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IPR036533 is a BAG domain superfamily.
<p>BAG domains are present in Bcl-2-associated athanogene 1 and silencer of death domains. The BAG proteins are modulators of chaperone activity, they bind to HSP70/HSC70 proteins and promote substrate release. The proteins have anti-apoptotic activity and increase the anti-cell death function of BCL-2 induced by various stimuli. BAG-1 binds to the serine/threonine kinase Raf-1 or Hsc70/Hsp70 in a mutually exclusive interaction. BAG-1 promotes cell growth by binding to and stimulating Raf-1 activity. The binding of Hsp70 to BAG-1 diminishes Raf-1 signalling and inhibits subsequent events, such as DNA synthesis, as well as arrests the cell cycle. BAG-1 has been suggested to function as a molecular switch that encourages cells to proliferate in normal conditions but become quiescent under a stressful environment [[cite:PUB00009773], [cite:PUB00028930]].</p> <p>BAG-family proteins contain a single BAG domain, except for human BAG-5 which has four BAG repeats [[cite:PUB00054479]]. The BAG domain is a conserved region located at the C terminus of the BAG-family proteins that binds the ATPase domain of Hsc70/Hsp70. The BAG domain is evolutionarily conserved, and BAG domain containing proteins have been described and/or proven in a variety of organisms including Mus musculus (Mouse), Xenopus spp., Drosophila spp., Bombyx mori (Silk moth), Caenorhabditis elegans, Saccharomyces cerevisiae (Baker's yeast), Schizosaccharomyces pombe (Fission yeast), and Arabidopsis thaliana (Mouse-ear cress).</p> <p>The BAG domain has 110-124 amino acids and is comprised of three anti-parallel α-helices, each approximately 30-40 amino acids in length. The first and second helices interact with the serine/threonine kinase Raf-1 and the second and third helices are the sites of the BAG domain interaction with the ATPase domain of Hsc70/Hsp70. Binding of the BAG domain to the ATPase domain is mediated by both electrostatic and hydrophobic interactions in BAG-1 and is energy requiring.</p>
This description is obtained from EB-eye REST.
GO predictions are based solely on the InterPro-to-GO mappings published by EMBL-EBI, which are in turn based on the mapping of predicted domains to the InterPro dataset. The InterPro-to-GO mapping was last updated on , while the GO metadata was last updated on .
| GO term | Namespace | Name | Definition | Relationships |
|---|---|---|---|---|
| Molecular function | Chaperone binding | Interacting selectively and non-covalently with a chaperone protein, a class of proteins that bind to nascent or unfolded polypeptides and ensure correct folding or transport. |
| Transcript | Name | Description | Predicted domains | Domain count |
|---|---|---|---|---|
| – | BAG family molecular chaperone regulator; TAIR: AT3G51780.1 BCL-2-associated athanogene 4; Swiss-Prot: sp|Q8RX71|BAG4_ARATH BAG family molecular chaperone regulator 4; TrEMBL-Plants: tr|A0A1J7H3I9|A0A1J7H3I9_LUPAN Uncharacterized protein; Found in the gene: LotjaGi1g1v0444400 | 17 | ||
| – | BAG family molecular chaperone regulator-like protein; TAIR: AT5G52060.1 BCL-2-associated athanogene 1; Swiss-Prot: sp|Q0WUQ1|BAG1_ARATH BAG family molecular chaperone regulator 1; TrEMBL-Plants: tr|V7C4X6|V7C4X6_PHAVU Uncharacterized protein; Found in the gene: LotjaGi2g1v0149400 | 17 | ||
| – | BAG family molecular chaperone regulator; TAIR: AT3G51780.1 BCL-2-associated athanogene 4; Swiss-Prot: sp|Q8RX71|BAG4_ARATH BAG family molecular chaperone regulator 4; TrEMBL-Plants: tr|A0A0L9VSI6|A0A0L9VSI6_PHAAN Uncharacterized protein; Found in the gene: LotjaGi3g1v0196400 | 19 | ||
| – | BAG family molecular chaperone regulator 6; TAIR: AT2G46240.1 BCL-2-associated athanogene 6; Swiss-Prot: sp|O82345|BAG6_ARATH BAG family molecular chaperone regulator 6; TrEMBL-Plants: tr|K7MEY5|K7MEY5_SOYBN Uncharacterized protein; Found in the gene: LotjaGi3g1v0389500 | 12 | ||
| – | BAG family molecular chaperone regulator 7; TAIR: AT5G62390.1 BCL-2-associated athanogene 7; Swiss-Prot: sp|Q9LVA0|BAG7_ARATH BAG family molecular chaperone regulator 7; TrEMBL-Plants: tr|A0A0R4J460|A0A0R4J460_SOYBN Uncharacterized protein; Found in the gene: LotjaGi3g1v0553100 | 10 | ||
| – | BAG family molecular chaperone regulator-like protein; TAIR: AT5G52060.1 BCL-2-associated athanogene 1; Swiss-Prot: sp|Q0WUQ1|BAG1_ARATH BAG family molecular chaperone regulator 1; TrEMBL-Plants: tr|A0A151SLE5|A0A151SLE5_CAJCA Uncharacterized protein; Found in the gene: LotjaGi4g1v0220000 | 18 | ||
| – | BAG family molecular chaperone regulator-like protein; TAIR: AT5G52060.1 BCL-2-associated athanogene 1; Swiss-Prot: sp|Q0WUQ1|BAG1_ARATH BAG family molecular chaperone regulator 1; TrEMBL-Plants: tr|A0A1J7GEV2|A0A1J7GEV2_LUPAN Uncharacterized protein; Found in the gene: LotjaGi5g1v0304300 | 17 | ||
| – | BAG family molecular chaperone regulator 5; TAIR: AT1G12060.1 BCL-2-associated athanogene 5; Swiss-Prot: sp|O65373|BAG5_ARATH BAG family molecular chaperone regulator 5, mitochondrial; TrEMBL-Plants: tr|Q2HT37|Q2HT37_MEDTR BAG family molecular chaperone regulator 5; Found in the gene: LotjaGi6g1v0287100 | 13 | ||
| – | BAG family molecular chaperone regulator; TAIR: AT5G07220.1 BCL-2-associated athanogene 3; Swiss-Prot: sp|Q9LYP4|BAG3_ARATH BAG family molecular chaperone regulator 3; TrEMBL-Plants: tr|A0A0B2PCD3|A0A0B2PCD3_GLYSO BAG family molecular chaperone regulator 2; Found in the gene: LotjaGi6g1v0312300 | 17 |
A list of co-occurring predicted domains within the L. japonicus gene space:
| Predicted domain | Source | Observations | Saturation (%) |
|---|---|---|---|
| mobidb-lite | MobiDBLite | 1 | 11.11 |