| + |
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 |
| + |
CSNK2A1 | up-regulates quantity by stabilization
phosphorylation
|
KIR3DL1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276077 |
Ser385 |
AGNRTANsEDSDEQD |
in vitro |
|
| 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.Both CKII and PKC phosphorylate KIR3DL1 in vitro. Ser364 can be phosphorylated after phosphorylation of Ser367 by CKII. It seems that phosphorylation of 3DL1 by CK does not significantly affect receptor inhibitory function or turnover, at least in the assays that we have used so far. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276078 |
Ser388 |
RTANSEDsDEQDPEE |
in vitro |
|
| 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.Both CKII and PKC phosphorylate KIR3DL1 in vitro. Ser364 can be phosphorylated after phosphorylation of Ser367 by CKII. It seems that phosphorylation of 3DL1 by CK does not significantly affect receptor inhibitory function or turnover, at least in the assays that we have used so far. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
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 |
| + |
PRKCB | down-regulates activity
phosphorylation
|
KIR3DL1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276079 |
Ser415 |
QRKITRPsQRPKTPP |
in vitro |
|
| 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.Both CKII and PKC phosphorylate KIR3DL1 in vitro. Ser364 can be phosphorylated after phosphorylation of Ser367 by CKII. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PRKCA | down-regulates activity
phosphorylation
|
KIR3DL1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276080 |
Ser415 |
QRKITRPsQRPKTPP |
in vitro |
|
| 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.Both CKII and PKC phosphorylate KIR3DL1 in vitro. Ser364 can be phosphorylated after phosphorylation of Ser367 by CKII. |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
KIR3DL1
- 
- 