+ |
NUP62 | up-regulates activity
binding
|
SASS6 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261256 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
24107630 |
Furthermore, we found interactions and co-localization with γ-tubulin and SAS-6. Our results also point to a potential role of Nup62 in targeting gamma-tubulin and SAS-6 to the centrioles. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
FBXW5 | down-regulates quantity by destabilization
ubiquitination
|
SASS6 |
0.553 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275478 |
|
|
|
|
pmid |
sentence |
21725316 |
We identify the centriolar protein HsSAS-6 (refs 4,5) as a critical substrate of the SCF-FBXW5 complex. FBXW5 binds HsSAS-6 and promotes its ubiquitylation in vivo. |expression of the wild-type form of FBXW5 accelerated the degradation of HsSAS-6 to a half-life of less than two hours |
|
Publications: |
1 |
+ |
CEP135 | up-regulates activity
binding
|
SASS6 |
0.616 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269676 |
|
|
Homo sapiens |
|
pmid |
sentence |
23511974 |
In this study, we demonstrate that the human microcephaly protein, CEP135, directly interacts with hSAS-6 via its carboxyl-terminus and with MTs via its amino-terminus. Unexpectedly, CEP135 also interacts with another microcephaly protein CPAP via its amino terminal domain. Depletion of CEP135 not only perturbed the centriolar localization of CPAP, but also blocked CPAP-induced centriole elongation. We propose that CEP135 may serve as a linker protein that directly connects the central hub protein, hSAS-6, to the outer MTs, and suggest that this interaction stabilizes the proper cartwheel structure for further CPAP-mediated centriole elongation. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |