1C4Z
STRUCTURE OF AN E6AP-UBCH7 COMPLEX: INSIGHTS INTO THE UBIQUITINATION PATHWAY
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000209 | biological_process | protein polyubiquitination |
| A | 0004842 | molecular_function | ubiquitin-protein transferase activity |
| A | 0061630 | molecular_function | ubiquitin protein ligase activity |
| B | 0000209 | biological_process | protein polyubiquitination |
| B | 0004842 | molecular_function | ubiquitin-protein transferase activity |
| B | 0061630 | molecular_function | ubiquitin protein ligase activity |
| C | 0000209 | biological_process | protein polyubiquitination |
| C | 0004842 | molecular_function | ubiquitin-protein transferase activity |
| C | 0061630 | molecular_function | ubiquitin protein ligase activity |
| D | 0000151 | cellular_component | ubiquitin ligase complex |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0000209 | biological_process | protein polyubiquitination |
| D | 0003713 | molecular_function | transcription coactivator activity |
| D | 0003723 | molecular_function | RNA binding |
| D | 0004842 | molecular_function | ubiquitin-protein transferase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005634 | cellular_component | nucleus |
| D | 0005654 | cellular_component | nucleoplasm |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0006355 | biological_process | regulation of DNA-templated transcription |
| D | 0006511 | biological_process | ubiquitin-dependent protein catabolic process |
| D | 0008283 | biological_process | cell population proliferation |
| D | 0016567 | biological_process | protein ubiquitination |
| D | 0016740 | molecular_function | transferase activity |
| D | 0019787 | molecular_function | ubiquitin-like protein transferase activity |
| D | 0019899 | molecular_function | enzyme binding |
| D | 0031398 | biological_process | positive regulation of protein ubiquitination |
| D | 0031625 | molecular_function | ubiquitin protein ligase binding |
| D | 0032446 | biological_process | protein modification by small protein conjugation |
| D | 0036211 | biological_process | protein modification process |
| D | 0044770 | biological_process | cell cycle phase transition |
| D | 0045893 | biological_process | positive regulation of DNA-templated transcription |
| D | 0061631 | molecular_function | ubiquitin conjugating enzyme activity |
| D | 0070979 | biological_process | protein K11-linked ubiquitination |
| D | 0071383 | biological_process | cellular response to steroid hormone stimulus |
| D | 0071385 | biological_process | cellular response to glucocorticoid stimulus |
| D | 0097027 | molecular_function | ubiquitin-protein transferase activator activity |
| D | 1903955 | biological_process | positive regulation of protein targeting to mitochondrion |
Functional Information from PROSITE/UniProt
| site_id | PS00183 |
| Number of Residues | 16 |
| Details | UBC_1 Ubiquitin-conjugating (UBC) active site signature. YHPNIdek.GqVCLpvI |
| Chain | Residue | Details |
| D | TYR75-ILE90 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Glycyl thioester intermediate"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphotyrosine; by ABL1","evidences":[{"source":"PubMed","id":"23581475","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Glycyl thioester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10133","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 6 |
| Details | a catalytic site defined by CSA, PubMed 10558980 |
| Chain | Residue | Details |
| A | GLU550 | |
| A | ARG506 | |
| A | CYS820 | |
| A | HIS818 | |
| A | GLU539 | |
| A | ASP607 |
| site_id | CSA2 |
| Number of Residues | 6 |
| Details | a catalytic site defined by CSA, PubMed 10558980 |
| Chain | Residue | Details |
| B | GLU550 | |
| B | ARG506 | |
| B | CYS820 | |
| B | HIS818 | |
| B | GLU539 | |
| B | ASP607 |
| site_id | CSA3 |
| Number of Residues | 6 |
| Details | a catalytic site defined by CSA, PubMed 10558980 |
| Chain | Residue | Details |
| C | GLU550 | |
| C | ARG506 | |
| C | CYS820 | |
| C | HIS818 | |
| C | GLU539 | |
| C | ASP607 |
| site_id | MCSA1 |
| Number of Residues | 1 |
| Details | M-CSA 438 |
| Chain | Residue | Details |
| D | CYS86 | nucleofuge |
| A | GLU539 | unknown |
| A | GLU550 | unknown |
| A | ASP607 | electrostatic stabiliser |
| A | HIS818 | |
| A | CYS820 | covalent catalysis |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 438 |
| Chain | Residue | Details |
| B | ARG506 | unknown |
| B | GLU539 | unknown |
| B | GLU550 | unknown |
| B | ASP607 | electrostatic stabiliser |
| B | HIS818 | |
| B | CYS820 | covalent catalysis |
| site_id | MCSA3 |
| Number of Residues | 6 |
| Details | M-CSA 438 |
| Chain | Residue | Details |
| C | ARG506 | unknown |
| C | GLU539 | unknown |
| C | GLU550 | unknown |
| C | ASP607 | electrostatic stabiliser |
| C | HIS818 | |
| C | CYS820 | covalent catalysis |
