| + |
PRKAA1 | up-regulates activity 
phosphorylation
|
CCNY |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273011 |
Ser326 |
SARKRSAsADNLTLP |
|
|
| pmid |
sentence |
| 32723157 |
Our in vitro and cellular analyses supported the mass spectrometry data that implicated serine 326 (S326) as the phospho-acceptor site on CCNY by AMPK. |Mechanistically the S326 phosphorylation by AMPK promotes the interaction of CCNY with CDK16, which in turn autophosphorylates S336, which serves as a marker for active CCNY-CDK16 |
|
| Publications: |
1 |
| + |
AMPK | up-regulates activity
phosphorylation
|
CCNY |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273001 |
Ser326 |
SARKRSAsADNLTLP |
Homo sapiens |
|
| pmid |
sentence |
| 32723157 |
Our in vitro and cellular analyses supported the mass spectrometry data that implicated serine 326 (S326) as the phospho-acceptor site on CCNY by AMPK. |Mechanistically the S326 phosphorylation by AMPK promotes the interaction of CCNY with CDK16, which in turn autophosphorylates S336, which serves as a marker for active CCNY-CDK16 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CDK14 | down-regulates quantity by destabilization 
phosphorylation
|
CCNY |
0.824 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273008 |
Ser71 |
RASTIFLsKSQTDVR |
Homo sapiens |
Hep-G2 Cell |
| pmid |
sentence |
| 24794231 |
Phosphorylation of cyclin Y by CDK14 induces its ubiquitination and degradation|Phosphorylation of CCNY at Serines 71 and 73 creates a putative phospho-degron that controls its association with an SCF complex |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273007 |
Ser73 |
STIFLSKsQTDVREK |
Homo sapiens |
Hep-G2 Cell |
| pmid |
sentence |
| 24794231 |
Phosphorylation of cyclin Y by CDK14 induces its ubiquitination and degradation|Phosphorylation of CCNY at Serines 71 and 73 creates a putative phospho-degron that controls its association with an SCF complex |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CyclinY/CDK14 | down-regulates quantity by destabilization
phosphorylation
|
CCNY |
0.824 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273010 |
Ser71 |
RASTIFLsKSQTDVR |
Homo sapiens |
Hep-G2 Cell |
| pmid |
sentence |
| 24794231 |
Phosphorylation of cyclin Y by CDK14 induces its ubiquitination and degradation|Phosphorylation of CCNY at Serines 71 and 73 creates a putative phospho-degron that controls its association with an SCF complex |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273009 |
Ser73 |
STIFLSKsQTDVREK |
Homo sapiens |
Hep-G2 Cell |
| pmid |
sentence |
| 24794231 |
Phosphorylation of cyclin Y by CDK14 induces its ubiquitination and degradation|Phosphorylation of CCNY at Serines 71 and 73 creates a putative phospho-degron that controls its association with an SCF complex |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CCNY | up-regulates
binding
|
CDK14 |
0.824 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-162920 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 20059949 |
L63 and its vertebrate homolog pftk are regulated by the membrane tethered g2/m cyclin, cyclin y, which mediates binding to and phosphorylation of lrp6. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CCNY | form complex 
binding
|
CyclinY/CDK14 |
0.824 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273004 |
|
|
|
|
| pmid |
sentence |
| 19524571 |
A novel cyclin, CCNY, was identified as a PFTK1 interacting protein in a yeast two-hybrid screen. The cyclin box in CCNY and the PFTAIRE motif in PFTK1 are both required for the interaction which was confirmed by in vivo and in vitro assays. |
|
| Publications: |
1 |
| + |
CCNY | form complex
binding
|
CyclinY/CDK16 |
0.691 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273002 |
|
|
|
|
| pmid |
sentence |
| 30992425 |
CDK16 (also known as PCTAIRE1 or PCTK1) is an atypical member of the cyclin-dependent kinase (CDK) family that forms an active complex with cyclin Y (CCNY). |
|
| Publications: |
1 |
3.0
CCNY
- 
- 