| + |
PRKCA |
phosphorylation
|
HAND1 |
0.292 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249242 |
Ser109 |
KERRRTEsINSAFAE |
Homo sapiens |
|
| pmid |
sentence |
| 14636580 |
In vitro and in vivo phosphorylation studies show that both PKA and PKC can phosphorylate HAND1 and -2. In addition, phosphopeptide mapping analysis of wild-type and mutant forms of HAND1 shows that three of these conserved residues, T107; S109 within helix I and S98 within the basic domain, are the phosphorylated residues. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249243 |
Ser98 |
RLGRRKGsGPKKERR |
Homo sapiens |
|
| pmid |
sentence |
| 14636580 |
In vitro and in vivo phosphorylation studies show that both PKA and PKC can phosphorylate HAND1 and -2. In addition, phosphopeptide mapping analysis of wild-type and mutant forms of HAND1 shows that three of these conserved residues, T107; S109 within helix I and S98 within the basic domain, are the phosphorylated residues. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249244 |
Thr107 |
PKKERRRtESINSAF |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 14636580 |
In vitro and in vivo phosphorylation studies show that both PKA and PKC can phosphorylate HAND1 and -2. In addition, phosphopeptide mapping analysis of wild-type and mutant forms of HAND1 shows that three of these conserved residues, T107; S109 within helix I and S98 within the basic domain, are the phosphorylated residues. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PRKACA | down-regulates activity 
phosphorylation
|
HAND1 |
0.3 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249989 |
Ser109 |
KERRRTEsINSAFAE |
Rattus norvegicus |
Rcho-1 Cell |
| pmid |
sentence |
| 14636580 |
In vitro and in vivo phosphorylation studies show that both PKA and PKC can phosphorylate HAND1 and -2. T107; S109 within helix I and S98 within the basic domain, are the phosphorylated residues. We determined that modification of HAND1 at residues 107 and 109 affects dimerization affinities with E-proteins, thus changing the bHLH dimer equilibrium within the cell. These modifications also affect HAND1 function. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249991 |
Thr107 |
PKKERRRtESINSAF |
Rattus norvegicus |
Rcho-1 Cell |
| pmid |
sentence |
| 14636580 |
In vitro and in vivo phosphorylation studies show that both PKA and PKC can phosphorylate HAND1 and -2. T107; S109 within helix I and S98 within the basic domain, are the phosphorylated residues. We determined that modification of HAND1 at residues 107 and 109 affects dimerization affinities with E-proteins, thus changing the bHLH dimer equilibrium within the cell. These modifications also affect HAND1 function. |
|
| Publications: |
2 |
Organism: |
Rattus Norvegicus |
| + |
PRKACA |
phosphorylation
|
HAND1 |
0.3 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249990 |
Ser98 |
RLGRRKGsGPKKERR |
Rattus norvegicus |
Rcho-1 Cell |
| pmid |
sentence |
| 14636580 |
In vitro and in vivo phosphorylation studies show that both PKA and PKC can phosphorylate HAND1 and -2. T107; S109 within helix I and S98 within the basic domain, are the phosphorylated residues. We determined that modification of HAND1 at residues 107 and 109 affects dimerization affinities with E-proteins, thus changing the bHLH dimer equilibrium within the cell. These modifications also affect HAND1 function. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
SMAD1 | up-regulates quantity 
transcriptional regulation
|
HAND1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268936 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 22219353 |
Chromatin immunoprecipitation (ChIP) revealed a subset of the BIG (BMP4 induced genes) signature, including Satb2, Smad6, Hand1, Gadd45γ and Gata3, that was bound by Smad1/5 in the developing mandible, revealing direct Smad-mediated regulation |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
SMAD5 | up-regulates quantity
transcriptional regulation
|
HAND1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268941 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 22219353 |
Chromatin immunoprecipitation (ChIP) revealed a subset of the BIG (BMP4 induced genes) signature, including Satb2, Smad6, Hand1, Gadd45γ and Gata3, that was bound by Smad1/5 in the developing mandible, revealing direct Smad-mediated regulation |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
3.0
HAND1
- 
- 