| + |
UHMK1 | up-regulates 
phosphorylation
|
CDKN1B |
0.364 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-90274 |
Ser10 |
NVRVSNGsPSLERMD |
Homo sapiens |
|
| pmid |
sentence |
| 12093740 |
Hkis is a nuclear protein that binds the c-terminal domain of p27(kip1) and phosphorylates it on s10 in vitro and in vivo, promoting its nuclear export to the cytoplasm.Phosphorylation at serine 10, a major phosphorylation site of p27(kip1), increases its protein stability |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-77705 |
Ser10 |
NVRVSNGsPSLERMD |
Homo sapiens |
|
| pmid |
sentence |
| 10831586 |
Hkis is a nuclear protein that binds the c-terminal domain of p27(kip1) and phosphorylates it on s10 in vitro and in vivo, promoting its nuclear export to the cytoplasm.Phosphorylation at serine 10, a major phosphorylation site of p27(kip1), increases its protein stability |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
UHMK1 | up-regulates
phosphorylation
|
PIMREG |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-192702 |
Ser131 |
GAQKGSGsPTHSLSQ |
Homo sapiens |
|
| pmid |
sentence |
| 23419774 |
Cats is a substrate of kis and mapped the phosphorylation site to cats serine 131 (s131). Kis enhances the transcriptional repressor activity of cats |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
UHMK1 | down-regulates 
phosphorylation
|
MBP |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-78895 |
Ser299 |
GRDSRSGsPMARR |
Homo sapiens |
|
| pmid |
sentence |
| 10880969 |
Phosphorylation decreased the ability of mbp to polymerize actin and to bundle actin filaments but had no effect on the dissociation constant of the mbp-actin complex or on the ability of ca2+-calmodulin to dissociate the complex. The most significant effect of phosphorylation on the mbp-actin complex was a dramatic reduction in its ability to bind to negatively charged lipid bilayers. Mass spectrometry and peptide sequencing allowed us to identify serine 164 of mbp as the unique site phosphorylated by kis. Phosphorylation of synthetic peptides indicated the importance of the proline residue at position +1. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-143485 |
Ser299 |
GRDSRSGsPMARR |
Homo sapiens |
|
| pmid |
sentence |
| 16401070 |
Phosphorylation decreased the ability of mbp to polymerize actin and to bundle actin filaments but had no effect on the dissociation constant of the mbp-actin complex or on the ability of ca2+-calmodulin to dissociate the complex. The most significant effect of phosphorylation on the mbp-actin complex was a dramatic reduction in its ability to bind to negatively charged lipid bilayers. Mass spectrometry and peptide sequencing allowed us to identify serine 164 of mbp as the unique site phosphorylated by kis. Phosphorylation of synthetic peptides indicated the importance of the proline residue at position +1. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Tissue: |
Brain |
| + |
UHMK1 | down-regulates
phosphorylation
|
STMN1 |
0.499 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-182489 |
Ser38 |
SVPEFPLsPPKKKDL |
Homo sapiens |
|
| pmid |
sentence |
| 19033656 |
This promigratory phenotype resulted from increased stathmin protein levels, caused by a lack of kis-mediated stathmin phosphorylation at serine 38 and diminished stathmin protein degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
UHMK1 |
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4.0
UHMK1
- 
- 