| + |
CSNK2A1 |
phosphorylation
|
HMGA1 |
0.335 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250892 |
Ser102 |
EEGISQEsSEEEQ |
in vitro |
|
| pmid |
sentence |
| 2806554 |
Sequence analysis of the native peptide (90-107) after treatment, which specifically converts phosphoserine residues to S-ethylcysteine, revealed that 70-80% of serine residues 102 and 103 were phosphorylated in vivo. Both residues were fully phosphorylated in vitro by incubation with casein kinase II. These results suggest that casein kinase II is involved in the regulation of HMG-I function in the cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250893 |
Ser103 |
EGISQESsEEEQ |
in vitro |
|
| pmid |
sentence |
| 2806554 |
Sequence analysis of the native peptide (90-107) after treatment, which specifically converts phosphoserine residues to S-ethylcysteine, revealed that 70-80% of serine residues 102 and 103 were phosphorylated in vivo. Both residues were fully phosphorylated in vitro by incubation with casein kinase II. These results suggest that casein kinase II is involved in the regulation of HMG-I function in the cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250894 |
Ser99 |
KEEEEGIsQESSEEE |
in vitro |
|
| pmid |
sentence |
| 2806554 |
Sequence analysis of the native peptide (90-107) after treatment, which specifically converts phosphoserine residues to S-ethylcysteine, revealed that 70-80% of serine residues 102 and 103 were phosphorylated in vivo. Both residues were fully phosphorylated in vitro by incubation with casein kinase II. These results suggest that casein kinase II is involved in the regulation of HMG-I function in the cells. | After an 80 min incubation with CK-II, both serines were fully phosphorylated to 1 mol/mol and serine-99 to 0.3 mol/mol. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
CSNK2A2 |
phosphorylation
|
HMGA1 |
0.333 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251004 |
Ser102 |
EEGISQEsSEEEQ |
in vitro |
|
| pmid |
sentence |
| 2806554 |
Sequence analysis of the native peptide (90-107) after treatment, which specifically converts phosphoserine residues to S-ethylcysteine, revealed that 70-80% of serine residues 102 and 103 were phosphorylated in vivo. Both residues were fully phosphorylated in vitro by incubation with casein kinase II. These results suggest that casein kinase II is involved in the regulation of HMG-I function in the cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251005 |
Ser103 |
EGISQESsEEEQ |
in vitro |
|
| pmid |
sentence |
| 2806554 |
Sequence analysis of the native peptide (90-107) after treatment, which specifically converts phosphoserine residues to S-ethylcysteine, revealed that 70-80% of serine residues 102 and 103 were phosphorylated in vivo. Both residues were fully phosphorylated in vitro by incubation with casein kinase II. These results suggest that casein kinase II is involved in the regulation of HMG-I function in the cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251006 |
Ser99 |
KEEEEGIsQESSEEE |
in vitro |
|
| pmid |
sentence |
| 2806554 |
Sequence analysis of the native peptide (90-107) after treatment, which specifically converts phosphoserine residues to S-ethylcysteine, revealed that 70-80% of serine residues 102 and 103 were phosphorylated in vivo. Both residues were fully phosphorylated in vitro by incubation with casein kinase II. These results suggest that casein kinase II is involved in the regulation of HMG-I function in the cells. | After an 80 min incubation with CK-II, both serines were fully phosphorylated to 1 mol/mol and serine-99 to 0.3 mol/mol. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
HIPK2 | down-regulates 
phosphorylation
|
HMGA1 |
0.508 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-158616 |
Ser36 |
PRKQPPVsPGTALVG |
Homo sapiens |
|
| pmid |
sentence |
| 17960875 |
Here, we found that hipk2 phosphorylates hmga1a at ser-35, thr-52, and thr-77, and hmga1b at thr-41 and thr-66. In addition, we demonstrated that cdc2, which is known to phosphorylate hmga1 proteins, could induce the phosphorylation of hmga1 proteins at the same ser/thr sites. we found that the hipk2-phosphorylated hmga1a reduced the binding affinity of hmga1a to human germ line promoter, and the drop in binding affinity induced by hipk2 phosphorylation was lower than that introduced by cdc2 phosphorylation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-158620 |
Thr53 |
KEPSEVPtPKRPRGR |
Homo sapiens |
|
| pmid |
sentence |
| 17960875 |
Here, we found that hipk2 phosphorylates hmga1a at ser-35, thr-52, and thr-77, and hmga1b at thr-41 and thr-66. In addition, we demonstrated that cdc2, which is known to phosphorylate hmga1 proteins, could induce the phosphorylation of hmga1 proteins at the same ser/thr sites. we found that the hipk2-phosphorylated hmga1a reduced the binding affinity of hmga1a to human germ line promoter, and the drop in binding affinity induced by hipk2 phosphorylation was lower than that introduced by cdc2 phosphorylation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
CDK1 | down-regulates
phosphorylation
|
HMGA1 |
0.392 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-158604 |
Ser36 |
PRKQPPVsPGTALVG |
Homo sapiens |
|
| pmid |
sentence |
| 17960875 |
Here, we found that hipk2 phosphorylates hmga1a at ser-35, thr-52, and thr-77, and hmga1b at thr-41 and thr-66. In addition, we demonstrated that cdc2, which is known to phosphorylate hmga1 proteins, could induce the phosphorylation of hmga1 proteins at the same ser/thr sites. we found that the hipk2-phosphorylated hmga1a reduced the binding affinity of hmga1a to human germ line promoter, and the drop in binding affinity induced by hipk2 phosphorylation was lower than that introduced by cdc2 phosphorylation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-158608 |
Thr53 |
KEPSEVPtPKRPRGR |
Homo sapiens |
|
| pmid |
sentence |
| 17960875 |
Here, we found that hipk2 phosphorylates hmga1a at ser-35, thr-52, and thr-77, and hmga1b at thr-41 and thr-66. In addition, we demonstrated that cdc2, which is known to phosphorylate hmga1 proteins, could induce the phosphorylation of hmga1 proteins at the same ser/thr sites. we found that the hipk2-phosphorylated hmga1a reduced the binding affinity of hmga1a to human germ line promoter, and the drop in binding affinity induced by hipk2 phosphorylation was lower than that introduced by cdc2 phosphorylation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-22338 |
Thr78 |
KTRKTTTtPGRKPRG |
Homo sapiens |
|
| pmid |
sentence |
| 1939057 |
Phosphorylation of the dna-binding domain of nonhistone high-mobility group i protein by cdc2 kinase: reduction of binding affinity |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
CDK2 | down-regulates
phosphorylation
|
HMGA1 |
0.267 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-158612 |
Ser36 |
PRKQPPVsPGTALVG |
Homo sapiens |
|
| pmid |
sentence |
| 17960875 |
Here, we found that hipk2 phosphorylates hmga1a at ser-35, thr-52, and thr-77, and hmga1b at thr-41 and thr-66. In addition, we demonstrated that cdc2, which is known to phosphorylate hmga1 proteins, could induce the phosphorylation of hmga1 proteins at the same ser/thr sites. we found that the hipk2-phosphorylated hmga1a reduced the binding affinity of hmga1a to human germ line promoter, and the drop in binding affinity induced by hipk2 phosphorylation was lower than that introduced by cdc2 phosphorylation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKCD | down-regulates
phosphorylation
|
HMGA1 |
0.267 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-73606 |
Ser44 |
PGTALVGsQKEPSEV |
Homo sapiens |
|
| pmid |
sentence |
| 10617144 |
In this study, we showed that the pkc-mediated phosphorylation of hmg-i exerted a very potent inhibition on the binding of this protein to the at-rich promoter regions of both pkc g and ng genes. The purified hmg-i can be phosphorylated by pkc a,b, g, and d but is poorly phosphorylated by pkc e and z. We have mapped two major sites of phosphorylation by pkc at ser44 and ser64 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-73610 |
Ser64 |
PRGRPKGsKNKGAAK |
Homo sapiens |
|
| pmid |
sentence |
| 10617144 |
In this study, we showed that the pkc-mediated phosphorylation of hmg-i exerted a very potent inhibition on the binding of this protein to the at-rich promoter regions of both pkc g and ng genes. The purified hmg-i can be phosphorylated by pkc a,b, g, and d but is poorly phosphorylated by pkc e and z. We have mapped two major sites of phosphorylation by pkc at ser44 and ser64 |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
HMGA1 | up-regulates quantity by expression 
transcriptional regulation
|
KITLG |
0.335 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254426 |
|
|
Homo sapiens |
MCF-7 Cell |
| pmid |
sentence |
| 15378028 |
Human KIT ligand promoter is positively regulated by HMGA1 in breast and ovarian cancer cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HMGA1 | up-regulates activity 
binding
|
POU3F1 |
0.311 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-240155 |
|
|
Homo sapiens |
U-138MG Cell |
| pmid |
sentence |
| 7791781 |
Direct contacts were identified between the POU domain of Tst-1/Oct-6 and a short stretch of 10 amino acids in the central portion of HMG-I/Y. In the presence of HMG-I/Y, Tst-1/Oct-6 exhibited an increased affinity for this AT-rich element. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HMGA1 | up-regulates quantity by expression
transcriptional regulation
|
SLC2A3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254427 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22706202 |
CAV1 was shown to stimulate GLUT3 transcription via an HMGA1-binding site within the GLUT3 promoter. HMGA1 was found to interact with and activate the GLUT3 promoter and CAV1 increased the HMGA1 activity by enhancing its nuclear localization. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CAV1 | up-regulates activity
relocalization
|
HMGA1 |
0.269 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254428 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 22706202 |
CAV1 was shown to stimulate GLUT3 transcription via an HMGA1-binding site within the GLUT3 promoter. HMGA1 was found to interact with and activate the GLUT3 promoter and CAV1 increased the HMGA1 activity by enhancing its nuclear localization. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
HMGA1
- 
- 