+ |
BRSK1 | up-regulates
phosphorylation
|
TUBG1 |
0.251 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-187405 |
Ser131 |
READGSDsLEGFVLC |
Homo sapiens |
|
pmid |
sentence |
19648910 |
Sadb kinases associate and phosphorylate gamma-tubulin on ser 131 s131d gamma-tubulin expression amplifies centrosome duplication |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
g-TuRC complex | up-regulates activity
binding
|
TUBG1 |
0.864 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262325 |
|
|
in vitro |
|
pmid |
sentence |
31862189 |
Despite its asymmetric architecture, the γ-TuRC arranges γ-tubulins into a helical geometry poised to nucleate microtubules. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
vincaleukoblastine sulfate | down-regulates activity
chemical inhibition
|
TUBG1 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-259259 |
|
|
Homo sapiens |
|
pmid |
sentence |
15579115 |
Tubulin binding molecules have generated considerable interest after the successful introduction of the taxanes into clinical oncology and the widespread use of the vinca alkaloids vincristine and vinblastine. These compounds inhibit cell mitosis by binding to the protein tubulin in the mitotic spindle and preventing polymerization into the MTs. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NUP62 | up-regulates activity
binding
|
TUBG1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261257 |
|
|
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 |
+ |
TUBG1 | up-regulates
|
Microtubule_polimerization |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261423 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
19029337 |
It has been reported that NEDD1 directly interacts with and recruits the γ-tubulin ring complex to centrosomes and to spindle MTs to promote MT nucleation and spindle assembly |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NUMA1 | up-regulates
binding
|
TUBG1 |
0.604 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-117203 |
|
|
Homo sapiens |
|
pmid |
sentence |
11956313 |
Direct binding of numa to tubulin is mediated by a novel sequence motif in the tail domain that bundles and stabilizes microtubules. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CDK5RAP2 | up-regulates activity
binding
|
TUBG1 |
0.637 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260310 |
|
|
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
17959831 |
Immunoprecipitation of CDK5RAP2 specifically coprecipitated _TuRC components, as detected on immunoblots of _-tubulin and GCP3 (Figure 3A).| Perturbing CDK5RAP2 function delocalized gamma-tubulin from the centrosomes and inhibited centrosomal microtubule nucleation, thus leading to disorganization of interphase microtubule arrays and formation of anastral mitotic spindles. Together, CDK5RAP2 is a pericentriolar structural component that functions in gammaTuRC attachment and therefore in the microtubule organizing function of the centrosome. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |