STIP1
Description
The STIP1 (stress induced phosphoprotein 1) is a protein-coding gene located on chromosome 11.
STIP1, also known as Stress-induced-phosphoprotein 1 (STI1) or Hsp70-Hsp90 organizing protein (Hop), is encoded by the human STIP1 gene. It acts as a co-chaperone, reversibly linking the protein chaperones Hsp70 and Hsp90. STIP1 belongs to a large group of co-chaperones that regulate and assist major chaperones, mainly heat shock proteins. It is one of the best studied co-chaperones of the Hsp70-Hsp90 complex. First discovered in yeast, homologues have been identified in humans, mice, rats, insects, plants, parasites, and viruses. The family of these proteins is referred to as STI1 (stress inducible protein) and can be divided into yeast, plant, and animal STI1 (Hop). STIP1 is located on chromosome 11q13.1 and consists of 14 exons. STI proteins are characterized by nine tetratricopeptide repeat (TPR) motifs clustered into domains of three TPRs. The TPR motif is a common structural feature used by many proteins and provides the ability of directing protein-protein interactions. Crystallographic structural information is available for the N-terminal TPR1 and the central TPR2A domains in complex with Hsp90.
STIP1 acts as a co-chaperone for HSP90AA1, facilitating the interaction between the molecular chaperones HSPA8/HSC70 and HSP90.
STIP1 is also known as HEL-S-94n, HOP, IEF-SSP-3521, P60, STI1, STI1L.
