+ |
PRKCB | down-regulates activity
phosphorylation
|
CASR |
0.323 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-249176 |
Thr888 |
FKVAARAtLRRSNVS |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
12356761 |
Expression of a mutant CaR in which the major PKC phosphorylation site is altered by substitution of alanine for threonine (T888A) eliminated oscillatory behavior, producing [Ca(2+)](i) responses almost identical to those produced by the wild type CaR exposed to PKC inhibitors. These results support a model in which phosphorylation of the CaR at the inhibitory threonine 888 by PKC provides the negative feedback needed to cause [Ca(2+)](i) oscillations mediated by this receptor. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PRKCA | down-regulates
phosphorylation
|
CASR |
0.358 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-170334 |
Thr888 |
FKVAARAtLRRSNVS |
Homo sapiens |
|
pmid |
sentence |
21135065 |
Casr(t888) is a protein kinase c (pkc) phosphorylation site in the receptor's intracellular domain that has previously been identified as a critical negative regulator of casr downstream signaling in vitro, thus, casr(t888) represents a functionally important, inhibitory phosphorylation site that contributes to the control of pth secretion. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
GCM2 | up-regulates quantity by expression
transcriptional regulation
|
CASR |
0.471 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-254199 |
|
|
Homo sapiens |
Parathyroid Hormone Secreting Cell |
pmid |
sentence |
18712808 |
we show that both promoters (P1 and P2) of the calcium-sensing receptor (CASR) gene, a differentiation marker for the parathyroid gland, are transactivated by wild-type GCM2. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Ovary |
+ |
RNF19A | down-regulates quantity by destabilization
ubiquitination
|
CASR |
0.39 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-271456 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
16513638 |
Coexpression with dorfin decreased the amount of total CaR protein and increased CaR ubiquitination, whereas a dominant negative fragment of dorfin had opposite effects. dorfin-mediated proteasomal degradation of immature CaR occurs from the endoplasmic reticulum. Because endogenous CaR in Madin-Darby canine kidney cells is also subject to degradation from the endoplasmic reticulum, dorfin-mediated ubiquitination may contribute to a general mechanism for CaR quality control during biosynthesis. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |