protein
| binding to the EEVD motif of HSP70 and HSP90 families through the TPR domain |
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likely binds to both monomers of HSP90 in the form of a clamp, interacting with residues in the middle domain of HSP90, thus preventing ATP hydrolysis, possibly by the prevention of association of N-terminal and middle domains in individual HSP90 monomers |
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interacting with WDR36 |
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interacting with PRNP (enhances neuronal PRNP synthesis via MTOR) |
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directly binds to chaperones to regulate their activities |
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interacts with tubulin and colocalizes with microtubules in endothelial cells |
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direct interaction between STIP1 and PIAS1 is involved in the accumulation of nuclear STIP1, and this retention mechanism could facilitate nuclear chaperone activity |
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cytoplasmic STIP1 directly interacts with the GTPase RND1 |
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may be part of the cancer gene signature induced by a combination of mutant TP53 and mutated RAS that is associated with cellular transformation |
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STIP1 acts as a scaffold promoting the interaction between KDM1A and GSK3B |
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STIP1 interacted with Axin, enhanced the interaction between Axin and DVL2, thus activated beta-catenin/TCF signaling |
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IL7 stimulation induced the phosphorylation of the proteins STIP1, ATIC and HNRNPH, involved in pathways related to survival, proliferation and gene expression, respectively, and increased the phosphorylation of CRKL |
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is a co-chaperone of HSPA4 and HSP90AA1 that regulates a number of cell biology processes via interactions with cellular proteins |
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STIP1 stabilises EMD and loss of STIP1 alters nuclear structure via EMD degradation |