9CB3
E2F1-Cyclin F Interface
Functional Information from GO Data
Chain | GOid | namespace | contents |
B | 0000209 | biological_process | protein polyubiquitination |
B | 0005515 | molecular_function | protein binding |
B | 0005634 | cellular_component | nucleus |
B | 0005654 | cellular_component | nucleoplasm |
B | 0005737 | cellular_component | cytoplasm |
B | 0005813 | cellular_component | centrosome |
B | 0005829 | cellular_component | cytosol |
B | 0006338 | biological_process | chromatin remodeling |
B | 0006511 | biological_process | ubiquitin-dependent protein catabolic process |
B | 0006513 | biological_process | protein monoubiquitination |
B | 0006915 | biological_process | apoptotic process |
B | 0008013 | molecular_function | beta-catenin binding |
B | 0016567 | biological_process | protein ubiquitination |
B | 0019005 | cellular_component | SCF ubiquitin ligase complex |
B | 0019904 | molecular_function | protein domain specific binding |
B | 0031146 | biological_process | SCF-dependent proteasomal ubiquitin-dependent protein catabolic process |
B | 0031467 | cellular_component | Cul7-RING ubiquitin ligase complex |
B | 0031519 | cellular_component | PcG protein complex |
B | 0043161 | biological_process | proteasome-mediated ubiquitin-dependent protein catabolic process |
B | 0051457 | biological_process | maintenance of protein location in nucleus |
B | 0061564 | biological_process | axon development |
B | 0070936 | biological_process | protein K48-linked ubiquitination |
B | 0097602 | molecular_function | cullin family protein binding |
B | 0140677 | molecular_function | molecular function activator activity |
B | 0160072 | molecular_function | ubiquitin ligase complex scaffold activity |
B | 1904037 | biological_process | positive regulation of epithelial cell apoptotic process |
B | 1990444 | molecular_function | F-box domain binding |
B | 1990756 | molecular_function | ubiquitin-like ligase-substrate adaptor activity |
B | 1990757 | molecular_function | ubiquitin ligase activator activity |
Functional Information from PROSITE/UniProt
site_id | PS00292 |
Number of Residues | 32 |
Details | CYCLINS Cyclins signature. RyiLidWLvevatmkdFtslcLhlTVeCVDRY |
Chain | Residue | Details |
A | ARG310-TYR341 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 47 |
Details | Domain: {"description":"F-box","evidences":[{"source":"PROSITE-ProRule","id":"PRU00080","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 117 |
Details | Domain: {"description":"Cyclin N-terminal","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | Motif: {"description":"D box 1","evidences":[{"source":"PubMed","id":"27653696","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | Motif: {"description":"D box 2","evidences":[{"source":"PubMed","id":"27653696","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | Motif: {"description":"D box 3","evidences":[{"source":"PubMed","id":"27653696","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 3 |
Details | Motif: {"description":"D box 4","evidences":[{"source":"PubMed","id":"27653696","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)","evidences":[{"source":"PubMed","id":"25114211","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |