+ |
SIK2 | down-regulates
phosphorylation
|
CEP250 |
0.326 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-167488 |
Ser2392 |
AGLHHSLsHSLLAVA |
Homo sapiens |
|
pmid |
sentence |
20708153 |
Here, we show that the salt inducible kinase 2 (sik2) localizes at the centrosome, plays a key role in the initiation of mitosis, and regulates the localization of the centrosome linker protein, c-nap1, through s2392 phosphorylation |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NEK2 | down-regulates
phosphorylation
|
CEP250 |
0.766 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-204833 |
Ser2392 |
AGLHHSLsHSLLAVA |
Homo sapiens |
|
pmid |
sentence |
24695856 |
Our data support a model in which centrosome disjunction is triggered by the hyperphosphorylation of c-nap1, a major linker component. This occurs in response to a shift in the balance of activities of the nek2?_Pp1 bi-stable switch. C-nap1 hyperphosphorylation triggers the loss of both oligomerization and, crucially, interaction with the core centriole proximal-end protein, cep135. All three of these sites were identified in our in vivo analysis but only two (s2234 and s2394) were identified as nek2 phosphorylation sites in vitro. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-204837 |
Ser2394 |
LHHSLSHsLLAVAQA |
Homo sapiens |
|
pmid |
sentence |
24695856 |
C-nap1 hyperphosphorylation triggers the loss of both oligomerization and, crucially, interaction with the core centriole proximal-end protein, cep135. All three of these sites were identified in our in vivo analysis but only two (s2234 and s2394) were identified as nek2 phosphorylation sites in vitro. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
SIK2 |
phosphorylation
|
CEP250 |
0.326 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-167492 |
Ser2394 |
LHHSLSHsLLAVAQA |
Homo sapiens |
|
pmid |
sentence |
20708153 |
Remarkably, lc-ms confirmed that the predominant serine phosphorylation site of the recombinant carboxy-terminal domain of c-nap1 is s2392 at the predicted consensus phosphorylation sequence and to a lesser extent s2394. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CEP250 | up-regulates activity
relocalization
|
CCDC102B |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275625 |
|
|
|
|
pmid |
sentence |
30404835 |
CCDC102B is recruited to the centrosome by C-Nap1 (also known as CEP250) and interacts with the centrosome linker components rootletin and LRRC45. CCDC102B decorates and facilitates the formation of rootletin filaments. Furthermore, CCDC102B is phosphorylated by Nek2A (an isoform encoded by NEK2) and is disassociated from the centrosome at the onset of mitosis. |
|
Publications: |
1 |
+ |
PCM1 | up-regulates
relocalization
|
CEP250 |
0.532 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-133334 |
|
|
Homo sapiens |
|
pmid |
sentence |
15659651 |
Recruitment of nek2 and c-nap1 to the centrosome is dependent on pcm-1 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CEP250 | down-regulates
|
Centrosome_separation |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273705 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
24035387 |
C-Nap1 and rootletin have been previously reported to be the important centrosome linker components involved in centrosome cohesion. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
CEP250 | down-regulates
|
Centrosome_separation |
0.7 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265498 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
24769208 |
C-NAP1 which is located in the proximal ends of the centriole is an important factor for maintaining cohesion of centrioles in interphase |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
SCYL1 | down-regulates activity
relocalization
|
CEP250 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265497 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
24769208 |
Moreover, TEIF closely co-localized with C-NAP1 at the proximal ends of centrioles, and centriolar loading of TEIF stimulated by EGF/Akt could displace C-NAP1, resulting in centrosome splitting. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
LRRC45 | up-regulates activity
binding
|
CEP250 |
0.419 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273703 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
24035387 |
Here, we show that LRRC45 is a centrosome linker that localizes at the proximal ends of the centrioles and forms fiber-like structures between them. Depletion of LRRC45 results in centrosome splitting during interphase. LRRC45 interacts with C-Nap1 and rootletin |
|
Publications: |
1 |
Organism: |
Homo Sapiens |