| + |
PRKCA | down-regulates 
phosphorylation
|
HMGN1 |
0.31 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-76282 |
Ser21 |
KEEPKRRsARLSAKP |
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-76286 |
Ser25 |
KRRSARLsAKPPAKV |
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 |
| + |
RPS6KA3 | down-regulates activity
phosphorylation
|
HMGN1 |
0.372 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249100 |
Ser21 |
KEEPKRRsARLSAKP |
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-249101 |
Ser25 |
KRRSARLsAKPPAKV |
Homo sapiens |
|
| 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 |
| + |
CSNK2A1 | down-regulates
phosphorylation
|
HMGN1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-76266 |
Ser7 |
sSAEGAAK |
Homo sapiens |
|
| pmid |
sentence |
| 10739259 |
Peptide mass and sequence analysis showed major and minor phosphorylation sites, respectively, at ser24 and ser28 in hmg-17, and ser20 and ser24 in hmg-14 a third phosphorylation site in hmg-14 was located at either ser6 or ser7phosphorylation of ser6 and ser7 may compromise the binding of hmgn1 protein to the binding domain of importin proteins, which in turn affects the nuclear transport and sub-cellular localization of hmgn1 protein. Protein kinase ck2 could potentially be an enzyme that regulates this process. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-76270 |
Ser8 |
MPKRKVSsAEGAAKE |
Homo sapiens |
|
| pmid |
sentence |
| 10739259 |
Peptide mass and sequence analysis showed major and minor phosphorylation sites, respectively, at ser24 and ser28 in hmg-17, and ser20 and ser24 in hmg-14 a third phosphorylation site in hmg-14 was located at either ser6 or ser7phosphorylation of ser6 and ser7 may compromise the binding of hmgn1 protein to the binding domain of importin proteins, which in turn affects the nuclear transport and sub-cellular localization of hmgn1 protein. Protein kinase ck2 could potentially be an enzyme that regulates this process. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-76274 |
Ser89 |
KTEESPAsDEAGEKE |
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-76278 |
Ser99 |
AGEKEAKsD |
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: |
4 |
Organism: |
Homo Sapiens |
| + |
RPS6KA3 |
phosphorylation
|
HMGN1 |
0.372 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249215 |
Ser7 |
sSAEGAAK |
Mus musculus |
|
| pmid |
sentence |
| 12773393 |
The results presented here show that MSK2 and, to a lesser extent, MSK1 are the major protein kinases required for the phosphorylation of histone H3 at both Ser10 and Ser28 and HMG-14 at Ser6 after stimulation of primary embryonic fibroblasts by TPA or anisomycin. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
RPS6KA5 | down-regulates activity
phosphorylation
|
HMGN1 |
0.6 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262988 |
Ser7 |
sSAEGAAK |
|
|
| pmid |
sentence |
| 12213813 |
HMGN1 (formerly known as HMG-14) phosphorylation at Ser6 occurs concomitantly with IE gene expression. | MSK2 seems to be the most important kinase responsible for this modification |Accordingly, it was suggested that HMGN1 phosphorylation reduces binding of the protein to the nucleosomes |
|
| Publications: |
1 |
| + |
PRKACA | down-regulates activity
phosphorylation
|
HMGN1 |
0.31 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249993 |
Ser7 |
sSAEGAAK |
Homo sapiens |
|
| pmid |
sentence |
| 11438671 |
PKA preferentially phosphorylates serine 6 in human HMGN1. specific phosphorylation of the NBD of HMGN proteins serves to prevent the interaction of these proteins with their chromatin targets during mitosis. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
RPS6KA4 |
phosphorylation
|
HMGN1 |
0.341 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249216 |
Ser7 |
sSAEGAAK |
Mus musculus |
Fibroblast |
| pmid |
sentence |
| 12773393 |
The results presented here show that MSK2 and, to a lesser extent, MSK1 are the major protein kinases required for the phosphorylation of histone H3 at both Ser10 and Ser28 and HMG-14 at Ser6 after stimulation of primary embryonic fibroblasts by TPA or anisomycin. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
HMGN1 | down-regulates 
|
Chromatine_condensation |
0.7 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262989 |
|
|
in vitro |
|
| pmid |
sentence |
| 12213813 |
In vitro, binding of HMGN1 proteins to the nucleosomes reduces chromatin compaction and promotes overall accessibility to the nucleosomes |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
HMGN1
- 
- 