8WG5
Cryo-EM structure of USP16 bound to H2AK119Ub nucleosome
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000786 | cellular_component | nucleosome |
| A | 0003677 | molecular_function | DNA binding |
| A | 0030527 | molecular_function | structural constituent of chromatin |
| A | 0046982 | molecular_function | protein heterodimerization activity |
| B | 0003677 | molecular_function | DNA binding |
| B | 0030527 | molecular_function | structural constituent of chromatin |
| B | 0046982 | molecular_function | protein heterodimerization activity |
| C | 0000786 | cellular_component | nucleosome |
| C | 0003677 | molecular_function | DNA binding |
| C | 0030527 | molecular_function | structural constituent of chromatin |
| C | 0046982 | molecular_function | protein heterodimerization activity |
| D | 0000786 | cellular_component | nucleosome |
| D | 0003677 | molecular_function | DNA binding |
| D | 0030527 | molecular_function | structural constituent of chromatin |
| D | 0046982 | molecular_function | protein heterodimerization activity |
| E | 0000786 | cellular_component | nucleosome |
| E | 0003677 | molecular_function | DNA binding |
| E | 0030527 | molecular_function | structural constituent of chromatin |
| E | 0046982 | molecular_function | protein heterodimerization activity |
| F | 0003677 | molecular_function | DNA binding |
| F | 0030527 | molecular_function | structural constituent of chromatin |
| F | 0046982 | molecular_function | protein heterodimerization activity |
| G | 0000786 | cellular_component | nucleosome |
| G | 0003677 | molecular_function | DNA binding |
| G | 0030527 | molecular_function | structural constituent of chromatin |
| G | 0046982 | molecular_function | protein heterodimerization activity |
| H | 0000786 | cellular_component | nucleosome |
| H | 0003677 | molecular_function | DNA binding |
| H | 0030527 | molecular_function | structural constituent of chromatin |
| H | 0046982 | molecular_function | protein heterodimerization activity |
| M | 0000278 | biological_process | mitotic cell cycle |
| M | 0003713 | molecular_function | transcription coactivator activity |
| M | 0004197 | molecular_function | cysteine-type endopeptidase activity |
| M | 0004843 | molecular_function | cysteine-type deubiquitinase activity |
| M | 0005634 | cellular_component | nucleus |
| M | 0005654 | cellular_component | nucleoplasm |
| M | 0005737 | cellular_component | cytoplasm |
| M | 0006325 | biological_process | chromatin organization |
| M | 0006338 | biological_process | chromatin remodeling |
| M | 0006357 | biological_process | regulation of transcription by RNA polymerase II |
| M | 0006508 | biological_process | proteolysis |
| M | 0006974 | biological_process | DNA damage response |
| M | 0008233 | molecular_function | peptidase activity |
| M | 0008234 | molecular_function | cysteine-type peptidase activity |
| M | 0008270 | molecular_function | zinc ion binding |
| M | 0010468 | biological_process | regulation of gene expression |
| M | 0016579 | biological_process | protein deubiquitination |
| M | 0016787 | molecular_function | hydrolase activity |
| M | 0035520 | biological_process | monoubiquitinated protein deubiquitination |
| M | 0042393 | molecular_function | histone binding |
| M | 0043024 | molecular_function | ribosomal small subunit binding |
| M | 0043130 | molecular_function | ubiquitin binding |
| M | 0045893 | biological_process | positive regulation of DNA-templated transcription |
| M | 0045901 | biological_process | positive regulation of translational elongation |
| M | 0045944 | biological_process | positive regulation of transcription by RNA polymerase II |
| M | 0046872 | molecular_function | metal ion binding |
| M | 0051289 | biological_process | protein homotetramerization |
| M | 0051301 | biological_process | cell division |
| M | 0051726 | biological_process | regulation of cell cycle |
| M | 0090070 | biological_process | positive regulation of ribosome biogenesis |
| M | 0140014 | biological_process | mitotic nuclear division |
| M | 0140950 | molecular_function | histone H2A deubiquitinase activity |
Functional Information from PROSITE/UniProt
| site_id | PS00046 |
| Number of Residues | 7 |
| Details | HISTONE_H2A Histone H2A signature. AGLqFPV |
| Chain | Residue | Details |
| C | ALA21-VAL27 |
| site_id | PS00299 |
| Number of Residues | 26 |
| Details | UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD |
| Chain | Residue | Details |
| U | LYS27-ASP52 |
| site_id | PS00357 |
| Number of Residues | 23 |
| Details | HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG |
| Chain | Residue | Details |
| D | ARG92-GLY114 |
| site_id | PS00959 |
| Number of Residues | 9 |
| Details | HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI |
| Chain | Residue | Details |
| A | PRO66-ILE74 |
| site_id | PS00972 |
| Number of Residues | 16 |
| Details | USP_1 Ubiquitin specific protease (USP) domain signature 1. GLsnlGNtCFFNAvMQ |
| Chain | Residue | Details |
| M | GLY197-GLN212 |
| site_id | PS00973 |
| Number of Residues | 18 |
| Details | USP_2 Ubiquitin specific protease (USP) domain signature 2. YsLyGVveHsGtmrs..GHY |
| Chain | Residue | Details |
| M | TYR742-TYR759 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 |
| Chain | Residue | Details |
| D | LYS34 | |
| D | LYS116 | |
| D | LYS120 | |
| H | LYS34 | |
| H | LYS116 | |
| H | LYS120 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: PolyADP-ribosyl glutamic acid => ECO:0000250|UniProtKB:Q64475 |
| Chain | Residue | Details |
| D | GLU35 | |
| H | GLU35 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by AMPK => ECO:0000250|UniProtKB:Q8CGP1 |
| Chain | Residue | Details |
| D | SER36 | |
| H | SER36 | |
| G | LYS74 | |
| G | LYS75 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732 |
| Chain | Residue | Details |
| D | LYS43 | |
| M | HIS103 | |
| M | CYS116 | |
| M | CYS119 | |
| D | LYS85 | |
| H | LYS43 | |
| H | LYS85 | |
| M | CYS74 | |
| M | CYS77 | |
| M | CYS82 | |
| M | HIS90 | |
| M | HIS94 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:16627869 |
| Chain | Residue | Details |
| D | LYS46 | |
| D | LYS108 | |
| H | LYS46 | |
| H | LYS108 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000269|PubMed:24681537 |
| Chain | Residue | Details |
| D | LYS57 | |
| H | LYS57 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Dimethylated arginine => ECO:0000250|UniProtKB:Q96A08 |
| Chain | Residue | Details |
| D | ARG79 | |
| H | ARG79 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | MOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08 |
| Chain | Residue | Details |
| D | ARG86 | |
| D | ARG92 | |
| H | ARG86 | |
| H | ARG92 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q00729 |
| Chain | Residue | Details |
| D | THR115 | |
| H | THR115 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | CARBOHYD: O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 |
| Chain | Residue | Details |
| D | SER112 | |
| H | SER112 | |
| F | LYS91 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:21726816 |
| Chain | Residue | Details |
| D | LYS34 | |
| H | LYS34 | |
| F | LYS59 | |
| F | LYS79 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 4 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:16627869, ECO:0000269|PubMed:16713563 |
| Chain | Residue | Details |
| D | LYS120 | |
| H | LYS120 |
