STI1Heat shock chaperonin-binding motif.
|SMART accession number:||SM00727|
|Interpro abstract (IPR006636):|
This describes a heat shock chaperonin-binding motif found in the stress-inducible phosphoprotein STI1. Both N- and C-termini of STI1 are capable of binding heat shock proteins [(PUBMED:8999875)] and the domain is found both singly and duplicated in other proteins.
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- Evolution (species in which this domain is found)
Taxonomic distribution of proteins containing STI1 domain.
This tree includes only several representative species. The complete taxonomic breakdown of all proteins with STI1 domain is also avaliable.
Click on the protein counts, or double click on taxonomic names to display all proteins containing STI1 domain in the selected taxonomic class.
- Cellular role (predicted cellular role)
Cellular role: signalling
Binding / catalysis: Heat shock chaperonin-binding
- Literature (relevant references for this domain)
Primary literature is listed below; Automatically-derived, secondary literature is also avaliable.
- Kaye FJ et al.
- A family of ubiquitin-like proteins binds the ATPase domain of Hsp70-like Stch.
- FEBS Lett. 2000; 467: 348-55
- Display abstract
We have isolated two human ubiquitin-like (UbL) proteins that bind to a short peptide within the ATPase domain of the Hsp70-like Stch protein. Chap1 is a duplicated homologue of the yeast Dsk2 gene that is required for transit through the G2/M phase of the cell cycle and expression of the human full-length cDNA restored viability and suppressed the G2/M arrest phenotype of dsk2Delta rad23Delta Saccharomyces cerevisiae mutants. Chap2 is a homologue for Xenopus scythe which is an essential component of reaper-induced apoptosis in egg extracts. While the N-terminal UbL domains were not essential for Stch binding, Chap1/Dsk2 contains a Sti1-like repeat sequence that is required for binding to Stch and is also conserved in the Hsp70 binding proteins, Hip and p60/Sti1/Hop. These findings extend the association between Hsp70 members and genes encoding UbL sequences and suggest a broader role for the Hsp70-like ATPase family in regulating cell cycle and cell death events.
- Lassle M, Blatch GL, Kundra V, Takatori T, Zetter BR
- Stress-inducible, murine protein mSTI1. Characterization of binding domains for heat shock proteins and in vitro phosphorylation by different kinases.
- J Biol Chem. 1997; 272: 1876-84
- Display abstract
We have recently isolated the cDNA for the murine homologue of the stress-inducible phosphoprotein STI1 (also known as IEF SSP 3521 or p60). STI1 was previously shown to be 2-fold up-regulated in MRC-5 fibroblasts upon viral transformation and to exist in a macromolecular complex with heat shock proteins of the HSP 70 and 90 families. By peptide-sequencing we have identified the two heat shock proteins that bind to murine STI1 (mSTI1) as HSC 70 and HSP 84/86. We describe two separate binding regions within mSTI1 for the two heat shock proteins. In the presence of cell extracts, the N-terminal region of mSTI1 binds preferentially to HSC 70, whereas the C-terminal portion of the molecule promotes the binding of HSP 84/86. Heat treatment caused a strong induction of mSTI1 message without affecting the steady-state level of the protein significantly. In addition, heat treatment led to changes in the isoform-composition of mSTI1. pp70(s6k), pp90(rsk), and mitogen-activated protein kinase-activated protein kinase 2 were tested as possible STI1 kinases in vitro using recombinant mSTI1 as a substrate: only pp90(rsk) was able to phosphorylate recombinant mSTI1. In vitro kinase assays using casein kinase II suggest serine 189 to be a likely phosphorylation site in mSTI1.
- Hohfeld J, Minami Y, Hartl FU
- Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle.
- Cell. 1995; 83: 589-98
- Display abstract
The Hsc70-interacting protein Hip, a tetratricopeptide repeat protein, participates in the regulation of the eukaryotic 70 kDa heat shock cognate Hsc70. One Hip oligomer binds the ATPase domains of at least two Hsc70 molecules dependent on activation of the Hsc70 ATPase by Hsp40. While hydrolysis remains the rate-limiting step in the ATPase cycle, Hip stabilizes the ADP state of Hsc70 that has a high affinity for substrate protein. Through its own chaperone activity, Hip may contribute to the interaction of Hsc70 with various target proteins. We propose a mechanism for the regulation of eukaryotic Hsc70 that is distinct from that of bacterial Hsp70. The Hsc70/Hsp40/Hip system is apparently independent of a GrpE-like nucleotide exchange factor.
- Structure (3D structures containing this domain)
3D Structures of STI1 domains in PDB
PDB code Main view Title 1oqy Structure of the DNA repair protein hHR23a 1pve Solution structure of XPC binding domain of hHR23B 1qze HHR23a protein structure based on residual dipolar coupling data 1tp4 Solution structure of the XPC binding domain of hHR23A protein 1x3w Structure of a peptide:N-glycanase-Rad23 complex 1x3z Structure of a peptide:N-glycanase-Rad23 complex 2f4m The Mouse PNGase-HR23 Complex Reveals a Complete Remodulation of the Protein-Protein Interface Compared to its Yeast Orthologs 2f4o The Mouse PNGase-HR23 Complex Reveals a Complete Remodulation of the Protein-Protein Interface Compared to its Yeast Orthologs 2llv Solution structure of the yeast Sti1 DP1 domain 2llw Solution structure of the yeast Sti1 DP2 domain 2lnm Solution structure of the C-terminal NP-repeat domain of Tic40, a co-chaperone during protein import into chloroplasts 2qsf Crystal structure of the Rad4-Rad23 complex 2qsg Crystal structure of Rad4-Rad23 bound to a UV-damaged DNA 2qsh Crystal structure of Rad4-Rad23 bound to a mismatch DNA
- Links (links to other resources describing this domain)