+ |
VRK1 |
phosphorylation
|
H3C1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-158436 |
Ser11 |
TKQTARKsTGGKAPR |
Homo sapiens |
|
pmid |
sentence |
17938195 |
We show that histone h3 is phosphorylated by vaccinia-related kinase 1 (vrk1). Direct phosphorylation of thr3 and ser10 in h3 by vrk1 both in vitro and in vivo was observed. Loss of vrk1 activity was associated with a marked decrease in h3 phosphorylation during mitosis. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PLK3 | up-regulates
phosphorylation
|
VRK1 |
0.487 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-182858 |
Ser342 |
DDGKLDLsVVENGGL |
Homo sapiens |
|
pmid |
sentence |
19103756 |
Vrk1 does not phosphorylate plk3, but plk3 phosphorylates the c-terminal region of vrk1 in ser342. Vrk1 with substitutions in s342 is catalytically active but blocks golgi fragmentation, indicating that its specific phosphorylation is necessary for this process. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
VRK1 | down-regulates
phosphorylation
|
BANF1 |
0.873 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-143285 |
Ser4 |
sQKHRDFV |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
16371512 |
We demonstrate that phosphorylation of ser4 and/or thr2/thr3 abrogates the interaction of baf with dna and reduces its interaction with the lem domain. Coexpression of vrk1 and gfp-baf greatly diminishes the association of baf with the nuclear chromatin/matrix and leads to its dispersal throughout the cell |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-144783 |
Ser4 |
sQKHRDFV |
Homo sapiens |
|
pmid |
sentence |
16495336 |
We demonstrate that phosphorylation of ser4 and/or thr2/thr3 abrogates the interaction of baf with dna and reduces its interaction with the lem domain. Coexpression of vrk1 and gfp-baf greatly diminishes the association of baf with the nuclear chromatin/matrix and leads to its dispersal throughout the cell |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-144787 |
Thr2 |
tTSQKHRD |
Homo sapiens |
|
pmid |
sentence |
16495336 |
Herein, we demonstrate that b1, vrk1, and vrk2 efficiently phosphorylate the extreme n' terminus of the baf protein. We demonstrate that phosphorylation of ser4 and/or thr2/thr3 abrogates the interaction of baf with dna and reduces its interaction with the lem domain |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-144791 |
Thr3 |
tSQKHRDF |
Homo sapiens |
|
pmid |
sentence |
16495336 |
We demonstrate that phosphorylation of ser4 and/or thr2/thr3 abrogates the interaction of baf with dna and reduces its interaction with the lem domain. Coexpression of vrk1 and gfp-baf greatly diminishes the association of baf with the nuclear chromatin/matrix and leads to its dispersal throughout the cell |
|
Publications: |
4 |
Organism: |
Homo Sapiens |
+ |
VRK1 | up-regulates
phosphorylation
|
ATF2 |
0.379 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-124330 |
Ser62 |
FGPARNDsVIVADQT |
Homo sapiens |
|
pmid |
sentence |
15105425 |
Vrk1 phosphorylates atf2 mainly on thr-73, stabilizing the atf2 protein and increasing its intracellular level. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-124334 |
Thr73 |
ADQTPTPtRFLKNCE |
Homo sapiens |
|
pmid |
sentence |
15105425 |
Vrk1 phosphorylates atf2 mainly on thr-73, stabilizing the atf2 protein and increasing its intracellular level. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
VRK1 | up-regulates
phosphorylation
|
JUN |
0.528 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-127069 |
Ser63 |
KNSDLLTsPDVGLLK |
Homo sapiens |
|
pmid |
sentence |
15378002 |
Vrk1 phosphorylates c-jun in ser63 and ser73 in vitro...VRK1 Activates c-jun dependent transcription |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-127073 |
Ser73 |
VGLLKLAsPELERLI |
Homo sapiens |
|
pmid |
sentence |
15378002 |
Vrk1 phosphorylates c-jun in ser63 and ser73 in vitro...VRK1 Activates c-jun dependent transcription |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
VRK1 | up-regulates
phosphorylation
|
TP53 |
0.538 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-81222 |
Thr18 |
EPPLSQEtFSDLWKL |
Homo sapiens |
HeLa Cell |
pmid |
sentence |
10951572 |
Vrk1 phosphorylates murine p53 in threonine 18. This threonine is within the p53 hydrophobic loop (residues 13-23) required for the interaction of p53 with the cleft of its inhibitor mdm-2. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
ANKLE2 | down-regulates
|
VRK1 |
0.79 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-198103 |
|
|
Homo sapiens |
|
pmid |
sentence |
22770216 |
Lem4 inhibits the activity of baf's kinase vrk-1 during mitotic exit |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
VRK1 | up-regulates
phosphorylation
|
TP53BP1 |
0.408 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-197625 |
|
|
Homo sapiens |
|
pmid |
sentence |
22621922 |
The kinase vrk1 is activated by dna double strand breaks induced by ionizing radiation (ir) and specifically phosphorylates 53bp1 in serum-starved cells./ Vrk1 knockdown resulted in the defective formation of 53bp1 foci in response to ir both in number and size |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
VRK1 |
phosphorylation
|
Histone H3 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265371 |
|
|
Homo sapiens |
|
pmid |
sentence |
17938195 |
We show that histone h3 is phosphorylated by vaccinia-related kinase 1 (vrk1). Direct phosphorylation of thr3 and ser10 in h3 by vrk1 both in vitro and in vivo was observed. Loss of vrk1 activity was associated with a marked decrease in h3 phosphorylation during mitosis. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |