6HR1
Crystal structure of the YFPnano fusion protein
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000086 | biological_process | G2/M transition of mitotic cell cycle |
| A | 0000922 | cellular_component | spindle pole |
| A | 0002027 | biological_process | regulation of heart rate |
| A | 0005246 | molecular_function | calcium channel regulator activity |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005513 | biological_process | detection of calcium ion |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005634 | cellular_component | nucleus |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005813 | cellular_component | centrosome |
| A | 0005819 | cellular_component | spindle |
| A | 0005829 | cellular_component | cytosol |
| A | 0005876 | cellular_component | spindle microtubule |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006091 | biological_process | generation of precursor metabolites and energy |
| A | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| A | 0008076 | cellular_component | voltage-gated potassium channel complex |
| A | 0008218 | biological_process | bioluminescence |
| A | 0010856 | molecular_function | adenylate cyclase activator activity |
| A | 0010880 | biological_process | regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum |
| A | 0010881 | biological_process | regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion |
| A | 0016020 | cellular_component | membrane |
| A | 0016240 | biological_process | autophagosome membrane docking |
| A | 0019855 | molecular_function | calcium channel inhibitor activity |
| A | 0019901 | molecular_function | protein kinase binding |
| A | 0021762 | biological_process | substantia nigra development |
| A | 0030017 | cellular_component | sarcomere |
| A | 0030672 | cellular_component | synaptic vesicle membrane |
| A | 0031432 | molecular_function | titin binding |
| A | 0031514 | cellular_component | motile cilium |
| A | 0031982 | cellular_component | vesicle |
| A | 0032465 | biological_process | regulation of cytokinesis |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0034704 | cellular_component | calcium channel complex |
| A | 0035458 | biological_process | cellular response to interferon-beta |
| A | 0043209 | cellular_component | myelin sheath |
| A | 0043539 | molecular_function | protein serine/threonine kinase activator activity |
| A | 0044305 | cellular_component | calyx of Held |
| A | 0044325 | molecular_function | transmembrane transporter binding |
| A | 0046427 | biological_process | positive regulation of receptor signaling pathway via JAK-STAT |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0048306 | molecular_function | calcium-dependent protein binding |
| A | 0050848 | biological_process | regulation of calcium-mediated signaling |
| A | 0051592 | biological_process | response to calcium ion |
| A | 0055117 | biological_process | regulation of cardiac muscle contraction |
| A | 0060291 | biological_process | long-term synaptic potentiation |
| A | 0060314 | biological_process | regulation of ryanodine-sensitive calcium-release channel activity |
| A | 0060315 | biological_process | negative regulation of ryanodine-sensitive calcium-release channel activity |
| A | 0071346 | biological_process | cellular response to type II interferon |
| A | 0072542 | molecular_function | protein phosphatase activator activity |
| A | 0097225 | cellular_component | sperm midpiece |
| A | 0097720 | biological_process | calcineurin-mediated signaling |
| A | 0098901 | biological_process | regulation of cardiac muscle cell action potential |
| A | 0099523 | cellular_component | presynaptic cytosol |
| A | 0140056 | biological_process | organelle localization by membrane tethering |
| A | 0140238 | biological_process | presynaptic endocytosis |
| A | 0141110 | molecular_function | transporter inhibitor activity |
| A | 1901842 | biological_process | negative regulation of high voltage-gated calcium channel activity |
| A | 1901844 | biological_process | regulation of cell communication by electrical coupling involved in cardiac conduction |
| A | 1902494 | cellular_component | catalytic complex |
| A | 1905913 | biological_process | negative regulation of calcium ion export across plasma membrane |
| A | 1990456 | biological_process | mitochondrion-endoplasmic reticulum membrane tethering |
| B | 0000086 | biological_process | G2/M transition of mitotic cell cycle |
| B | 0000922 | cellular_component | spindle pole |
| B | 0002027 | biological_process | regulation of heart rate |
| B | 0005246 | molecular_function | calcium channel regulator activity |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005513 | biological_process | detection of calcium ion |
| B | 0005515 | molecular_function | protein binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005634 | cellular_component | nucleus |
| B | 0005654 | cellular_component | nucleoplasm |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005813 | cellular_component | centrosome |
| B | 0005819 | cellular_component | spindle |
| B | 0005829 | cellular_component | cytosol |
| B | 0005876 | cellular_component | spindle microtubule |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006091 | biological_process | generation of precursor metabolites and energy |
| B | 0007186 | biological_process | G protein-coupled receptor signaling pathway |
| B | 0008076 | cellular_component | voltage-gated potassium channel complex |
| B | 0008218 | biological_process | bioluminescence |
| B | 0010856 | molecular_function | adenylate cyclase activator activity |
| B | 0010880 | biological_process | regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum |
| B | 0010881 | biological_process | regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion |
| B | 0016020 | cellular_component | membrane |
| B | 0016240 | biological_process | autophagosome membrane docking |
| B | 0019855 | molecular_function | calcium channel inhibitor activity |
| B | 0019901 | molecular_function | protein kinase binding |
| B | 0021762 | biological_process | substantia nigra development |
| B | 0030017 | cellular_component | sarcomere |
| B | 0030672 | cellular_component | synaptic vesicle membrane |
| B | 0031432 | molecular_function | titin binding |
| B | 0031514 | cellular_component | motile cilium |
| B | 0031982 | cellular_component | vesicle |
| B | 0032465 | biological_process | regulation of cytokinesis |
| B | 0032991 | cellular_component | protein-containing complex |
| B | 0034704 | cellular_component | calcium channel complex |
| B | 0035458 | biological_process | cellular response to interferon-beta |
| B | 0043209 | cellular_component | myelin sheath |
| B | 0043539 | molecular_function | protein serine/threonine kinase activator activity |
| B | 0044305 | cellular_component | calyx of Held |
| B | 0044325 | molecular_function | transmembrane transporter binding |
| B | 0046427 | biological_process | positive regulation of receptor signaling pathway via JAK-STAT |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0048306 | molecular_function | calcium-dependent protein binding |
| B | 0050848 | biological_process | regulation of calcium-mediated signaling |
| B | 0051592 | biological_process | response to calcium ion |
| B | 0055117 | biological_process | regulation of cardiac muscle contraction |
| B | 0060291 | biological_process | long-term synaptic potentiation |
| B | 0060314 | biological_process | regulation of ryanodine-sensitive calcium-release channel activity |
| B | 0060315 | biological_process | negative regulation of ryanodine-sensitive calcium-release channel activity |
| B | 0071346 | biological_process | cellular response to type II interferon |
| B | 0072542 | molecular_function | protein phosphatase activator activity |
| B | 0097225 | cellular_component | sperm midpiece |
| B | 0097720 | biological_process | calcineurin-mediated signaling |
| B | 0098901 | biological_process | regulation of cardiac muscle cell action potential |
| B | 0099523 | cellular_component | presynaptic cytosol |
| B | 0140056 | biological_process | organelle localization by membrane tethering |
| B | 0140238 | biological_process | presynaptic endocytosis |
| B | 0141110 | molecular_function | transporter inhibitor activity |
| B | 1901842 | biological_process | negative regulation of high voltage-gated calcium channel activity |
| B | 1901844 | biological_process | regulation of cell communication by electrical coupling involved in cardiac conduction |
| B | 1902494 | cellular_component | catalytic complex |
| B | 1905913 | biological_process | negative regulation of calcium ion export across plasma membrane |
| B | 1990456 | biological_process | mitochondrion-endoplasmic reticulum membrane tethering |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | binding site for residue TLA A 901 |
| Chain | Residue |
| A | GLY24 |
| A | HIS25 |
| A | LYS26 |
| A | ARG358 |
| A | LYS367 |
| A | LEU368 |
| A | HOH1024 |
| A | HOH1031 |
| A | HOH1063 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 902 |
| Chain | Residue |
| A | ASP272 |
| A | ASP274 |
| A | ASP276 |
| A | THR278 |
| A | GLU283 |
| A | HOH1007 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 903 |
| Chain | Residue |
| A | ASP308 |
| A | ASP310 |
| A | ASN312 |
| A | THR314 |
| A | GLU319 |
| A | HOH1003 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 904 |
| Chain | Residue |
| A | ASP381 |
| A | ASP383 |
| A | ASP385 |
| A | GLN387 |
| A | GLU392 |
| A | HOH1030 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue CA A 905 |
| Chain | Residue |
| A | ASP345 |
| A | ASP347 |
| A | ASN349 |
| A | TYR351 |
| A | GLU356 |
| A | HOH1102 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 906 |
| Chain | Residue |
| A | ARG109 |
| A | ARG122 |
| A | GLU124 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 907 |
| Chain | Residue |
| A | LYS107 |
| A | LYS126 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 908 |
| Chain | Residue |
| A | LYS-27 |
| A | LYS52 |
| A | SER269 |
| A | GLY365 |
| A | LYS367 |
| A | HOH1036 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 909 |
| Chain | Residue |
| A | LYS101 |
| A | ASP102 |
| A | VAL176 |
| A | GLN177 |
| A | LEU178 |
| A | HOH1132 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 910 |
| Chain | Residue |
| A | ASN164 |
| A | PHE165 |
| A | LYS166 |
| A | ASP180 |
| A | HIS181 |
| A | TYR182 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 501 |
| Chain | Residue |
| B | ASP272 |
| B | ASP274 |
| B | ASP276 |
| B | THR278 |
| B | GLU283 |
| B | HOH692 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 502 |
| Chain | Residue |
| B | ASP345 |
| B | ASP347 |
| B | ASN349 |
| B | TYR351 |
| B | GLU356 |
| B | HOH741 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 503 |
| Chain | Residue |
| B | ASP308 |
| B | ASP310 |
| B | ASN312 |
| B | THR314 |
| B | GLU319 |
| B | HOH691 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue CA B 504 |
| Chain | Residue |
| B | ASP381 |
| B | ASP383 |
| B | ASP385 |
| B | GLN387 |
| B | GLU392 |
| B | HOH643 |
| site_id | AD6 |
| Number of Residues | 3 |
| Details | binding site for residue NA B 505 |
| Chain | Residue |
| B | GLU111 |
| B | LYS113 |
| B | HOH735 |
| site_id | AD7 |
| Number of Residues | 4 |
| Details | binding site for residue NA B 506 |
| Chain | Residue |
| B | LYS113 |
| B | GLU115 |
| B | ARG122 |
| B | HOH748 |
| site_id | AD8 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 507 |
| Chain | Residue |
| B | ILE382 |
| B | GLN395 |
| site_id | AD9 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 508 |
| Chain | Residue |
| B | ARG109 |
| B | ARG122 |
| B | GLU124 |
| site_id | AE1 |
| Number of Residues | 1 |
| Details | binding site for residue EDO B 509 |
| Chain | Residue |
| B | LYS107 |
| site_id | AE2 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 510 |
| Chain | Residue |
| B | SER2 |
| B | GLU5 |
| B | GLN80 |
| site_id | AE3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 511 |
| Chain | Residue |
| B | GLN184 |
| B | ARG96 |
| B | THR97 |
| B | TYR182 |
| site_id | AE4 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 512 |
| Chain | Residue |
| B | GLU379 |
| B | HOH638 |
| site_id | AE5 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 513 |
| Chain | Residue |
| B | ARG338 |
| B | ARG342 |
| B | HOH778 |
| site_id | AE6 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 514 |
| Chain | Residue |
| A | ASN149 |
| A | TYR151 |
| A | TYR200 |
| B | GLU142 |
| B | GLU172 |
| site_id | AE7 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 515 |
| Chain | Residue |
| B | LYS101 |
| B | ASP102 |
| B | ASN135 |
| B | VAL176 |
| B | GLN177 |
| B | LEU178 |
| B | HOH641 |
| B | HOH680 |
Functional Information from PROSITE/UniProt
| site_id | PS00018 |
| Number of Residues | 13 |
| Details | EF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL |
| Chain | Residue | Details |
| A | ASP274-THR286 | |
| A | ASP310-THR322 | |
| A | ASP347-HIS359 | |
| A | ASP383-GLN395 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | Region: {"description":"Calmodulin-binding"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 70 |
| Details | Domain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 35 |
| Details | Domain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| 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_FI5 |
| Number of Residues | 20 |
| Details | Binding 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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 10 |
| Details | Binding 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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 10 |
| Details | Binding 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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"7093203","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Bensaad K.","Vousden K.H."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25944712","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine; by CaMK4","evidences":[{"source":"UniProtKB","id":"P0DP29","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | Modified 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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"24129315","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 4 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P62157","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI19 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"(Z)-2,3-didehydrotyrosine","evidences":[{"source":"PubMed","id":"8448132","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI20 |
| Number of Residues | 4 |
| Details | Cross-link: {"description":"5-imidazolinone (Ser-Gly)","evidences":[{"source":"PubMed","id":"8448132","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
