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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8XYA

hPhK alpha-beta-gamma-delta subcomplex in inactive state

Functional Information from GO Data
ChainGOidnamespacecontents
A0004689molecular_functionphosphorylase kinase activity
A0005516molecular_functioncalmodulin binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005964cellular_componentphosphorylase kinase complex
A0005975biological_processcarbohydrate metabolic process
A0005977biological_processglycogen metabolic process
A0005980biological_processglycogen catabolic process
A0006091biological_processgeneration of precursor metabolites and energy
A0045819biological_processpositive regulation of glycogen catabolic process
B0005515molecular_functionprotein binding
B0005516molecular_functioncalmodulin binding
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0005964cellular_componentphosphorylase kinase complex
B0005975biological_processcarbohydrate metabolic process
B0005977biological_processglycogen metabolic process
B0005980biological_processglycogen catabolic process
B0006091biological_processgeneration of precursor metabolites and energy
C0000166molecular_functionnucleotide binding
C0004672molecular_functionprotein kinase activity
C0004674molecular_functionprotein serine/threonine kinase activity
C0004689molecular_functionphosphorylase kinase activity
C0005516molecular_functioncalmodulin binding
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005964cellular_componentphosphorylase kinase complex
C0005975biological_processcarbohydrate metabolic process
C0005977biological_processglycogen metabolic process
C0005980biological_processglycogen catabolic process
C0006468biological_processprotein phosphorylation
C0007165biological_processsignal transduction
C0016301molecular_functionkinase activity
C0016740molecular_functiontransferase activity
C0019899molecular_functionenzyme binding
C0050321molecular_functiontau-protein kinase activity
C0106310molecular_functionprotein serine kinase activity
D0000922cellular_componentspindle pole
D0002027biological_processregulation of heart rate
D0005246molecular_functioncalcium channel regulator activity
D0005509molecular_functioncalcium ion binding
D0005513biological_processdetection of calcium ion
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0005813cellular_componentcentrosome
D0005819cellular_componentspindle
D0005829cellular_componentcytosol
D0005876cellular_componentspindle microtubule
D0005886cellular_componentplasma membrane
D0007186biological_processG protein-coupled receptor signaling pathway
D0008076cellular_componentvoltage-gated potassium channel complex
D0010856molecular_functionadenylate cyclase activator activity
D0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
D0010881biological_processregulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
D0016020cellular_componentmembrane
D0016240biological_processautophagosome membrane docking
D0019855molecular_functioncalcium channel inhibitor activity
D0019901molecular_functionprotein kinase binding
D0021762biological_processsubstantia nigra development
D0030017cellular_componentsarcomere
D0031432molecular_functiontitin binding
D0031514cellular_componentmotile cilium
D0031982cellular_componentvesicle
D0032465biological_processregulation of cytokinesis
D0032991cellular_componentprotein-containing complex
D0034704cellular_componentcalcium channel complex
D0035458biological_processcellular response to interferon-beta
D0043209cellular_componentmyelin sheath
D0043539molecular_functionprotein serine/threonine kinase activator activity
D0044305cellular_componentcalyx of Held
D0044325molecular_functiontransmembrane transporter binding
D0046427biological_processpositive regulation of receptor signaling pathway via JAK-STAT
D0046872molecular_functionmetal ion binding
D0048306molecular_functioncalcium-dependent protein binding
D0051592biological_processresponse to calcium ion
D0055117biological_processregulation of cardiac muscle contraction
D0060291biological_processlong-term synaptic potentiation
D0060314biological_processregulation of ryanodine-sensitive calcium-release channel activity
D0060315biological_processnegative regulation of ryanodine-sensitive calcium-release channel activity
D0071346biological_processcellular response to type II interferon
D0072542molecular_functionprotein phosphatase activator activity
D0097225cellular_componentsperm midpiece
D0097720biological_processcalcineurin-mediated signaling
D0098901biological_processregulation of cardiac muscle cell action potential
D0099523cellular_componentpresynaptic cytosol
D0140056biological_processorganelle localization by membrane tethering
D0140238biological_processpresynaptic endocytosis
D0141110molecular_functiontransporter inhibitor activity
D1901842biological_processnegative regulation of high voltage-gated calcium channel activity
D1901844biological_processregulation of cell communication by electrical coupling involved in cardiac conduction
D1902494cellular_componentcatalytic complex
D1905913biological_processnegative regulation of calcium ion export across plasma membrane
D1990456biological_processmitochondrion-endoplasmic reticulum membrane tethering
Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL
ChainResidueDetails
DASP21-LEU33
DASP57-PHE69
DASP94-LEU106
DASP130-PHE142
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGRGVSSVVRrCihkptsqe..........YAVK
ChainResidueDetails
CLEU26-LYS49
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDLKpeNILL
ChainResidueDetails
CILE146-LEU158
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues88
DetailsRegion: {"description":"Calmodulin-binding","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q64649","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues1
DetailsLipidation: {"description":"S-farnesyl cysteine","evidences":[{"source":"UniProtKB","id":"P18688","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues1
DetailsLipidation: {"description":"S-farnesyl cysteine","evidences":[{"source":"UniProtKB","id":"P12798","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues35
DetailsDomain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues35
DetailsDomain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues35
DetailsDomain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues10
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 Residues5
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 Residues5
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 Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by CaMK4","evidences":[{"source":"UniProtKB","id":"P0DP29","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues1
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_FI17
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues1
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"24129315","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P62157","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues268
DetailsDomain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues24
DetailsRegion: {"description":"Calmodulin-binding (domain-N)"}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues24
DetailsRegion: {"description":"Calmodulin-binding (domain-C)"}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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