6S9K
Structure of 14-3-3 gamma in complex with caspase-2 peptide containing 14-3-3 binding motif Ser139 and NLS
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0002842 | biological_process | positive regulation of T cell mediated immune response to tumor cell |
| A | 0003723 | molecular_function | RNA binding |
| A | 0005080 | molecular_function | protein kinase C binding |
| A | 0005159 | molecular_function | insulin-like growth factor receptor binding |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0005829 | cellular_component | cytosol |
| A | 0005925 | cellular_component | focal adhesion |
| A | 0006469 | biological_process | negative regulation of protein kinase activity |
| A | 0007165 | biological_process | signal transduction |
| A | 0008104 | biological_process | intracellular protein localization |
| A | 0008426 | molecular_function | protein kinase C inhibitor activity |
| A | 0009966 | biological_process | regulation of signal transduction |
| A | 0016020 | cellular_component | membrane |
| A | 0019904 | molecular_function | protein domain specific binding |
| A | 0022409 | biological_process | positive regulation of cell-cell adhesion |
| A | 0030971 | molecular_function | receptor tyrosine kinase binding |
| A | 0031982 | cellular_component | vesicle |
| A | 0032869 | biological_process | cellular response to insulin stimulus |
| A | 0032880 | biological_process | regulation of protein localization |
| A | 0042149 | biological_process | cellular response to glucose starvation |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0045202 | cellular_component | synapse |
| A | 0045664 | biological_process | regulation of neuron differentiation |
| A | 0048167 | biological_process | regulation of synaptic plasticity |
| A | 0050870 | biological_process | positive regulation of T cell activation |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0098793 | cellular_component | presynapse |
| A | 0140031 | molecular_function | phosphorylation-dependent protein binding |
| A | 0140311 | molecular_function | protein sequestering activity |
| A | 1904262 | biological_process | negative regulation of TORC1 signaling |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | binding site for residue CFH A 301 |
| Chain | Residue |
| A | GLU15 |
| A | ASN43 |
| A | LEU44 |
| A | VAL47 |
| A | HOH416 |
| B | PRO143 |
| B | CYS145 |
| B | SER147 |
| B | CYS148 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue CFH A 302 |
| Chain | Residue |
| A | LEU221 |
| A | LEU225 |
| A | ASP228 |
| B | LEU150 |
| B | TYR151 |
| B | LEU154 |
| B | THR158 |
| B | HOH207 |
Functional Information from PROSITE/UniProt
| site_id | PS00796 |
| Number of Residues | 11 |
| Details | 1433_1 14-3-3 proteins signature 1. RNLLSVAYKNV |
| Chain | Residue | Details |
| A | ARG42-VAL52 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Site: {"description":"Interaction with phosphoserine on interacting protein","evidences":[{"source":"PubMed","id":"17085597","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylvaline; partial","evidences":[{"source":"PubMed","id":"14534293","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Boldt K.","von Kriegsheim A.F.","Zebisch A.","Kolch W."]}},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2005","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Claeys D."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P61983","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Boldt K.","von Kriegsheim A.F.","Zebisch A.","Kolch W."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P61983","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
