heat shock 70 kD protein 1B (HSPA1B)
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Function
- in cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation & mediate folding of newly translated polypeptides in the cytosol as well as within organelles
- Hsp70s precognize nonnative conformations of other proteins
- they bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation & membrane translocation, or following stress-induced damage
- in the case of rotavirus A infection, HSPA1A serves as a post- attachment receptor for the virus to facilitate entry into the cell
- essential for STUB1-mediated ubiquitination & degradation of FOXP3 in regulatory T-cells (treg) during inflammation
- component of the catsper complex
- identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs
- interacts with CHCHD3, DNAJC7, IRAK1BP1, PPP5C & TSC2
- interacts with TERT
- interacts with TRIM5 (via B30.2/SPRY domain)
- interacts with METTL21A
- interacts with PARK2
- interacts with FOXP3
- interacts with NOD2
- interaction enhances NOD2 stability
- interacts with DNAJC9 (via J domain)
- interacts with ATF5
- interaction protects ATF5 from degradation via proteasome-dependent & caspase-dependent processes
Structure
belongs to the heat shock protein 70 family
Compartment
Expression
- HSPA1B is testis-specific
- induced by heat shock
Notes
localized in cytoplasmic mRNP granules containing untranslated mRNAs
More general terms
References
- ↑ UniProt http://www.uniprot.org/uniprot/P0DMV9.html
- ↑ NIEHS-SNPs http://egp.gs.washington.edu/data/hspa1b/
Database
- Entrez gene: http://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Retrieve&dopt=Graphics&list_uids=3303
- Entrez gene: http://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Retrieve&dopt=Graphics&list_uids=3304
- Kegg: http://www.genome.jp/dbget-bin/www_bget?hsa:3303
- Kegg: http://www.genome.jp/dbget-bin/www_bget?hsa:3304
- OMIM: https://mirror.omim.org/entry/140550
- OMIM: https://mirror.omim.org/entry/603012
- UniProt: http://www.uniprot.org/uniprot/P0DMV9.html