+ |
CSNK1D | up-regulates
phosphorylation
|
KIR3DL1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-158121 |
Ser385 |
AGNRTANsEDSDEQD |
Homo sapiens |
|
pmid |
sentence |
17911614 |
In this study, we have mapped constitutive phosphorylation sites for casein kinases, protein kinase c, and an unidentified kinase on the kir cytoplasmic domain. Three of these phosphorylation sites are highly conserved in human inhibitory kir. Functional studies of the wild-type receptor and serine/threonine mutants indicated that phosphorylation of ser(394) by protein kinase c slightly suppresses kir3dl1 inhibitory function, and reduces receptor internalization and turnover. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-158125 |
Ser388 |
RTANSEDsDEQDPEE |
Homo sapiens |
|
pmid |
sentence |
17911614 |
In this study, we have mapped constitutive phosphorylation sites for casein kinases, protein kinase c, and an unidentified kinase on the kir cytoplasmic domain. Three of these phosphorylation sites are highly conserved in human inhibitory kir. Functional studies of the wild-type receptor and serine/threonine mutants indicated that phosphorylation of ser(394) by protein kinase c slightly suppresses kir3dl1 inhibitory function, and reduces receptor internalization and turnover. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
+ |
PRKCG | down-regulates
phosphorylation
|
KIR3DL1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-158133 |
Ser415 |
QRKITRPsQRPKTPP |
Homo sapiens |
|
pmid |
sentence |
17911614 |
Functional studies of the wild-type receptor and serine/threonine mutants indicated that phosphorylation of ser(394) by protein kinase c slightly suppresses kir3dl1 inhibitory function, and reduces receptor internalization and turnover. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRKCE | down-regulates
phosphorylation
|
KIR3DL1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-158129 |
Ser415 |
QRKITRPsQRPKTPP |
Homo sapiens |
|
pmid |
sentence |
17911614 |
Functional studies of the wild-type receptor and serine/threonine mutants indicated that phosphorylation of ser(394) by protein kinase c slightly suppresses kir3dl1 inhibitory function, and reduces receptor internalization and turnover. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |