| + |
CDK2 | down-regulates activity 
phosphorylation
|
CCP110 |
0.531 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265958 |
Ser170 |
RDSEGFNsPKQCDSS |
in vitro |
|
| pmid |
sentence |
| 12361598 |
GST-tagged recombinant CP110 (GST-wt) was robustly phosphorylated by cyclin E/CDK2 (Figure 2A). Expression of a mutant derivative of CP110 refractory to CDK phosphorylation provokes marked polyploidy. We localized the majority (nine of ten) of potential CDK2 phosphorylation sites in CP110 to an amino-terminal fragment (GST-ΔN1; Figure 1B) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265960 |
Ser366 |
GSYAKLPsPEPSMSP |
in vitro |
|
| pmid |
sentence |
| 12361598 |
GST-tagged recombinant CP110 (GST-wt) was robustly phosphorylated by cyclin E/CDK2 (Figure 2A). Expression of a mutant derivative of CP110 refractory to CDK phosphorylation provokes marked polyploidy. We localized the majority (nine of ten) of potential CDK2 phosphorylation sites in CP110 to an amino-terminal fragment (GST-ΔN1; Figure 1B) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265962 |
Ser372 |
PSPEPSMsPKMHRRR |
in vitro |
|
| pmid |
sentence |
| 12361598 |
GST-tagged recombinant CP110 (GST-wt) was robustly phosphorylated by cyclin E/CDK2 (Figure 2A). Expression of a mutant derivative of CP110 refractory to CDK phosphorylation provokes marked polyploidy. We localized the majority (nine of ten) of potential CDK2 phosphorylation sites in CP110 to an amino-terminal fragment (GST-ΔN1; Figure 1B) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265956 |
Ser400 |
PINACELsPKGKEQA |
in vitro |
|
| pmid |
sentence |
| 12361598 |
GST-tagged recombinant CP110 (GST-wt) was robustly phosphorylated by cyclin E/CDK2 (Figure 2A). Expression of a mutant derivative of CP110 refractory to CDK phosphorylation provokes marked polyploidy. We localized the majority (nine of ten) of potential CDK2 phosphorylation sites in CP110 to an amino-terminal fragment (GST-ΔN1; Figure 1B) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265957 |
Ser45 |
FHGVAILsPLLNIEK |
in vitro |
|
| pmid |
sentence |
| 12361598 |
GST-tagged recombinant CP110 (GST-wt) was robustly phosphorylated by cyclin E/CDK2 (Figure 2A). Expression of a mutant derivative of CP110 refractory to CDK phosphorylation provokes marked polyploidy. We localized the majority (nine of ten) of potential CDK2 phosphorylation sites in CP110 to an amino-terminal fragment (GST-ΔN1; Figure 1B) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265963 |
Ser516 |
ASSQCIAsPNFGTVS |
in vitro |
|
| pmid |
sentence |
| 12361598 |
GST-tagged recombinant CP110 (GST-wt) was robustly phosphorylated by cyclin E/CDK2 (Figure 2A). Expression of a mutant derivative of CP110 refractory to CDK phosphorylation provokes marked polyploidy. We localized the majority (nine of ten) of potential CDK2 phosphorylation sites in CP110 to an amino-terminal fragment (GST-ΔN1; Figure 1B) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265961 |
Thr194 |
FPKTSSAtPQETLIS |
in vitro |
|
| pmid |
sentence |
| 12361598 |
GST-tagged recombinant CP110 (GST-wt) was robustly phosphorylated by cyclin E/CDK2 (Figure 2A). Expression of a mutant derivative of CP110 refractory to CDK phosphorylation provokes marked polyploidy. We localized the majority (nine of ten) of potential CDK2 phosphorylation sites in CP110 to an amino-terminal fragment (GST-ΔN1; Figure 1B) |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265959 |
Thr566 |
NTRQQMDtPMVSCGN |
in vitro |
|
| pmid |
sentence |
| 12361598 |
GST-tagged recombinant CP110 (GST-wt) was robustly phosphorylated by cyclin E/CDK2 (Figure 2A). Expression of a mutant derivative of CP110 refractory to CDK phosphorylation provokes marked polyploidy. We localized the majority (nine of ten) of potential CDK2 phosphorylation sites in CP110 to an amino-terminal fragment (GST-ΔN1; Figure 1B) |
|
| Publications: |
8 |
Organism: |
In Vitro |
| + |
CCP110 | up-regulates activity 
binding
|
CETN1 |
0.497 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265966 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16760425 |
We report that CP110 interacts with two different Ca2+-binding proteins, calmodulin (CaM) and centrin, in vivo. our data demonstrate a functional role for CaM binding to CP110 and suggest that CP110 cooperates with CaM and centrin to regulate progression through cytokinesis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CCP110 | up-regulates activity
binding
|
CETN3 |
0.43 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265968 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16760425 |
We report that CP110 interacts with two different Ca2+-binding proteins, calmodulin (CaM) and centrin, in vivo. our data demonstrate a functional role for CaM binding to CP110 and suggest that CP110 cooperates with CaM and centrin to regulate progression through cytokinesis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CCP110 | up-regulates activity
binding
|
CALM3 |
0.334 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266348 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16760425 |
We report that CP110 interacts with two different Ca2+-binding proteins, calmodulin (CaM) and centrin, in vivo. our data demonstrate a functional role for CaM binding to CP110 and suggest that CP110 cooperates with CaM and centrin to regulate progression through cytokinesis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CCP110 | up-regulates activity
binding
|
CALM1 |
0.325 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265965 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16760425 |
We report that CP110 interacts with two different Ca2+-binding proteins, calmodulin (CaM) and centrin, in vivo. our data demonstrate a functional role for CaM binding to CP110 and suggest that CP110 cooperates with CaM and centrin to regulate progression through cytokinesis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CCP110 | up-regulates activity
binding
|
CALM2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266332 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 16760425 |
We report that CP110 interacts with two different Ca2+-binding proteins, calmodulin (CaM) and centrin, in vivo. our data demonstrate a functional role for CaM binding to CP110 and suggest that CP110 cooperates with CaM and centrin to regulate progression through cytokinesis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CCP110 | up-regulates activity
binding
|
CETN2 |
0.687 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265967 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16760425 |
We report that CP110 interacts with two different Ca2+-binding proteins, calmodulin (CaM) and centrin, in vivo. our data demonstrate a functional role for CaM binding to CP110 and suggest that CP110 cooperates with CaM and centrin to regulate progression through cytokinesis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CCNF | down-regulates quantity by destabilization
ubiquitination
|
CCP110 |
0.556 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266364 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20596027 |
Using a mode of substrate binding distinct from other F-box protein-substrate pairs, CP110 and Cyclin F physically associate on the centrioles during the G2 phase of the cell cycle, and CP110 is ubiquitylated by the SCF(Cyclin F) ubiquitin ligase complex, leading to its degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CCP110 | down-regulates 
|
Centrosome_separation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265964 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12361598 |
Reduction in CP110 Protein Levels or Loss of CP110 Phosphorylation Promotes Centrosome Separation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
CCP110
- 
- 