SMART: STI1 domain annotation

STI1 Heat shock chaperonin-binding motif.

SMART accession number:	SM00727
Description:
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.
Family alignment:	View or

There are 1623 STI1 domains in 926 proteins in SMART's nrdb database.

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Evolution (species in which this domain is found)
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This tree shows only several representative species. The complete taxonomic breakdown of all proteins with STI1 domain is also avaliable.

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Go to specific node: Anopheles gambiae, Arabidopsis thaliana, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus, Saccharomyces cerevisiae, Takifugu rubripes
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)

Links (links to other resources describing this domain)
INTERPRO IPR006636

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
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
3esw		Complex of yeast pngase with glcnac2-iac.

STI1

3D Structures of STI1 domains in PDB