| Type | Description |
|---|---|
| Definition | calmodulin 3 |
| Date | Results | Publications |
|---|---|---|
| 2010-12-11 10:50:00 | Results support the hypothesis that Ca(2)(+) binding to CaM's C-terminal acts as the switch converting CaM from a RyR1 activator into a channel inhibitor. | 20815817 |
| 2010-01-21 00:00:00 | Results describe the mechanism of switching of alpha-calcium-calmodulin-dependent protein kinase II between two types of activity: Ca(2+)-independent partial activity and Ca(2+)/calmodulin-activated full activity. | 15147211 |
| 2010-01-21 00:00:00 | calmodulin behaves as an activator of ammodytoxin under both nonreducing and reducing (cytosol-like) conditions by stimulating its enzymatic activity up to 21-fold | 19839601 |
| 2010-01-21 00:00:00 | Met124 was required for both high-affinity CaM binding to RyR2 and for maximal CaM inhibition. These results thus identify a Met residue critical for the productive association of CaM with RyR2 channels. | 16199479 |
| Type | IDs |
|---|---|
| Gene |
UniProtKB-ID:
A0A4X1SGS5_PIG,
F2Z5G3_PIG
UniprotKB:
A0A4X1SGS5,
F2Z5G3
UniParc:
UPI00000000C1
EMBL:
DQIR01171804,
AEMK02000061,
AEMK02000041,
AEMK02000021,
DQIR01140571
Ensembl:
ENSSSCG00000022545,
ENSSSCG00000008433,
ENSSSCG00000025768,
ENSSSCG00070000755,
ENSSSCG00070003824,
ENSSSCG00070028203
KO:
ssc:100522926,
ssc:100154056,
ssc:396838
|
| Nucleutide sequences |
EMBL-CDS:
HDA96047.1,
HDB27281.1
Ensembl_TRS:
ENSSSCT00070007183,
ENSSSCT00070001414,
ENSSSCT00070056576,
ENSSSCT00070056577,
ENSSSCT00000068935,
ENSSSCT00000032084,
ENSSSCT00000043548,
ENSSSCT00000009234,
ENSSSCT00000031940
|
| Protein sequencees |
Ensembl_PRO:
ENSSSCP00070001223,
ENSSSCP00070048068,
ENSSSCP00070005878,
ENSSSCP00070048067,
ENSSSCP00000009000,
ENSSSCP00000022607,
ENSSSCP00000053816,
ENSSSCP00000028062,
ENSSSCP00000072892
RefSeq:
NP_001231138.1
|
| Others |
UniRef100:
UniRef100_P0DP23
UniRef90:
UniRef90_P0DP23
UniRef50:
UniRef50_P0DP23
UniGene:
Ssc.50156,
Ssc.61001
|
| {{proteinIndex+1}} | mRNA | Protein | UniprotKB | Description | ||||
|---|---|---|---|---|---|---|---|---|
| Refseq |
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