about
Abnormal spindle microtubule assemblyPotassium voltage-gated channel, subfamily Q, member 1Myosin, heavy polypeptide 7, cardiac muscle, betaMyelin basic proteinTransient receptor potential cation channel subfamily V member 6Transient receptor potential cation channel, subfamily V, member 6Sodium channel, voltage-gated, type V, alphaCalcium channel, voltage-dependent, L type, alpha 1C subunitGrowth associated protein 43Erythrocyte membrane protein band 4.1Transient receptor potential cation channel, subfamily V, member 1Sphingosine kinase 1Myosin VIIAPotassium voltage-gated channel, subfamily Q, member 2Potassium voltage-gated channel, subfamily Q, member 3Calcium voltage-gated channel subunit alpha1 CMyosin VATransient receptor potential cation channel, subfamily M, member 4Transient receptor potential cation channel, subfamily V, member 4Transient receptor potential cation channel subfamily V member 5Nitric oxide synthase 3, endothelial cellInositol-trisphosphate 3-kinase BFas cell surface death receptorIQ motif containing GTPase activating protein 1Tight junction protein 1Protein phosphatase 3 catalytic subunit gammaCalcium/calmodulin dependent protein kinase II deltaF-box and leucine rich repeat protein 2Myosin IEMyristoylated alanine rich protein kinase C substrateAE binding protein 1Sperm autoantigenic protein 17CAMP regulated phosphoprotein 21Calponin 1Cyclic nucleotide gated channel subunit alpha 2ATP synthase inhibitory factor subunit 1Calcium/calmodulin dependent serine protein kinaseIQ motif containing F5IQ motif containing F6IQ motif containing F3
P680
Ca2+/Calmodulin reverses phosphatidylinositol 3,4, 5-trisphosphate-dependent inhibition of regulators of G protein-signaling GTPase-activating protein activityZinedin, SG2NA, and striatin are calmodulin-binding, WD repeat proteins principally expressed in the brainMutations in calmodulin cause ventricular tachycardia and sudden cardiac deathThe KCNQ1 (Kv7.1) COOH terminus, a multitiered scaffold for subunit assembly and protein interactionCalmodulin is a phospholipase C-beta interacting proteinMyo6 facilitates the translocation of endocytic vesicles from cell peripheriesSolution NMR structure of Apo-calmodulin in complex with the IQ motif of human cardiac sodium channel NaV1.5Cloning of human striatin cDNA (STRN), gene mapping to 2p22-p21, and preferential expression in brainThe complex structure of calmodulin bound to a calcineurin peptideDomain Swapping and Different Oligomeric States for the Complex Between Calmodulin and the Calmodulin-Binding Domain of Calcineurin AStructural insights into the mechanism of calmodulin binding to death receptorsDistinctive malfunctions of calmodulin mutations associated with heart RyR2-mediated arrhythmic diseaseFRET detection of calmodulin binding to the cardiac RyR2 calcium release channelNovel CPVT-Associated Calmodulin Mutation in CALM3 (CALM3-A103V) Activates Arrhythmogenic Ca Waves and Sparks.The calmodulin regulator protein, PEP-19, sensitizes ATP-induced Ca2+ releaseATP2B1 gene Silencing Increases Insulin Sensitivity through Facilitating Akt Activation via the Ca2+/calmodulin Signaling Pathway and Ca2+-associated eNOS Activation in Endothelial Cells.1H, 15N, and 13C chemical shift assignments of the regulatory domain of human calcineurin.
P921
Q14860490-AFCE15A9-9CCF-4064-B2D1-8A8B942BC183Q14865158-44DB519C-F8A7-4A71-B583-32BAD50E9A42Q14865158-E972F5B3-33D2-47D7-82A6-292338871D8EQ14876111-46DA2F45-E92A-4DA0-B249-57E98A4A1DD7Q14876145-F704F417-2CDF-4A41-9894-A1D50B5EEF91Q14891582-AD48B827-7BF1-441E-AF6C-8E73F98D6DF1Q14891589-8A02D58B-3470-4AC7-A395-D572C7D075D6Q14905733-36CF1092-114D-45B0-94A1-22E73E2EC9B3Q14905748-362751DD-38F8-4156-B2EF-FCF6D08E21FBQ14905748-4774F0D8-1D58-42B4-BF6D-9E072C931572Q14906270-14734DB3-6B75-4F17-B752-0605B3C44E94Q14906270-2AE8460E-9235-4578-89E9-837083E75549Q14908150-8FDF762C-3447-41FE-8189-F676B4DA3A0EQ14908176-78508186-785B-4ECE-B201-3966D2CB0D3FQ14913839-B2858627-C762-4716-936D-3813BCCD20FEQ14914032-64AB2AFF-84DD-4401-8899-B1033F4EBA00Q14914310-65C5399C-124A-4B21-8E15-09068796F762Q14914310-B5055FD8-22AD-48D4-B7CA-FE9E0D9838B2Q14914320-18F96170-A651-48B2-A361-E23781D69A0DQ14914320-1C34ECAE-418F-44BA-9C27-C4F479A70DD3Q1499998-46EA7EA6-D2D7-4E5C-B589-E29D5D4798F8Q1499998-DD8C4AD5-07A2-425D-A34F-80508C8DF3FFQ15320975-96B52B79-F890-4B83-AFB1-A49A846117C9Q15323770-65D66C72-A19F-4028-B8BC-1993D3A89367Q15324125-879C8EFC-72D0-4230-912D-67656B7C1054Q15327766-861D3FD3-F778-4B45-A4CA-DD4AC17DDB06Q15328616-3DEB9AFC-3E3C-4AE4-A520-D27AA385CB51Q15331777-1B3E05D5-A30F-43FB-B3D3-2B1C15BD5A56Q1649375-F9928FBB-CD68-46E7-B616-5B6412E3211AQ21096417-5A1BD45B-5CFF-4153-98B2-5617B6B58287Q21096429-8BD2DD96-FA26-4A63-8710-C1CCB80CD85CQ21097390-73E875CC-EB02-4044-AF62-0DF95B5C03E8Q21097390-CC53AB04-339A-44B9-BC11-128FF77BD5A7Q21100382-2921C9B5-880A-45A2-A5B3-AFF189FF75AFQ21100382-7CC7FD35-2501-4ACE-8A17-765F4493DBA2Q21101384-B0BC4652-21DE-4341-AF06-83F810600709Q21101842-2331923D-4F40-4981-8279-C72FD4EE88DBQ21104654-C4EED0AF-D01C-4B82-9783-769F3C78DD26Q21104965-B2B4F3C9-A642-4671-91BB-94C0EA0F245EQ21105083-2D2AFC11-C6CB-4FB1-A670-A541948BC481
P680
Q22253430-6615A1B9-BA4A-4503-92AE-D872820C64E7Q22253439-119C7FA9-A8EA-482D-9796-7E4D4E24CC87Q24300356-4C226DD5-12AD-4B92-BD2C-3E7E2464AA4BQ24305236-F9409590-276C-4E9F-8687-4E1BEC3290F2Q24306238-CF83D6D3-2D85-4B8B-A14E-EC1593780E64Q24307920-B8473A57-8114-4261-8939-8BED94E129C2Q24317459-3E788B3B-FADE-49A9-A505-A23589DEBAC7Q24321531-D19D08D6-8AF9-42D7-97D6-DCB5BA208C46Q27650207-B7E486BA-72A4-4BAE-8CF3-D78424892995Q27655328-3F4E78F9-C9F4-45E5-99C8-F55556E8A1DCQ28771748-5F8F217F-D9C6-4BF2-8BD6-F05160BAFB31Q29147453-13DCC453-6526-4DA2-B3A2-AD025CE2FD0DQ29147483-66EA98D5-4A6E-499D-858E-0202EA680E60Q29347555-85A3F9AE-CA6D-497D-B94C-6576FCC22B28Q30668614-729C2132-2043-448F-A19D-D857B7D845FEQ44303541-CD033D12-C96F-4701-B02E-2BF0721F8914Q47959452-2102914B-7A60-411F-B3A5-6E29B19FC806
P921
description
Interacting selectively and no ...... bound and calcium-free states.
@en
Interactions sélectives et non ...... ats calciques et sans calcium.
@fr
biologisch proces
@nl
name
calmodulin binding
@en
fixation de la calmoduline
@fr
legare de calmodulină
@ro
type
label
calmodulin binding
@en
fixation de la calmoduline
@fr
legare de calmodulină
@ro
altLabel
GO:0005516
@en
prefLabel
calmodulin binding
@en
fixation de la calmoduline
@fr
legare de calmodulină
@ro
P279
P2888
P686
GO:0005516