| + |
NEDD1 | up-regulates activity 
binding
|
g-TuRC complex |
0.757 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261422 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19029337 |
It has been reported that NEDD1 directly interacts with and recruits the gamma-tubulin ring complex to centrosomes and to spindle MTs to promote MT nucleation and spindle assembly |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
TUBGCP4 | form complex 
binding
|
g-TuRC complex |
0.809 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262328 |
|
|
in vitro |
|
| pmid |
sentence |
| 31862189 |
Here, we present a cryo-EM reconstruction of the native human gamma-TuRC at 3.8A resolution, revealing an asymmetric, cone-shaped structure. Pseudo-atomic models indicate that GCP4, GCP5, and GCP6 form distinct Y-shaped assemblies that structurally mimic GCP2/GCP3 subcomplexes distal to the gamma-TuRC “seam.” |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
TUBGCP2 | form complex
binding
|
g-TuRC complex |
0.792 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262326 |
|
|
in vitro |
|
| pmid |
sentence |
| 31862189 |
Here, we present a cryo-EM reconstruction of the native human gamma-TuRC at 3.8A resolution, revealing an asymmetric, cone-shaped structure. Pseudo-atomic models indicate that GCP4, GCP5, and GCP6 form distinct Y-shaped assemblies that structurally mimic GCP2/GCP3 subcomplexes distal to the gamma-TuRC “seam.” |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
TUBGCP6 | form complex
binding
|
g-TuRC complex |
0.77 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262330 |
|
|
in vitro |
|
| pmid |
sentence |
| 31862189 |
Here, we present a cryo-EM reconstruction of the native human gamma-TuRC at 3.8A resolution, revealing an asymmetric, cone-shaped structure. Pseudo-atomic models indicate that GCP4, GCP5, and GCP6 form distinct Y-shaped assemblies that structurally mimic GCP2/GCP3 subcomplexes distal to the gamma-TuRC “seam.” |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
TUBGCP5 | form complex
binding
|
g-TuRC complex |
0.812 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262329 |
|
|
in vitro |
|
| pmid |
sentence |
| 31862189 |
Here, we present a cryo-EM reconstruction of the native human gamma-TuRC at 3.8A resolution, revealing an asymmetric, cone-shaped structure. Pseudo-atomic models indicate that GCP4, GCP5, and GCP6 form distinct Y-shaped assemblies that structurally mimic GCP2/GCP3 subcomplexes distal to the gamma-TuRC “seam.” |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
g-TuRC complex | up-regulates activity
binding
|
TUBG1 |
0.862 |
| 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 |
| + |
TUBGCP3 | form complex
binding
|
g-TuRC complex |
0.766 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262327 |
|
|
in vitro |
|
| pmid |
sentence |
| 31862189 |
Here, we present a cryo-EM reconstruction of the native human gamma-TuRC at 3.8A resolution, revealing an asymmetric, cone-shaped structure. Pseudo-atomic models indicate that GCP4, GCP5, and GCP6 form distinct Y-shaped assemblies that structurally mimic GCP2/GCP3 subcomplexes distal to the gamma-TuRC “seam.” |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
g-TuRC complex