| + |
RPS6KA3 | down-regulates activity 
phosphorylation
|
HMGN2 |
0.293 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249102 |
Ser25 |
KDEPQRRsARLSAKP |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 11438671 |
We report here that the NBD of the HMGN1 and -N2 protein family is highly and specifically phosphorylated during mitosis and that this phosphorylation has a major functional consequence: it abolishes the interaction of the proteins with its chromatin targets. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249103 |
Ser29 |
QRRSARLsAKPAPPK |
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 11438671 |
We report here that the NBD of the HMGN1 and -N2 protein family is highly and specifically phosphorylated during mitosis and that this phosphorylation has a major functional consequence: it abolishes the interaction of the proteins with its chromatin targets. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKCA | down-regulates
phosphorylation
|
HMGN2 |
0.293 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-76320 |
Ser25 |
KDEPQRRsARLSAKP |
Homo sapiens |
|
| pmid |
sentence |
| 10739259 |
Protein kinases that phosphorylate hmg-14 17 at the major sites have been implicated from previous in vitro studies. Protein kinase c and a similar calcium phospholipid-dependent kinase have been reported to phosphorylate both proteins in vitro, where the phosphorylation of hmg-17 occurs predominantly at ser24 and to a lesser degree at ser28. Phosphorylation of hmg-14 at ser6 by camp- or cgmp-dependent kinases has also been reported. Thus, other kinases may contribute to phosphorylation at ser6 in response to oa. Ser88 and ser98 on hmg-14 are also phosphorylated by casein kinase ii in vitro. we conclude that the correlation we observe reflects a causal relationship, in which phosphorylation somehow facilitates the redistribution of hmg-14 and -17 toward non-nuclear pools. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-76324 |
Ser29 |
QRRSARLsAKPAPPK |
Homo sapiens |
|
| pmid |
sentence |
| 10739259 |
Protein kinases that phosphorylate hmg-14 17 at the major sites have been implicated from previous in vitro studies. Protein kinase c and a similar calcium phospholipid-dependent kinase have been reported to phosphorylate both proteins in vitro, where the phosphorylation of hmg-17 occurs predominantly at ser24 and to a lesser degree at ser28. Phosphorylation of hmg-14 at ser6 by camp- or cgmp-dependent kinases has also been reported. Thus, other kinases may contribute to phosphorylation at ser6 in response to oa. Ser88 and ser98 on hmg-14 are also phosphorylated by casein kinase ii in vitro. we conclude that the correlation we observe reflects a causal relationship, in which phosphorylation somehow facilitates the redistribution of hmg-14 and -17 toward non-nuclear pools. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
3.0
HMGN2
- 
- 