Basic information
PhaSepDB ID psother130 Reference 30244836 Uniprot Entry P62877 Gene names Rbx1
Class PS-other Location Nucleus MLO Nuclear speckle
LLPS related evidences
Publication note We first tested whether other subunits of the CRL3SPOP ubiquitin ligase are present in the SPOP/DAXX bodies. Transient expression of Myc-Cul3, the scaffold that bridges the substrate and the E2 ubiquitin-conjugating enzyme in Cullin/RING ubiquitin ligases, resulted in its diffuse localization in the cytoplasm in the absence of SPOP. In contrast, Myc-Cul3 localized in nuclear speckles in the presence of SPOP, and in SPOP/DAXX bodies in the presence of both SPOP and DAXX. Therefore, Cul3 is recruited to liquid organelles by SPOP. HA-Rbx1, the RING protein associating with Cul3, also localizes to SPOP/DAXX bodies. In vitro, the active form of the scaffold, i.e. neddylated Cul3/Rbx1 (N8~Cul3/Rbx1), likewise partitioned into the mesoscale assemblies. Therefore, it is plausible that CRL3SPOP could carry out its function in cellular SPOP-containing liquid assemblies.
(Organism: Homo sapiens; Cell line: HeLa cells)
Material state _ : _
LLPS region 1-108 Key domains _ : _
LLPS partner
Protein partner

DAXX,SPOP,Cul3 ( Q9UER7,O43791,Q13618 )

 the tendency of H-cDAXX to undergo phase separation is strongly enhanced in the presence of SPOP, and this was the case in the presence of both polymer and protein crowders. Myc-Cul3 localized in nuclear speckles in the presence of SPOP, and in SPOP/DAXX bodies in the presence of both SPOP and DAXX. HA-Rbx1, the RING protein associating with Cul3, also localizes to SPOP/DAXX bodies.
RNA partner

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Others

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LLPS regulation
PTM

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Mutation

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Alternative splicing _
Repeat _
Oligomerization _