4R62
Structure of Rad6~Ub
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000209 | biological_process | protein polyubiquitination |
| A | 0000722 | biological_process | telomere maintenance via recombination |
| A | 0000724 | biological_process | double-strand break repair via homologous recombination |
| A | 0000781 | cellular_component | chromosome, telomeric region |
| A | 0000785 | cellular_component | chromatin |
| A | 0003697 | molecular_function | single-stranded DNA binding |
| A | 0004842 | molecular_function | ubiquitin-protein transferase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006281 | biological_process | DNA repair |
| A | 0006325 | biological_process | chromatin organization |
| A | 0006353 | biological_process | DNA-templated transcription termination |
| A | 0006366 | biological_process | transcription by RNA polymerase II |
| A | 0006511 | biological_process | ubiquitin-dependent protein catabolic process |
| A | 0009302 | biological_process | sno(s)RNA transcription |
| A | 0016567 | biological_process | protein ubiquitination |
| A | 0016740 | molecular_function | transferase activity |
| A | 0017116 | molecular_function | single-stranded DNA helicase activity |
| A | 0030435 | biological_process | sporulation resulting in formation of a cellular spore |
| A | 0031509 | biological_process | subtelomeric heterochromatin formation |
| A | 0031571 | biological_process | mitotic G1 DNA damage checkpoint signaling |
| A | 0032508 | biological_process | DNA duplex unwinding |
| A | 0033503 | cellular_component | HULC complex |
| A | 0034620 | biological_process | cellular response to unfolded protein |
| A | 0036503 | biological_process | ERAD pathway |
| A | 0042138 | biological_process | meiotic DNA double-strand break formation |
| A | 0042275 | biological_process | error-free postreplication DNA repair |
| A | 0042276 | biological_process | error-prone translesion synthesis |
| A | 0043161 | biological_process | proteasome-mediated ubiquitin-dependent protein catabolic process |
| A | 0061631 | molecular_function | ubiquitin conjugating enzyme activity |
| A | 0070628 | molecular_function | proteasome binding |
| A | 0070987 | biological_process | error-free translesion synthesis |
| A | 0071596 | biological_process | ubiquitin-dependent protein catabolic process via the N-end rule pathway |
| A | 0071629 | biological_process | cytoplasm protein quality control by the ubiquitin-proteasome system |
| A | 0090089 | biological_process | regulation of dipeptide transport |
| A | 0097505 | cellular_component | Rad6-Rad18 complex |
| A | 0120174 | biological_process | stress-induced homeostatically regulated protein degradation pathway |
| A | 1990303 | cellular_component | UBR1-RAD6 ubiquitin ligase complex |
| A | 1990304 | cellular_component | MUB1-RAD6-UBR2 ubiquitin ligase complex |
| A | 1990305 | cellular_component | RAD6-UBR2 ubiquitin ligase complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT A 201 |
| Chain | Residue |
| A | HIS69 |
| A | VAL70 |
| A | ILE87 |
Functional Information from PROSITE/UniProt
| site_id | PS00299 |
| Number of Residues | 26 |
| Details | UBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD |
| Chain | Residue | Details |
| B | LYS27-ASP52 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | SITE: Interacts with activating enzyme |
| Chain | Residue | Details |
| B | ARG54 | |
| B | ARG72 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | SITE: Essential for function |
| Chain | Residue | Details |
| B | HIS68 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by PINK1 => ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291 |
| Chain | Residue | Details |
| B | SER65 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: (Microbial infection) ADP-ribosylthreonine => ECO:0000269|PubMed:32330457 |
| Chain | Residue | Details |
| B | THR66 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: ADP-ribosylglycine => ECO:0000269|PubMed:28525742 |
| Chain | Residue | Details |
| B | GLY76 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603 |
| Chain | Residue | Details |
| B | LYS6 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) |
| Chain | Residue | Details |
| B | GLY76 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16443603, ECO:0000269|PubMed:16543144 |
| Chain | Residue | Details |
| B | LYS11 | |
| B | LYS48 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:15466860 |
| Chain | Residue | Details |
| B | LYS27 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| 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 |
| B | LYS29 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:25752577 |
| Chain | Residue | Details |
| B | LYS33 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:18719106 |
| Chain | Residue | Details |
| B | LYS63 |
Catalytic Information from CSA
