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6ALE

A V-to-F substitution in SK2 channels causes Ca2+ hypersensitivity and improves locomotion in a C. elegans ALS model

Functional Information from GO Data
ChainGOidnamespacecontents
B0005516molecular_functioncalmodulin binding
B0006813biological_processpotassium ion transport
B0015269molecular_functioncalcium-activated potassium channel activity
B0016020cellular_componentmembrane
B0016286molecular_functionsmall conductance calcium-activated potassium channel activity
R0000086biological_processG2/M transition of mitotic cell cycle
R0000922cellular_componentspindle pole
R0001975biological_processresponse to amphetamine
R0002027biological_processregulation of heart rate
R0005509molecular_functioncalcium ion binding
R0005513biological_processdetection of calcium ion
R0005515molecular_functionprotein binding
R0005737cellular_componentcytoplasm
R0005739cellular_componentmitochondrion
R0005813cellular_componentcentrosome
R0005819cellular_componentspindle
R0005856cellular_componentcytoskeleton
R0005876cellular_componentspindle microtubule
R0008076cellular_componentvoltage-gated potassium channel complex
R0008179molecular_functionadenylate cyclase binding
R0010856molecular_functionadenylate cyclase activator activity
R0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
R0016020cellular_componentmembrane
R0016240biological_processautophagosome membrane docking
R0019855molecular_functioncalcium channel inhibitor activity
R0019901molecular_functionprotein kinase binding
R0030017cellular_componentsarcomere
R0030235molecular_functionnitric-oxide synthase regulator activity
R0030426cellular_componentgrowth cone
R0030672cellular_componentsynaptic vesicle membrane
R0031432molecular_functiontitin binding
R0031966cellular_componentmitochondrial membrane
R0031982cellular_componentvesicle
R0032465biological_processregulation of cytokinesis
R0032991cellular_componentprotein-containing complex
R0034704cellular_componentcalcium channel complex
R0035307biological_processpositive regulation of protein dephosphorylation
R0035458biological_processcellular response to interferon-beta
R0043209cellular_componentmyelin sheath
R0043539molecular_functionprotein serine/threonine kinase activator activity
R0044325molecular_functiontransmembrane transporter binding
R0046427biological_processpositive regulation of receptor signaling pathway via JAK-STAT
R0046872molecular_functionmetal ion binding
R0048306molecular_functioncalcium-dependent protein binding
R0050848biological_processregulation of calcium-mediated signaling
R0050998molecular_functionnitric-oxide synthase binding
R0051412biological_processresponse to corticosterone
R0051592biological_processresponse to calcium ion
R0055117biological_processregulation of cardiac muscle contraction
R0060315biological_processnegative regulation of ryanodine-sensitive calcium-release channel activity
R0071346biological_processcellular response to type II interferon
R0072542molecular_functionprotein phosphatase activator activity
R0090150biological_processestablishment of protein localization to membrane
R0090151biological_processestablishment of protein localization to mitochondrial membrane
R0098685cellular_componentSchaffer collateral - CA1 synapse
R0098901biological_processregulation of cardiac muscle cell action potential
R0099524cellular_componentpostsynaptic cytosol
R0140056biological_processorganelle localization by membrane tethering
R1900242biological_processregulation of synaptic vesicle endocytosis
R1902494cellular_componentcatalytic complex
R1905913biological_processnegative regulation of calcium ion export across plasma membrane
R1990456biological_processmitochondrion-endoplasmic reticulum membrane tethering
R2000300biological_processregulation of synaptic vesicle exocytosis
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue SO4 B 501
ChainResidue
BARG429
BLYS451
BHIS452
BLYS455

site_idAC2
Number of Residues2
Detailsbinding site for residue SO4 B 502
ChainResidue
BARG454
BLYS455

site_idAC3
Number of Residues3
Detailsbinding site for residue SO4 B 503
ChainResidue
BLYS402
RLYS77
RTHR79

site_idAC4
Number of Residues10
Detailsbinding site for residue 1KP B 504
ChainResidue
BGLU404
BASN409
BPHE410
BALA477
BVAL481
RMET51
RGLU54
RVAL55
RMET71
RLYS75

site_idAC5
Number of Residues1
Detailsbinding site for residue GOL B 505
ChainResidue
BALA447

site_idAC6
Number of Residues5
Detailsbinding site for residue CA R 1001
ChainResidue
RASP20
RASP22
RASP24
RTHR26
RGLU31

site_idAC7
Number of Residues6
Detailsbinding site for residue CA R 1002
ChainResidue
RASP56
RASP58
RASN60
RTHR62
RASP64
RGLU67

site_idAC8
Number of Residues4
Detailsbinding site for residue SO4 R 1003
ChainResidue
RHIS107
RASN111
RHOH1102
RHOH1141

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL
ChainResidueDetails
RASP20-LEU32
RASP56-PHE68
RASP93-LEU105
RASP129-PHE141

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
ChainResidueDetails
RASP20
RGLU67
RASP93
RASP95
RASN97
RTYR99
RGLU104
RASP129
RASP131
RASP133
RGLN135
RASP22
RGLU140
RASP24
RTHR26
RGLU31
RASP56
RASP58
RASN60
RTHR62

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P0DP24
ChainResidueDetails
RLYS21

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by CaMK4 => ECO:0000269|PubMed:12392717
ChainResidueDetails
RTHR44

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P0DP24
ChainResidueDetails
RSER81

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P0DP24
ChainResidueDetails
RLYS94

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:22673903
ChainResidueDetails
RTYR99

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:22673903
ChainResidueDetails
RSER101

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P0DP24
ChainResidueDetails
RTHR110

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:P0DP24
ChainResidueDetails
RLYS115

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P0DP24
ChainResidueDetails
RTYR138

site_idSWS_FT_FI11
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62157
ChainResidueDetails
RLYS21

219140

PDB entries from 2024-05-01

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