| protein
| binding to the C terminus of heat shock proteins HSP70 and HSC70 |
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interaction with MAPT (inducing ubiquitination of MAPT and increasing MAPT aggregation) |
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interacting with SMAD(inhibiting the transcriptional activities of the SMAD1/SMAD4 complex induced by BMP signal) |
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associates not only with the polyQ-expanded ataxin-1 but also with the normal ataxin-1 |
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binds the co-chaperone/ubiquitin ligase STUB1 (C terminus of Hsc-70-interacting protein) through a unique N-terminal PEST domain in FBXO2  |
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with the N-terminus of HSF1 (this interaction requires conformational change of HSF1 by heat stress) |
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binding to the RAF1/Hsp90 complex |
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stabilizes malin by modulating the activity of HSPA4 (NHLRC1 is unstable, and the aggregate-prone protein and co-chaperone STUB1 can modulate its stability) |
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UBE2N and UBE2D1 had distinct effects on the conformational dynamics of STUB1, suggesting different roles of the STUB1-E2 interaction in the ubiquitination of substrates and interaction with chaperones |
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STUB1 and Hsp90 interplay with a client alternately under non-stress and stress conditions, and the choice between stabilization and degradation is made by the redox state of the client |
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STUB1 and USP2 show antagonistic functions in the control of AIFM1-mediated cell death, and implicate the role of the enzymes as a switch for cells to live or die under stresses that cause truncated AIFM1 release |
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strongly inhibited the nuclear localization and the transcriptional activity of NFKB1 |
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FBXO2 interacts with another protein known for glycoprotein homeostasis, STUB1, a co-chaperon with ubiquitin ligase properties |
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STUB1 binds, ubiquitinates and regulates expression of histone deacetylase 6 (HDAC6) |
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may also facilitate MAPT degradation by abrogating the protein folding function of HDAC6 |
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RNF8 interacts with UBE2N in a manner that is similar to that of the RING-type E3 ubiquitin ligase TRAF6 and the U-box-type E3 ubiquitin ligase, STUB1 |
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ER stress reduced the binding between MAPT and STUB1, ubiquitin E3 ligase for MAPT (STUB1 binds to MAPT and is thought to promote the degradation of MAPT by its ubiquitination through ubiquitin–proteasome system) |
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is a CARD11 associated protein |
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UBE2N activity and its interaction with STUB1 precede endocytosis of GHR |
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dynamic C-terminal region of HSPA8 provides for flexibility between STUB1 and the chaperone |
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USP47 plays a crucial role in the control of axonal growth during neuronal development by antagonizing STUB1-mediated KATNA1 degradation |
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EIF5A is a target of STUB1, an E3 ligase with a U-box domain |
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STUB1 ubiquitinated FMR1 for proteasomal degradation in a molecular chaperone-independent manner |
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E3 ubiquitin ligase STUB1 is a negative regulator of both RUNX1 and RUNX1-RUNX1T1 |
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STUB1, a chaperone-dependent E3 ubiquitin ligase, modulates TFEB activity by preferentially targeting inactive phosphorylated TFEB for degradation by the ubiquitin-proteasome pathway |
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DNAJA2 and DNAJA1 were both important for CFTR folding, however overexpressing DNAJA2 but not DNAJA1 enhanced CFTR degradation at the endoplasmic reticulum by HSPA4/HSPA8 and the E3 ubiquitin ligase STUB1 |
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STUB1 is a ubiquitin ligase for OTUD3 |
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STUB1 is a negative regulator of OTUD3 and suppresses lung cancer metastasis through inhibiting OTUD3-HSPA5 signaling axis |
