Basic information
| PhaSepDB ID | psself280 | Reference | 33218630,26553976 | Uniprot Entry | P16333 | Gene names | Nck |
|---|---|---|---|---|---|---|---|
| Class | PS-self | Location | Nucleus | MLO | Receptor cluster | ||
LLPS related evidences
| Publication note | Here, we show that the 50-residue linker between the first two SH3 domains of Nck enhances phase separation of Nck/N-WASP/nephrin assemblies. Two linear motifs within this element, as well as its overall positively charged character, are important for this effect. The linker increases the driving force for self-assembly of Nck, likely through weak interactions with the second SH3 domain, and this effect appears to promote phase separation. The linker sequence is highly conserved, suggesting that the sequence determinants of the driving forces for phase separation may be generally important to Nck functions. (Organism: Homo sapiens; Cell line: _) |
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|---|---|---|---|
| Material state | liquid : Upon mixing 3 μM p-nephrin, 2 μM N-WASP (10% Alexa488-labeled), and 10 μM Nck, micrometer-scale droplets can be visualized. | ||
| LLPS region | 1-377 | Key domains | Linker between the first and second SH3 domain,SH3 domain : Linker between the first and second SH3 domains can promote phase separation of Nck constructs. Phase separation is dependent on both the number of SH3 domains in Nck and the number of pTyr sites in p-nephrin. |
LLPS partner
| Protein partner | N-WASP,nephrin ( O00401,O60500 ) |
The 50-residue linker between the first two SH3 domains of Nck enhances phase separation of Nck/N-WASP/nephrin assemblies. |
|---|---|---|
| RNA partner | _ |
_ |
| Others | _ |
_ |
LLPS regulation
| PTM | _ |
_ |
|---|---|---|
| Mutation | _ |
_ |
| Alternative splicing | _ | |
| Repeat | _ | |
| Oligomerization | _ | |