HSPB1
Gene Ontology Biological Process
- cellular response to vascular endothelial growth factor stimulus [ISO]
- intracellular signal transduction [ISO]
- negative regulation of apoptotic signaling pathway [IDA]
- negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway [IDA]
- negative regulation of protein kinase activity [IDA]
- negative regulation of protein serine/threonine kinase activity [IDA]
- platelet aggregation [ISO]
- positive regulation of angiogenesis [ISO]
- positive regulation of blood vessel endothelial cell migration [ISO]
- positive regulation of endothelial cell chemotaxis [ISO]
- positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway [ISO]
- positive regulation of interleukin-1 beta production [IDA]
- positive regulation of tumor necrosis factor biosynthetic process [IDA]
- regulation of I-kappaB kinase/NF-kappaB signaling [IDA]
- response to unfolded protein [NAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
CS
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Reconstituted Complex
An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator.
Publication
Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor alpha by phosphorylation.
The small heat shock proteins (sHsps) from human (Hsp27) and mouse (Hsp25) form large oligomers which can act as molecular chaperones in vitro and protect cells from heat shock and oxidative stress when overexpressed. In addition, mammalian sHsps are rapidly phosphorylated by MAPKAP kinase 2/3 at two or three serine residues in response to various extracellular stresses. Here we analyze ... [more]
Throughput
- Low Throughput
Curated By
- BioGRID