| + |
LRRK1 | up-regulates activity 
phosphorylation
|
CDK5RAP2 |
0.52 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275468 |
Ser140 |
SLAEAGGsEIQRVKE |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 26192437 |
Interestingly, LRRK1 in turn phosphorylates CDK5RAP2(Cep215), a human homologue of Drosophila Centrosomin (Cnn), in its gamma-tubulin-binding motif, thus promoting the interaction of CDK5RAP2 with gamma-tubulin. LRRK1 phosphorylation of CDK5RAP2 Ser 140 is necessary for CDK5RAP2-dependent microtubule nucleation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK5RAP2 | up-regulates quantity by stabilization
phosphorylation
|
APP |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260818 |
Thr743 |
VEVDAAVtPEERHLS |
Homo sapiens |
|
| pmid |
sentence |
| 15178331 |
The APPcyt is phosphorylated at Thr668 in vivo specifically in the brain. Cyclin‐dependent kinase 5 (Cdk5), a unique member of the Cdk family that is implicated in central nervous system development, participates in this phosphorylation. | In the present study, we demonstrate that APP phosphorylated at Thr668 is less vulnerable to cytoplasmic cleavage by caspase-3 and caspase-8. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PCNT | up-regulates activity
binding
|
CDK5RAP2 |
0.812 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260309 |
|
|
Homo sapiens |
U2-OS Cell |
| pmid |
sentence |
| 18042621 |
Our observation that Cep215 may function downstream of pericentrin suggests that the two proteins affect centrosome cohesion through a common mechanism. |Finally, depletion of pericentrin caused an almost complete loss of Cep215 from centrosomes, a detectable reduction in centrosomal levels of Cep68 and rootletin, but no significant effect on C-Nap1 (Fig. 6C and Table 1). Taken together, these results point to functional (and perhaps molecular) interactions between (1) Cep68 and rootletin and (2) Cep215 and pericentrin. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SPAG5 | up-regulates activity
relocalization
|
CDK5RAP2 |
0.478 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271719 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 26297806 |
By bringing CDK5RAP2 to the centrosome, the centriolar satellite proteins CEP72 and SPAG5 are required for the centrosomal localization of the other three MCPH proteins despite not interacting with them biochemically. |
|
| 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 |
| + |
CEP68 | up-regulates activity
relocalization
|
CDK5RAP2 |
0.464 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-275624 |
|
|
|
|
| pmid |
sentence |
| 25503564 |
We also found that Cep68 forms a complex with Cep215 (also known as Cdk5Rap2) and PCNT (also known as pericentrin), two PCM (pericentriolar material) proteins involved in centriole engagement. |Retention of Cep68 or PCNT in late mitosis prevents the removal of Cep215 |
|
| Publications: |
1 |
| + |
CDK5RAP2 | up-regulates quantity by expression
transcriptional regulation
|
BUB1B |
0.274 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260312 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19282672 |
These data indicate that CDK5RAP2 is a positive regulator of both the BUBR1 promoter and the MAD2 promoter |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CEP72 | up-regulates activity
relocalization
|
CDK5RAP2 |
0.65 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271720 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 26297806 |
By bringing CDK5RAP2 to the centrosome, the centriolar satellite proteins CEP72 and SPAG5 are required for the centrosomal localization of the other three MCPH proteins despite not interacting with them biochemically. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK5RAP2 | up-regulates activity
relocalization
|
WDR62 |
0.563 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271723 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 26297806 |
Primary microcephaly (MCPH) associated proteins CDK5RAP2, CEP152, WDR62 and CEP63 colocalize at the centrosome. We found that they interact to promote centriole duplication and form a hierarchy in which each is required to localize another to the centrosome, with CDK5RAP2 at the apex, and CEP152, WDR62 and CEP63 at sequentially lower positions. MCPH proteins interact with distinct centriolar satellite proteins; CDK5RAP2 interacts with SPAG5 and CEP72, CEP152 with CEP131, WDR62 with MOONRAKER, and CEP63 with CEP90 and CCDC14. These satellite proteins localize their cognate MCPH interactors to centrosomes and also promote centriole duplication. Consistent with a role for satellites in microcephaly, homozygous mutations in one satellite gene, CEP90, may cause MCPH. The satellite proteins, with the exception of CCDC14, and MCPH proteins promote centriole duplication by recruiting CDK2 to the centrosome. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK5RAP2 | up-regulates activity
relocalization
|
CEP152 |
0.747 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271721 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 26297806 |
Primary microcephaly (MCPH) associated proteins CDK5RAP2, CEP152, WDR62 and CEP63 colocalize at the centrosome. We found that they interact to promote centriole duplication and form a hierarchy in which each is required to localize another to the centrosome, with CDK5RAP2 at the apex, and CEP152, WDR62 and CEP63 at sequentially lower positions. MCPH proteins interact with distinct centriolar satellite proteins; CDK5RAP2 interacts with SPAG5 and CEP72, CEP152 with CEP131, WDR62 with MOONRAKER, and CEP63 with CEP90 and CCDC14. These satellite proteins localize their cognate MCPH interactors to centrosomes and also promote centriole duplication. Consistent with a role for satellites in microcephaly, homozygous mutations in one satellite gene, CEP90, may cause MCPH. The satellite proteins, with the exception of CCDC14, and MCPH proteins promote centriole duplication by recruiting CDK2 to the centrosome. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK5RAP2 | up-regulates activity
relocalization
|
CEP63 |
0.68 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271722 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 26297806 |
Primary microcephaly (MCPH) associated proteins CDK5RAP2, CEP152, WDR62 and CEP63 colocalize at the centrosome. We found that they interact to promote centriole duplication and form a hierarchy in which each is required to localize another to the centrosome, with CDK5RAP2 at the apex, and CEP152, WDR62 and CEP63 at sequentially lower positions. MCPH proteins interact with distinct centriolar satellite proteins; CDK5RAP2 interacts with SPAG5 and CEP72, CEP152 with CEP131, WDR62 with MOONRAKER, and CEP63 with CEP90 and CCDC14. These satellite proteins localize their cognate MCPH interactors to centrosomes and also promote centriole duplication. Consistent with a role for satellites in microcephaly, homozygous mutations in one satellite gene, CEP90, may cause MCPH. The satellite proteins, with the exception of CCDC14, and MCPH proteins promote centriole duplication by recruiting CDK2 to the centrosome. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK5RAP2 | down-regulates activity 
binding
|
CDC20 |
0.318 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260311 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 19282672 |
We show here that inhibition of CDK5RAP2 expression causes chromosome mis-segregation, fails to maintain the spindle checkpoint, and is associated with reduced expression of the spindle checkpoint proteins BUBR1 and MAD2 and an increase in chromatin-associated CDC20.|We found that the APC activator CDC20, but not others we exam-ined, was present in the CDK5RAP2 immunocomplex in HeLa cell extracts (Fig. 3A). CDK5RAP2 was detected in the CDC20 immunocomplex as well (Fig. 3B). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK5RAP2 | up-regulates quantity by expression
transcriptional regulation
|
MAD2L1 |
0.313 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260313 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 19282672 |
These data indicate that CDK5RAP2 is a positive regulator of both the BUBR1 promoter and the MAD2 promoter |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
CDK5RAP2
- 
- 