9B9G
Structure of the PI4KA complex bound to Calcineurin
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004430 | molecular_function | 1-phosphatidylinositol 4-kinase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0005925 | cellular_component | focal adhesion |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006661 | biological_process | phosphatidylinositol biosynthetic process |
| A | 0007165 | biological_process | signal transduction |
| A | 0016020 | cellular_component | membrane |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030660 | cellular_component | Golgi-associated vesicle membrane |
| A | 0044788 | biological_process | host-mediated perturbation of viral process |
| A | 0045296 | molecular_function | cadherin binding |
| A | 0046854 | biological_process | phosphatidylinositol phosphate biosynthetic process |
| A | 0048015 | biological_process | phosphatidylinositol-mediated signaling |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0140754 | biological_process | reorganization of cellular membranes to establish viral sites of replication |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004430 | molecular_function | 1-phosphatidylinositol 4-kinase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0005925 | cellular_component | focal adhesion |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006661 | biological_process | phosphatidylinositol biosynthetic process |
| B | 0007165 | biological_process | signal transduction |
| B | 0016020 | cellular_component | membrane |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0030660 | cellular_component | Golgi-associated vesicle membrane |
| B | 0044788 | biological_process | host-mediated perturbation of viral process |
| B | 0045296 | molecular_function | cadherin binding |
| B | 0046854 | biological_process | phosphatidylinositol phosphate biosynthetic process |
| B | 0048015 | biological_process | phosphatidylinositol-mediated signaling |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0140754 | biological_process | reorganization of cellular membranes to establish viral sites of replication |
| D | 0005515 | molecular_function | protein binding |
| D | 0005829 | cellular_component | cytosol |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0046854 | biological_process | phosphatidylinositol phosphate biosynthetic process |
| D | 0072659 | biological_process | protein localization to plasma membrane |
| F | 0005515 | molecular_function | protein binding |
| F | 0005829 | cellular_component | cytosol |
| F | 0005886 | cellular_component | plasma membrane |
| F | 0046854 | biological_process | phosphatidylinositol phosphate biosynthetic process |
| F | 0072659 | biological_process | protein localization to plasma membrane |
| H | 0004721 | molecular_function | phosphoprotein phosphatase activity |
| H | 0004723 | molecular_function | calcium-dependent protein serine/threonine phosphatase activity |
| H | 0005509 | molecular_function | calcium ion binding |
| H | 0005515 | molecular_function | protein binding |
| H | 0005516 | molecular_function | calmodulin binding |
| H | 0005654 | cellular_component | nucleoplasm |
| H | 0005829 | cellular_component | cytosol |
| H | 0005886 | cellular_component | plasma membrane |
| H | 0005955 | cellular_component | calcineurin complex |
| H | 0008597 | molecular_function | calcium-dependent protein serine/threonine phosphatase regulator activity |
| H | 0019902 | molecular_function | phosphatase binding |
| H | 0019904 | molecular_function | protein domain specific binding |
| H | 0033173 | biological_process | calcineurin-NFAT signaling cascade |
| H | 0042383 | cellular_component | sarcolemma |
| H | 0045202 | cellular_component | synapse |
| H | 0045944 | biological_process | positive regulation of transcription by RNA polymerase II |
| H | 0046872 | molecular_function | metal ion binding |
| H | 0070886 | biological_process | positive regulation of calcineurin-NFAT signaling cascade |
| H | 0098685 | cellular_component | Schaffer collateral - CA1 synapse |
| H | 0098686 | cellular_component | hippocampal mossy fiber to CA3 synapse |
| H | 0098688 | cellular_component | parallel fiber to Purkinje cell synapse |
| H | 0098693 | biological_process | regulation of synaptic vesicle cycle |
| H | 0098794 | cellular_component | postsynapse |
| H | 0098978 | cellular_component | glutamatergic synapse |
| H | 0099149 | biological_process | regulation of postsynaptic neurotransmitter receptor internalization |
| H | 0099170 | biological_process | postsynaptic modulation of chemical synaptic transmission |
| H | 1905665 | biological_process | positive regulation of calcium ion import across plasma membrane |
| H | 1905949 | biological_process | negative regulation of calcium ion import across plasma membrane |
| I | 0016787 | molecular_function | hydrolase activity |
| I | 0033192 | molecular_function | calmodulin-dependent protein phosphatase activity |
| I | 0097720 | biological_process | calcineurin-mediated signaling |
| J | 0004721 | molecular_function | phosphoprotein phosphatase activity |
| J | 0004723 | molecular_function | calcium-dependent protein serine/threonine phosphatase activity |
| J | 0005509 | molecular_function | calcium ion binding |
| J | 0005515 | molecular_function | protein binding |
| J | 0005516 | molecular_function | calmodulin binding |
| J | 0005654 | cellular_component | nucleoplasm |
| J | 0005829 | cellular_component | cytosol |
| J | 0005886 | cellular_component | plasma membrane |
| J | 0005955 | cellular_component | calcineurin complex |
| J | 0008597 | molecular_function | calcium-dependent protein serine/threonine phosphatase regulator activity |
| J | 0019902 | molecular_function | phosphatase binding |
| J | 0019904 | molecular_function | protein domain specific binding |
| J | 0033173 | biological_process | calcineurin-NFAT signaling cascade |
| J | 0042383 | cellular_component | sarcolemma |
| J | 0045202 | cellular_component | synapse |
| J | 0045944 | biological_process | positive regulation of transcription by RNA polymerase II |
| J | 0046872 | molecular_function | metal ion binding |
| J | 0070886 | biological_process | positive regulation of calcineurin-NFAT signaling cascade |
| J | 0098685 | cellular_component | Schaffer collateral - CA1 synapse |
| J | 0098686 | cellular_component | hippocampal mossy fiber to CA3 synapse |
| J | 0098688 | cellular_component | parallel fiber to Purkinje cell synapse |
| J | 0098693 | biological_process | regulation of synaptic vesicle cycle |
| J | 0098794 | cellular_component | postsynapse |
| J | 0098978 | cellular_component | glutamatergic synapse |
| J | 0099149 | biological_process | regulation of postsynaptic neurotransmitter receptor internalization |
| J | 0099170 | biological_process | postsynaptic modulation of chemical synaptic transmission |
| J | 1905665 | biological_process | positive regulation of calcium ion import across plasma membrane |
| J | 1905949 | biological_process | negative regulation of calcium ion import across plasma membrane |
| K | 0016787 | molecular_function | hydrolase activity |
| K | 0033192 | molecular_function | calmodulin-dependent protein phosphatase activity |
| K | 0097720 | biological_process | calcineurin-mediated signaling |
Functional Information from PROSITE/UniProt
| site_id | PS00018 |
| Number of Residues | 13 |
| Details | EF_HAND_1 EF-hand calcium-binding domain. DLDNSGSLSveEF |
| Chain | Residue | Details |
| H | ASP31-PHE43 | |
| H | ASP63-PHE75 | |
| H | ASP100-LEU112 | |
| H | ASP141-PHE153 |
| site_id | PS00063 |
| Number of Residues | 16 |
| Details | ALDOKETO_REDUCTASE_3 Aldo/keto reductase family putative active site signature. LARSLAvqRPaSLeKV |
| Chain | Residue | Details |
| A | LEU38-VAL53 |
| site_id | PS00125 |
| Number of Residues | 6 |
| Details | SER_THR_PHOSPHATASE Serine/threonine specific protein phosphatases signature. LRGNHE |
| Chain | Residue | Details |
| I | LEU147-GLU152 |
| site_id | PS00915 |
| Number of Residues | 15 |
| Details | PI3_4_KINASE_1 Phosphatidylinositol 3- and 4-kinases signature 1. FKvg.DDCRQDmlalQ |
| Chain | Residue | Details |
| A | PHE1849-GLN1863 |
| site_id | PS00916 |
| Number of Residues | 21 |
| Details | PI3_4_KINASE_2 Phosphatidylinositol 3- and 4-kinases signature 2. SmAaysLllFLLqIkDRHngN |
| Chain | Residue | Details |
| A | SER1942-ASN1962 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 376 |
| Details | Domain: {"description":"PIK helical","evidences":[{"source":"PROSITE-ProRule","id":"PRU00878","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Region: {"description":"G-loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Region: {"description":"Catalytic loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 66 |
| Details | Repeat: {"description":"TPR 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 66 |
| Details | Repeat: {"description":"TPR 3"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 66 |
| Details | Repeat: {"description":"TPR 4"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 70 |
| Details | Repeat: {"description":"TPR 5"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 64 |
| Details | Repeat: {"description":"TPR 6"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 66 |
| Details | Repeat: {"description":"TPR 7"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 66 |
| Details | Repeat: {"description":"TPR 8"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 66 |
| Details | Repeat: {"description":"TPR 9"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 64 |
| Details | Repeat: {"description":"TPR 10"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 66 |
| Details | Repeat: {"description":"TPR 11"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 56 |
| Details | Domain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 70 |
| Details | Domain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 70 |
| Details | Domain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 70 |
| Details | Domain: {"description":"EF-hand 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI19 |
| Number of Residues | 10 |
| Details | Region: {"description":"Calcineurin A binding","evidences":[{"source":"PubMed","id":"12218175","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12357034","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17498738","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22343722","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23468591","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26794871","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27974827","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8524402","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI20 |
| Number of Residues | 30 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12218175","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12357034","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17498738","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22343722","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23468591","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26794871","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27974827","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8524402","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AUI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1M63","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1MF8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2P6B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3LL8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4F0Z","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4OR9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ORA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ORC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5SVE","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI21 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12218175","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12357034","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17498738","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22343722","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23468591","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26794871","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27974827","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31375679","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8524402","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6NUC","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"1AUI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1M63","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1MF8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2P6B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3LL8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4F0Z","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4OR9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ORA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ORC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5SVE","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI22 |
| Number of Residues | 4 |
| Details | Site: {"description":"Interaction with PxVP motif in substrates of the catalytic subunit","evidences":[{"source":"PubMed","id":"23468591","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI23 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q63810","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI24 |
| Number of Residues | 18 |
| Details | Region: {"description":"Interaction with PxIxIF motif in substrate","evidences":[{"source":"PubMed","id":"17498738","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17502104","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22343722","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23468591","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26248042","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI25 |
| Number of Residues | 56 |
| Details | Region: {"description":"Calcineurin B binding","evidences":[{"source":"PubMed","id":"12218175","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12357034","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17498738","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23468591","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27974827","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8524402","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI26 |
| Number of Residues | 8 |
| Details | Motif: {"description":"SAPNY motif","evidences":[{"source":"PubMed","id":"26248042","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI27 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"8524402","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI28 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12218175","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17498738","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22343722","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26248042","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27974827","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31375679","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8524402","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AUI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1M63","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2P6B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3LL8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5C1V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5SVE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NUC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NUU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6UUQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI29 |
| Number of Residues | 2 |
| Details | Site: {"description":"Interaction with PxVP motif in substrate","evidences":[{"source":"PubMed","id":"23468591","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27974827","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI30 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"UniProtKB","id":"P63328","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 10 |
| Details | M-CSA 406 |
| Chain | Residue | Details |
| H | GLU89 | metal ligand |
| H | LYS91 | metal ligand |
| H | LYS117 | metal ligand |
| H | VAL120 | electrostatic stabiliser |
| H | GLY121 | transition state stabiliser |
| H | SER149 | metal ligand |
| H | PHE150 | proton shuttle (general acid/base) |
| site_id | MCSA2 |
| Number of Residues | 10 |
| Details | M-CSA 406 |
| Chain | Residue | Details |
| J | GLU89 | metal ligand |
| J | LYS91 | metal ligand |
| J | LYS117 | metal ligand |
| J | VAL120 | electrostatic stabiliser |
| J | GLY121 | transition state stabiliser |
| J | SER149 | metal ligand |
| J | PHE150 | proton shuttle (general acid/base) |






