+ |
PRKACA | up-regulates activity
phosphorylation
|
CACNB2 |
0.416 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249714 |
Ser514 |
SAPIRSAsQAEEEPS |
|
|
pmid |
sentence |
10441130 |
Voltage-dependent L-type calcium (Ca) channels are heteromultimeric proteins that are regulated through phosphorylation by cAMP-dependent protein kinase (PKA) Mutagenesis of a single residue at Ser459 resulted in the loss of one site of phosphorylation by PKA, and mutagenesis of two residues at Ser478/479 resulted in the loss of approximately two sites of PKA-mediated phosphorylation |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250340 |
Ser533 |
KKSQHRSsSSAPHHN |
|
|
pmid |
sentence |
10441130 |
Voltage-dependent L-type calcium (Ca) channels are heteromultimeric proteins that are regulated through phosphorylation by cAMP-dependent protein kinase (PKA) Mutagenesis of a single residue at Ser459 resulted in the loss of one site of phosphorylation by PKA, and mutagenesis of two residues at Ser478/479 resulted in the loss of approximately two sites of PKA-mediated phosphorylation |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250341 |
Ser534 |
KSQHRSSsSAPHHNH |
|
|
pmid |
sentence |
10441130 |
Voltage-dependent L-type calcium (Ca) channels are heteromultimeric proteins that are regulated through phosphorylation by cAMP-dependent protein kinase (PKA) Mutagenesis of a single residue at Ser459 resulted in the loss of one site of phosphorylation by PKA, and mutagenesis of two residues at Ser478/479 resulted in the loss of approximately two sites of PKA-mediated phosphorylation |
|
Publications: |
3 |
+ |
CAMK2D | up-regulates
phosphorylation
|
CACNB2 |
0.399 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-164067 |
Thr554 |
RGLSRQEtFDSETQE |
Homo sapiens |
|
pmid |
sentence |
20194790 |
We recently identified ca(v)1.2 beta(2a) residues critical for camkii phosphorylation (thr 498) beta(2a) thr 498 and leu 493 are required for ca(v)1.2 activation by camkii in native cells. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
GEM | down-regulates activity
binding
|
CACNB2 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261710 |
|
|
Homo sapiens |
|
pmid |
sentence |
14701738 |
Two functions for Gem have been demonstrated, including inhibition of voltage-gated calcium channel activity and inhibition of Rho kinase-mediated cytoskeletal reorganization, such as stress fiber formation and neurite retraction. These functions for Gem have been ascribed to its interaction with the calcium channel Β subunit and Rho kinase Β, respectively. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261720 |
|
|
Homo sapiens |
|
pmid |
sentence |
14701738 |
Two functions for Gem have been demonstrated, including inhibition of voltage-gated calcium channel activity and inhibition of Rho kinase-mediated cytoskeletal reorganization, such as stress fiber formation and neurite retraction. These functions for Gem have been ascribed to its interaction with the calcium channel Β subunit and Rho kinase Β, respectively. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |