| + |
PRKCB |
phosphorylation
|
SDC2 |
0.326 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248974 |
Ser187 |
DLGERKPsSAAYQKA |
in vitro |
|
| pmid |
sentence |
| 9244383 |
We investigated phosphorylation of syndecan-2 cytoplasmic domain by PKC | Peptide mapping and substitution studies showed that both serines were phosphoacceptors, but each had slightly different affinity, with that of serine-197 being higher than serine-198. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248977 |
Ser188 |
LGERKPSsAAYQKAP |
in vitro |
|
| pmid |
sentence |
| 9244383 |
We investigated phosphorylation of syndecan-2 cytoplasmic domain by PKC | Peptide mapping and substitution studies showed that both serines were phosphoacceptors, but each had slightly different affinity, with that of serine-197 being higher than serine-198. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
PRKCG |
phosphorylation
|
SDC2 |
0.351 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248975 |
Ser187 |
DLGERKPsSAAYQKA |
in vitro |
|
| pmid |
sentence |
| 9244383 |
We investigated phosphorylation of syndecan-2 cytoplasmic domain by PKC | Peptide mapping and substitution studies showed that both serines were phosphoacceptors, but each had slightly different affinity, with that of serine-197 being higher than serine-198. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248978 |
Ser188 |
LGERKPSsAAYQKAP |
in vitro |
|
| pmid |
sentence |
| 9244383 |
We investigated phosphorylation of syndecan-2 cytoplasmic domain by PKC | Peptide mapping and substitution studies showed that both serines were phosphoacceptors, but each had slightly different affinity, with that of serine-197 being higher than serine-198. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
PRKCA |
phosphorylation
|
SDC2 |
0.37 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248973 |
Ser187 |
DLGERKPsSAAYQKA |
in vitro |
|
| pmid |
sentence |
| 9244383 |
We investigated phosphorylation of syndecan-2 cytoplasmic domain by PKC | Peptide mapping and substitution studies showed that both serines were phosphoacceptors, but each had slightly different affinity, with that of serine-197 being higher than serine-198. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248976 |
Ser188 |
LGERKPSsAAYQKAP |
in vitro |
|
| pmid |
sentence |
| 9244383 |
We investigated phosphorylation of syndecan-2 cytoplasmic domain by PKC | Peptide mapping and substitution studies showed that both serines were phosphoacceptors, but each had slightly different affinity, with that of serine-197 being higher than serine-198. |
|
| Publications: |
2 |
Organism: |
In Vitro |
4.0
SDC2
- 
- 