7AY2
Crystal structure of truncated USP1-UAF1 reacted with ubiquitin-prg
Functional Information from GO Data
Chain | GOid | namespace | contents |
B | 0004197 | molecular_function | cysteine-type endopeptidase activity |
B | 0004843 | molecular_function | cysteine-type deubiquitinase activity |
B | 0006282 | biological_process | regulation of DNA repair |
B | 0016579 | biological_process | protein deubiquitination |
E | 0004197 | molecular_function | cysteine-type endopeptidase activity |
E | 0004843 | molecular_function | cysteine-type deubiquitinase activity |
E | 0006282 | biological_process | regulation of DNA repair |
E | 0016579 | biological_process | protein deubiquitination |
Functional Information from PROSITE/UniProt
site_id | PS00299 |
Number of Residues | 26 |
Details | UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD |
Chain | Residue | Details |
C | LYS27-ASP52 |
site_id | PS00972 |
Number of Residues | 16 |
Details | USP_1 Ubiquitin specific protease (USP) domain signature 1. GLnnlGNtCYLNSiLQ |
Chain | Residue | Details |
B | GLY82-GLN97 |
site_id | PS00973 |
Number of Residues | 19 |
Details | USP_2 Ubiquitin specific protease (USP) domain signature 2. YgLfAVvmHsGitiss.GHY |
Chain | Residue | Details |
B | TYR576-TYR594 |
site_id | PS00678 |
Number of Residues | 15 |
Details | WD_REPEATS_1 Trp-Asp (WD) repeats signature. LISAssDtTVKVWNA |
Chain | Residue | Details |
A | LEU90-ALA104 | |
A | VAL132-VAL146 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:15694335, ECO:0000269|PubMed:16531995, ECO:0000269|PubMed:26388029 |
Chain | Residue | Details |
B | CYS90 | |
E | CYS90 | |
F | ARG54 | |
F | ARG72 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10092, ECO:0000255|PROSITE-ProRule:PRU10093 |
Chain | Residue | Details |
C | HIS68 | |
F | HIS68 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: Cleavage; by autolysis => ECO:0000269|PubMed:16531995 |
Chain | Residue | Details |
C | SER65 | |
F | SER65 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
B | SER67 | |
E | SER67 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
B | GLU507 | |
E | GLU507 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
C | LYS63 | |
F | LYS63 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q8BJQ2 |
Chain | Residue | Details |
C | LYS11 | |
C | LYS48 | |
F | LYS11 | |
F | LYS48 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860 |
Chain | Residue | Details |
C | LYS27 | |
F | LYS27 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577, ECO:0000269|PubMed:34239127 |
Chain | Residue | Details |
C | LYS29 | |
F | LYS29 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577 |
Chain | Residue | Details |
C | LYS33 | |
F | LYS33 |