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5VMS

CryoEM structure of Xenopus KCNQ1 channel

Functional Information from GO Data
ChainGOidnamespacecontents
A0005216molecular_functionmonoatomic ion channel activity
A0005249molecular_functionvoltage-gated potassium channel activity
A0006811biological_processmonoatomic ion transport
A0006813biological_processpotassium ion transport
A0008076cellular_componentvoltage-gated potassium channel complex
A0016020cellular_componentmembrane
A0055085biological_processtransmembrane transport
B0000086biological_processG2/M transition of mitotic cell cycle
B0000922cellular_componentspindle pole
B0002027biological_processregulation of heart rate
B0005509molecular_functioncalcium ion binding
B0005513biological_processdetection of calcium ion
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005813cellular_componentcentrosome
B0005819cellular_componentspindle
B0005829cellular_componentcytosol
B0005856cellular_componentcytoskeleton
B0005876cellular_componentspindle microtubule
B0005886cellular_componentplasma membrane
B0005929cellular_componentcilium
B0007186biological_processG protein-coupled receptor signaling pathway
B0008076cellular_componentvoltage-gated potassium channel complex
B0010800biological_processpositive regulation of peptidyl-threonine phosphorylation
B0010801biological_processnegative regulation of peptidyl-threonine phosphorylation
B0010856molecular_functionadenylate cyclase activator activity
B0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
B0010881biological_processregulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
B0016020cellular_componentmembrane
B0016240biological_processautophagosome membrane docking
B0019855molecular_functioncalcium channel inhibitor activity
B0019901molecular_functionprotein kinase binding
B0021762biological_processsubstantia nigra development
B0030017cellular_componentsarcomere
B0030234molecular_functionenzyme regulator activity
B0031432molecular_functiontitin binding
B0031514cellular_componentmotile cilium
B0031954biological_processpositive regulation of protein autophosphorylation
B0031982cellular_componentvesicle
B0032465biological_processregulation of cytokinesis
B0032516biological_processpositive regulation of phosphoprotein phosphatase activity
B0032991cellular_componentprotein-containing complex
B0034704cellular_componentcalcium channel complex
B0035307biological_processpositive regulation of protein dephosphorylation
B0035458biological_processcellular response to interferon-beta
B0042995cellular_componentcell projection
B0043209cellular_componentmyelin sheath
B0043539molecular_functionprotein serine/threonine kinase activator activity
B0044325molecular_functiontransmembrane transporter binding
B0046427biological_processpositive regulation of receptor signaling pathway via JAK-STAT
B0046872molecular_functionmetal ion binding
B0048306molecular_functioncalcium-dependent protein binding
B0050848biological_processregulation of calcium-mediated signaling
B0051343biological_processpositive regulation of cyclic-nucleotide phosphodiesterase activity
B0051592biological_processresponse to calcium ion
B0055117biological_processregulation of cardiac muscle contraction
B0060314biological_processregulation of ryanodine-sensitive calcium-release channel activity
B0060315biological_processnegative regulation of ryanodine-sensitive calcium-release channel activity
B0060316biological_processpositive regulation of ryanodine-sensitive calcium-release channel activity
B0071346biological_processcellular response to type II interferon
B0071902biological_processpositive regulation of protein serine/threonine kinase activity
B0072542molecular_functionprotein phosphatase activator activity
B0097225cellular_componentsperm midpiece
B0098901biological_processregulation of cardiac muscle cell action potential
B0140056biological_processorganelle localization by membrane tethering
B1901842biological_processnegative regulation of high voltage-gated calcium channel activity
B1901844biological_processregulation of cell communication by electrical coupling involved in cardiac conduction
B1902494cellular_componentcatalytic complex
B1905913biological_processnegative regulation of calcium ion export across plasma membrane
B1990456biological_processmitochondrion-endoplasmic reticulum membrane tethering
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue CA B 201
ChainResidue
BASP21
BASP23
BTHR27

site_idAC2
Number of Residues4
Detailsbinding site for residue CA B 202
ChainResidue
BASP59
BASN61
BTHR63
BASP65

site_idAC3
Number of Residues2
Detailsbinding site for residue CA B 203
ChainResidue
BASP134
BGLN136

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL
ChainResidueDetails
BASP21-LEU33
BASP57-PHE69
BASP94-LEU106
BASP130-PHE142

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, 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
ChainResidueDetails
BASP21
BGLU68
BASP23
BASP25
BTHR27
BGLU32
BASP57
BASP59
BASN61
BTHR63

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:1474585, ECO:0000269|PubMed:27564677, ECO:0007744|PDB:1CLL, ECO:0007744|PDB:5J03
ChainResidueDetails
BASP94
BGLU141
BASP96
BASN98
BTYR100
BGLU105
BASP130
BASP132
BASP134
BGLN136

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:7093203, ECO:0000269|Ref.7, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712
ChainResidueDetails
BALA2

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
BLYS22
ASER215-ARG227

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by CaMK4 => ECO:0000250|UniProtKB:P0DP29
ChainResidueDetails
BTHR45

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER82

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
BLYS95

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332
ChainResidueDetails
BTYR100

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
BSER102

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:24275569
ChainResidueDetails
BTHR111

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0007744|PubMed:24129315
ChainResidueDetails
BLYS116

site_idSWS_FT_FI12
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19690332
ChainResidueDetails
BTYR139

site_idSWS_FT_FI13
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62157
ChainResidueDetails
BLYS22

218853

PDB entries from 2024-04-24

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