9R2I
Cryo-EM structure of the complex CDK16:CCNY:14-3-3
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0002028 | biological_process | regulation of sodium ion transport |
| A | 0003779 | molecular_function | actin binding |
| A | 0005159 | molecular_function | insulin-like growth factor receptor binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006713 | biological_process | glucocorticoid catabolic process |
| A | 0006886 | biological_process | intracellular protein transport |
| A | 0007165 | biological_process | signal transduction |
| A | 0008104 | biological_process | intracellular protein localization |
| A | 0014704 | cellular_component | intercalated disc |
| A | 0017080 | molecular_function | sodium channel regulator activity |
| A | 0019899 | molecular_function | enzyme binding |
| A | 0019904 | molecular_function | protein domain specific binding |
| A | 0021762 | biological_process | substantia nigra development |
| A | 0035259 | molecular_function | nuclear glucocorticoid receptor binding |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042921 | biological_process | nuclear receptor-mediated glucocorticoid signaling pathway |
| A | 0044325 | molecular_function | transmembrane transporter binding |
| A | 0045202 | cellular_component | synapse |
| A | 0045664 | biological_process | regulation of neuron differentiation |
| A | 0045893 | biological_process | positive regulation of DNA-templated transcription |
| A | 0046982 | molecular_function | protein heterodimerization activity |
| A | 0048167 | biological_process | regulation of synaptic plasticity |
| A | 0050774 | biological_process | negative regulation of dendrite morphogenesis |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0086010 | biological_process | membrane depolarization during action potential |
| A | 0098793 | cellular_component | presynapse |
| A | 0098978 | cellular_component | glutamatergic synapse |
| A | 0099171 | biological_process | presynaptic modulation of chemical synaptic transmission |
| A | 0150048 | cellular_component | cerebellar granule cell to Purkinje cell synapse |
| B | 0002028 | biological_process | regulation of sodium ion transport |
| B | 0003779 | molecular_function | actin binding |
| B | 0005159 | molecular_function | insulin-like growth factor receptor binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006713 | biological_process | glucocorticoid catabolic process |
| B | 0006886 | biological_process | intracellular protein transport |
| B | 0007165 | biological_process | signal transduction |
| B | 0008104 | biological_process | intracellular protein localization |
| B | 0014704 | cellular_component | intercalated disc |
| B | 0017080 | molecular_function | sodium channel regulator activity |
| B | 0019899 | molecular_function | enzyme binding |
| B | 0019904 | molecular_function | protein domain specific binding |
| B | 0021762 | biological_process | substantia nigra development |
| B | 0035259 | molecular_function | nuclear glucocorticoid receptor binding |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042921 | biological_process | nuclear receptor-mediated glucocorticoid signaling pathway |
| B | 0044325 | molecular_function | transmembrane transporter binding |
| B | 0045202 | cellular_component | synapse |
| B | 0045664 | biological_process | regulation of neuron differentiation |
| B | 0045893 | biological_process | positive regulation of DNA-templated transcription |
| B | 0046982 | molecular_function | protein heterodimerization activity |
| B | 0048167 | biological_process | regulation of synaptic plasticity |
| B | 0050774 | biological_process | negative regulation of dendrite morphogenesis |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0086010 | biological_process | membrane depolarization during action potential |
| B | 0098793 | cellular_component | presynapse |
| B | 0098978 | cellular_component | glutamatergic synapse |
| B | 0099171 | biological_process | presynaptic modulation of chemical synaptic transmission |
| B | 0150048 | cellular_component | cerebellar granule cell to Purkinje cell synapse |
| D | 0000086 | biological_process | G2/M transition of mitotic cell cycle |
| D | 0000307 | cellular_component | cyclin-dependent protein kinase holoenzyme complex |
| D | 0000308 | cellular_component | cytoplasmic cyclin-dependent protein kinase holoenzyme complex |
| D | 0005515 | molecular_function | protein binding |
| D | 0005634 | cellular_component | nucleus |
| D | 0005654 | cellular_component | nucleoplasm |
| D | 0005730 | cellular_component | nucleolus |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0007283 | biological_process | spermatogenesis |
| D | 0010508 | biological_process | positive regulation of autophagy |
| D | 0016538 | molecular_function | cyclin-dependent protein serine/threonine kinase regulator activity |
| D | 0045737 | biological_process | positive regulation of cyclin-dependent protein serine/threonine kinase activity |
| D | 0060828 | biological_process | regulation of canonical Wnt signaling pathway |
| D | 0061575 | molecular_function | cyclin-dependent protein serine/threonine kinase activator activity |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGTYATVYkGkskltdnl..........VALK |
| Chain | Residue | Details |
| C | LEU171-LYS194 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpqNLLI |
| Chain | Residue | Details |
| C | VAL282-ILE294 |
| site_id | PS00796 |
| Number of Residues | 11 |
| Details | 1433_1 14-3-3 proteins signature 1. RNLLSVAYKNV |
| Chain | Residue | Details |
| A | ARG42-VAL52 |
| site_id | PS00797 |
| Number of Residues | 20 |
| Details | 1433_2 14-3-3 proteins signature 2. YKDSTLIMQLLRDNLTLWTS |
| Chain | Residue | Details |
| A | TYR216-SER235 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Site: {"description":"Interaction with phosphoserine on interacting protein"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylglycine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"AUG-2005","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P68510","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 281 |
| Details | Domain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q04735","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q04735","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 122 |
| Details | Domain: {"description":"Cyclin N-terminal"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine; by CDK14","evidences":[{"source":"PubMed","id":"24794231","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphoserine; by CDK14","evidences":[{"source":"PubMed","id":"24794231","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24794231","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI19 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q8BGU5","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI20 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22184064","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24794231","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
