Summary
HSP20-like chaperone superfamily
The small heat shock proteins (sHSPs) prevent protein aggregation during heat shock and oppose regulated cell death. A conserved arginine residue in the HSP20/alpha-crystallin domain (Pfam:PF00011) has in fact been implicated in the development of cataracts and myopathies [1]. The CS family (Pfam:PF04969) includes proteins that are known to bind HSP90 [2], as well as p23 (Swiss:Q15185), which is an HSP90 co-chaperone [3].
This clan contains 5 families and the total number of domains in the clan is 6137.
Literature references
- van Montfort RL, Basha E, Friedrich KL, Slingsby C, Vierling E; , Nat Struct Biol 2001;8:1025-1030.: Crystal structure and assembly of a eukaryotic small heat shock protein. 11702068
- Lee YT, Jacob J, Michowski W, Nowotny M, Kuznicki J, Chazin WJ; , J Biol Chem 2004;279:16511-16517.: Human Sgt1 binds HSP90 through the CHORD-Sgt1 domain and not the tetratricopeptide repeat domain. 14761955
- Weaver AJ, Sullivan WP, Felts SJ, Owen BA, Toft DO; , J Biol Chem 2000;275:23045-23052.: Crystal structure and activity of human p23, a heat shock protein 90 co-chaperone. 10811660
Members
This clan contains the following 5 member families:
CS DUF1872 GvpH HSP20 PIH1External database links
| SCOP: | 49764 |
Domain organisation
Below is a listing of the unique domain organisations or architectures from this clan. More...
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Alignments
The table below shows the number of occurrences of each domain throughout the sequence database. More...
| Pfam family | Num. domains | Alignment |
|---|---|---|
| HSP20 (PF00011) | 4703 (76.6%) | View |
| CS (PF04969) | 1154 (18.8%) | View |
| PIH1 (PF08190) | 252 (4.1%) | View |
| DUF1872 (PF08959) | 14 (0.2%) | View |
| GvpH (PF05455) | 14 (0.2%) | View |
| Total: 5 | Total: 6137 | Clan alignment |
Please note: Clan alignments can be very large and can cause problems for some browsers. Read the note above before viewing.
Family relationships
This diagram shows the relationships between members of this clan. More...
Species distribution
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HideThis tree shows the occurrence of the domains in this clan across different species. More...
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Interactions
Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the MSD group, to allow us to map Pfam domains onto UniProt three-dimensional structures. The table below shows the mapping between the Pfam families in this clan, the corresponding UniProt entries, and the region of the three-dimensional structures that are available for that sequence.
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