UniProtKB - P0DP23 (CALM1_HUMAN)
Protein
Calmodulin-1
Gene
CALM1
Organism
Homo sapiens (Human)
Status
Functioni
Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis (PubMed:16760425). Mediates calcium-dependent inactivation of CACNA1C (PubMed:26969752). Positively regulates calcium-activated potassium channel activity of KCNN2 (PubMed:27165696).4 Publications
Miscellaneous
This protein has four functional calcium-binding sites.2 Publications
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Calcium bindingi | 21 – 32 | 1Combined sources2 PublicationsAdd BLAST | 12 | |
Calcium bindingi | 57 – 68 | 2Combined sources2 PublicationsAdd BLAST | 12 | |
Calcium bindingi | 94 – 105 | 3Combined sources2 PublicationsAdd BLAST | 12 | |
Calcium bindingi | 130 – 141 | 4Combined sources2 PublicationsAdd BLAST | 12 |
GO - Molecular functioni
- adenylate cyclase activator activity Source: UniProtKB
- adenylate cyclase binding Source: CAFA
- calcium channel inhibitor activity Source: UniProtKB
- calcium-dependent protein binding Source: Ensembl
- calcium ion binding Source: UniProtKB
- disordered domain specific binding Source: CAFA
- inositol-1,4,5-trisphosphate 3-kinase activity Source: Reactome
- ion channel binding Source: UniProtKB
- nitric-oxide synthase binding Source: Ensembl
- nitric-oxide synthase regulator activity Source: Ensembl
- N-terminal myristoylation domain binding Source: UniProtKB
- phosphatidylinositol 3-kinase binding Source: Ensembl
- protein domain specific binding Source: UniProtKB
- protein kinase binding Source: BHF-UCL
- protein phosphatase activator activity Source: BHF-UCL
- protein serine/threonine kinase activator activity Source: BHF-UCL
- Ras guanyl-nucleotide exchange factor activity Source: Reactome
- titin binding Source: BHF-UCL
- type 3 metabotropic glutamate receptor binding Source: Ensembl
GO - Biological processi
- activation of adenylate cyclase activity Source: Ensembl
- cofactor metabolic process Source: Reactome
- detection of calcium ion Source: BHF-UCL
- establishment of protein localization to mitochondrial membrane Source: Ensembl
- Fc-epsilon receptor signaling pathway Source: Reactome
- G protein-coupled receptor signaling pathway Source: UniProtKB
- inositol phosphate metabolic process Source: Reactome
- MAPK cascade Source: Reactome
- muscle contraction Source: Reactome
- negative regulation of peptidyl-threonine phosphorylation Source: BHF-UCL
- negative regulation of ryanodine-sensitive calcium-release channel activity Source: UniProtKB
- platelet degranulation Source: Reactome
- positive regulation by host of symbiont cAMP-mediated signal transduction Source: CAFA
- positive regulation of cyclic-nucleotide phosphodiesterase activity Source: BHF-UCL
- positive regulation of nitric-oxide synthase activity Source: Ensembl
- positive regulation of peptidyl-threonine phosphorylation Source: BHF-UCL
- positive regulation of phosphoprotein phosphatase activity Source: BHF-UCL
- positive regulation of protein autophosphorylation Source: BHF-UCL
- positive regulation of protein dephosphorylation Source: BHF-UCL
- positive regulation of protein serine/threonine kinase activity Source: BHF-UCL
- positive regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
- regulation of cardiac muscle contraction Source: BHF-UCL
- regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion Source: BHF-UCL
- regulation of cell communication by electrical coupling involved in cardiac conduction Source: BHF-UCL
- regulation of cytokinesis Source: UniProtKB
- regulation of heart rate Source: BHF-UCL
- regulation of high voltage-gated calcium channel activity Source: Ensembl
- regulation of nitric-oxide synthase activity Source: Reactome
- regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: BHF-UCL
- regulation of rhodopsin mediated signaling pathway Source: Reactome
- regulation of ryanodine-sensitive calcium-release channel activity Source: UniProtKB
- regulation of synaptic vesicle endocytosis Source: Ensembl
- regulation of synaptic vesicle exocytosis Source: Ensembl
- response to amphetamine Source: Ensembl
- response to calcium ion Source: BHF-UCL
- response to corticosterone Source: Ensembl
- substantia nigra development Source: UniProtKB
- Wnt signaling pathway, calcium modulating pathway Source: Reactome
Keywordsi
Ligand | Calcium, Metal-binding |
Enzyme and pathway databases
Reactomei | R-HSA-111932 CaMK IV-mediated phosphorylation of CREB R-HSA-111933 Calmodulin induced events R-HSA-111957 Cam-PDE 1 activation R-HSA-111997 CaM pathway R-HSA-114608 Platelet degranulation R-HSA-1445148 Translocation of SLC2A4 (GLUT4) to the plasma membrane R-HSA-1474151 Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation R-HSA-163615 PKA activation R-HSA-180024 DARPP-32 events R-HSA-1855204 Synthesis of IP3 and IP4 in the cytosol R-HSA-2025928 Calcineurin activates NFAT R-HSA-203615 eNOS activation R-HSA-2151201 Transcriptional activation of mitochondrial biogenesis R-HSA-2514859 Inactivation, recovery and regulation of the phototransduction cascade R-HSA-2672351 Stimuli-sensing channels R-HSA-2871809 FCERI mediated Ca+2 mobilization R-HSA-4086398 Ca2+ pathway R-HSA-418359 Reduction of cytosolic Ca++ levels R-HSA-425561 Sodium/Calcium exchangers R-HSA-438066 Unblocking of NMDA receptors, glutamate binding and activation R-HSA-442720 CREB1 phosphorylation through the activation of Adenylate Cyclase R-HSA-442729 CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde R-HSA-442982 Ras activation upon Ca2+ influx through NMDA receptor R-HSA-445355 Smooth Muscle Contraction R-HSA-451308 Activation of Ca-permeable Kainate Receptor R-HSA-5210891 Uptake and function of anthrax toxins R-HSA-5218920 VEGFR2 mediated vascular permeability R-HSA-5218921 VEGFR2 mediated cell proliferation R-HSA-5576892 Phase 0 - rapid depolarisation R-HSA-5578775 Ion homeostasis R-HSA-5607763 CLEC7A (Dectin-1) induces NFAT activation R-HSA-5626467 RHO GTPases activate IQGAPs R-HSA-5627123 RHO GTPases activate PAKs R-HSA-5673000 RAF activation R-HSA-5673001 RAF/MAP kinase cascade R-HSA-6802946 Signaling by moderate kinase activity BRAF mutants R-HSA-6802949 Signaling by RAS mutants R-HSA-6802952 Signaling by BRAF and RAF fusions R-HSA-6802955 Paradoxical activation of RAF signaling by kinase inactive BRAF R-HSA-70221 Glycogen breakdown (glycogenolysis) R-HSA-8876725 Protein methylation R-HSA-9022535 Loss of phosphorylation of MECP2 at T308 R-HSA-9022692 Regulation of MECP2 expression and activity R-HSA-936837 Ion transport by P-type ATPases R-HSA-9617324 Negative regulation of NMDA receptor-mediated neuronal transmission R-HSA-9619229 Activation of RAC1 downstream of NMDARs R-HSA-9619483 Activation of AMPK downstream of NMDARs R-HSA-9620244 Long-term potentiation R-HSA-983695 Antigen activates B Cell Receptor (BCR) leading to generation of second messengers |
Protein family/group databases
MoonDBi | P0DP23 Predicted |
Names & Taxonomyi
Protein namesi | Recommended name: Calmodulin-1Imported |
Gene namesi | |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:1442 CALM1 |
MIMi | 114180 gene |
neXtProti | NX_P0DP23 |
Subcellular locationi
Cytoskeleton
- spindle 1 Publication
- spindle pole 1 Publication
- centrosome 1 Publication
Note: Distributed throughout the cell during interphase, but during mitosis becomes dramatically localized to the spindle poles and the spindle microtubules.
Cytoskeleton
- centrosome Source: UniProtKB
- spindle microtubule Source: UniProtKB
- spindle pole Source: UniProtKB
Cytosol
- cytosol Source: Reactome
Extracellular region or secreted
- extracellular region Source: Reactome
Mitochondrion
- mitochondrial membrane Source: Ensembl
Nucleus
- nucleoplasm Source: Reactome
- nucleus Source: UniProtKB
Plasma Membrane
- plasma membrane Source: UniProtKB
Other locations
- calcium channel complex Source: BHF-UCL
- catalytic complex Source: CAFA
- cytoplasm Source: UniProtKB
- growth cone Source: Ensembl
- myelin sheath Source: Ensembl
- protein-containing complex Source: CAFA
- sarcomere Source: BHF-UCL
- synaptic vesicle membrane Source: Ensembl
- vesicle Source: UniProtKB
Keywords - Cellular componenti
Cytoplasm, CytoskeletonPathology & Biotechi
Involvement in diseasei
Ventricular tachycardia, catecholaminergic polymorphic, 4 (CPVT4)4 Publications
The disease is caused by mutations affecting the gene represented in this entry. Mutations in CALM1 are the cause of CPVT4.
Disease descriptionAn arrhythmogenic disorder characterized by stress-induced, bidirectional ventricular tachycardia that may degenerate into cardiac arrest and cause sudden death. Patients present with recurrent syncope, seizures, or sudden death after physical activity or emotional stress. CPVT4 inheritance is autosomal dominant.
See also OMIM:614916Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_069222 | 54 | N → I in CPVT4; increased RYR2 calcium-release channel activity; not changed calcium-dependent inactivation of L-type calcium channel; not changed protein abundance; not changed structure; not changed thermal stability both in the absence and presence of calcium; no effect on the calcium binding affinity; significantly increased binding of RYR2; increased ryanodine-sensitive calcium-release channel activity; decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane. 4 PublicationsCorresponds to variant dbSNP:rs267607276EnsemblClinVar. | 1 | |
Natural variantiVAR_078541 | 98 | N → S in CPVT4; the mutant has significantly reduced calcium affinity compared to wild-type; calmodulin-RYR2 interaction is defective at low intracellular Ca(2+) concentrations and restored at moderate to high Ca(2+) concentrations; increased RYR2 calcium-release channel activity; decreased calcium-dependent inactivation of L-type calcium channel; not changed protein abundance; not changed structure; significantly reduced ryanodine-sensitive calcium-release channel activity; decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane. 4 PublicationsCorresponds to variant dbSNP:rs398124647EnsemblClinVar. | 1 |
Long QT syndrome 14 (LQT14)5 Publications
The disease is caused by mutations affecting the gene represented in this entry. Mutations in CALM1 are the cause of LQT14.
Disease descriptionA form of long QT syndrome, a heart disorder characterized by a prolonged QT interval on the ECG and polymorphic ventricular arrhythmias. They cause syncope and sudden death in response to exercise or emotional stress, and can present with a sentinel event of sudden cardiac death in infancy.
See also OMIM:616247Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_073275 | 90 | F → L in LQT14; significantly decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane. 2 PublicationsCorresponds to variant dbSNP:rs730882253EnsemblClinVar. | 1 | |
Natural variantiVAR_078542 | 130 | D → G in LQT14; reduction in calcium affinity; not changed protein abundance; not changed structure; significantly decreased thermal stability in presence of clacium; significantly decreased RYR2 interaction; increased ryanodine-sensitive calcium-release channel activity; decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane. 4 PublicationsCorresponds to variant dbSNP:rs730882252EnsemblClinVar. | 1 | |
Natural variantiVAR_078263 | 141 | E → G in LQT14; decreased calcium affinity; loss of CACNA1C calcium-dependent-inactivation; no effect on intracellular RYR2-mediated calcium release. 1 Publication | 1 | |
Natural variantiVAR_073282 | 142 | F → L in LQT14; reduction in calcium affinity; not changed protein abundance; not changed structure; significantly decreased thermal stability in presence of calcium; no effect on RYR2 interaction; significantly reduced ryanodine-sensitive calcium-release channel activity. 3 PublicationsCorresponds to variant dbSNP:rs11551462Ensembl. | 1 |
Keywords - Diseasei
Disease mutation, Long QT syndromeOrganism-specific databases
GeneReviewsi | CALM1 |
MalaCardsi | CALM1 |
MIMi | 614916 phenotype 616247 phenotype |
OpenTargetsi | ENSG00000143933 ENSG00000160014 ENSG00000198668 |
Chemistry databases
ChEMBLi | CHEMBL6093 |
Polymorphism and mutation databases
BioMutai | CALM1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedCombined sources2 Publications | |||
ChainiPRO_0000439932 | 2 – 149 | Calmodulin-1Add BLAST | 148 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylalanineCombined sources2 Publications | 1 | |
Modified residuei | 22 | N6-acetyllysine; alternateCombined sources | 1 | |
Cross-linki | 22 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources | ||
Cross-linki | 22 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity | ||
Modified residuei | 45 | Phosphothreonine; by CaMK4By similarity | 1 | |
Modified residuei | 82 | PhosphoserineCombined sources | 1 | |
Modified residuei | 95 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 100 | PhosphotyrosineCombined sources | 1 | |
Modified residuei | 102 | PhosphoserineCombined sources | 1 | |
Modified residuei | 111 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 116 | N6,N6,N6-trimethyllysine; alternateCombined sources1 Publication | 1 | |
Modified residuei | 116 | N6-methyllysine; alternateCombined sources | 1 | |
Modified residuei | 139 | PhosphotyrosineCombined sources | 1 |
Post-translational modificationi
Ubiquitination results in a strongly decreased activity.By similarity
Phosphorylation results in a decreased activity.By similarity
Keywords - PTMi
Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugationProteomic databases
jPOSTi | P0DP23 |
PeptideAtlasi | P0DP23 |
PRIDEi | P0DP23 |
PTM databases
iPTMneti | P0DP23 |
PhosphoSitePlusi | P0DP23 |
Expressioni
Gene expression databases
ExpressionAtlasi | P0DP23 baseline and differential |
Organism-specific databases
HPAi | HPA044999 |
Interactioni
Subunit structurei
Interacts with MYO1C, MYO5A and RRAD. Interacts with MYO10 (By similarity). Interacts with CEP97, CCP110, TTN/titin and SRY (PubMed:9804419, PubMed:12871148, PubMed:15746192, PubMed:16760425, PubMed:17719545). Interacts with USP6; the interaction is calcium dependent (PubMed:16127172). Interacts with CDK5RAP2 (PubMed:20466722). Interacts with SCN5A (PubMed:21167176). Interacts with RYR1 (PubMed:18650434). Interacts with FCHO1 (PubMed:22484487). Interacts with MIP in a 1:2 stoichiometry; the interaction with the cytoplasmic domains from two MIP subunits promotes MIP water channel closure (PubMed:23893133). Interacts with ORAI1; this may play a role in the regulation of ORAI1-mediated calcium transport (By similarity). Interacts with IQCF1 (By similarity). Interacts with SYT7 (By similarity). Interacts with CEACAM1 (via cytoplasmic domain); this interaction is in a calcium dependent manner and reduces homophilic cell adhesion through dissociation of dimer (By similarity). Interacts with RYR2; regulates RYR2 calcium-release channel activity (PubMed:27516456, PubMed:18650434, PubMed:26164367). Interacts with PCP4; regulates calmodulin calcium-binding (PubMed:27876793). Interacts with the heterotetrameric KCNQ2 and KCNQ3 channel; the interaction is calcium-independent, constitutive and participates to the proper assembly of a functional heterotetrameric M channel (PubMed:27564677). Interacts with alpha-synuclein/SNCA (PubMed:23607618).By similarity21 Publications
(Microbial infection) Interacts with Rubella virus protease/methyltransferase p150.1 Publication
GO - Molecular functioni
- adenylate cyclase binding Source: CAFA
- calcium-dependent protein binding Source: Ensembl
- disordered domain specific binding Source: CAFA
- ion channel binding Source: UniProtKB
- nitric-oxide synthase binding Source: Ensembl
- N-terminal myristoylation domain binding Source: UniProtKB
- phosphatidylinositol 3-kinase binding Source: Ensembl
- protein domain specific binding Source: UniProtKB
- protein kinase binding Source: BHF-UCL
- Ras guanyl-nucleotide exchange factor activity Source: Reactome
- titin binding Source: BHF-UCL
- type 3 metabotropic glutamate receptor binding Source: Ensembl
Chemistry databases
BindingDBi | P0DP23 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1AJI | model | - | A | 5-148 | [»] | |
1CDL | X-ray | 2.00 | A/B/C/D | 2-148 | [»] | |
1CLL | X-ray | 1.70 | A | 2-149 | [»] | |
1CTR | X-ray | 2.45 | A | 2-149 | [»] | |
1IWQ | X-ray | 2.00 | A | 2-149 | [»] | |
1J7O | NMR | - | A | 2-77 | [»] | |
1J7P | NMR | - | A | 83-149 | [»] | |
1K90 | X-ray | 2.75 | D/E/F | 2-149 | [»] | |
1K93 | X-ray | 2.95 | D/E/F | 6-149 | [»] | |
1L7Z | X-ray | 2.30 | A | 2-149 | [»] | |
1LVC | X-ray | 3.60 | D/E/F | 1-149 | [»] | |
1NKF | NMR | - | A | 94-105 | [»] | |
1PK0 | X-ray | 3.30 | D/E/F | 2-148 | [»] | |
1S26 | X-ray | 3.00 | D/E/F | 2-149 | [»] | |
1SK6 | X-ray | 3.20 | D/E/F | 2-149 | [»] | |
1SW8 | NMR | - | A | 2-80 | [»] | |
1UP5 | X-ray | 1.90 | A/B | 2-149 | [»] | |
1WRZ | X-ray | 2.00 | A | 1-149 | [»] | |
1XFU | X-ray | 3.35 | O/P/Q/R/S/T | 1-149 | [»] | |
1XFV | X-ray | 3.35 | O/P/Q/R/S/T | 1-149 | [»] | |
1XFW | X-ray | 3.40 | O/P/Q/R/S/T | 1-149 | [»] | |
1XFX | X-ray | 3.20 | O/P/Q/R/S/T | 1-149 | [»] | |
1XFY | X-ray | 3.30 | O/P/Q/R/S/T | 1-149 | [»] | |
1XFZ | X-ray | 3.25 | O/P/Q/R/S/T | 1-149 | [»] | |
1Y6W | X-ray | 2.40 | A | 2-149 | [»] | |
1YR5 | X-ray | 1.70 | A | 2-149 | [»] | |
1YRT | X-ray | 2.10 | B | 76-149 | [»] | |
1YRU | X-ray | 2.50 | B | 76-149 | [»] | |
1ZOT | X-ray | 2.20 | B | 80-148 | [»] | |
1ZUZ | X-ray | 1.91 | A | 1-149 | [»] | |
2BE6 | X-ray | 2.00 | A/B/C | 1-149 | [»] | |
2F3Y | X-ray | 1.45 | A | 2-149 | [»] | |
2F3Z | X-ray | 1.60 | A | 2-149 | [»] | |
2HF5 | NMR | - | A | 47-114 | [»] | |
2I08 | X-ray | 2.00 | A | 3-79 | [»] | |
2JZI | NMR | - | A | 2-149 | [»] | |
2K0E | NMR | - | A | 2-149 | [»] | |
2K0F | NMR | - | A | 2-149 | [»] | |
2K0J | NMR | - | A | 3-149 | [»] | |
2K61 | NMR | - | A | 2-149 | [»] | |
2KNE | NMR | - | A | 2-149 | [»] | |
2KUG | NMR | - | A | 2-77 | [»] | |
2KUH | NMR | - | A | 83-149 | [»] | |
2L53 | NMR | - | A | 2-149 | [»] | |
2L7L | NMR | - | A | 2-149 | [»] | |
2LGF | NMR | - | A | 3-149 | [»] | |
2LL6 | NMR | - | A | 2-149 | [»] | |
2LL7 | NMR | - | A | 2-149 | [»] | |
2LQC | NMR | - | A | 2-78 | [»] | |
2LQP | NMR | - | A | 79-149 | [»] | |
2LV6 | Other | - | A | 2-149 | [»] | |
2M0J | NMR | - | A | 2-149 | [»] | |
2M0K | NMR | - | A | 2-149 | [»] | |
2M55 | NMR | - | A | 2-149 | [»] | |
2MG5 | NMR | - | A | 2-149 | [»] | |
2N27 | NMR | - | A | 2-149 | [»] | |
2N6A | NMR | - | A | 6-147 | [»] | |
2N77 | NMR | - | A | 77-149 | [»] | |
2N8J | NMR | - | A | 2-149 | [»] | |
2R28 | X-ray | 1.86 | A/B | 1-149 | [»] | |
2V01 | X-ray | 2.15 | A | 2-149 | [»] | |
2V02 | X-ray | 2.20 | A | 2-149 | [»] | |
2VAY | X-ray | 1.94 | A | 4-149 | [»] | |
2W73 | X-ray | 1.45 | A/B/E/F | 1-149 | [»] | |
2WEL | X-ray | 1.90 | D | 1-149 | [»] | |
2X0G | X-ray | 2.20 | B | 2-149 | [»] | |
2Y4V | X-ray | 1.80 | A | 1-149 | [»] | |
3BYA | X-ray | 1.85 | A | 2-149 | [»] | |
3DVE | X-ray | 2.35 | A | 2-149 | [»] | |
3DVJ | X-ray | 2.80 | A | 2-149 | [»] | |
3DVK | X-ray | 2.30 | A | 2-149 | [»] | |
3DVM | X-ray | 2.60 | A | 2-149 | [»] | |
3EWT | X-ray | 2.40 | A | 2-149 | [»] | |
3EWV | X-ray | 2.60 | A | 2-149 | [»] | |
3G43 | X-ray | 2.10 | A/B/C/D | 2-149 | [»] | |
3HR4 | X-ray | 2.50 | B/D/F/H | 1-149 | [»] | |
3J41 | electron microscopy | 25.0 | E/F | 1-149 | [»] | |
3O77 | X-ray | 2.35 | A | 1-149 | [»] | |
3O78 | X-ray | 2.60 | A/B | 1-149 | [»] | |
3OXQ | X-ray | 2.55 | A/B/C/D | 1-149 | [»] | |
3SUI | X-ray | 1.95 | A | 1-149 | [»] | |
3UCT | X-ray | 1.90 | A/B | 2-80 | [»] | |
3UCW | X-ray | 1.76 | A/B/C/D | 2-80 | [»] | |
3UCY | X-ray | 1.80 | A | 2-80 | [»] | |
4BW7 | X-ray | 1.81 | A/C | 1-149 | [»] | |
4BW8 | X-ray | 1.80 | A/B | 1-149 | [»] | |
4BYF | X-ray | 2.74 | B/D | 1-149 | [»] | |
4DCK | X-ray | 2.20 | B | 1-149 | [»] | |
4DJC | X-ray | 1.35 | A | 1-149 | [»] | |
4GOW | X-ray | 2.60 | D | 4-147 | [»] | |
4JPZ | X-ray | 3.02 | C/I | 1-149 | [»] | |
4JQ0 | X-ray | 3.84 | C | 1-149 | [»] | |
4L79 | X-ray | 2.30 | B | 1-149 | [»] | |
4LZX | X-ray | 1.50 | A | 2-149 | [»] | |
4M1L | X-ray | 2.10 | A | 2-149 | [»] | |
4OVN | X-ray | 2.80 | A/B/C/D/E | 1-149 | [»] | |
4Q57 | X-ray | 1.80 | A | 10-74 | [»] | |
4Q5U | X-ray | 1.95 | A | 1-149 | [»] | |
4UMO | X-ray | 3.00 | C/D | 1-149 | [»] | |
4UPU | X-ray | 2.34 | A | 2-149 | [»] | |
4V0C | X-ray | 2.86 | C/D | 1-149 | [»] | |
5COC | X-ray | 2.67 | A | 5-78 | [»] | |
5DBR | X-ray | 2.25 | A | 5-149 | [»] | |
5DOW | X-ray | 1.70 | A/C/E/G | 2-149 | [»] | |
5DSU | X-ray | 1.93 | A | 3-78 | [»] | |
5GGM | NMR | - | A | 2-149 | [»] | |
5I0I | X-ray | 3.15 | C/E | 3-147 | [»] | |
G | 84-126 | [»] | ||||
I | 84-147 | [»] | ||||
5J03 | X-ray | 2.00 | B | 1-149 | [»] | |
5J8H | NMR | - | A | 2-149 | [»] | |
5JQA | X-ray | 1.80 | A | 1-149 | [»] | |
5JTH | X-ray | 1.84 | A | 1-149 | [»] | |
5K7L | electron microscopy | 3.78 | B | 1-149 | [»] | |
5K8Q | X-ray | 1.74 | A | 1-149 | [»] | |
5OEO | NMR | - | A | 1-149 | [»] | |
5TP5 | NMR | - | A | 2-149 | [»] | |
5TP6 | NMR | - | A | 2-149 | [»] | |
5V02 | X-ray | 1.78 | R | 1-149 | [»] | |
5V03 | X-ray | 1.58 | R | 1-149 | [»] | |
5V7X | X-ray | 3.14 | B | 1-149 | [»] | |
5WBX | X-ray | 1.90 | R | 5-148 | [»] | |
5WC5 | X-ray | 2.30 | R | 5-148 | [»] | |
6B8L | X-ray | 2.30 | B/D/F/H | 1-149 | [»] | |
6B8M | X-ray | 2.30 | B/D/F/H | 1-149 | [»] | |
6B8N | X-ray | 2.20 | B/D/F/H | 1-149 | [»] | |
6B8P | X-ray | 2.20 | B/D/F/H | 1-149 | [»] | |
6B8Q | X-ray | 2.60 | B/D/F/H | 1-149 | [»] | |
6C1D | electron microscopy | 3.20 | R | 2-149 | [»] | |
6C1G | electron microscopy | 3.80 | R | 2-149 | [»] | |
6C1H | electron microscopy | 3.90 | R | 2-149 | [»] | |
6CNM | electron microscopy | 3.40 | E/F/G/H | 1-149 | [»] | |
6CNN | electron microscopy | 3.50 | E/F/G/H | 1-149 | [»] | |
6CNO | electron microscopy | 4.70 | E/F/G/H | 1-149 | [»] | |
6DAD | X-ray | 1.65 | A/B | 2-149 | [»] | |
6DAE | X-ray | 2.00 | A/B | 2-149 | [»] | |
6DAF | X-ray | 2.40 | A/B | 2-149 | [»] | |
6DAH | X-ray | 2.50 | A/B/C/D | 1-149 | [»] | |
6E2F | electron microscopy | 3.90 | E | 1-149 | [»] | |
6E2G | electron microscopy | 3.60 | E | 1-149 | [»] | |
6FEG | NMR | - | B | 1-149 | [»] | |
6FEH | NMR | - | B | 1-149 | [»] | |
6GDK | NMR | - | A | 2-149 | [»] | |
6GDL | NMR | - | A | 2-80 | [»] | |
6HCS | X-ray | 2.00 | A/C/E/G | 1-149 | [»] | |
SMRi | P0DP23 | |||||
ModBasei | Search... | |||||
MobiDBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 8 – 43 | EF-hand 1PROSITE-ProRule annotationAdd BLAST | 36 | |
Domaini | 44 – 79 | EF-hand 2PROSITE-ProRule annotationAdd BLAST | 36 | |
Domaini | 81 – 116 | EF-hand 3PROSITE-ProRule annotationAdd BLAST | 36 | |
Domaini | 117 – 149 | EF-hand 4PROSITE-ProRule annotationAdd BLAST | 33 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 77 – 149 | Necessary and sufficient for interaction with PCP41 PublicationAdd BLAST | 73 |
Sequence similaritiesi
Belongs to the calmodulin family.Curated
Keywords - Domaini
RepeatPhylogenomic databases
KOi | K02183 |
OMAi | PHESSNQ |
OrthoDBi | 1386217at2759 |
Family and domain databases
CDDi | cd00051 EFh, 2 hits |
InterProi | View protein in InterPro IPR039030 Calmodulin IPR011992 EF-hand-dom_pair IPR018247 EF_Hand_1_Ca_BS IPR002048 EF_hand_dom |
PANTHERi | PTHR23050:SF311 PTHR23050:SF311, 1 hit |
Pfami | View protein in Pfam PF13499 EF-hand_7, 2 hits |
SMARTi | View protein in SMART SM00054 EFh, 4 hits |
SUPFAMi | SSF47473 SSF47473, 1 hit |
PROSITEi | View protein in PROSITE PS00018 EF_HAND_1, 4 hits PS50222 EF_HAND_2, 4 hits |
(1+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry has 1 described isoform and 9 potential isoforms that are computationally mapped.Show allAlign All
P0DP23-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ
60 70 80 90 100
DMINEVDADG NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY
110 120 130 140
ISAAELRHVM TNLGEKLTDE EVDEMIREAD IDGDGQVNYE EFVQMMTAK
Computationally mapped potential isoform sequencesi
There are 9 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketQ96HY3 | Q96HY3_HUMAN | CALM1 protein | CALM1 CALM2, CALM3, hCG_17033, hCG_20313 | 113 | Annotation score: | ||
M0QZ52 | M0QZ52_HUMAN | Calmodulin 3 (Phosphorylase kinase,... | CALM1 CALM2, CALM3, hCG_20313 | 83 | Annotation score: | ||
G3V361 | G3V361_HUMAN | Calmodulin-1 | CALM1 | 98 | Annotation score: | ||
E7ETZ0 | E7ETZ0_HUMAN | Calmodulin-1 | CALM1 | 150 | Annotation score: | ||
G3V226 | G3V226_HUMAN | Calmodulin-1 | CALM1 | 76 | Annotation score: | ||
H0Y7A7 | H0Y7A7_HUMAN | Calmodulin-2 | CALM2 | 187 | Annotation score: | ||
E7EMB3 | E7EMB3_HUMAN | Calmodulin-2 | CALM2 | 196 | Annotation score: | ||
F8WBR5 | F8WBR5_HUMAN | Calmodulin-2 | CALM2 | 65 | Annotation score: | ||
G3V479 | G3V479_HUMAN | Calmodulin-1 | CALM1 | 83 | Annotation score: |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_069222 | 54 | N → I in CPVT4; increased RYR2 calcium-release channel activity; not changed calcium-dependent inactivation of L-type calcium channel; not changed protein abundance; not changed structure; not changed thermal stability both in the absence and presence of calcium; no effect on the calcium binding affinity; significantly increased binding of RYR2; increased ryanodine-sensitive calcium-release channel activity; decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane. 4 PublicationsCorresponds to variant dbSNP:rs267607276EnsemblClinVar. | 1 | |
Natural variantiVAR_073275 | 90 | F → L in LQT14; significantly decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane. 2 PublicationsCorresponds to variant dbSNP:rs730882253EnsemblClinVar. | 1 | |
Natural variantiVAR_078541 | 98 | N → S in CPVT4; the mutant has significantly reduced calcium affinity compared to wild-type; calmodulin-RYR2 interaction is defective at low intracellular Ca(2+) concentrations and restored at moderate to high Ca(2+) concentrations; increased RYR2 calcium-release channel activity; decreased calcium-dependent inactivation of L-type calcium channel; not changed protein abundance; not changed structure; significantly reduced ryanodine-sensitive calcium-release channel activity; decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane. 4 PublicationsCorresponds to variant dbSNP:rs398124647EnsemblClinVar. | 1 | |
Natural variantiVAR_078542 | 130 | D → G in LQT14; reduction in calcium affinity; not changed protein abundance; not changed structure; significantly decreased thermal stability in presence of clacium; significantly decreased RYR2 interaction; increased ryanodine-sensitive calcium-release channel activity; decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane. 4 PublicationsCorresponds to variant dbSNP:rs730882252EnsemblClinVar. | 1 | |
Natural variantiVAR_078263 | 141 | E → G in LQT14; decreased calcium affinity; loss of CACNA1C calcium-dependent-inactivation; no effect on intracellular RYR2-mediated calcium release. 1 Publication | 1 | |
Natural variantiVAR_073282 | 142 | F → L in LQT14; reduction in calcium affinity; not changed protein abundance; not changed structure; significantly decreased thermal stability in presence of calcium; no effect on RYR2 interaction; significantly reduced ryanodine-sensitive calcium-release channel activity. 3 PublicationsCorresponds to variant dbSNP:rs11551462Ensembl. | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M27319 mRNA Translation: AAA35635.1 U12022, U11886 Genomic DNA Translation: AAB60644.1 BT006818 mRNA Translation: AAP35464.1 AC006536 Genomic DNA Translation: AAD45181.1 AL512791 Genomic DNA No translation available. BC000454 mRNA Translation: AAH00454.1 BC008597 mRNA Translation: AAH08597.1 BC011834 mRNA Translation: AAH11834.1 BC047523 mRNA No translation available. |
CCDSi | CCDS9892.1 |
PIRi | S48728 MCHU |
RefSeqi | NP_001316851.1, NM_001329922.1 NP_001734.1, NM_001743.5 NP_005175.2, NM_005184.3 NP_008819.1, NM_006888.4 |
UniGenei | Hs.282410 Hs.468442 Hs.515487 |
Genome annotation databases
Ensembli | ENST00000356978; ENSP00000349467; ENSG00000198668 |
GeneIDi | 801 805 808 |
KEGGi | hsa:801 hsa:805 hsa:808 |
Keywords - Coding sequence diversityi
PolymorphismSimilar proteinsi
Cross-referencesi
Web resourcesi
Protein Spotlight A question of length - Issue 105 of May 2009 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M27319 mRNA Translation: AAA35635.1 U12022, U11886 Genomic DNA Translation: AAB60644.1 BT006818 mRNA Translation: AAP35464.1 AC006536 Genomic DNA Translation: AAD45181.1 AL512791 Genomic DNA No translation available. BC000454 mRNA Translation: AAH00454.1 BC008597 mRNA Translation: AAH08597.1 BC011834 mRNA Translation: AAH11834.1 BC047523 mRNA No translation available. |
CCDSi | CCDS9892.1 |
PIRi | S48728 MCHU |
RefSeqi | NP_001316851.1, NM_001329922.1 NP_001734.1, NM_001743.5 NP_005175.2, NM_005184.3 NP_008819.1, NM_006888.4 |
UniGenei | Hs.282410 Hs.468442 Hs.515487 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1AJI | model | - | A | 5-148 | [»] | |
1CDL | X-ray | 2.00 | A/B/C/D | 2-148 | [»] | |
1CLL | X-ray | 1.70 | A | 2-149 | [»] | |
1CTR | X-ray | 2.45 | A | 2-149 | [»] | |
1IWQ | X-ray | 2.00 | A | 2-149 | [»] | |
1J7O | NMR | - | A | 2-77 | [»] | |
1J7P | NMR | - | A | 83-149 | [»] | |
1K90 | X-ray | 2.75 | D/E/F | 2-149 | [»] | |
1K93 | X-ray | 2.95 | D/E/F | 6-149 | [»] | |
1L7Z | X-ray | 2.30 | A | 2-149 | [»] | |
1LVC | X-ray | 3.60 | D/E/F | 1-149 | [»] | |
1NKF | NMR | - | A | 94-105 | [»] | |
1PK0 | X-ray | 3.30 | D/E/F | 2-148 | [»] | |
1S26 | X-ray | 3.00 | D/E/F | 2-149 | [»] | |
1SK6 | X-ray | 3.20 | D/E/F | 2-149 | [»] | |
1SW8 | NMR | - | A | 2-80 | [»] | |
1UP5 | X-ray | 1.90 | A/B | 2-149 | [»] | |
1WRZ | X-ray | 2.00 | A | 1-149 | [»] | |
1XFU | X-ray | 3.35 | O/P/Q/R/S/T | 1-149 | [»] | |
1XFV | X-ray | 3.35 | O/P/Q/R/S/T | 1-149 | [»] | |
1XFW | X-ray | 3.40 | O/P/Q/R/S/T | 1-149 | [»] | |
1XFX | X-ray | 3.20 | O/P/Q/R/S/T | 1-149 | [»] | |
1XFY | X-ray | 3.30 | O/P/Q/R/S/T | 1-149 | [»] | |
1XFZ | X-ray | 3.25 | O/P/Q/R/S/T | 1-149 | [»] | |
1Y6W | X-ray | 2.40 | A | 2-149 | [»] | |
1YR5 | X-ray | 1.70 | A | 2-149 | [»] | |
1YRT | X-ray | 2.10 | B | 76-149 | [»] | |
1YRU | X-ray | 2.50 | B | 76-149 | [»] | |
1ZOT | X-ray | 2.20 | B | 80-148 | [»] | |
1ZUZ | X-ray | 1.91 | A | 1-149 | [»] | |
2BE6 | X-ray | 2.00 | A/B/C | 1-149 | [»] | |
2F3Y | X-ray | 1.45 | A | 2-149 | [»] | |
2F3Z | X-ray | 1.60 | A | 2-149 | [»] | |
2HF5 | NMR | - | A | 47-114 | [»] | |
2I08 | X-ray | 2.00 | A | 3-79 | [»] | |
2JZI | NMR | - | A | 2-149 | [»] | |
2K0E | NMR | - | A | 2-149 | [»] | |
2K0F | NMR | - | A | 2-149 | [»] | |
2K0J | NMR | - | A | 3-149 | [»] | |
2K61 | NMR | - | A | 2-149 | [»] | |
2KNE | NMR | - | A | 2-149 | [»] | |
2KUG | NMR | - | A | 2-77 | [»] | |
2KUH | NMR | - | A | 83-149 | [»] | |
2L53 | NMR | - | A | 2-149 | [»] | |
2L7L | NMR | - | A | 2-149 | [»] | |
2LGF | NMR | - | A | 3-149 | [»] | |
2LL6 | NMR | - | A | 2-149 | [»] | |
2LL7 | NMR | - | A | 2-149 | [»] | |
2LQC | NMR | - | A | 2-78 | [»] | |
2LQP | NMR | - | A | 79-149 | [»] | |
2LV6 | Other | - | A | 2-149 | [»] | |
2M0J | NMR | - | A | 2-149 | [»] | |
2M0K | NMR | - | A | 2-149 | [»] | |
2M55 | NMR | - | A | 2-149 | [»] | |
2MG5 | NMR | - | A | 2-149 | [»] | |
2N27 | NMR | - | A | 2-149 | [»] | |
2N6A | NMR | - | A | 6-147 | [»] | |
2N77 | NMR | - | A | 77-149 | [»] | |
2N8J | NMR | - | A | 2-149 | [»] | |
2R28 | X-ray | 1.86 | A/B | 1-149 | [»] | |
2V01 | X-ray | 2.15 | A | 2-149 | [»] | |
2V02 | X-ray | 2.20 | A | 2-149 | [»] | |
2VAY | X-ray | 1.94 | A | 4-149 | [»] | |
2W73 | X-ray | 1.45 | A/B/E/F | 1-149 | [»] | |
2WEL | X-ray | 1.90 | D | 1-149 | [»] | |
2X0G | X-ray | 2.20 | B | 2-149 | [»] | |
2Y4V | X-ray | 1.80 | A | 1-149 | [»] | |
3BYA | X-ray | 1.85 | A | 2-149 | [»] | |
3DVE | X-ray | 2.35 | A | 2-149 | [»] | |
3DVJ | X-ray | 2.80 | A | 2-149 | [»] | |
3DVK | X-ray | 2.30 | A | 2-149 | [»] | |
3DVM | X-ray | 2.60 | A | 2-149 | [»] | |
3EWT | X-ray | 2.40 | A | 2-149 | [»] | |
3EWV | X-ray | 2.60 | A | 2-149 | [»] | |
3G43 | X-ray | 2.10 | A/B/C/D | 2-149 | [»] | |
3HR4 | X-ray | 2.50 | B/D/F/H | 1-149 | [»] | |
3J41 | electron microscopy | 25.0 | E/F | 1-149 | [»] | |
3O77 | X-ray | 2.35 | A | 1-149 | [»] | |
3O78 | X-ray | 2.60 | A/B | 1-149 | [»] | |
3OXQ | X-ray | 2.55 | A/B/C/D | 1-149 | [»] | |
3SUI | X-ray | 1.95 | A | 1-149 | [»] | |
3UCT | X-ray | 1.90 | A/B | 2-80 | [»] | |
3UCW | X-ray | 1.76 | A/B/C/D | 2-80 | [»] | |
3UCY | X-ray | 1.80 | A | 2-80 | [»] | |
4BW7 | X-ray | 1.81 | A/C | 1-149 | [»] | |
4BW8 | X-ray | 1.80 | A/B | 1-149 | [»] | |
4BYF | X-ray | 2.74 | B/D | 1-149 | [»] | |
4DCK | X-ray | 2.20 | B | 1-149 | [»] | |
4DJC | X-ray | 1.35 | A | 1-149 | [»] | |
4GOW | X-ray | 2.60 | D | 4-147 | [»] | |
4JPZ | X-ray | 3.02 | C/I | 1-149 | [»] | |
4JQ0 | X-ray | 3.84 | C | 1-149 | [»] | |
4L79 | X-ray | 2.30 | B | 1-149 | [»] | |
4LZX | X-ray | 1.50 | A | 2-149 | [»] | |
4M1L | X-ray | 2.10 | A | 2-149 | [»] | |
4OVN | X-ray | 2.80 | A/B/C/D/E | 1-149 | [»] | |
4Q57 | X-ray | 1.80 | A | 10-74 | [»] | |
4Q5U | X-ray | 1.95 | A | 1-149 | [»] | |
4UMO | X-ray | 3.00 | C/D | 1-149 | [»] | |
4UPU | X-ray | 2.34 | A | 2-149 | [»] | |
4V0C | X-ray | 2.86 | C/D | 1-149 | [»] | |
5COC | X-ray | 2.67 | A | 5-78 | [»] | |
5DBR | X-ray | 2.25 | A | 5-149 | [»] | |
5DOW | X-ray | 1.70 | A/C/E/G | 2-149 | [»] | |
5DSU | X-ray | 1.93 | A | 3-78 | [»] | |
5GGM | NMR | - | A | 2-149 | [»] | |
5I0I | X-ray | 3.15 | C/E | 3-147 | [»] | |
G | 84-126 | [»] | ||||
I | 84-147 | [»] | ||||
5J03 | X-ray | 2.00 | B | 1-149 | [»] | |
5J8H | NMR | - | A | 2-149 | [»] | |
5JQA | X-ray | 1.80 | A | 1-149 | [»] | |
5JTH | X-ray | 1.84 | A | 1-149 | [»] | |
5K7L | electron microscopy | 3.78 | B | 1-149 | [»] | |
5K8Q | X-ray | 1.74 | A | 1-149 | [»] | |
5OEO | NMR | - | A | 1-149 | [»] | |
5TP5 | NMR | - | A | 2-149 | [»] | |
5TP6 | NMR | - | A | 2-149 | [»] | |
5V02 | X-ray | 1.78 | R | 1-149 | [»] | |
5V03 | X-ray | 1.58 | R | 1-149 | [»] | |
5V7X | X-ray | 3.14 | B | 1-149 | [»] | |
5WBX | X-ray | 1.90 | R | 5-148 | [»] | |
5WC5 | X-ray | 2.30 | R | 5-148 | [»] | |
6B8L | X-ray | 2.30 | B/D/F/H | 1-149 | [»] | |
6B8M | X-ray | 2.30 | B/D/F/H | 1-149 | [»] | |
6B8N | X-ray | 2.20 | B/D/F/H | 1-149 | [»] | |
6B8P | X-ray | 2.20 | B/D/F/H | 1-149 | [»] | |
6B8Q | X-ray | 2.60 | B/D/F/H | 1-149 | [»] | |
6C1D | electron microscopy | 3.20 | R | 2-149 | [»] | |
6C1G | electron microscopy | 3.80 | R | 2-149 | [»] | |
6C1H | electron microscopy | 3.90 | R | 2-149 | [»] | |
6CNM | electron microscopy | 3.40 | E/F/G/H | 1-149 | [»] | |
6CNN | electron microscopy | 3.50 | E/F/G/H | 1-149 | [»] | |
6CNO | electron microscopy | 4.70 | E/F/G/H | 1-149 | [»] | |
6DAD | X-ray | 1.65 | A/B | 2-149 | [»] | |
6DAE | X-ray | 2.00 | A/B | 2-149 | [»] | |
6DAF | X-ray | 2.40 | A/B | 2-149 | [»] | |
6DAH | X-ray | 2.50 | A/B/C/D | 1-149 | [»] | |
6E2F | electron microscopy | 3.90 | E | 1-149 | [»] | |
6E2G | electron microscopy | 3.60 | E | 1-149 | [»] | |
6FEG | NMR | - | B | 1-149 | [»] | |
6FEH | NMR | - | B | 1-149 | [»] | |
6GDK | NMR | - | A | 2-149 | [»] | |
6GDL | NMR | - | A | 2-80 | [»] | |
6HCS | X-ray | 2.00 | A/C/E/G | 1-149 | [»] | |
SMRi | P0DP23 | |||||
ModBasei | Search... | |||||
MobiDBi | Search... |
Chemistry databases
BindingDBi | P0DP23 |
ChEMBLi | CHEMBL6093 |
Protein family/group databases
MoonDBi | P0DP23 Predicted |
PTM databases
iPTMneti | P0DP23 |
PhosphoSitePlusi | P0DP23 |
Polymorphism and mutation databases
BioMutai | CALM1 |
Proteomic databases
jPOSTi | P0DP23 |
PeptideAtlasi | P0DP23 |
PRIDEi | P0DP23 |
Protocols and materials databases
Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembli | ENST00000356978; ENSP00000349467; ENSG00000198668 |
GeneIDi | 801 805 808 |
KEGGi | hsa:801 hsa:805 hsa:808 |
Organism-specific databases
CTDi | 801 805 808 |
GeneCardsi | CALM1 |
GeneReviewsi | CALM1 |
HGNCi | HGNC:1442 CALM1 |
HPAi | HPA044999 |
MalaCardsi | CALM1 |
MIMi | 114180 gene 614916 phenotype 616247 phenotype |
neXtProti | NX_P0DP23 |
OpenTargetsi | ENSG00000143933 ENSG00000160014 ENSG00000198668 |
GenAtlasi | Search... |
Phylogenomic databases
KOi | K02183 |
OMAi | PHESSNQ |
OrthoDBi | 1386217at2759 |
Enzyme and pathway databases
Reactomei | R-HSA-111932 CaMK IV-mediated phosphorylation of CREB R-HSA-111933 Calmodulin induced events R-HSA-111957 Cam-PDE 1 activation R-HSA-111997 CaM pathway R-HSA-114608 Platelet degranulation R-HSA-1445148 Translocation of SLC2A4 (GLUT4) to the plasma membrane R-HSA-1474151 Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation R-HSA-163615 PKA activation R-HSA-180024 DARPP-32 events R-HSA-1855204 Synthesis of IP3 and IP4 in the cytosol R-HSA-2025928 Calcineurin activates NFAT R-HSA-203615 eNOS activation R-HSA-2151201 Transcriptional activation of mitochondrial biogenesis R-HSA-2514859 Inactivation, recovery and regulation of the phototransduction cascade R-HSA-2672351 Stimuli-sensing channels R-HSA-2871809 FCERI mediated Ca+2 mobilization R-HSA-4086398 Ca2+ pathway R-HSA-418359 Reduction of cytosolic Ca++ levels R-HSA-425561 Sodium/Calcium exchangers R-HSA-438066 Unblocking of NMDA receptors, glutamate binding and activation R-HSA-442720 CREB1 phosphorylation through the activation of Adenylate Cyclase R-HSA-442729 CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde R-HSA-442982 Ras activation upon Ca2+ influx through NMDA receptor R-HSA-445355 Smooth Muscle Contraction R-HSA-451308 Activation of Ca-permeable Kainate Receptor R-HSA-5210891 Uptake and function of anthrax toxins R-HSA-5218920 VEGFR2 mediated vascular permeability R-HSA-5218921 VEGFR2 mediated cell proliferation R-HSA-5576892 Phase 0 - rapid depolarisation R-HSA-5578775 Ion homeostasis R-HSA-5607763 CLEC7A (Dectin-1) induces NFAT activation R-HSA-5626467 RHO GTPases activate IQGAPs R-HSA-5627123 RHO GTPases activate PAKs R-HSA-5673000 RAF activation R-HSA-5673001 RAF/MAP kinase cascade R-HSA-6802946 Signaling by moderate kinase activity BRAF mutants R-HSA-6802949 Signaling by RAS mutants R-HSA-6802952 Signaling by BRAF and RAF fusions R-HSA-6802955 Paradoxical activation of RAF signaling by kinase inactive BRAF R-HSA-70221 Glycogen breakdown (glycogenolysis) R-HSA-8876725 Protein methylation R-HSA-9022535 Loss of phosphorylation of MECP2 at T308 R-HSA-9022692 Regulation of MECP2 expression and activity R-HSA-936837 Ion transport by P-type ATPases R-HSA-9617324 Negative regulation of NMDA receptor-mediated neuronal transmission R-HSA-9619229 Activation of RAC1 downstream of NMDARs R-HSA-9619483 Activation of AMPK downstream of NMDARs R-HSA-9620244 Long-term potentiation R-HSA-983695 Antigen activates B Cell Receptor (BCR) leading to generation of second messengers |
Miscellaneous databases
ChiTaRSi | CALM1 human |
PROi | PR:P0DP23 |
SOURCEi | Search... |
Gene expression databases
ExpressionAtlasi | P0DP23 baseline and differential |
Family and domain databases
CDDi | cd00051 EFh, 2 hits |
InterProi | View protein in InterPro IPR039030 Calmodulin IPR011992 EF-hand-dom_pair IPR018247 EF_Hand_1_Ca_BS IPR002048 EF_hand_dom |
PANTHERi | PTHR23050:SF311 PTHR23050:SF311, 1 hit |
Pfami | View protein in Pfam PF13499 EF-hand_7, 2 hits |
SMARTi | View protein in SMART SM00054 EFh, 4 hits |
SUPFAMi | SSF47473 SSF47473, 1 hit |
PROSITEi | View protein in PROSITE PS00018 EF_HAND_1, 4 hits PS50222 EF_HAND_2, 4 hits |
ProtoNeti | Search... |
Entry informationi
Entry namei | CALM1_HUMAN | |
Accessioni | P0DP23Primary (citable) accession number: P0DP23 Secondary accession number(s): P02593 Q96HK3 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 10, 2017 |
Last sequence update: | May 10, 2017 | |
Last modified: | February 13, 2019 | |
This is version 21 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families - Human chromosome 14
Human chromosome 14: entries, gene names and cross-references to MIM - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - Protein Spotlight
Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries