| + |
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 |
| + |
VRK2 | down-regulates
phosphorylation
|
BANF1 |
0.517 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-143368 |
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-144795 |
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-144799 |
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-144803 |
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 |
| + |
VRK3 | down-regulates activity
phosphorylation
|
BANF1 |
0.506 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264564 |
Ser4 |
sQKHRDFV |
in vitro |
|
| pmid |
sentence |
| 25899223 |
Although VRK3 has been regarded as a genuine pseudokinase from structural and biochemical studies, recent reports suggest that VRK3 acts as an active kinase as well as a signaling scaffold in cells. Here, we demonstrate that VRK3 phosphorylates the nuclear envelope protein barrier-to-autointegration factor (BAF) on Ser4.|Ectopic expression of VRK3 induces the translocation of BAF from the nucleus to the cytoplasm. I |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PPP4C | up-regulates 
dephosphorylation
|
BANF1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-203281 |
Ser4 |
sQKHRDFV |
Homo sapiens |
|
| pmid |
sentence |
| 24265311 |
Herein, we demonstrate 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. We have identified the major phosphatase responsible for dephosphorylation of ser-4 to be protein phosphatase 4 catalytic subunit. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-144779 |
Ser4 |
sQKHRDFV |
Homo sapiens |
|
| pmid |
sentence |
| 16495336 |
Herein, we demonstrate 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. We have identified the major phosphatase responsible for dephosphorylation of ser-4 to be protein phosphatase 4 catalytic subunit. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
3.0
BANF1
- 
- 