5K1B
Crystal structure of the UAF1/USP12 complex in F222 space group
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004197 | molecular_function | cysteine-type endopeptidase activity |
| A | 0004843 | molecular_function | cysteine-type deubiquitinase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006508 | biological_process | proteolysis |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0008234 | molecular_function | cysteine-type peptidase activity |
| A | 0016579 | biological_process | protein deubiquitination |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0031647 | biological_process | regulation of protein stability |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0101005 | molecular_function | deubiquitinase activity |
| B | 0000724 | biological_process | double-strand break repair via homologous recombination |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003690 | molecular_function | double-stranded DNA binding |
| B | 0003697 | molecular_function | single-stranded DNA binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005654 | cellular_component | nucleoplasm |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005764 | cellular_component | lysosome |
| B | 0005770 | cellular_component | late endosome |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006281 | biological_process | DNA repair |
| B | 0006974 | biological_process | DNA damage response |
| B | 0035800 | molecular_function | deubiquitinase activator activity |
| B | 0043130 | molecular_function | ubiquitin binding |
| B | 0046427 | biological_process | positive regulation of receptor signaling pathway via JAK-STAT |
| B | 0060255 | biological_process | regulation of macromolecule metabolic process |
| B | 0080090 | biological_process | regulation of primary metabolic process |
| B | 0090263 | biological_process | positive regulation of canonical Wnt signaling pathway |
| B | 1905168 | biological_process | positive regulation of double-strand break repair via homologous recombination |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 401 |
| Chain | Residue |
| A | CYS186 |
| A | CYS189 |
| A | CYS233 |
| A | CYS236 |
Functional Information from PROSITE/UniProt
| site_id | PS00678 |
| Number of Residues | 15 |
| Details | WD_REPEATS_1 Trp-Asp (WD) repeats signature. LISAssDtTVKVWNA |
| Chain | Residue | Details |
| B | LEU90-ALA104 | |
| B | VAL132-VAL146 |
| site_id | PS00972 |
| Number of Residues | 16 |
| Details | USP_1 Ubiquitin specific protease (USP) domain signature 1. GLvnfGNtCYCNSvLQ |
| Chain | Residue | Details |
| A | GLY40-GLN55 |
| site_id | PS00973 |
| Number of Residues | 19 |
| Details | USP_2 Ubiquitin specific protease (USP) domain signature 2. YdLvAVvvHcGsgpnr.GHY |
| Chain | Residue | Details |
| A | TYR300-TYR318 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 39 |
| Details | Repeat: {"description":"WD 1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 39 |
| Details | Repeat: {"description":"WD 2","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 39 |
| Details | Repeat: {"description":"WD 3","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 39 |
| Details | Repeat: {"description":"WD 4","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 39 |
| Details | Repeat: {"description":"WD 5","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 39 |
| Details | Repeat: {"description":"WD 8","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q8BH57","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU01035","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"27373336","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU01035","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"5K16","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5K1A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5K1B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5L8W","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"5K16","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5K1A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5K1B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5K1C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5L8W","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
