IED Industry Enzyme Database

Detail Information for IndEnz0002005860
IED ID IndEnz0002005860
Enzyme Type ID protease005860
Protein Name Calmodulin-1
Gene Name CALM1 CALM CAM CAM1
Organism Homo sapiens (Human)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Primates Haplorrhini Simiiformes Catarrhini Hominoidea (apes) Hominidae (great apes) Homininae Homo Homo sapiens (Human)
Enzyme Sequence MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK
Enzyme Length 149
Uniprot Accession Number P0DP23
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding CA_BIND 21..32; /note="1"; /evidence="ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03"; CA_BIND 57..68; /note="2"; /evidence="ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:25441029, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:4UMO, ECO:0007744|PDB:4V0C, ECO:0007744|PDB:5J03"; CA_BIND 94..105; /note="3"; /evidence="ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03"; CA_BIND 130..141; /note="4"; /evidence="ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03"
catalytic Activity
DNA Binding
EC Number
Enzyme Function FUNCTION: 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). {ECO:0000269|PubMed:16760425, ECO:0000269|PubMed:23893133, ECO:0000269|PubMed:26969752, ECO:0000269|PubMed:27165696, ECO:0000269|PubMed:28890335, ECO:0000269|PubMed:31454269}.; FUNCTION: (Microbial infection) Required for Legionella pneumophila SidJ glutamylase activity. {ECO:0000269|PubMed:31330532}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (7); Calcium binding (4); Chain (1); Cross-link (2); Domain (4); Helix (9); Initiator methionine (1); Modified residue (11); Natural variant (7); Region (1); Turn (1)
Keywords 3D-structure;Acetylation;Calcium;Cytoplasm;Cytoskeleton;Direct protein sequencing;Disease variant;Host-virus interaction;Isopeptide bond;Long QT syndrome;Metal-binding;Methylation;Phosphoprotein;Reference proteome;Repeat;Ubl conjugation
Interact With O75874
Induction
Subcellular Location SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:16760425}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:16760425}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843}. Note=Distributed throughout the cell during interphase, but during mitosis becomes dramatically localized to the spindle poles and the spindle microtubules.
Modified Residue MOD_RES 2; /note="N-acetylalanine"; /evidence="ECO:0000269|PubMed:7093203, ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"; MOD_RES 22; /note="N6-acetyllysine; alternate"; /evidence="ECO:0007744|PubMed:19608861"; MOD_RES 45; /note="Phosphothreonine; by CaMK4"; /evidence="ECO:0000250|UniProtKB:P0DP29"; MOD_RES 82; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:23186163"; MOD_RES 95; /note="N6-acetyllysine"; /evidence="ECO:0007744|PubMed:19608861"; MOD_RES 100; /note="Phosphotyrosine"; /evidence="ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332"; MOD_RES 102; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"; MOD_RES 111; /note="Phosphothreonine"; /evidence="ECO:0007744|PubMed:24275569"; MOD_RES 116; /note="N6,N6,N6-trimethyllysine; alternate"; /evidence="ECO:0000269|PubMed:7093203, ECO:0007744|PubMed:24129315"; MOD_RES 116; /note="N6-methyllysine; alternate"; /evidence="ECO:0007744|PubMed:24129315"; MOD_RES 139; /note="Phosphotyrosine"; /evidence="ECO:0007744|PubMed:19690332"
Post Translational Modification PTM: Ubiquitination results in a strongly decreased activity. {ECO:0000250}.; PTM: Phosphorylation results in a decreased activity. {ECO:0000250}.
Signal Peptide
Structure 3D NMR spectroscopy (41); Electron microscopy (26); X-ray crystallography (119)
Cross Reference PDB 1CDL; 1CLL; 1CTR; 1IWQ; 1J7O; 1J7P; 1K90; 1K93; 1L7Z; 1LVC; 1NKF; 1PK0; 1S26; 1SK6; 1SW8; 1UP5; 1WRZ; 1XFU; 1XFV; 1XFW; 1XFX; 1XFY; 1XFZ; 1Y6W; 1YR5; 1YRT; 1YRU; 1ZOT; 1ZUZ; 2BE6; 2F3Y; 2F3Z; 2HF5; 2I08; 2JZI; 2K0E; 2K0F; 2K0J; 2K61; 2KNE; 2KUG; 2KUH; 2L53; 2L7L; 2LGF; 2LL6; 2LL7; 2LQC; 2LQP; 2LV6; 2M0J; 2M0K; 2M55; 2MG5; 2N27; 2N6A; 2N77; 2N8J; 2R28; 2V01; 2V02; 2VAY; 2W73; 2WEL; 2X0G; 2Y4V; 3BYA; 3DVE; 3DVJ; 3DVK; 3DVM; 3EWT; 3EWV; 3G43; 3HR4; 3J41; 3O77; 3O78; 3OXQ; 3SUI; 3UCT; 3UCW; 3UCY; 4BW7; 4BW8; 4BYF; 4DCK; 4DJC; 4GOW; 4JPZ; 4JQ0; 4L79; 4LZX; 4M1L; 4OVN; 4Q57; 4Q5U; 4UMO; 4UPU; 4V0C; 5COC; 5DBR; 5DOW; 5DSU; 5GGM; 5I0I; 5J03; 5J8H; 5JQA; 5JTH; 5K7L; 5K8Q; 5OEO; 5TP5; 5TP6; 5V02; 5V03; 5V7X; 5WBX; 5WC5; 6B8L; 6B8M; 6B8N; 6B8P; 6B8Q; 6BUT; 6C1D; 6C1G; 6C1H; 6CNM; 6CNN; 6CNO; 6DAD; 6DAE; 6DAF; 6DAH; 6E2F; 6E2G; 6EEB; 6FEG; 6FEH; 6GDK; 6GDL; 6HCS; 6HR1; 6JI8; 6JII; 6JIU; 6JIY; 6JRS; 6JV2; 6K4K; 6K4L; 6K4R; 6M2W; 6M7H; 6MUD; 6MUE; 6N5W; 6O5G; 6OS4; 6PAW; 6PBX; 6PBY; 6U39; 6U3A; 6U3B; 6U3D; 6UZZ; 6V00; 6V01; 6X32; 6X33; 6X35; 6X36; 6XXX; 6XY3; 6XYR; 6Y4P; 6Y94; 6Y95; 6YNS; 6YNU; 6ZBI; 7BF1; 7BF2; 7KL5;
Mapped Pubmed ID 10075700; 10102820; 10205168; 10207003; 10373510; 10376602; 10376603; 10469573; 10487978; 10712905; 10777564; 10781589; 10830164; 10860980; 11015619; 11030334; 11032810; 11042191; 11231878; 11290418; 11325826; 11585916; 11879202; 11988487; 12015605; 12244094; 12406570; 12482967; 12551923; 12687004; 12727204; 12747803; 12799359; 12807427; 12821674; 12825073; 12930917; 12975316; 1309946; 13115432; 1317063; 1374913; 14500339; 14527397; 14551202; 14561760; 14594800; 14622581; 14627618; 14630798; 14765114; 14960328; 14978283; 15035987; 15063758; 15087444; 15100408; 15131111; 15147735; 15147738; 1519061; 15225611; 15229223; 15262966; 15272012; 15299715; 15316014; 15467163; 15476407; 15522886; 15550383; 15583004; 15591024; 15630448; 156362; 15710605; 15713486; 15746150; 15754088; 15817490; 15883051; 15899852; 15916532; 16013055; 16030015; 16043511; 16054096; 16084495; 16093354; 16120608; 16138079; 16154564; 16338416; 16359877; 16364920; 16508002; 16525015; 16545345; 16613843; 16880514; 16920709; 17018604; 17046689; 17097642; 17244649; 17473011; 17502104; 17569884; 17580302; 17603482; 17603483; 17654480; 17671360; 17687619; 17699613; 17765682; 17881003; 17884685; 17975119; 18001530; 18178620; 18182391; 18184567; 18184654; 18294816; 18296442; 18335582; 18384083; 18452398; 18462678; 18662992; 18773891; 18940010; 18940602; 18974108; 19001277; 19023099; 19034380; 19080622; 19133300; 19158341; 19225110; 19279214; 19317469; 19342380; 193860; 19404396; 19406745; 19467855; 19473981; 19584346; 19658100; 19667195; 19713936; 19851316; 19855925; 19913121; 19933846; 19968963; 19996092; 20052757; 20103772; 20130576; 20133723; 20141835; 20179705; 20198394; 20298697; 20379146; 20379614; 20388639; 20416930; 20418879; 20468064; 20526349; 20628086; 20668654; 20738160; 20802526; 20820846; 20953164; 20975703; 21047202; 21102635; 21124984; 21127070; 2114169; 21148297; 21170358; 21299499; 21360154; 21372320; 21424530; 21439835; 21555518; 21566136; 21640070; 21664913; 21730051; 21779496; 21817159; 21901608; 22002721; 22009783; 22009847; 22043453; 22044025; 22100452; 22163646; 22179043; 22295092; 22323446; 22331908; 22342729; 22451665; 22486744; 22510884; 22514276; 22518098; 22588125; 22592532; 22633975; 22705208; 22711531; 22721555; 22745804; 22767601; 22768143; 22801425; 22803592; 22826437; 22856685; 22877078; 22908308; 22908850; 22944912; 22971080; 2298749; 22996592; 23019329; 23109716; 23159936; 23178170; 2321095; 23235156; 23285036; 23300090; 23303910; 23315338; 23322042; 23352230; 23362265; 23437200; 23457304; 23552119; 23583981; 23624269; 23632248; 23658780; 23662433; 23680146; 23743201; 23760276; 23770565; 23770587; 23804213; 23831686; 23838429; 23967355; 23993095; 24032677; 24081810; 24088894; 24135138; 24202393; 24345920; 24374234; 24419375; 24420768; 24420770; 24469830; 24495081; 24530797; 24551838; 24636949; 24713697; 24725411; 24779925; 24787902; 24816216; 24907274; 24914971; 24917665; 24937142; 24957944; 25005783; 25101901; 25144868; 25145833; 25204415; 25232683; 25251320; 2526655; 25268113; 25303525; 2536303; 25370050; 25435214; 25470139; 25550383; 25703379; 2573431; 25751535; 25759176; 25907612; 25956027; 26001204; 26085527; 26148514; 26196381; 26214590; 26391397; 26421717; 26487174; 26494044; 26529318; 26559977; 26590425; 26618792; 26675311; 2667896; 26828872; 26858457; 26980593; 27009875; 27100291; 27129269; 27226555; 27325704; 27339229; 27374306; 27410739; 27499441; 27516594; 27563101; 27580874; 27632770; 2764880; 27696828; 27760856; 27787197; 27790916; 27791178; 27798963; 27815504; 27856935; 27927985; 27933776; 27956550; 28003368; 28045382; 28092099; 28121131; 28130124; 28174300; 28222617; 28288938; 28295264; 28335032; 28360104; 28422741; 28449373; 28462395; 28666118; 28823028; 28842480; 28849027; 28976808; 28978262; 29089333; 29214998; 29240297; 29247668; 29298900; 29311131; 29358376; 29409956; 29429937; 29463698; 29463791; 29494137; 29505720; 2953725; 29576321; 29584409; 29606593; 29663486; 29713907; 29724949; 29880196; 29932249; 29934532; 30013092; 30053538; 30116787; 30142967; 30200150; 30279205; 30317608; 30348784; 30354306; 30474048; 30639287; 3079756; 30808708; 30877334; 30928430; 31072926; 31140879; 31230402; 31278385; 31330531; 31337679; 31401388; 31483676; 31490124; 31682223; 31724397; 31763755; 31883792; 31914408; 31983428; 31991573; 32012279; 32186935; 32234958; 32317284; 32554053; 32807966; 32948286; 33080786; 33191766; 33321095; 33338532; 33547325; 33634591; 33655882; 33754699; 33770503; 33788723; 33890716; 33951696; 33977052; 34021086; 34235492; 34533024; 34572507; 34575961; 34587504; 34888671; 3722161; 3780718; 3839510; 5461220; 6328915; 6330098; 7407067; 7479966; 7525588; 7526403; 7526779; 7542586; 7545680; 7588753; 7637786; 7641687; 7657645; 7678445; 7702581; 7708705; 7847371; 7889407; 7901336; 7929371; 8021246; 8385275; 8397339; 8576111; 8625412; 8631904; 8684469; 8702940; 8756646; 8782602; 8782898; 8799126; 8809036; 8876196; 8896567; 8910504; 9009191; 9020159; 9106655; 9173876; 9188442; 9197267; 9199170; 9234708; 9312192; 9368021; 9395096; 9405465; 9442023; 9515967; 9580552; 9625352; 9648857; 9694809; 9727000; 9753452; 9822657; 9823899; 9875237;
Motif
Gene Encoded By
Mass 16,838
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda