Search Keyword:


Search option:


IID50180
 UniprotQ60739
ProteinBAG family molecular chaperone regulator 1
GeneBag1
OrganismMus musculus
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
 Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
355
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 137-233 Hetero dimer : IID00579Complex
 Evidence NMR 2m8s A Reference
       Region 2m8s A 137-233 order
Seq 137-233 Monomer :
 Evidence NMR 2lwp A Reference
       Region 2lwp A 137-233 order
       Region 2lwp A 137-137 high_rmsd
Seq 226-355 Monomer :
 Evidence NMR 1i6z A Reference
       Region 1i6z A 226-355 order
       Region 1i6z A 226-232 high_rmsd
       Region 1i6z A 348-355 high_rmsd
 
Prediction
NeProc
Disorder 1-150
Order 151-355
ProS 1-25,52-71,76-88
AlphaFold
Disorder 1-153,169-178,193-197,209-211,213-213,217-217,230-237,307-311,350-350,352-355
Order 154-168,179-192,198-208,212-212,214-216,218-229,238-306,312-349,351-351
Pfam Hmmer
PF02179 256-336 9.4e-17
SEG 14-31 ,69-79 ,117-134 ,140-151 ,235-248
Function
Function in SwissProt
Co-chaperone for HSP70 and HSC70 chaperone proteins (PubMed:9873016). 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. Inhibits the pro-apoptotic function of PPP1R15A, and has anti-apoptotic activity. Markedly increases the anti-cell death function of BCL2 induced by various stimuli (By similarity).