USC-OGP 2-DE database Two-dimensional polyacrylamide gel electrophoresis database

USC-OGP 2-DE database  Search by                Maps             Select Remote Interfaces [All Interfaces] SWISS-2DPAGE World-2DPAGE Portal World-2DPAGE Repository Exclude local DBs has only effect if a remote interface is selected

Searching in 'USC-OGP 2-DE database' for entry matching: CALM_HUMAN USC-OGP 2-DE database:  CALM_HUMAN CALM_HUMAN General information about the entry View entry in simple text format Entry name CALM_HUMAN Primary accession number P62158 Secondary accession number(s) P02593 integrated into USC-OGP 2-DE database on  January 17, 2017 (release 1) 2D Annotations were last modified on January 17, 2017 (version 1) General Annotations were last modified on  April 5, 2017 (version 2) Name and origin of the protein Description RecName: Full=Calmodulin; Short=CaM;. Gene name Name=CALM1 Synonyms=CALM, CAM, CAM1    and Name=CALM2 Synonyms=CAM2, CAMB    and Name=CALM3 Synonyms=CALML2, CAM3, CAMC, CAMIII Annotated species Homo sapiens (Human) [TaxID: 9606] Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. References [1]   2D GEL CHARACTERIZATION Author 1., Author 2. Submitted (Mar-2011) to Current 2D PAGE maps for identified proteins How to interpret a protein PLATELET_4-5 {PLATELET 4-5} Homo sapiens (Human)   map experimental info   PLATELET_4-5 MAP LOCATIONS: SPOT OGP-0245: pI=4.45; Mw=17550 Cross-references UniProtKB/Swiss-Prot P62158; CALM_HUMAN. 2D PAGE maps for identified proteins How to interpret a protein map You may obtain an estimated location of the protein on various 2D PAGE maps, provided the whole amino acid sequence is known. The estimation is obtained according to the computed protein's pI and Mw. Warning 1: the displayed region reflects an area around the theoretical pI and molecular weight of the protein and is only provided for the user's information. It should be used with caution, as the experimental and theoretical positions of a protein may differ significantly. Warning 2: the 2D PAGE map is built on demand. This may take some few seconds to be computed. External data extracted from UniProtKB/Swiss-Prot Extracted from UniProtKB/Swiss-Prot, release: 0.0 Entry name CALM_HUMAN Primary accession number P62158 Secondary accession number(s) P02593 P70667 P99014 Q13942 Q53S29 Q61379 Q61380 Q96HK3 Sequence was last modified on  January 23, 2007 (version 2) Annotations were last modified on  March 15, 2017 (version 171) Name and origin of the protein Description RecName: Full=Calmodulin; Short=CaM; Gene name Name=CALM1 Synonyms=CALM, CAM, CAM1    and Name=CALM2 Synonyms=CAM2, CAMB    and Name=CALM3 Synonyms=CALML2, CAM3, CAMC, CAMIII Encoded on Name=CALM1; Synonyms=CALM, CAM, CAM1; and Name=CALM2; Synonyms=CAM2, CAMB; and Name=CALM3; Synonyms=CALML2, CAM3, CAMC, CAMIII Keywords 3D-structure; Acetylation; Calcium; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Disease mutation; Isopeptide bond; Long QT syndrome; Metal-binding; Methylation; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Ubl conjugation. Copyright Copyrighted by the UniProt Consortium, see http://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License Cross-references EMBL J04046; AAA51918.1; -; mRNA EMBL M19311; AAA35641.1; -; mRNA EMBL M27319; AAA35635.1; -; mRNA EMBL X52606; CAA36839.1; ALT_SEQ; Genomic_DNA EMBL X52607; CAA36839.1; JOINED; Genomic_DNA EMBL X52608; CAA36839.1; JOINED; Genomic_DNA EMBL U12022; AAB60644.1; -; Genomic_DNA EMBL U11886; AAB60644.1; JOINED; Genomic_DNA EMBL D45887; BAA08302.1; -; mRNA EMBL U94728; AAC83174.1; -; Genomic_DNA EMBL U94725; AAC83174.1; JOINED; Genomic_DNA EMBL U94726; AAC83174.1; JOINED; Genomic_DNA EMBL BT006818; AAP35464.1; -; mRNA EMBL BT006855; AAP35501.1; -; mRNA EMBL BT009916; AAP88918.1; -; mRNA EMBL CR541990; CAG46787.1; -; mRNA EMBL CR542021; CAG46818.1; -; mRNA EMBL AC006536; AAD45181.1; -; Genomic_DNA EMBL AC073283; AAY24085.1; -; Genomic_DNA EMBL BC000454; AAH00454.1; -; mRNA EMBL BC003354; AAH03354.1; -; mRNA EMBL BC005137; AAH05137.1; -; mRNA EMBL BC006464; AAH06464.1; -; mRNA EMBL BC008437; AAH08437.1; -; mRNA EMBL BC008597; AAH08597.1; -; mRNA EMBL BC011834; AAH11834.1; -; mRNA EMBL BC017385; AAH17385.1; -; mRNA EMBL BC018677; AAH18677.1; -; mRNA EMBL BC026065; AAH26065.1; -; mRNA EMBL BC047523; -; NOT_ANNOTATED_CDS; mRNA CCDS CCDS1832.1; -; . CCDS CCDS33061.1; -; . CCDS CCDS9892.1; -; . PIR S48728; MCHU; . RefSeq NP_001292553.1; NM_001305624.1; . RefSeq NP_001292554.1; NM_001305625.1; . RefSeq NP_001292555.1; NM_001305626.1; . RefSeq NP_001316851.1; NM_001329922.1; . RefSeq NP_001316852.1; NM_001329923.1; . RefSeq NP_001316853.1; NM_001329924.1; . RefSeq NP_001316854.1; NM_001329925.1; . RefSeq NP_001316855.1; NM_001329926.1; . RefSeq NP_001734.1; NM_001743.5; . RefSeq NP_005175.2; NM_005184.3; . RefSeq NP_008819.1; NM_006888.4; . UniGene Hs.282410; -; . UniGene Hs.468442; -; . UniGene Hs.515487; -; . PDB 1AJI; Model; -; A=5-148 PDB 1CDL; X-ray; 2.00 A; A/B/C/D=2-148 PDB 1CLL; X-ray; 1.70 A; A=2-149 PDB 1CTR; X-ray; 2.45 A; A=2-149 PDB 1IWQ; X-ray; 2.00 A; A=2-149 PDB 1J7O; NMR; -; A=2-77 PDB 1J7P; NMR; -; A=83-149 PDB 1K90; X-ray; 2.75 A; D/E/F=2-149 PDB 1K93; X-ray; 2.95 A; D/E/F=6-149 PDB 1L7Z; X-ray; 2.30 A; A=2-149 PDB 1LVC; X-ray; 3.60 A; D/E/F=1-149 PDB 1NKF; NMR; -; A=99-105 PDB 1PK0; X-ray; 3.30 A; D/E/F=2-148 PDB 1S26; X-ray; 3.00 A; D/E/F=2-149 PDB 1SK6; X-ray; 3.20 A; D/E/F=2-149 PDB 1SW8; NMR; -; A=2-80 PDB 1WRZ; X-ray; 2.00 A; A=1-149 PDB 1XFU; X-ray; 3.35 A; O/P/Q/R/S/T=1-149 PDB 1XFV; X-ray; 3.35 A; O/P/Q/R/S/T=1-149 PDB 1XFW; X-ray; 3.40 A; O/P/Q/R/S/T=1-149 PDB 1XFX; X-ray; 3.20 A; O/P/Q/R/S/T=1-149 PDB 1XFY; X-ray; 3.30 A; O/P/Q/R/S/T=1-149 PDB 1XFZ; X-ray; 3.25 A; O/P/Q/R/S/T=1-149 PDB 1Y6W; X-ray; 2.40 A; A=2-149 PDB 1YR5; X-ray; 1.70 A; A=2-149 PDB 1YRT; X-ray; 2.10 A; B=76-149 PDB 1YRU; X-ray; 2.50 A; B=76-149 PDB 1ZOT; X-ray; 2.20 A; B=80-148 PDB 1ZUZ; X-ray; 1.91 A; A=1-149 PDB 2BE6; X-ray; 2.00 A; A/B/C=1-149 PDB 2F3Y; X-ray; 1.45 A; A=2-149 PDB 2F3Z; X-ray; 1.60 A; A=2-149 PDB 2HF5; NMR; -; A=47-114 PDB 2I08; X-ray; 2.00 A; A=3-79 PDB 2JZI; NMR; -; A=2-149 PDB 2K0E; NMR; -; A=2-149 PDB 2K0F; NMR; -; A=2-149 PDB 2K0J; NMR; -; A=3-149 PDB 2K61; NMR; -; A=2-149 PDB 2KNE; NMR; -; A=2-149 PDB 2KUG; NMR; -; A=2-77 PDB 2KUH; NMR; -; A=83-149 PDB 2L53; NMR; -; A=2-149 PDB 2L7L; NMR; -; A=2-149 PDB 2LGF; NMR; -; A=3-149 PDB 2LL6; NMR; -; A=2-149 PDB 2LL7; NMR; -; A=2-149 PDB 2LQC; NMR; -; A=2-78 PDB 2LQP; NMR; -; A=79-149 PDB 2LV6; Other; -; A=2-149 PDB 2M0J; NMR; -; A=2-149 PDB 2M0K; NMR; -; A=2-149 PDB 2M55; NMR; -; A=2-149 PDB 2MG5; NMR; -; A=2-149 PDB 2N27; NMR; -; A=2-149 PDB 2N6A; NMR; -; A=6-147 PDB 2N77; NMR; -; A=77-149 PDB 2N8J; NMR; -; A=2-149 PDB 2R28; X-ray; 1.86 A; A/B=1-149 PDB 2V01; X-ray; 2.15 A; A=2-149 PDB 2V02; X-ray; 2.20 A; A=2-149 PDB 2VAY; X-ray; 1.94 A; A=4-149 PDB 2W73; X-ray; 1.45 A; A/B/E/F=1-149 PDB 2WEL; X-ray; 1.90 A; D=1-149 PDB 2X0G; X-ray; 2.20 A; B=2-149 PDB 2Y4V; X-ray; 1.80 A; A=1-149 PDB 3BYA; X-ray; 1.85 A; A=2-149 PDB 3DVE; X-ray; 2.35 A; A=2-149 PDB 3DVJ; X-ray; 2.80 A; A=2-149 PDB 3DVK; X-ray; 2.30 A; A=2-149 PDB 3DVM; X-ray; 2.60 A; A=2-149 PDB 3EWT; X-ray; 2.40 A; A=2-149 PDB 3EWV; X-ray; 2.60 A; A=2-149 PDB 3G43; X-ray; 2.10 A; A/B/C/D=2-149 PDB 3HR4; X-ray; 2.50 A; B/D/F/H=1-149 PDB 3J41; EM; 25.0 A; E/F=1-149 PDB 3O77; X-ray; 2.35 A; A=1-149 PDB 3O78; X-ray; 2.60 A; A/B=1-149 PDB 3OXQ; X-ray; 2.55 A; A/B/C/D=1-149 PDB 3SUI; X-ray; 1.95 A; A=1-149 PDB 3UCT; X-ray; 1.90 A; A/B=2-80 PDB 3UCW; X-ray; 1.76 A; A/B/C/D=2-80 PDB 3UCY; X-ray; 1.80 A; A=2-80 PDB 4BW7; X-ray; 1.81 A; A/C=1-149 PDB 4BW8; X-ray; 1.80 A; A/B=1-149 PDB 4BYF; X-ray; 2.74 A; B/D=1-149 PDB 4DCK; X-ray; 2.20 A; B=1-149 PDB 4DJC; X-ray; 1.35 A; A=1-149 PDB 4GOW; X-ray; 2.60 A; D=4-147 PDB 4JPZ; X-ray; 3.02 A; C/I=1-149 PDB 4JQ0; X-ray; 3.84 A; C=1-149 PDB 4L79; X-ray; 2.30 A; B=1-149 PDB 4LZX; X-ray; 1.50 A; A=2-149 PDB 4M1L; X-ray; 2.10 A; A=2-149 PDB 4OVN; X-ray; 2.80 A; A/B/C/D/E=1-149 PDB 4Q57; X-ray; 1.80 A; A=10-74 PDB 4Q5U; X-ray; 1.95 A; A=1-149 PDB 4UMO; X-ray; 3.00 A; C/D=1-149 PDB 4UPU; X-ray; 2.34 A; A=2-149 PDB 4V0C; X-ray; 2.86 A; C/D=1-149 PDB 5COC; X-ray; 2.67 A; A=5-78 PDB 5DOW; X-ray; 1.70 A; A/C/E/G=2-149 PDB 5DSU; X-ray; 1.93 A; A=3-78 PDB 5GGM; NMR; -; A=2-149 PDB 5I0I; X-ray; 3.15 A; C/E=3-147 G=84-126 I=84-147; PDB; 5J03; X-ray 2.00 A B=1-149; PDB; 5J8H; NMR - A=2-149; PDB; 5K7L; EM 3.78 A B=1-149; PDB; 5K8Q; X-ray 1.74 A A=1-149; PDBsum; 1AJI; - PDBsum 1CDL; -; . PDBsum 1CLL; -; . PDBsum 1CTR; -; . PDBsum 1IWQ; -; . PDBsum 1J7O; -; . PDBsum 1J7P; -; . PDBsum 1K90; -; . PDBsum 1K93; -; . PDBsum 1L7Z; -; . PDBsum 1LVC; -; . PDBsum 1NKF; -; . PDBsum 1PK0; -; . PDBsum 1S26; -; . PDBsum 1SK6; -; . PDBsum 1SW8; -; . PDBsum 1WRZ; -; . PDBsum 1XFU; -; . PDBsum 1XFV; -; . PDBsum 1XFW; -; . PDBsum 1XFX; -; . PDBsum 1XFY; -; . PDBsum 1XFZ; -; . PDBsum 1Y6W; -; . PDBsum 1YR5; -; . PDBsum 1YRT; -; . PDBsum 1YRU; -; . PDBsum 1ZOT; -; . PDBsum 1ZUZ; -; . PDBsum 2BE6; -; . PDBsum 2F3Y; -; . PDBsum 2F3Z; -; . PDBsum 2HF5; -; . PDBsum 2I08; -; . PDBsum 2JZI; -; . PDBsum 2K0E; -; . PDBsum 2K0F; -; . PDBsum 2K0J; -; . PDBsum 2K61; -; . PDBsum 2KNE; -; . PDBsum 2KUG; -; . PDBsum 2KUH; -; . PDBsum 2L53; -; . PDBsum 2L7L; -; . PDBsum 2LGF; -; . PDBsum 2LL6; -; . PDBsum 2LL7; -; . PDBsum 2LQC; -; . PDBsum 2LQP; -; . PDBsum 2LV6; -; . PDBsum 2M0J; -; . PDBsum 2M0K; -; . PDBsum 2M55; -; . PDBsum 2MG5; -; . PDBsum 2N27; -; . PDBsum 2N6A; -; . PDBsum 2N77; -; . PDBsum 2N8J; -; . PDBsum 2R28; -; . PDBsum 2V01; -; . PDBsum 2V02; -; . PDBsum 2VAY; -; . PDBsum 2W73; -; . PDBsum 2WEL; -; . PDBsum 2X0G; -; . PDBsum 2Y4V; -; . PDBsum 3BYA; -; . PDBsum 3DVE; -; . PDBsum 3DVJ; -; . PDBsum 3DVK; -; . PDBsum 3DVM; -; . PDBsum 3EWT; -; . PDBsum 3EWV; -; . PDBsum 3G43; -; . PDBsum 3HR4; -; . PDBsum 3J41; -; . PDBsum 3O77; -; . PDBsum 3O78; -; . PDBsum 3OXQ; -; . PDBsum 3SUI; -; . PDBsum 3UCT; -; . PDBsum 3UCW; -; . PDBsum 3UCY; -; . PDBsum 4BW7; -; . PDBsum 4BW8; -; . PDBsum 4BYF; -; . PDBsum 4DCK; -; . PDBsum 4DJC; -; . PDBsum 4GOW; -; . PDBsum 4JPZ; -; . PDBsum 4JQ0; -; . PDBsum 4L79; -; . PDBsum 4LZX; -; . PDBsum 4M1L; -; . PDBsum 4OVN; -; . PDBsum 4Q57; -; . PDBsum 4Q5U; -; . PDBsum 4UMO; -; . PDBsum 4UPU; -; . PDBsum 4V0C; -; . PDBsum 5COC; -; . PDBsum 5DOW; -; . PDBsum 5DSU; -; . PDBsum 5GGM; -; . PDBsum 5I0I; -; . PDBsum 5J03; -; . PDBsum 5J8H; -; . PDBsum 5K7L; -; . PDBsum 5K8Q; -; . ProteinModelPortal P62158; -; . SMR P62158; -; . BioGrid 107252; 399; . BioGrid 107256; 38; . BioGrid 107259; 32; . DIP DIP-31794N; -; . IntAct P62158; 248; . MINT MINT-4999725; -; . STRING 9606.ENSP00000349467; -; . BindingDB P62158; -; . ChEMBL CHEMBL6093; -; . DrugBank DB03900; 2-Methyl-2-Propanol; . DrugBank DB01429; Aprindine; . DrugBank DB01244; Bepridil; . DrugBank DB01373; Calcium; . DrugBank DB00477; Chlorpromazine; . DrugBank DB00527; Cinchocaine; . DrugBank DB01023; Felodipine; . DrugBank DB04841; Flunarizine; . DrugBank DB00623; Fluphenazine; . DrugBank DB00753; Isoflurane; . DrugBank DB00836; Loperamide; . DrugBank DB01065; Melatonin; . DrugBank DB08231; MYRISTIC ACID; . DrugBank DB04513; N-(6-Aminohexyl)-5-Chloro-1-Naphthalenesulfonamide; . DrugBank DB03977; N-Trimethyllysine; . DrugBank DB00622; Nicardipine; . DrugBank DB01115; Nifedipine; . DrugBank DB00850; Perphenazine; . DrugBank DB00925; Phenoxybenzamine; . DrugBank DB01100; Pimozide; . DrugBank DB04825; Prenylamine; . DrugBank DB01069; Promethazine; . DrugBank DB00831; Trifluoperazine; . TCDB 8.A.82.1.1; the calmodulin calcium binding protein (calmodulin) family; . iPTMnet P62158; -; . PhosphoSitePlus P62158; -; . BioMuta CALM1; -; . DMDM 49037474; -; . DOSAC-COBS-2DPAGE P62158; -; . OGP P02593; -; . SWISS-2DPAGE P62158; -; . EPD P62158; -; . MaxQB P62158; -; . PaxDb P62158; -; . PeptideAtlas P62158; -; . PRIDE P62158; -; . TopDownProteomics P62158; -; . DNASU 801; -; . DNASU 805; -; . DNASU 808; -; . Ensembl ENST00000272298; ENSP00000272298; ENSG00000143933; . Ensembl ENST00000291295; ENSP00000291295; ENSG00000160014; . Ensembl ENST00000356978; ENSP00000349467; ENSG00000198668; . Ensembl ENST00000596362; ENSP00000472141; ENSG00000160014; . GeneID 801; -; . GeneID 805; -; . GeneID 808; -; . KEGG hsa:801; -; . KEGG hsa:805; -; . KEGG hsa:808; -; . UCSC uc001xyl.3; human; . CTD 801; -; . CTD 805; -; . CTD 808; -; . DisGeNET 801; -; . DisGeNET 805; -; . DisGeNET 808; -; . GeneCards CALM1; -; . GeneCards CALM2; -; . GeneCards CALM3; -; . GeneReviews CALM1; -; . HGNC HGNC:1442; CALM1; . HGNC HGNC:1445; CALM2; . HGNC HGNC:1449; CALM3; . HPA CAB007790; -; . HPA CAB018558; -; . HPA HPA044999; -; . MalaCards CALM1; -; . MalaCards CALM2; -; . MalaCards CALM3; -; . MIM 114180; gene; . MIM 114182; gene; . MIM 114183; gene; . MIM 614916; phenotype; . MIM 616247; phenotype; . MIM 616249; phenotype; . neXtProt NX_P62158; -; . OpenTargets ENSG00000143933; -; . OpenTargets ENSG00000160014; -; . OpenTargets ENSG00000198668; -; . Orphanet 3286; Catecholaminergic polymorphic ventricular tachycardia; . PharmGKB PA26042; -; . eggNOG KOG0027; Eukaryota; . eggNOG COG5126; LUCA; . GeneTree ENSGT00760000118901; -; . HOVERGEN HBG012180; -; . InParanoid P62158; -; . KO K02183; -; . OMA HRISGKA; -; . OrthoDB EOG091G0V73; -; . PhylomeDB P62158; -; . TreeFam TF300912; -; . BioCyc MetaCyc:ENSG00000143933-MONOMER; -; . Reactome R-HSA-111932; CaMK IV-mediated phosphorylation of CREB; . Reactome R-HSA-111933; Calmodulin induced events; . Reactome R-HSA-111957; Cam-PDE 1 activation; . Reactome R-HSA-111997; CaM pathway; . Reactome R-HSA-114608; Platelet degranulation; . Reactome R-HSA-1445148; Translocation of GLUT4 to the plasma membrane; . Reactome R-HSA-1474151; Tetrahydrobiopterin (BH4) synthesis; recycling; salvage and regulation Reactome R-HSA-163615; PKA activation; . Reactome R-HSA-180024; DARPP-32 events; . Reactome R-HSA-1855204; Synthesis of IP3 and IP4 in the cytosol; . Reactome R-HSA-203615; eNOS activation; . Reactome R-HSA-2514859; Inactivation; recovery and regulation of the phototransduction cascade; . Reactome R-HSA-2672351; Stimuli-sensing channels; . Reactome R-HSA-2871809; FCERI mediated Ca+2 mobilization; . Reactome R-HSA-4086398; Ca2+ pathway; . Reactome R-HSA-418359; Reduction of cytosolic Ca++ levels; . Reactome R-HSA-425561; Sodium/Calcium exchangers; . Reactome R-HSA-442717; CREB phosphorylation through the activation of CaMKK; . Reactome R-HSA-442729; CREB phosphorylation through the activation of CaMKII; . Reactome R-HSA-442745; Activation of CaMK IV; . Reactome R-HSA-442982; Ras activation uopn Ca2+ infux through NMDA receptor; . Reactome R-HSA-445355; Smooth Muscle Contraction; . Reactome R-HSA-451308; Activation of Ca-permeable Kainate Receptor; . Reactome R-HSA-5210891; Uptake and function of anthrax toxins; . Reactome R-HSA-5218920; VEGFR2 mediated vascular permeability; . Reactome R-HSA-5218921; VEGFR2 mediated cell proliferation; . Reactome R-HSA-5576892; Phase 0 - rapid depolarisation; . Reactome R-HSA-5578775; Ion homeostasis; . Reactome R-HSA-5607763; CLEC7A (Dectin-1) induces NFAT activation; . Reactome R-HSA-5626467; RHO GTPases activate IQGAPs; . Reactome R-HSA-5627123; RHO GTPases activate PAKs; . Reactome R-HSA-5673001; RAF/MAP kinase cascade; . Reactome R-HSA-70221; Glycogen breakdown (glycogenolysis); . Reactome R-HSA-8876725; Protein methylation; . Reactome R-HSA-936837; Ion transport by P-type ATPases; . Reactome R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers; . SIGNOR P62158; -; . ChiTaRS CALM1; human; . ChiTaRS CALM3; human; . EvolutionaryTrace P62158; -; . GeneWiki CALM2; -; . GeneWiki CALM3; -; . GeneWiki Calmodulin_1; -; . PRO PR:P62158; -; . Proteomes UP000005640; Chromosome 14; . Proteomes UP000005640; Chromosome 19; . Proteomes UP000005640; Chromosome 2; . Bgee ENSG00000143933; -; . CleanEx HS_CALM1; -; . CleanEx HS_CALM2; -; . ExpressionAtlas P62158; baseline and differential; . Genevisible P62158; HS; . GO GO:0005813; C:centrosome; IDA:UniProtKB; . GO GO:0005737; C:cytoplasm; TAS:UniProtKB; . GO GO:0005829; C:cytosol; TAS:Reactome; . GO GO:0070062; C:extracellular exosome; IDA:UniProtKB; . GO GO:0005576; C:extracellular region; TAS:Reactome; . GO GO:0030426; C:growth cone; IEA:Ensembl; . GO GO:0005654; C:nucleoplasm; TAS:Reactome; . GO GO:0005634; C:nucleus; IDA:UniProtKB; . GO GO:0005886; C:plasma membrane; TAS:UniProtKB; . GO GO:0014069; C:postsynaptic density; IEA:Ensembl; . GO GO:0030017; C:sarcomere; IDA:BHF-UCL; . GO GO:0005876; C:spindle microtubule; IDA:UniProtKB; . GO GO:0000922; C:spindle pole; IDA:UniProtKB; . GO GO:0031982; C:vesicle; IDA:UniProtKB; . GO GO:0008076; C:voltage-gated potassium channel complex; IEA:Ensembl; . GO GO:0005509; F:calcium ion binding; IDA:BHF-UCL; . GO GO:0008440; F:inositol-1; 4; 5-trisphosphate 3-kinase activity TAS:Reactome . GO GO:0044325; F:ion channel binding; IPI:BHF-UCL; . GO GO:0015276; F:ligand-gated ion channel activity; TAS:Reactome; . GO GO:0031997; F:N-terminal myristoylation domain binding; IPI:UniProtKB; . GO GO:0030235; F:nitric-oxide synthase regulator activity; IEA:Ensembl; . GO GO:0043274; F:phospholipase binding; IPI:BHF-UCL; . GO GO:0019904; F:protein domain specific binding; IPI:UniProtKB; . GO GO:0019901; F:protein kinase binding; IPI:BHF-UCL; . GO GO:0072542; F:protein phosphatase activator activity; IDA:BHF-UCL; . GO GO:0043539; F:protein serine/threonine kinase activator activity; TAS:BHF-UCL; . GO GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; TAS:Reactome; . GO GO:0031996; F:thioesterase binding; IPI:UniProtKB; . GO GO:0031432; F:titin binding; IPI:BHF-UCL; . GO GO:0007190; P:activation of adenylate cyclase activity; IEA:Ensembl; . GO GO:0005513; P:detection of calcium ion; IMP:BHF-UCL; . GO GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome; . GO GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:UniProtKB; . GO GO:0000086; P:G2/M transition of mitotic cell cycle; IEA:Ensembl; . GO GO:0005980; P:glycogen catabolic process; TAS:Reactome; . GO GO:0043647; P:inositol phosphate metabolic process; TAS:Reactome; . GO GO:0000165; P:MAPK cascade; TAS:Reactome; . GO GO:0006936; P:muscle contraction; TAS:Reactome; . GO GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; TAS:BHF-UCL; . GO GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; ISS:BHF-UCL; . GO GO:0002576; P:platelet degranulation; TAS:Reactome; . GO GO:0030801; P:positive regulation of cyclic nucleotide metabolic process; IDA:BHF-UCL; . GO GO:0051343; P:positive regulation of cyclic-nucleotide phosphodiesterase activity; IDA:BHF-UCL; . GO GO:0043388; P:positive regulation of DNA binding; IEA:Ensembl; . GO GO:0051000; P:positive regulation of nitric-oxide synthase activity; IEA:Ensembl; . GO GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; TAS:BHF-UCL; . GO GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; IDA:BHF-UCL; . GO GO:0031954; P:positive regulation of protein autophosphorylation; TAS:BHF-UCL; . GO GO:0035307; P:positive regulation of protein dephosphorylation; IDA:BHF-UCL; . GO GO:0071902; P:positive regulation of protein serine/threonine kinase activity; TAS:BHF-UCL; . GO GO:0060316; P:positive regulation of ryanodine-sensitive calcium-release channel activity; IDA:BHF-UCL; . GO GO:0006479; P:protein methylation; TAS:Reactome; . GO GO:0055117; P:regulation of cardiac muscle contraction; IMP:BHF-UCL; . GO GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; IC:BHF-UCL; . GO GO:1901844; P:regulation of cell communication by electrical coupling involved in cardiac conduction; IC:BHF-UCL; . GO GO:0032465; P:regulation of cytokinesis; IMP:UniProtKB; . GO GO:0002027; P:regulation of heart rate; IMP:BHF-UCL; . GO GO:1901841; P:regulation of high voltage-gated calcium channel activity; IEA:Ensembl; . GO GO:0050999; P:regulation of nitric-oxide synthase activity; TAS:Reactome; . GO GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IDA:BHF-UCL; . GO GO:0022400; P:regulation of rhodopsin mediated signaling pathway; TAS:Reactome; . GO GO:0001975; P:response to amphetamine; IEA:Ensembl; . GO GO:0051592; P:response to calcium ion; IDA:BHF-UCL; . GO GO:0051412; P:response to corticosterone; IEA:Ensembl; . GO GO:0021762; P:substantia nigra development; IEP:UniProtKB; . GO GO:0007223; P:Wnt signaling pathway; calcium modulating pathway; TAS:Reactome CDD cd00051; EFh; 2; . Gene3D 1.10.238.10; -; 2; . InterPro IPR011992; EF-hand-dom_pair; . InterPro IPR018247; EF_Hand_1_Ca_BS; . InterPro IPR002048; EF_hand_dom; . Pfam PF13499; EF-hand_7; 2; . SMART SM00054; EFh; 4; . SUPFAM SSF47473; SSF47473; 1; . PROSITE PS00018; EF_HAND_1; 4; . PROSITE PS50222; EF_HAND_2; 4; .

Gateways to other related servers

• The World-2DPAGE Constellation - Entry point to the world-wide 2-DPAGE resources.
• World-2DPAGE Repository - A public repository for gel-based proteomics data linked to protein identification published in the literature.
• World-2DPAGE Portal - A dynamic portal to query simultaneously world-wide gel-based proteomics databases.
• SWISS-2DPAGE - The Geneva Two-dimensional polyacrylamide gel electrophoresis database.
• ExPASy - The resources web server of the Swiss Institute of Bioinformatics

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