UniProtKB - P0DP23 (CALM1_HUMAN)
Calmodulin-1
CALM1
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).
Is a regulator of voltage-dependent L-type calcium channels (PubMed:31454269).
Mediates calcium-dependent inactivation of CACNA1C (PubMed:26969752).
Positively regulates calcium-activated potassium channel activity of KCNN2 (PubMed:27165696).
Forms a potassium channel complex with KCNQ1 and regulates electrophysiological activity of the channel via calcium-binding (PubMed:25441029).
Acts as a sensor to modulate the endoplasmic reticulum contacts with other organelles mediated by VMP1:ATP2A2 (PubMed:28890335).
6 Publications(Microbial infection) Required for Legionella pneumophila SidJ glutamylase activity.
1 PublicationMiscellaneous
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 21 | Calcium 1PROSITE-ProRule annotationCombined sources3 Publications | 1 | |
Metal bindingi | 23 | Calcium 1PROSITE-ProRule annotationCombined sources3 Publications | 1 | |
Metal bindingi | 25 | Calcium 1PROSITE-ProRule annotationCombined sources3 Publications | 1 | |
Metal bindingi | 27 | Calcium 1PROSITE-ProRule annotationCombined sources3 Publications | 1 | |
Metal bindingi | 32 | Calcium 1PROSITE-ProRule annotationCombined sources3 Publications | 1 | |
Metal bindingi | 57 | Calcium 2PROSITE-ProRule annotationCombined sources3 Publications | 1 | |
Metal bindingi | 59 | Calcium 2PROSITE-ProRule annotationCombined sources3 Publications | 1 | |
Metal bindingi | 61 | Calcium 2PROSITE-ProRule annotationCombined sources3 Publications | 1 | |
Metal bindingi | 63 | Calcium 2PROSITE-ProRule annotationCombined sources3 Publications | 1 | |
Metal bindingi | 68 | Calcium 2PROSITE-ProRule annotationCombined sources3 Publications | 1 | |
Metal bindingi | 94 | Calcium 3PROSITE-ProRule annotationCombined sources2 Publications | 1 | |
Metal bindingi | 96 | Calcium 3PROSITE-ProRule annotationCombined sources2 Publications | 1 | |
Metal bindingi | 98 | Calcium 3PROSITE-ProRule annotationCombined sources2 Publications | 1 | |
Metal bindingi | 100 | Calcium 3PROSITE-ProRule annotationCombined sources2 Publications | 1 | |
Metal bindingi | 105 | Calcium 3PROSITE-ProRule annotationCombined sources2 Publications | 1 | |
Metal bindingi | 130 | Calcium 4PROSITE-ProRule annotationCombined sources2 Publications | 1 | |
Metal bindingi | 132 | Calcium 4PROSITE-ProRule annotationCombined sources2 Publications | 1 | |
Metal bindingi | 134 | Calcium 4PROSITE-ProRule annotationCombined sources2 Publications | 1 | |
Metal bindingi | 136 | Calcium 4PROSITE-ProRule annotationCombined sources2 Publications | 1 | |
Metal bindingi | 141 | Calcium 4PROSITE-ProRule annotationCombined sources2 Publications | 1 |
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
- enzyme regulator activity Source: GO_Central
- N-terminal myristoylation domain binding Source: UniProtKB
- 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
- titin binding Source: BHF-UCL
- transmembrane transporter binding Source: UniProtKB
GO - Biological processi
- autophagosome membrane docking Source: UniProtKB
- detection of calcium ion Source: BHF-UCL
- G2/M transition of mitotic cell cycle Source: Ensembl
- G protein-coupled receptor signaling pathway Source: UniProtKB
- mitochondrion-endoplasmic reticulum membrane tethering Source: UniProtKB
- negative regulation of calcium ion export across plasma membrane Source: Ensembl
- negative regulation of high voltage-gated calcium channel activity Source: UniProtKB
- negative regulation of peptidyl-threonine phosphorylation Source: BHF-UCL
- negative regulation of ryanodine-sensitive calcium-release channel activity Source: UniProtKB
- organelle localization by membrane tethering Source: UniProtKB
- positive regulation of cyclic-nucleotide phosphodiesterase activity Source: BHF-UCL
- positive regulation of DNA binding 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 calcium-mediated signaling Source: Ensembl
- regulation of cardiac muscle cell action potential Source: UniProtKB
- 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 release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: BHF-UCL
- regulation of ryanodine-sensitive calcium-release channel activity Source: UniProtKB
- response to calcium ion Source: BHF-UCL
- substantia nigra development Source: UniProtKB
Keywordsi
Biological process | Host-virus interaction |
Ligand | Calcium, Metal-binding |
Enzyme and pathway databases
PathwayCommonsi | P0DP23 |
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-6802952, Signaling by BRAF and RAF1 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-9009391, Extra-nuclear estrogen signaling 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-9648002, RAS processing R-HSA-9649948, Signaling downstream of RAS mutants R-HSA-9656223, Signaling by RAF1 mutants R-HSA-9664323, FCGR3A-mediated IL10 synthesis R-HSA-983695, Antigen activates B Cell Receptor (BCR) leading to generation of second messengers |
SignaLinki | P0DP23 |
SIGNORi | P0DP23 |
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 |
VEuPathDBi | HostDB:ENSG00000198668 |
Subcellular locationi
Cytoskeleton
- spindle 1 Publication
- spindle pole 1 Publication
- centrosome 1 Publication
Other locations
- flagellum By similarity
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
Nucleus
- nucleoplasm Source: Reactome
- nucleus Source: UniProtKB
Plasma Membrane
- plasma membrane Source: UniProtKB
- voltage-gated potassium channel complex Source: Ensembl
Other locations
- calcium channel complex Source: BHF-UCL
- catalytic complex Source: CAFA
- cytoplasm Source: UniProtKB
- myelin sheath Source: Ensembl
- protein-containing complex Source: CAFA
- sarcomere Source: BHF-UCL
- vesicle Source: UniProtKB
Keywords - Cellular componenti
Cell projection, Cilium, Cytoplasm, Cytoskeleton, FlagellumPathology & Biotechi
Involvement in diseasei
Ventricular tachycardia, catecholaminergic polymorphic, 4 (CPVT4)4 Publications
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_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 KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane. 4 PublicationsCorresponds to variant dbSNP:rs267607277EnsemblClinVar. | 1 |
Long QT syndrome 14 (LQT14)8 Publications
Feature 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; decreased thermal stability in presence of calcium ions; decreased interaction with RYR2. 3 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 calcium; 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. 3 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_083814 | 141 | E → V in LQT14; loss-of-function variant causing impaired negative regulation of high voltage-gated calcium channel activity; impaired regulation of cardiac muscle cell action potential; decreased calcium ion binding. 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; impaired negative regulation of high voltage-gated calcium channel activity; impaired regulation of cardiac muscle cell action potential. 4 PublicationsCorresponds to variants dbSNP:rs1085307479 and dbSNP:rs199744595EnsemblClinVarEnsembl. | 1 |
Keywords - Diseasei
Disease variant, Long QT syndromeOrganism-specific databases
DisGeNETi | 801 805 808 |
GeneReviewsi | CALM1 |
MalaCardsi | CALM1 |
MIMi | 614916, phenotype 616247, phenotype |
OpenTargetsi | ENSG00000143933 ENSG00000160014 ENSG00000198668 |
Orphaneti | 3286, Catecholaminergic polymorphic ventricular tachycardia 101016, Romano-Ward syndrome |
Miscellaneous databases
Pharosi | P0DP23, Tclin |
Chemistry databases
ChEMBLi | CHEMBL6093 |
DrugBanki | DB08039, (3Z)-N,N-DIMETHYL-2-OXO-3-(4,5,6,7-TETRAHYDRO-1H-INDOL-2-YLMETHYLIDENE)-2,3-DIHYDRO-1H-INDOLE-5-SULFONAMIDE DB01429, Aprindine DB01244, Bepridil DB01373, Calcium DB11093, Calcium citrate DB13800, Calcium levulinate DB11348, Calcium Phosphate DB14481, Calcium phosphate dihydrate DB00477, Chlorpromazine DB00527, Cinchocaine DB02868, Deacetoxyvinzolidine DB01023, Felodipine DB04841, Flunarizine DB00623, Fluphenazine DB00753, Isoflurane DB00836, Loperamide DB01065, Melatonin DB08231, Myristic acid DB04513, N-(6-Aminohexyl)-5-Chloro-1-Naphthalenesulfonamide DB00622, Nicardipine DB01115, Nifedipine DB00850, Perphenazine DB00925, Phenoxybenzamine DB01100, Pimozide DB04825, Prenylamine DB01069, Promethazine DB03900, tert-butanol DB00831, Trifluoperazine DB03977, Trimethyllysine |
DrugCentrali | P0DP23 |
Genetic variation 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
Keywords - PTMi
Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugationProteomic databases
jPOSTi | P0DP23 |
MassIVEi | P0DP23 |
PeptideAtlasi | P0DP23 |
PTM databases
GlyGeni | P0DP23, 1 site, 1 O-linked glycan (1 site) |
iPTMneti | P0DP23 |
MetOSitei | P0DP23 |
PhosphoSitePlusi | P0DP23 |
Expressioni
Gene expression databases
ExpressionAtlasi | P0DP23, baseline and differential |
Organism-specific databases
HPAi | ENSG00000198668, Low tissue specificity |
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 in the proper assembly of a functional heterotetrameric M channel (PubMed:27564677).
Interacts with alpha-synuclein/SNCA (PubMed:23607618).
Interacts with SLC9A1 in a calcium-dependent manner (PubMed:30287853). In the absence of Ca(+2), interacts with GIMAP4 (via IQ domain) (By similarity).
Interacts with SCN8A; the interaction modulates the inactivation rate of SCN8A (By similarity). Interaction with KIF1A; the interaction is increased in presence of calcium and increases neuronal dense core vesicles motility (PubMed:30021165).
Interacts with KCNN3 (PubMed:31155282).
Interacts with KCNQ1 (via C-terminus); forms a heterooctameric structure (with 4:4 KCNQ1:CALM stoichiometry) in a calcium-independent manner (PubMed:18165683,PubMed:25441029).
Interacts with PIK3C3; the interaction modulates PIK3C3 kinase activity (PubMed:28890335).
Interacts with HINT1; interaction increases in the presence of calcium ions (By similarity).
Interacts with HINT3 (By similarity).
Interacts with GARIN2; in mature sperm flagella (By similarity).
By similarity27 Publications(Microbial infection) Interacts with Rubella virus protease/methyltransferase p150.
1 Publication(Microbial infection) Interacts with Legionella pneumophila glutamylase SidJ.
1 PublicationBinary interactionsi
P0DP23
With | #Exp. | IntAct |
---|---|---|
IDH1 [O75874] | 7 | EBI-25817233,EBI-715695 |
GO - Molecular functioni
- adenylate cyclase binding Source: CAFA
- calcium-dependent protein binding Source: Ensembl
- disordered domain specific binding Source: CAFA
- N-terminal myristoylation domain binding Source: UniProtKB
- protein domain specific binding Source: UniProtKB
- protein kinase binding Source: BHF-UCL
- titin binding Source: BHF-UCL
- transmembrane transporter binding Source: UniProtKB
Protein-protein interaction databases
IntActi | P0DP23, 5 interactors |
MINTi | P0DP23 |
STRINGi | 9606.ENSP00000272298 |
Chemistry databases
BindingDBi | P0DP23 |
Miscellaneous databases
RNActi | P0DP23, protein |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | P0DP23 |
SASBDBi | P0DP23 |
SMRi | P0DP23 |
ModBasei | Search... |
PDBe-KBi | 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 |
Domaini
Sequence similaritiesi
Keywords - Domaini
RepeatPhylogenomic databases
eggNOGi | KOG0027, Eukaryota |
OMAi | SCDRHPP |
OrthoDBi | 1386217at2759 |
Family and domain databases
CDDi | cd00051, EFh, 2 hits |
InterProi | View protein in InterPro IPR011992, EF-hand-dom_pair IPR018247, EF_Hand_1_Ca_BS IPR002048, EF_hand_dom |
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 11 potential isoforms that are computationally mapped.Show allAlign All
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 11 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketG3V226 | G3V226_HUMAN | Calmodulin | CALM1 | 76 | Annotation score: | ||
Q96HY3 | Q96HY3_HUMAN | CALM1 protein | CALM2 CALM1, CALM3, hCG_17033, hCG_20313 | 113 | Annotation score: | ||
G3V361 | G3V361_HUMAN | Calmodulin-1 | CALM1 | 98 | Annotation score: | ||
A0A590UJC0 | A0A590UJC0_HUMAN | Calmodulin-2 | CALM2 | 59 | Annotation score: | ||
A0A590UJI2 | A0A590UJI2_HUMAN | Calmodulin-2 | CALM2 | 104 | Annotation score: | ||
M0QZ52 | M0QZ52_HUMAN | Calmodulin 3 (Phosphorylase kinase,... | CALM3 hCG_20313 | 83 | Annotation score: | ||
E7EMB3 | E7EMB3_HUMAN | Calmodulin-2 | CALM2 | 196 | Annotation score: | ||
G3V479 | G3V479_HUMAN | Calmodulin-1 | CALM1 | 83 | Annotation score: | ||
F8WBR5 | F8WBR5_HUMAN | Calmodulin-2 | CALM2 | 65 | Annotation score: | ||
A0A590UJD7 | A0A590UJD7_HUMAN | Calmodulin-3 | CALM3 | 36 | Annotation score: | ||
There is more potential isoformShow all |
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; decreased thermal stability in presence of calcium ions; decreased interaction with RYR2. 3 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 KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane. 4 PublicationsCorresponds to variant dbSNP:rs267607277EnsemblClinVar. | 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 calcium; 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. 3 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_083814 | 141 | E → V in LQT14; loss-of-function variant causing impaired negative regulation of high voltage-gated calcium channel activity; impaired regulation of cardiac muscle cell action potential; decreased calcium ion binding. 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; impaired negative regulation of high voltage-gated calcium channel activity; impaired regulation of cardiac muscle cell action potential. 4 PublicationsCorresponds to variants dbSNP:rs1085307479 and dbSNP:rs199744595EnsemblClinVarEnsembl. | 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 |
Genome annotation databases
Ensembli | ENST00000356978.9; ENSP00000349467.4; ENSG00000198668.14 |
GeneIDi | 801 805 808 |
KEGGi | hsa:801 hsa:805 hsa:808 |
MANE-Selecti | ENST00000272298.12; ENSP00000272298.7; NM_001743.6; NP_001734.1 ENST00000291295.14; ENSP00000291295.8; NM_005184.4; NP_005175.2 ENST00000356978.9; ENSP00000349467.4; NM_006888.6; NP_008819.1 |
Similar 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 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
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 | [»] | |
3EVV | X-ray | 2.60 | A | 5-149 | [»] | |
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 | 25.00 | 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 | [»] | |
6BUT | NMR | - | A | 2-149 | [»] | |
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 | [»] | |
6EEB | X-ray | 1.96 | A | 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 | [»] | |
6HR1 | X-ray | 1.90 | A/B | 2-149 | [»] | |
6JI8 | electron microscopy | 3.60 | C/F/I/L | 1-149 | [»] | |
6JII | electron microscopy | 4.20 | C/F/I/L | 1-149 | [»] | |
6JIU | electron microscopy | 4.20 | C/F/I/L | 1-149 | [»] | |
6JIY | electron microscopy | 3.90 | C/F/I/L | 1-149 | [»] | |
6JRS | electron microscopy | 3.70 | C/F/I/L | 1-149 | [»] | |
6JV2 | electron microscopy | 4.40 | B/D/F/H | 1-149 | [»] | |
6K4K | X-ray | 2.71 | C/D | 1-149 | [»] | |
6K4L | X-ray | 2.95 | C/D | 1-149 | [»] | |
6K4R | X-ray | 3.11 | C/D | 1-149 | [»] | |
6M2W | electron microscopy | 3.80 | C/F/I/L | 1-149 | [»] | |
6M7H | X-ray | 1.60 | A | 2-148 | [»] | |
6MUD | X-ray | 2.69 | A | 1-149 | [»] | |
6MUE | X-ray | 1.90 | A | 1-149 | [»] | |
6N5W | X-ray | 2.15 | C | 1-149 | [»] | |
6O5G | X-ray | 1.89 | A | 1-149 | [»] | |
6OS4 | X-ray | 2.05 | A | 2-149 | [»] | |
6PAW | X-ray | 2.95 | C/D/G/H | 1-149 | [»] | |
6PBX | electron microscopy | 4.00 | B/D/F/H | 1-149 | [»] | |
6PBY | electron microscopy | 3.67 | B/D/F/H | 1-149 | [»] | |
6U39 | X-ray | 2.40 | A/C/E/G/I/K/M/O/Q/S | 2-149 | [»] | |
6U3A | X-ray | 1.65 | A/B | 2-149 | [»] | |
6U3B | X-ray | 1.70 | A | 2-149 | [»] | |
6U3D | X-ray | 1.75 | A/B | 2-149 | [»] | |
6UZZ | electron microscopy | 3.10 | B/D/F/H | 1-149 | [»] | |
6V00 | electron microscopy | 3.10 | B/E/H/K | 1-149 | [»] | |
6V01 | electron microscopy | 3.90 | B/E/H/K | 1-149 | [»] | |
6X32 | electron microscopy | 3.80 | C/F/I/L | 3-148 | [»] | |
6X33 | electron microscopy | 4.20 | C/F/I/L | 1-148 | [»] | |
6X35 | electron microscopy | 4.20 | C/F/I/L | 1-148 | [»] | |
6X36 | electron microscopy | 4.70 | C/F/I/L | 1-148 | [»] | |
6XXX | X-ray | 1.25 | AAA | 1-149 | [»] | |
6XY3 | X-ray | 2.00 | AAA | 1-149 | [»] | |
6XYR | X-ray | 2.08 | A | 2-149 | [»] | |
6Y4P | X-ray | 2.13 | A | 1-149 | [»] | |
6Y94 | NMR | - | A | 2-149 | [»] | |
6Y95 | NMR | - | A | 2-149 | [»] | |
6YNS | X-ray | 3.94 | A/B/C/D/E/F/G/H/I/J/K/L | 2-149 | [»] | |
6YNU | X-ray | 3.12 | A/C | 2-149 | [»] | |
6ZBI | NMR | - | A | 2-149 | [»] | |
7BF1 | X-ray | 1.24 | AAA | 1-149 | [»] | |
7BF2 | X-ray | 1.43 | AAA | 1-149 | [»] | |
7KL5 | X-ray | 1.65 | A | 1-149 | [»] | |
7SX3 | electron microscopy | 3.10 | C | 1-149 | [»] | |
7SX4 | electron microscopy | 3.50 | C | 1-149 | [»] | |
AlphaFoldDBi | P0DP23 | |||||
SASBDBi | P0DP23 | |||||
SMRi | P0DP23 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
IntActi | P0DP23, 5 interactors |
MINTi | P0DP23 |
STRINGi | 9606.ENSP00000272298 |
Chemistry databases
BindingDBi | P0DP23 |
ChEMBLi | CHEMBL6093 |
DrugBanki | DB08039, (3Z)-N,N-DIMETHYL-2-OXO-3-(4,5,6,7-TETRAHYDRO-1H-INDOL-2-YLMETHYLIDENE)-2,3-DIHYDRO-1H-INDOLE-5-SULFONAMIDE DB01429, Aprindine DB01244, Bepridil DB01373, Calcium DB11093, Calcium citrate DB13800, Calcium levulinate DB11348, Calcium Phosphate DB14481, Calcium phosphate dihydrate DB00477, Chlorpromazine DB00527, Cinchocaine DB02868, Deacetoxyvinzolidine DB01023, Felodipine DB04841, Flunarizine DB00623, Fluphenazine DB00753, Isoflurane DB00836, Loperamide DB01065, Melatonin DB08231, Myristic acid DB04513, N-(6-Aminohexyl)-5-Chloro-1-Naphthalenesulfonamide DB00622, Nicardipine DB01115, Nifedipine DB00850, Perphenazine DB00925, Phenoxybenzamine DB01100, Pimozide DB04825, Prenylamine DB01069, Promethazine DB03900, tert-butanol DB00831, Trifluoperazine DB03977, Trimethyllysine |
DrugCentrali | P0DP23 |
Protein family/group databases
MoonDBi | P0DP23, Predicted |
PTM databases
GlyGeni | P0DP23, 1 site, 1 O-linked glycan (1 site) |
iPTMneti | P0DP23 |
MetOSitei | P0DP23 |
PhosphoSitePlusi | P0DP23 |
Genetic variation databases
BioMutai | CALM1 |
Proteomic databases
jPOSTi | P0DP23 |
MassIVEi | P0DP23 |
PeptideAtlasi | P0DP23 |
Protocols and materials databases
Antibodypediai | 4344, 534 antibodies from 33 providers |
DNASUi | 801 |
Genome annotation databases
Ensembli | ENST00000356978.9; ENSP00000349467.4; ENSG00000198668.14 |
GeneIDi | 801 805 808 |
KEGGi | hsa:801 hsa:805 hsa:808 |
MANE-Selecti | ENST00000272298.12; ENSP00000272298.7; NM_001743.6; NP_001734.1 ENST00000291295.14; ENSP00000291295.8; NM_005184.4; NP_005175.2 ENST00000356978.9; ENSP00000349467.4; NM_006888.6; NP_008819.1 |
Organism-specific databases
CTDi | 801 805 808 |
DisGeNETi | 801 805 808 |
GeneCardsi | CALM1 |
GeneReviewsi | CALM1 |
HGNCi | HGNC:1442, CALM1 |
HPAi | ENSG00000198668, Low tissue specificity |
MalaCardsi | CALM1 |
MIMi | 114180, gene 614916, phenotype 616247, phenotype |
neXtProti | NX_P0DP23 |
OpenTargetsi | ENSG00000143933 ENSG00000160014 ENSG00000198668 |
Orphaneti | 3286, Catecholaminergic polymorphic ventricular tachycardia 101016, Romano-Ward syndrome |
VEuPathDBi | HostDB:ENSG00000198668 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG0027, Eukaryota |
OMAi | SCDRHPP |
OrthoDBi | 1386217at2759 |
Enzyme and pathway databases
PathwayCommonsi | P0DP23 |
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-6802952, Signaling by BRAF and RAF1 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-9009391, Extra-nuclear estrogen signaling 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-9648002, RAS processing R-HSA-9649948, Signaling downstream of RAS mutants R-HSA-9656223, Signaling by RAF1 mutants R-HSA-9664323, FCGR3A-mediated IL10 synthesis R-HSA-983695, Antigen activates B Cell Receptor (BCR) leading to generation of second messengers |
SignaLinki | P0DP23 |
SIGNORi | P0DP23 |
Miscellaneous databases
BioGRID-ORCSi | 801, 10 hits in 1080 CRISPR screens 805, 35 hits in 960 CRISPR screens 808, 45 hits in 1080 CRISPR screens |
ChiTaRSi | CALM1, human |
Pharosi | P0DP23, Tclin |
PROi | PR:P0DP23 |
RNActi | P0DP23, protein |
SOURCEi | Search... |
Gene expression databases
ExpressionAtlasi | P0DP23, baseline and differential |
Family and domain databases
CDDi | cd00051, EFh, 2 hits |
InterProi | View protein in InterPro IPR011992, EF-hand-dom_pair IPR018247, EF_Hand_1_Ca_BS IPR002048, EF_hand_dom |
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 |
MobiDBi | 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: | May 25, 2022 | |
This is version 42 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, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 14
Human chromosome 14: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families - Protein Spotlight
Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries