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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

4JPZ

Voltage-gated sodium channel 1.2 C-terminal domain in complex with FGF13U and Ca2+/calmodulin

Functional Information from GO Data
ChainGOidnamespacecontents
A0008083molecular_functiongrowth factor activity
B0005261molecular_functionmonoatomic cation channel activity
B0005886cellular_componentplasma membrane
C0000922cellular_componentspindle pole
C0002027biological_processregulation of heart rate
C0005246molecular_functioncalcium channel regulator activity
C0005509molecular_functioncalcium ion binding
C0005513biological_processdetection of calcium ion
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005813cellular_componentcentrosome
C0005819cellular_componentspindle
C0005829cellular_componentcytosol
C0005876cellular_componentspindle microtubule
C0005886cellular_componentplasma membrane
C0007186biological_processG protein-coupled receptor signaling pathway
C0008076cellular_componentvoltage-gated potassium channel complex
C0010856molecular_functionadenylate cyclase activator activity
C0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
C0010881biological_processregulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
C0016020cellular_componentmembrane
C0016240biological_processautophagosome membrane docking
C0019855molecular_functioncalcium channel inhibitor activity
C0019901molecular_functionprotein kinase binding
C0021762biological_processsubstantia nigra development
C0030017cellular_componentsarcomere
C0031432molecular_functiontitin binding
C0031514cellular_componentmotile cilium
C0031982cellular_componentvesicle
C0032465biological_processregulation of cytokinesis
C0032991cellular_componentprotein-containing complex
C0034704cellular_componentcalcium channel complex
C0035458biological_processcellular response to interferon-beta
C0043209cellular_componentmyelin sheath
C0043539molecular_functionprotein serine/threonine kinase activator activity
C0044305cellular_componentcalyx of Held
C0044325molecular_functiontransmembrane transporter binding
C0046427biological_processpositive regulation of receptor signaling pathway via JAK-STAT
C0046872molecular_functionmetal ion binding
C0048306molecular_functioncalcium-dependent protein binding
C0051592biological_processresponse to calcium ion
C0055117biological_processregulation of cardiac muscle contraction
C0060291biological_processlong-term synaptic potentiation
C0060314biological_processregulation of ryanodine-sensitive calcium-release channel activity
C0060315biological_processnegative regulation of ryanodine-sensitive calcium-release channel activity
C0071346biological_processcellular response to type II interferon
C0072542molecular_functionprotein phosphatase activator activity
C0097225cellular_componentsperm midpiece
C0097720biological_processcalcineurin-mediated signaling
C0098901biological_processregulation of cardiac muscle cell action potential
C0099523cellular_componentpresynaptic cytosol
C0140056biological_processorganelle localization by membrane tethering
C0140238biological_processpresynaptic endocytosis
C0141110molecular_functiontransporter inhibitor activity
C1901842biological_processnegative regulation of high voltage-gated calcium channel activity
C1901844biological_processregulation of cell communication by electrical coupling involved in cardiac conduction
C1902494cellular_componentcatalytic complex
C1905913biological_processnegative regulation of calcium ion export across plasma membrane
C1990456biological_processmitochondrion-endoplasmic reticulum membrane tethering
E0008083molecular_functiongrowth factor activity
H0005261molecular_functionmonoatomic cation channel activity
H0005886cellular_componentplasma membrane
I0000922cellular_componentspindle pole
I0002027biological_processregulation of heart rate
I0005246molecular_functioncalcium channel regulator activity
I0005509molecular_functioncalcium ion binding
I0005513biological_processdetection of calcium ion
I0005515molecular_functionprotein binding
I0005576cellular_componentextracellular region
I0005634cellular_componentnucleus
I0005654cellular_componentnucleoplasm
I0005737cellular_componentcytoplasm
I0005813cellular_componentcentrosome
I0005819cellular_componentspindle
I0005829cellular_componentcytosol
I0005876cellular_componentspindle microtubule
I0005886cellular_componentplasma membrane
I0007186biological_processG protein-coupled receptor signaling pathway
I0008076cellular_componentvoltage-gated potassium channel complex
I0010856molecular_functionadenylate cyclase activator activity
I0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
I0010881biological_processregulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
I0016020cellular_componentmembrane
I0016240biological_processautophagosome membrane docking
I0019855molecular_functioncalcium channel inhibitor activity
I0019901molecular_functionprotein kinase binding
I0021762biological_processsubstantia nigra development
I0030017cellular_componentsarcomere
I0031432molecular_functiontitin binding
I0031514cellular_componentmotile cilium
I0031982cellular_componentvesicle
I0032465biological_processregulation of cytokinesis
I0032991cellular_componentprotein-containing complex
I0034704cellular_componentcalcium channel complex
I0035458biological_processcellular response to interferon-beta
I0043209cellular_componentmyelin sheath
I0043539molecular_functionprotein serine/threonine kinase activator activity
I0044305cellular_componentcalyx of Held
I0044325molecular_functiontransmembrane transporter binding
I0046427biological_processpositive regulation of receptor signaling pathway via JAK-STAT
I0046872molecular_functionmetal ion binding
I0048306molecular_functioncalcium-dependent protein binding
I0051592biological_processresponse to calcium ion
I0055117biological_processregulation of cardiac muscle contraction
I0060291biological_processlong-term synaptic potentiation
I0060314biological_processregulation of ryanodine-sensitive calcium-release channel activity
I0060315biological_processnegative regulation of ryanodine-sensitive calcium-release channel activity
I0071346biological_processcellular response to type II interferon
I0072542molecular_functionprotein phosphatase activator activity
I0097225cellular_componentsperm midpiece
I0097720biological_processcalcineurin-mediated signaling
I0098901biological_processregulation of cardiac muscle cell action potential
I0099523cellular_componentpresynaptic cytosol
I0140056biological_processorganelle localization by membrane tethering
I0140238biological_processpresynaptic endocytosis
I0141110molecular_functiontransporter inhibitor activity
I1901842biological_processnegative regulation of high voltage-gated calcium channel activity
I1901844biological_processregulation of cell communication by electrical coupling involved in cardiac conduction
I1902494cellular_componentcatalytic complex
I1905913biological_processnegative regulation of calcium ion export across plasma membrane
I1990456biological_processmitochondrion-endoplasmic reticulum membrane tethering
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA C 201
ChainResidue
CASP21
CASP23
CASP25
CTHR27
CGLU32
CHOH301
site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA C 202
ChainResidue
CTHR63
CGLU68
CHOH302
CASP57
CASP59
CASN61
site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA C 203
ChainResidue
CASP94
CASP96
CASN98
CTYR100
CHOH303
CHOH304
site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA C 204
ChainResidue
CASP130
CASP132
CASP134
CGLN136
CHOH305
CHOH306
site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA I 201
ChainResidue
IASP21
IASP23
IASP25
ITHR27
IGLU32
site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA I 202
ChainResidue
IASP57
IASP59
IASN61
ITHR63
IGLU68
site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA I 203
ChainResidue
IASP94
IASP96
IASN98
ITYR100
site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA I 204
ChainResidue
IASP130
IASP132
IASP134
IGLN136
Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL
ChainResidueDetails
CASP21-LEU33
CASP57-PHE69
CASP94-LEU106
CASP130-PHE142
site_idPS00247
Number of Residues24
DetailsHBGF_FGF HBGF/FGF family signature. GyLyTselftp.ECkFkEsvfenyY
ChainResidueDetails
AGLY76-TYR99
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues268
DetailsRegion: {"description":"Mediates interaction with sodium channels"}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues70
DetailsDomain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues70
DetailsDomain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues70
DetailsDomain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues64
DetailsDomain: {"description":"EF-hand 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues144
DetailsRegion: {"description":"Necessary and sufficient for interaction with PCP4","evidences":[{"source":"PubMed","id":"27876793","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1474585","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25441029","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27564677","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CLL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4UMO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4V0C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5J03","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1474585","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27564677","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29724949","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CLL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5J03","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6CNN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6CNO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1474585","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27564677","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CLL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5J03","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by CaMK4","evidences":[{"source":"UniProtKB","id":"P0DP29","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues2
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"24129315","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P62157","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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