| + |
CLK2 | up-regulates 
phosphorylation
|
CLK2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167344 |
Ser142 |
HSSRRAKsVEDDAEG |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 20682768 |
Clk2 was reported to regulate its nuclear localization by autophosphorylating serine 141 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CLK2 | up-regulates activity
phosphorylation
|
PTPN1 |
0.327 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250775 |
Ser242 |
MDKRKDPsSVDIKKV |
in vitro |
|
| pmid |
sentence |
| 10480872 |
The CLK family kinases, CLK1 and CLK2, phosphorylate and activate the tyrosine phosphatase, PTP-1B. | although CLK1 and CLK2 directly phosphorylate PTP-1B on both Ser50 and Ser242/Ser243, the preferred CLK phosphorylation site is Ser50, as it is preferentially phosphorylated at an approximate ratio of 9:1 over the Ser242/Ser243 site. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250776 |
Ser243 |
DKRKDPSsVDIKKVL |
in vitro |
|
| pmid |
sentence |
| 10480872 |
The CLK family kinases, CLK1 and CLK2, phosphorylate and activate the tyrosine phosphatase, PTP-1B. | although CLK1 and CLK2 directly phosphorylate PTP-1B on both Ser50 and Ser242/Ser243, the preferred CLK phosphorylation site is Ser50, as it is preferentially phosphorylated at an approximate ratio of 9:1 over the Ser242/Ser243 site. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-70603 |
Ser50 |
RNRYRDVsPFDHSRI |
Homo sapiens |
|
| pmid |
sentence |
| 10480872 |
The clk family kinases, clk1 and clk2, phosphorylate and activate the tyrosine phosphatase, ptp-1b.|Phosphorylation of PTP-1B at Ser(50) by CLK1 or CLK2 is responsible for its enzymatic activation. |
|
| Publications: |
3 |
Organism: |
In Vitro, Homo Sapiens |
| + |
AKT | up-regulates
phosphorylation
|
CLK2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244214 |
Ser34 |
HKRRRSRsWSSSSDR |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 20682768 |
Akt directly binds to and phosphorylates clk2 on serine 34 and threonine 127, in vitro and in vivo.Our results suggest that akt activation controls cell survival to ionizing radiation by phosphorylating clk2, revealing an important regulatory mechanism required for promoting cell surviva |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-244218 |
Thr127 |
RRRRRSRtFSRSSSQ |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 20682768 |
Akt directly binds to and phosphorylates clk2 on serine 34 and threonine 127, in vitro and in vivo.Our results suggest that akt activation controls cell survival to ionizing radiation by phosphorylating clk2, revealing an important regulatory mechanism required for promoting cell surviva |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
AKT1 | up-regulates
phosphorylation
|
CLK2 |
0.398 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167336 |
Ser34 |
HKRRRSRsWSSSSDR |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 20682768 |
Akt directly binds to and phosphorylates clk2 on serine 34 and threonine 127, in vitro and in vivo.Our results suggest that akt activation controls cell survival to ionizing radiation by phosphorylating clk2, revealing an important regulatory mechanism required for promoting cell surviva |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-167340 |
Thr127 |
RRRRRSRtFSRSSSQ |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 20682768 |
Akt directly binds to and phosphorylates clk2 on serine 34 and threonine 127, in vitro and in vivo.Our results suggest that akt activation controls cell survival to ionizing radiation by phosphorylating clk2, revealing an important regulatory mechanism required for promoting cell surviva |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CLK2 | up-regulates activity
phosphorylation
|
SRSF1 |
0.302 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273858 |
|
|
in vitro |
|
| pmid |
sentence |
| 8617202 |
In vitro, Clk/Sty efficiently phosphorylated the SR family member ASF/SF2 on serine residues located within its serine/arginine-rich region (the RS domain). Overexpression of the active Clk/Sty kinase caused a redistribution of SR proteins within the nucleus. These results suggest that Clk/Sty kinase directly regulates the activity and compartmentalization of SR splicing factors. |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
CLK2
- 
- 