+ |
CyclinY/CDK14 | up-regulates activity
phosphorylation
|
LRP6 |
0.35 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273015 |
Ser1490 |
AILNPPPsPATERSH |
Homo sapiens |
Hep-G2 Cell |
pmid |
sentence |
24794231 |
Compared with the wild-type CDK14, CDK14D256A mutant showed 2-fold reduced phosphorylation of LRP6 at Ser-1490, a known substrate of the CDK14/CCNY complex| It is also reported to be required for maximal phosphorylation of LRP6 on Ser 1490 and activation of Wnt signaling |
|
Publications: |
1 |
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 |
+ |
CDK14 | form complex
binding
|
CyclinY/CDK14 |
0.824 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273005 |
|
|
|
|
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/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 |