Q60739 · BAG1_MOUSE
- ProteinBAG family molecular chaperone regulator 1
- GeneBag1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids355 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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).
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).
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).
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).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | membrane | |
Cellular Component | nucleus | |
Cellular Component | perinuclear region of cytoplasm | |
Molecular Function | adenyl-nucleotide exchange factor activity | |
Molecular Function | protein-folding chaperone binding | |
Biological Process | apoptotic process | |
Biological Process | negative regulation of apoptotic process | |
Biological Process | negative regulation of motor neuron apoptotic process | |
Biological Process | negative regulation of protein phosphorylation | |
Biological Process | neuron differentiation | |
Biological Process | positive regulation of Schwann cell differentiation | |
Biological Process | positive regulation of smooth muscle cell apoptotic process | |
Biological Process | protein localization to mitochondrion | |
Biological Process | protein stabilization |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBAG family molecular chaperone regulator 1
- Short namesBAG-1
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ60739
- Secondary accessions
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000002782 | 1-355 | BAG family molecular chaperone regulator 1 | |||
Sequence: MAGRSAARRPRGDREPLGPRLRAPRPAREPRQSESRAERGLPPSQRSSVRSAASGHDRSTRGAPAGACKPRVKKKVRPRSSQSEKVGSSSRELTRSKKVTRSKNVTGTQVEEVTKIEEATQTEEVTVAEEVTQTDNMAKTEEMVQTEEMETPRLSVIVTHSNERYDLLVTPQQGNSEPVVQDLAQLVEEATGVPLPFQKLIFKGKSLKEMETPLSALGMQNGCRVMLIGEKSNPEEEVELKKLKDLEVSAEKIANHLQELNKELSGIQQGFLAKELQAEALCKLDRKVKATIEQFMKILEEIDTMVLPEQFKDSRLKRKNLVKKVQVFLAECDTVEQYICQETERLQSTNLALAE |
Post-translational modification
Ubiquitinated; mediated by SIAH1 or SIAH2 and leading to its subsequent proteasomal degradation.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Isoform 2 is expressed in the heart, lung, kidney and spinal cord. Isoform 1 and isoform 2 are expressed in hematopoietic cell lines. The levels of isoform 2 are relatively constant in all the cell lines examined while the levels of isoform 1 are more variable (at protein level). Isoform 1 is expressed in the lung and kidney. Isoform 2 is expressed in various tissues, with highest levels in testis and stomach.
Gene expression databases
Interaction
Subunit
Homodimer. Forms a heteromeric complex with HSP70/HSC70. Binds to the ATPase domain of HSP/HSC70 chaperones. Interacts with NR3C1. Interacts with the N-terminal region of MAPRE2. Interacts with PPP1R15A. Interacts with BCL2 in an ATP-dependent manner. Interacts with SIAH1, HSPA8 (via NBD), HSPA1A (via NBD) and HSPA1B (via NBD) (By similarity).
Interacts with SIAH2 (PubMed:11257006).
Interacts with ESR1; the interaction is promoted in the absence of estradiol (17-beta-estradiol/E2) (By similarity).
Interacts with SIAH2 (PubMed:11257006).
Interacts with ESR1; the interaction is promoted in the absence of estradiol (17-beta-estradiol/E2) (By similarity).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, repeat, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-112 | Disordered | ||||
Sequence: MAGRSAARRPRGDREPLGPRLRAPRPAREPRQSESRAERGLPPSQRSSVRSAASGHDRSTRGAPAGACKPRVKKKVRPRSSQSEKVGSSSRELTRSKKVTRSKNVTGTQVEE | ||||||
Compositional bias | 7-36 | Basic and acidic residues | ||||
Sequence: ARRPRGDREPLGPRLRAPRPAREPRQSESR | ||||||
Compositional bias | 38-55 | Polar residues | ||||
Sequence: ERGLPPSQRSSVRSAASG | ||||||
Repeat | 103-108 | 1 | ||||
Sequence: KNVTGT | ||||||
Repeat | 111-116 | 2 | ||||
Sequence: EEVTKI | ||||||
Region | 111-209 | 7 X 6 AA tandem repeat of E-E-X4 | ||||
Sequence: EEVTKIEEATQTEEVTVAEEVTQTDNMAKTEEMVQTEEMETPRLSVIVTHSNERYDLLVTPQQGNSEPVVQDLAQLVEEATGVPLPFQKLIFKGKSLKE | ||||||
Repeat | 117-122 | 3 | ||||
Sequence: EEATQT | ||||||
Repeat | 123-128 | 4 | ||||
Sequence: EEVTVA | ||||||
Repeat | 129-134 | 5 | ||||
Sequence: EEVTQT | ||||||
Region | 132-151 | Disordered | ||||
Sequence: TQTDNMAKTEEMVQTEEMET | ||||||
Repeat | 141-146 | 6 | ||||
Sequence: EEMVQT | ||||||
Repeat | 147-152 | 7 | ||||
Sequence: EEMETP | ||||||
Domain | 154-234 | Ubiquitin-like | ||||
Sequence: LSVIVTHSNERYDLLVTPQQGNSEPVVQDLAQLVEEATGVPLPFQKLIFKGKSLKEMETPLSALGMQNGCRVMLIGEKSNP | ||||||
Region | 182-229 | Interaction with HSPA8 | ||||
Sequence: DLAQLVEEATGVPLPFQKLIFKGKSLKEMETPLSALGMQNGCRVMLIG | ||||||
Region | 226-355 | Interaction with PPP1R15A | ||||
Sequence: MLIGEKSNPEEEVELKKLKDLEVSAEKIANHLQELNKELSGIQQGFLAKELQAEALCKLDRKVKATIEQFMKILEEIDTMVLPEQFKDSRLKRKNLVKKVQVFLAECDTVEQYICQETERLQSTNLALAE | ||||||
Domain | 256-336 | BAG | ||||
Sequence: HLQELNKELSGIQQGFLAKELQAEALCKLDRKVKATIEQFMKILEEIDTMVLPEQFKDSRLKRKNLVKKVQVFLAECDTVE |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative initiation.
Q60739-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- SynonymsBAG-1L, p50
- Length355
- Mass (Da)39,740
- Last updated1999-07-15 v3
- Checksum077A765CA869D3A7
Q60739-2
- Name2
- SynonymsBAG-1S, p32
- Differences from canonical
- 1-136: Missing
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F6TCF9 | F6TCF9_MOUSE | Bag1 | 355 |
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_018667 | 1-136 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 7-36 | Basic and acidic residues | ||||
Sequence: ARRPRGDREPLGPRLRAPRPAREPRQSESR | ||||||
Compositional bias | 38-55 | Polar residues | ||||
Sequence: ERGLPPSQRSSVRSAASG | ||||||
Sequence conflict | 64 | in Ref. 5; AAH93509/AAH69918/AAH03722 | ||||
Sequence: P → A |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF022223 EMBL· GenBank· DDBJ | AAC34259.1 EMBL· GenBank· DDBJ | mRNA | ||
AK009149 EMBL· GenBank· DDBJ | BAB26106.1 EMBL· GenBank· DDBJ | mRNA | ||
AL837521 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH466538 EMBL· GenBank· DDBJ | EDL05422.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC003722 EMBL· GenBank· DDBJ | AAH03722.2 EMBL· GenBank· DDBJ | mRNA | ||
BC069918 EMBL· GenBank· DDBJ | AAH69918.2 EMBL· GenBank· DDBJ | mRNA | ||
BC093509 EMBL· GenBank· DDBJ | AAH93509.2 EMBL· GenBank· DDBJ | mRNA |