sHsps have some structural features in common: Very characteristic is a homologous and highly conserved amino acid sequence, the so-called α-crystallin-domain at the C-terminus. These sequences consist of 80 to 100 residues with a homology between 20% and 60% and form β-sheets, which are important for the formation of stable dimers.
Hsp26p; HSP26; Small heat shock protein (sHSP) with chaperone activity; forms hollow, sphere-shaped oligomers that suppress unfolded proteins aggregation; oligomer activation requires a heat-induced conformational change; not expressed in unstressed cells
HSP26 involved in several pathways and played different roles in them. We selected most pathways HSP26 participated on our site, such as Protein processing in endoplasmic reticulum, which may be useful for your reference. Also, other proteins which involved in the same pathway with HSP26 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
HSP26 has several biochemical functions, for example, mRNA binding, unfolded protein binding. Some of the functions are cooperated with other proteins, some of the functions could acted by HSP26 itself. We selected most functions HSP26 had, and list some proteins which have the same functions with HSP26. You can find most of the proteins on our site.
Function mRNA binding
Related Protein CSTF2T; RPL13A; PTBP2; LIN28A; ZFP36L1; CELF3; CALR; DHFR; PARK7; RBM38
Function unfolded protein binding
Related Protein DNAJA3B; PFDN5; HSPA1A; CANX; CCT3; CLN3; HSP90AA1.2; ST13; LMAN1; DNAJB1A