| IED ID |
IndEnz0002018926 |
| Enzyme Type ID |
protease018926 |
| Protein Name |
Calmodulin-2
|
| Gene Name |
CALM2 CAM2 CAMB |
| 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 |
P0DP24 |
| Absorption |
|
| Active Site |
|
| Activity Regulation |
|
| Binding Site |
|
| Calcium Binding |
CA_BIND 21..32; /note=1; /evidence=ECO:0000269|PubMed:1474585; CA_BIND 57..68; /note=2; /evidence=ECO:0000269|PubMed:1474585; CA_BIND 94..105; /note=3; /evidence=ECO:0000269|PubMed:1474585; CA_BIND 130..141; /note=4; /evidence=ECO:0000269|PubMed:1474585 |
| 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). Mediates calcium-dependent inactivation of CACNA1C (PubMed:26969752). Positively regulates calcium-activated potassium channel activity of KCNN2 (PubMed:27165696). {ECO:0000269|PubMed:16760425, ECO:0000269|PubMed:26969752, ECO:0000269|PubMed:27165696}. |
| Temperature Dependency |
|
| PH Dependency |
|
| Pathway |
|
| nucleotide Binding |
|
| Features |
Beta strand (5); Calcium binding (4); Chain (1); Cross-link (2); Domain (4); Helix (7); Initiator methionine (1); Modified residue (11); Natural variant (8); Region (1); Sequence conflict (1) |
| Keywords |
3D-structure;Acetylation;Calcium;Cytoplasm;Cytoskeleton;Direct protein sequencing;Disease variant;Isopeptide bond;Long QT syndrome;Metal-binding;Methylation;Phosphoprotein;Reference proteome;Repeat;Ubl conjugation |
| Interact With |
P05067; P49407; P32121; Q13936; Q9UQM7; Q13557; O43303; O15078; P53355; P00533; P25445; P14136; P42858; Q15051; Q9H0B3; Q8WXH2; O95259; O95259-2; O15554; P51787-1; A0JP07; P02686-5; Q8NCR3; Q9HD67; P19404; Q96PM5; Q99250; Q14524; P37840; Q7Z699; Q8WZ42; P63104; P27884; Q05152; O35505; Q07652; P40136; P26645; Q6J8I9; Q9WTI7-2; Q9QXS1-3 |
| 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.9, 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:P0DP30"; 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 |
Electron microscopy (6); X-ray crystallography (11) |
| Cross Reference PDB |
3O77;
3O78;
5COC;
5J03;
5NIN;
5VMS;
5WSU;
5WSV;
6PLM;
6S5T;
6SZ5;
6XXF;
6Y4O;
7MIR;
7MIS;
7PPO;
7PQE;
|
| Mapped Pubmed ID |
12821674;
14551202;
14594800;
14960328;
15087444;
15147735;
15225611;
15229223;
15316014;
15522886;
15583004;
15746150;
15817490;
16013055;
16030015;
16084495;
16154564;
16299511;
16359877;
16545345;
16613843;
17569884;
17580302;
17654480;
17687619;
17884685;
17975119;
18001530;
18178620;
18452398;
18940010;
19023099;
19034380;
19080622;
19133300;
19584346;
19658100;
19667195;
19855925;
19913121;
20198394;
20379146;
20379614;
20468064;
20628086;
20738160;
21047202;
21124984;
21439835;
21555518;
21640070;
21664913;
21730051;
21901608;
22009783;
22009847;
22044025;
22100452;
22163646;
22295092;
22323446;
22331908;
22342729;
22451665;
22588125;
22633975;
22767601;
22768143;
22801425;
22803592;
22856685;
22996592;
23019329;
23040497;
23159936;
23235156;
23285036;
23300090;
23322042;
23352230;
23437200;
23457304;
23552119;
23624269;
23658780;
23662433;
23743201;
23760276;
23831686;
23838429;
23967355;
24032677;
24081810;
24088894;
24419375;
24420768;
24420770;
24530797;
24551838;
24713697;
24779925;
24816216;
24907274;
25005783;
25036739;
25145833;
25251320;
25268113;
25370050;
25470139;
25703379;
25751535;
25956027;
26001204;
26085527;
26148514;
26196381;
26391397;
26421717;
26487174;
26494044;
26529318;
26559977;
26618792;
26675311;
26828872;
26858457;
26980593;
27009875;
27100291;
27129269;
27226555;
27325704;
27374306;
27499441;
27632770;
27760856;
27787197;
27790916;
27798963;
27815504;
27856935;
27927985;
27933776;
27956550;
28003368;
28092099;
28130124;
28158429;
28174300;
28222617;
28262393;
28295264;
28335032;
28360104;
28422741;
28462395;
28575668;
28842480;
28849027;
28976808;
28978262;
29162807;
29240297;
29247668;
29298900;
29409956;
29463791;
29494137;
29505720;
29584409;
29606593;
29663486;
29713907;
29880196;
29932249;
30013092;
30142967;
30200150;
30279205;
30317608;
30354306;
30639287;
30808708;
30877334;
30928430;
31140879;
31230402;
31278385;
31330532;
31454269;
31483676;
31682223;
31724397;
31763755;
31785178;
31914408;
31983428;
31991573;
32012279;
32186935;
32234958;
32317284;
32554053;
32948286;
33080786;
33191766;
33321095;
33338532;
33634591;
33788723;
33890716;
33951696;
34021086;
34407442;
34533024;
34572507;
34575961;
34702826;
34888671;
|
| Motif |
|
| Gene Encoded By |
|
| Mass |
16,838 |
| Kinetics |
|
| Metal Binding |
|
| Rhea ID |
|
| Cross Reference Brenda |
|