAG1 | up-regulates activity
binding
|
HSPA8 |
0.891 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-254115 |
|
|
in vitro |
|
pmid |
sentence |
27474739 |
Heat shock cognate protein 70 (Hsc70) regulates protein homeostasis through its reversible interactions with client proteins. Hsc70 has two major domains: a nucleotide-binding domain (NBD), that hydrolyzes ATP, and a substrate-binding domain (SBD), where clients are bound. Members of the BAG family of co-chaperones, including Bag1 and Bag3, are known to accelerate release of both ADP and client from Hsc70. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
DNMT1 | up-regulates quantity by expression
transcriptional regulation
|
BAG1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-254108 |
|
|
Homo sapiens |
|
pmid |
sentence |
18413740 |
DNA methyltransferase 1 and 3B activate BAG-1 expression via recruitment of CTCFL/BORIS and modulation of promoter histone methylation |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CTCFL | up-regulates quantity by expression
transcriptional regulation
|
BAG1 |
0.285 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-254107 |
|
|
Rattus norvegicus |
Rat-1 Cell |
pmid |
sentence |
18413740 |
DNA methyltransferase 1 and 3B activate BAG-1 expression via recruitment of CTCFL/BORIS and modulation of promoter histone methylation |
|
Publications: |
1 |
Organism: |
Rattus Norvegicus |
+ |
BAG1 | down-regulates activity
|
PPP1R15A |
0.456 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-254117 |
|
|
Homo sapiens |
SW-480 Cell |
pmid |
sentence |
12724406 |
Human BAG-1 proteins bind to the cellular stress response protein GADD34 and interfere with GADD34 functions.|BAG-1 negatively modulates GADD34-bound PP1 activity, and the expression of BAG-1 isoforms can also mask GADD34-mediated inhibition of colony formation and suppression of transcription. Our findings suggest that BAG-1 may function to suppress the GADD34-mediated cellular stress response and support a role for BAG-1 in the survival of cells undergoing stress. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
BAG1 | up-regulates activity
binding
|
BCL2 |
0.424 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-254118 |
|
|
Homo sapiens |
JURKAT Cell |
pmid |
sentence |
7834747 |
Cloning and functional analysis of BAG-1: A novel Bcl-2-binding protein with anti-cell death activity| |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
DNMT3B | up-regulates quantity by expression
transcriptional regulation
|
BAG1 |
0.332 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-254109 |
|
|
Homo sapiens |
HCT-116 Cell |
pmid |
sentence |
18413740 |
DNA methyltransferase 1 and 3B activate BAG-1 expression via recruitment of CTCFL/BORIS and modulation of promoter histone methylation |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
BAG1 | down-regulates quantity by destabilization
binding
|
HSPA8 |
0.891 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272589 |
|
|
Chlorocebus aethiops |
COS-1 Cell |
pmid |
sentence |
11676916 |
BAG-1 stimulates CHIP-induced degradation of the glucocorticoid hormone receptor (GR). A model for the cooperation of CHIP and BAG-1 in coupling Hsc/Hsp70 to the ubiquitin/proteasome system. CHIP associates with Hsc/Hsp70 via its TPR chaperone adaptor (TPR) and, at the same time, recruits E2 ubiquitin-conjugating enzymes of the Ubc4/5 family to the chaperone complex. BAG-1 binds to Hsp70 via its BAG domain (BAG) and utilizes its ubiquitin-like domain (ubl) for proteasomal association |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |