6IIL
USP14 catalytic domain bind to IU1-47
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004843 | molecular_function | cysteine-type deubiquitinase activity |
| A | 0016579 | biological_process | protein deubiquitination |
| A | 0043161 | biological_process | proteasome-mediated ubiquitin-dependent protein catabolic process |
| B | 0004843 | molecular_function | cysteine-type deubiquitinase activity |
| B | 0016579 | biological_process | protein deubiquitination |
| B | 0043161 | biological_process | proteasome-mediated ubiquitin-dependent protein catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | binding site for residue A8F A 501 |
| Chain | Residue |
| A | GLN197 |
| A | TYR476 |
| A | GLN198 |
| A | ASP199 |
| A | PHE331 |
| A | LYS342 |
| A | SER431 |
| A | SER432 |
| A | SER433 |
| A | TYR436 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue A8F B 501 |
| Chain | Residue |
| B | GLU188 |
| B | GLN197 |
| B | GLN198 |
| B | ASP199 |
| B | PHE331 |
| B | SER431 |
| B | SER432 |
| B | SER433 |
| B | TYR436 |
| B | TYR476 |
Functional Information from PROSITE/UniProt
| site_id | PS00972 |
| Number of Residues | 16 |
| Details | USP_1 Ubiquitin specific protease (USP) domain signature 1. GLtnlGNtCYMNAtVQ |
| Chain | Residue | Details |
| A | GLY106-GLN121 |
| site_id | PS00973 |
| Number of Residues | 19 |
| Details | USP_2 Ubiquitin specific protease (USP) domain signature 2. YdLqAVltHqGrssss.GHY |
| Chain | Residue | Details |
| A | TYR418-TYR436 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"16211010","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10092","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10093","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19367720","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9JMA1","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
