protein | Q8054 |
P682 | biological process | cell cycle | Q188941 |
centrosome cycle | Q5063037 | ||
centrosome duplication | Q14862229 | ||
centriole replication | Q21097393 | ||
centriole assembly | Q21105841 | ||
centriole-centriole cohesion | Q21109726 | ||
ciliary basal body organization | Q21110637 | ||
P681 | cell component | cytoplasm | Q79899 |
centrosome | Q190769 | ||
cytoskeleton | Q154626 | ||
centriole | Q178355 | ||
microtubule organizing center | Q903644 | ||
cell projection | Q14353100 | ||
ciliary basal body | Q21096453 | ||
P702 | encoded by | Sas-6 | Q29725543 |
P703 | found in taxon | Drosophila melanogaster | Q130888 |
P527 | has part(s) | Spindle assembly abnormal protein 6, N-terminal | Q24720563 |
P680 | molecular function | protein binding | Q167149 |
molecular function | Q14860489 | ||
P361 | part of | SAS-6, N-terminal domain superfamily | Q54461444 |
Spindle assembly abnormal protein 6, N-terminal domain, protein family | Q83132719 |
Q30482514 | A multicomponent assembly pathway contributes to the formation of acentrosomal microtubule arrays in interphase Drosophila cells |
Q43138655 | A proximal centriole-like structure is present in Drosophila spermatids and can serve as a model to study centriole duplication |
Q42871178 | DSas-6 and Ana2 coassemble into tubules to promote centriole duplication and engagement |
Q57843392 | Differential regulation of transition zone and centriole proteins contributes to ciliary base diversity |
Q33643718 | Drosophila Ana2 is a conserved centriole duplication factor |
Q47070311 | Drosophila Cep135/Bld10 maintains proper centriole structure but is dispensable for cartwheel formation |
Q60227664 | Gorab is a Golgi protein required for structure and duplication of Drosophila centrioles |
Q35830134 | Overexpressing centriole-replication proteins in vivo induces centriole overduplication and de novo formation. |
Q28241376 | Sas-4 provides a scaffold for cytoplasmic complexes and tethers them in a centrosome |
Q29725543 | Sas-6 | encodes | P688 |
Search more.