3IHR
Crystal Structure of Uch37
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003723 | molecular_function | RNA binding |
| A | 0004843 | molecular_function | cysteine-type deubiquitinase activity |
| A | 0004866 | molecular_function | endopeptidase inhibitor activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005730 | cellular_component | nucleolus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006275 | biological_process | regulation of DNA replication |
| A | 0006338 | biological_process | chromatin remodeling |
| A | 0006511 | biological_process | ubiquitin-dependent protein catabolic process |
| A | 0016579 | biological_process | protein deubiquitination |
| A | 0031011 | cellular_component | Ino80 complex |
| A | 0032435 | biological_process | negative regulation of proteasomal ubiquitin-dependent protein catabolic process |
| A | 0033044 | biological_process | regulation of chromosome organization |
| A | 0045880 | biological_process | positive regulation of smoothened signaling pathway |
| A | 0045893 | biological_process | positive regulation of DNA-templated transcription |
| A | 0051726 | biological_process | regulation of cell cycle |
| A | 0060382 | biological_process | regulation of DNA strand elongation |
| A | 0061136 | biological_process | regulation of proteasomal protein catabolic process |
| A | 0070628 | molecular_function | proteasome binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE FMT A 329 |
| Chain | Residue |
| A | ALA80 |
| A | SER95 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FMT A 330 |
| Chain | Residue |
| A | TRP36 |
| A | SER37 |
| A | LEU38 |
| A | LYS265 |
| A | MSE268 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA A 331 |
| Chain | Residue |
| A | ASP75 |
| A | GLN119 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU01393","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01393","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"PROSITE-ProRule","id":"PRU01393","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Site: {"description":"Important for enzyme activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU01393","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9WUP7","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| 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 | 4 |
| Details | Annotated By Reference To The Literature 1uch |
| Chain | Residue | Details |
| A | ASP179 | |
| A | HIS164 | |
| A | CYS88 | |
| A | GLN82 |
