| + |
PRKACA | down-regulates activity 
phosphorylation
|
ITPR1 |
0.532 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249996 |
Ser1598 |
RNAARRDsVLAASRD |
in vitro |
|
| pmid |
sentence |
| 12529267 |
IP(3)R-I was phosphorylated by PKA and PKG in vitro and exclusively by PKG in vivo. Sequential phosphorylation by PKA and by PKG-Ialpha in vitro showed that PKA phosphorylated the same site as PKG (presumably S(1755)) and an additional PKA-specific site (S(1589)). Phosphorylation of IP(3)R-I in microsomes by PKG, PKA, or a combination of PKG and PKA inhibited IP(3)-induced Ca(2+) release to the same extent, implying that inhibition was mediated by phosphorylation of the PKG-specific site. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249997 |
Ser1764 |
RPSGRREsLTSFGNG |
in vitro |
|
| pmid |
sentence |
| 12529267 |
IP(3)R-I was phosphorylated by PKA and PKG in vitro and exclusively by PKG in vivo. Sequential phosphorylation by PKA and by PKG-Ialpha in vitro showed that PKA phosphorylated the same site as PKG (presumably S(1755)) and an additional PKA-specific site (S(1589)). Phosphorylation of IP(3)R-I in microsomes by PKG, PKA, or a combination of PKG and PKA inhibited IP(3)-induced Ca(2+) release to the same extent, implying that inhibition was mediated by phosphorylation of the PKG-specific site. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
PRKG1 |
phosphorylation
|
ITPR1 |
0.475 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248916 |
Ser1764 |
RPSGRREsLTSFGNG |
Rattus norvegicus |
Vascular Smooth Muscle Cell |
| pmid |
sentence |
| 8132598 |
Phosphorylation of the inositol 1,4,5-trisphosphate receptor by cyclic GMP-dependent protein kinase. | The synthetic peptide corresponding to serine 1755 (GRRESLTSFG) was phosphorylated with aKm in the range of 30-40 microM by both kinases. The kinetic analysis revealed that this peptide substrate is the best substrate described for cGMP kinase to date. Vascular smooth muscle cells prelabeled with [32P]orthophosphate and treated with atrial natriuretic peptide or sodium nitroprusside to elevate cGMP also resulted in increased labeling of the IP3 receptor. Phosphorylation of IP3 receptor by cGMP kinase may regulate the function of IP3 receptor in vascular smooth muscle cells and contribute to the effect of cGMP to regulate intracellular calcium levels. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
FYN | up-regulates 
phosphorylation
|
ITPR1 |
0.505 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-121795 |
Tyr353 |
NAQEKMVySLVSVPE |
Homo sapiens |
|
| pmid |
sentence |
| 14761954 |
We have identified tyrosine 353 (tyr353) in the ip3-binding domain of type 1 ip3r (ip3r1) as a phosphorylation site for fyntyrosine phosphorylation of ip3r1 increased ip3 binding at low ip3 concentrations (<10 nm). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ERP44 | down-regulates activity
binding
|
ITPR1 |
0.604 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261046 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 15652484 |
In this study, we found that ERp44, an ER lumenal protein of the thioredoxin family, directly interacts with the third lumenal loop of IP(3)R type 1 (IP(3)R1) and that the interaction is dependent on pH, Ca(2+) concentration, and redox state. In this study we demonstrated that ERp44 directly interacts with the L3V domain of IP3R1, thereby inhibiting its channel activity. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
1D-myo-inositol 1,4,5-trisphosphate | up-regulates activity
chemical activation
|
ITPR1 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256239 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24646566 |
The key event in activation of fluid secretion is an increase in intracellular [ca2+] ([ca2+]i) triggered by ip3-induced release of ca2+ from er via the ip3r. ip3rs determine the site of initiation and the pattern of [ca2+]i signal in the cell. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Dopaminergic Synapse, Glutamatergic synapse, Oxytocin signaling, VEGF Signaling |
| + |
RORA | up-regulates quantity by expression
transcriptional regulation
|
ITPR1 |
0.246 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-266847 |
|
|
Mus musculus |
Cerebellar Purkinje Cell |
| pmid |
sentence |
| 19381306 |
RORα regulates the expression of several genes in Purkinje cells. RORα becomes highly expressed in postmitotic Purkinje cells. It regulates their maturation, particularly dendritic differentiation. Dendritogenesis and the expression of several genes, including Shh, Itpr1, Pcp4, Calb1, Pcp2, and Slc1a6, normally expressed in mature Purkinje cells, are inhibited in RORα-deficient mice. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
RNF170 | down-regulates activity
polyubiquitination
|
ITPR1 |
0.444 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271913 |
|
|
Homo sapiens |
HeLa Cell |
| pmid |
sentence |
| 21610068 |
In summary, here we present evidence that RNF170 is an E3 ligase that mediates IP3 receptor ubiquitination and processing by the UPP and that it is recruited to activated IP3 receptors by the erlin1/2 complex to which it is constitutively bound. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ITPR1 | up-regulates quantity
chemical modification
|
calcium(2+) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-256238 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24646566 |
The key event in activation of fluid secretion is an increase in intracellular [ca2+] ([ca2+]i) triggered by ip3-induced release of ca2+ from er via the ip3r. ip3rs determine the site of initiation and the pattern of [ca2+]i signal in the cell. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Dopaminergic Synapse, Glutamatergic synapse, Neurotransmitters release, Oxytocin signaling, VEGF Signaling |
| + |
Erlin | down-regulates quantity by destabilization
binding
|
ITPR1 |
0.511 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-271915 |
|
|
Rattus fuscipes |
Rat-1 Cell |
| pmid |
sentence |
| 19240031 |
Here we report that the ER membrane protein SPFH1 and its homolog SPFH2 form a heteromeric approximately 2 MDa complex that binds to IP(3)R tetramers immediately after their activation and is required for their processing. The complex is ring-shaped (diameter approximately 250A(),) and RNA interference-mediated depletion of SPFH1 and SPFH2 blocks IP(3)R polyubiquitination and degradation. |
|
| Publications: |
1 |
Organism: |
Rattus Fuscipes |
| + |
ITPRIPL1 | up-regulates
binding
|
ITPR1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-172497 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 21368195 |
Recruitment of g protein also can activate phospholipase c (plc) that in turn increases inositol triphosphate (ip3) levels and induces ca2+ release from internal stores. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
ITPR1
- 
- 