4F8C
Structure of the Cif:Nedd8 complex - Yersinia pseudotuberculosis Cycle Inhibiting Factor in complex with human Nedd8
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005654 | cellular_component | nucleoplasm |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006357 | biological_process | regulation of transcription by RNA polymerase II |
| B | 0006508 | biological_process | proteolysis |
| B | 0006511 | biological_process | ubiquitin-dependent protein catabolic process |
| B | 0008104 | biological_process | intracellular protein localization |
| B | 0009653 | biological_process | anatomical structure morphogenesis |
| B | 0016567 | biological_process | protein ubiquitination |
| B | 0019941 | biological_process | modification-dependent protein catabolic process |
| B | 0030162 | biological_process | regulation of proteolysis |
| B | 0031386 | molecular_function | protein tag activity |
| B | 0031625 | molecular_function | ubiquitin protein ligase binding |
| B | 0036211 | biological_process | protein modification process |
| B | 0045116 | biological_process | protein neddylation |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0072757 | biological_process | cellular response to camptothecin |
| B | 0098794 | cellular_component | postsynapse |
| B | 0098978 | cellular_component | glutamatergic synapse |
| B | 0150052 | biological_process | regulation of postsynapse assembly |
| D | 0005515 | molecular_function | protein binding |
| D | 0005634 | cellular_component | nucleus |
| D | 0005654 | cellular_component | nucleoplasm |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0006357 | biological_process | regulation of transcription by RNA polymerase II |
| D | 0006508 | biological_process | proteolysis |
| D | 0006511 | biological_process | ubiquitin-dependent protein catabolic process |
| D | 0008104 | biological_process | intracellular protein localization |
| D | 0009653 | biological_process | anatomical structure morphogenesis |
| D | 0016567 | biological_process | protein ubiquitination |
| D | 0019941 | biological_process | modification-dependent protein catabolic process |
| D | 0030162 | biological_process | regulation of proteolysis |
| D | 0031386 | molecular_function | protein tag activity |
| D | 0031625 | molecular_function | ubiquitin protein ligase binding |
| D | 0036211 | biological_process | protein modification process |
| D | 0045116 | biological_process | protein neddylation |
| D | 0070062 | cellular_component | extracellular exosome |
| D | 0072757 | biological_process | cellular response to camptothecin |
| D | 0098794 | cellular_component | postsynapse |
| D | 0098978 | cellular_component | glutamatergic synapse |
| D | 0150052 | biological_process | regulation of postsynapse assembly |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 301 |
| Chain | Residue |
| A | LEU57 |
| A | ASN60 |
| A | VAL61 |
| A | SER108 |
| A | SER109 |
| A | ARG111 |
| A | HOH510 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 302 |
| Chain | Residue |
| A | ILE235 |
| A | ASP236 |
| A | HIS239 |
| A | ILE240 |
| A | HIS226 |
| A | GLY229 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO C 301 |
| Chain | Residue |
| C | THR225 |
| C | HIS226 |
| C | ILE235 |
| C | ASP236 |
| C | HIS239 |
| C | ILE240 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO C 302 |
| Chain | Residue |
| C | LEU57 |
| C | ASN60 |
| C | VAL61 |
| C | SER108 |
| C | ARG111 |
| C | HOH530 |
Functional Information from PROSITE/UniProt
| site_id | PS00299 |
| Number of Residues | 26 |
| Details | UBIQUITIN_1 Ubiquitin domain signature. KerVeEkegIPpqqQrLIYsGkqmnD |
| Chain | Residue | Details |
| B | LYS27-ASP52 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"19308257","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"22691497","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"evidences":[{"source":"UniProtKB","id":"Q63KH5","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Region: {"description":"Interaction with UBE1C","evidences":[{"source":"PubMed","id":"14690597","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Site: {"description":"Interaction with UBE1C","evidences":[{"source":"PubMed","id":"14690597","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"(Microbial infection) Deamidated glutamine","evidences":[{"source":"PubMed","id":"20688984","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21903097","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23175788","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23589306","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26632597","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P29595","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
