+ |
CAMK2A | up-regulates activity
phosphorylation
|
ATP2A2 |
0.406 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250616 |
Ser38 |
KLKERWGsNELPAEE |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
7929371 |
SERCA2 and SERCA2 mutants S38A, S167A, and S531A were expressed in HEK-293 cells and tested for phosphorylation with CaM kinase. Mutant S38A was not phosphorylated, while mutants S167A and S531A were phosphorylated, suggesting that Ser38 is the site of CaM kinase phosphorylation in SERCA2. This conclusion was supported by the observation that phosphorylation of SERCA2 and mutants S167A and S531A by CaM kinase increased the Vmax for Ca2+ transport, while the Vmax for Ca2+ transport by mutant S38A was unaffected by exposure to a phosphorylation reaction mix. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
HRC | down-regulates activity
binding
|
ATP2A2 |
0.384 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-273662 |
|
|
Rattus norvegicus |
H9c2 Cell |
pmid |
sentence |
28784772 |
Furthermore, a Ser96Asp HRC variant, which mimics constitutive phosphorylation of Ser96, diminished delayed aftercontractions in HRC null cardiac myocytes. This HRC phosphomimetic variant was also able to rescue the aftercontractions elicited by the Ser96Ala variant, demonstrating that phosphorylation of Ser96 is critical for the cardioprotective function of HRC. Phosphorylation of HRC on Ser96 regulated the interactions of HRC with both triadin and SERCA2a, suggesting a unique mechanism for regulation of SR Ca homeostasis. |
|
Publications: |
1 |
Organism: |
Rattus Norvegicus |
+ |
ATP2A2 | up-regulates quantity
relocalization
|
calcium(2+) |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262050 |
|
|
Homo sapiens |
|
pmid |
sentence |
16402920 |
In the present study, we have analysed the expression and functional characteristics of SERCA2c relative to SERCA2a and SERCA2b isoforms upon their stable heterologous expression in HEK-293 cells (human embryonic kidney 293 cells). All SERCA2 proteins induced an increased Ca2+ content in the ER of intact transfected cells. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
thapsigargin | down-regulates activity
chemical inhibition
|
ATP2A2 |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262021 |
|
|
Chlorocebus aethiops |
|
pmid |
sentence |
30814986 |
Treatment of Vero cells with SERCA-specific inhibitor (Thapsigargin) at a concentration that is nontoxic to the cells significantly reduced Peste des petits ruminants virus (PPRV) and Newcastle disease virus (NDV) replication. |Thapsigargin inhibits NDV-induced SERCA2 expression in Vero cells |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
PLN | down-regulates activity
binding
|
ATP2A2 |
0.746 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-252031 |
|
|
Mus musculus |
|
pmid |
sentence |
12838339 |
Heart failure can be traced, in part, to alterations in the activity of the sarcoplasmic reticulum Ca2+ pump that are induced by its interactions with phospholamban, a reversible inhibitor. |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
SLN | down-regulates activity
binding
|
ATP2A2 |
0.52 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-264779 |
|
|
in vitro |
|
pmid |
sentence |
23455424 |
The structure suggests a mechanism for selective Ca2+ loading and activation of SERCA, and provides new insight into how SLN and PLB inhibition arises from stabilization of this E1 intermediate state without bound Ca2+. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
PDE3A | down-regulates activity
binding
|
ATP2A2 |
0.348 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262051 |
|
|
Homo sapiens |
|
pmid |
sentence |
25593322 |
Regulation of sarcoplasmic reticulum Ca2+ ATPase 2 (SERCA2) activity by phosphodiesterase 3A (PDE3A) in human myocardium: phosphorylation-dependent interaction of PDE3A1 with SERCA2.|PDE3A co-localized with PLB, SERCA2, and an AKAP18 variant|our studies show that PDE3-selective inhibition (but not PDE4 inhibition) potentiates the phosphorylation of PLB by endogenous PKA and stimulation of SERCA2 activity and Ca2+ uptake in SR-enriched vesicles prepared from human myocardium. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Cardiac Muscle |
+ |
HAX1 | down-regulates quantity by destabilization
binding
|
ATP2A2 |
0.38 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262052 |
|
|
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
18971376 |
The anti-apoptotic protein HAX-1 interacts with SERCA2 and regulates its protein levels to promote cell survival.|Importantly, HAX-1 overexpression was associated with down-regulation of SERCA2 expression levels, resulting in significant reduction of apparent ER Ca(2+) levels. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
HAX1 | down-regulates quantity by repression
transcriptional regulation
|
ATP2A2 |
0.38 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-254222 |
|
|
Homo sapiens |
|
pmid |
sentence |
18971376 |
HAX-1 overexpression was associated with down-regulation of SERCA2 expression levels, resulting in significant reduction of apparent ER Ca(2+) levels. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |