7PYV
Crystal structure of human UBA6 in complex with the ubiquitin-like modifier FAT10
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008641 | molecular_function | ubiquitin-like modifier activating enzyme activity |
A | 0036211 | biological_process | protein modification process |
B | 0008641 | molecular_function | ubiquitin-like modifier activating enzyme activity |
B | 0036211 | biological_process | protein modification process |
C | 0001650 | cellular_component | fibrillar center |
C | 0005515 | molecular_function | protein binding |
C | 0005634 | cellular_component | nucleus |
C | 0005654 | cellular_component | nucleoplasm |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0006508 | biological_process | proteolysis |
C | 0006511 | biological_process | ubiquitin-dependent protein catabolic process |
C | 0006950 | biological_process | response to stress |
C | 0016235 | cellular_component | aggresome |
C | 0016567 | biological_process | protein ubiquitination |
C | 0032446 | biological_process | protein modification by small protein conjugation |
C | 0034341 | biological_process | response to type II interferon |
C | 0034612 | biological_process | response to tumor necrosis factor |
C | 0043011 | biological_process | myeloid dendritic cell differentiation |
C | 0043065 | biological_process | positive regulation of apoptotic process |
C | 0043123 | biological_process | positive regulation of canonical NF-kappaB signal transduction |
C | 0070628 | molecular_function | proteasome binding |
C | 0070842 | biological_process | aggresome assembly |
C | 1901990 | biological_process | regulation of mitotic cell cycle phase transition |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | SITE: Activation by thioester intermediate formation with UBA6 |
Chain | Residue | Details |
C | GLY164 | |
A | ASN505 | |
A | ASP569 | |
B | ARG46 | |
B | ASN505 | |
B | ASP569 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000305|PubMed:35986001, ECO:0007744|PDB:7SOL |
Chain | Residue | Details |
A | ALA470 | |
A | GLN509 | |
B | ALA470 | |
B | GLN509 |
site_id | SWS_FT_FI3 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000269|PubMed:35970836, ECO:0000305|PubMed:35986001, ECO:0007744|PDB:7PVN, ECO:0007744|PDB:7SOL |
Chain | Residue | Details |
A | ASP497 | |
B | ASN570 | |
A | ARG508 | |
A | LYS521 | |
A | VAL545 | |
A | ASN570 | |
B | ASP497 | |
B | ARG508 | |
B | LYS521 | |
B | VAL545 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P22515 |
Chain | Residue | Details |
A | ASP499 | |
A | GLU502 | |
B | ASP499 | |
B | GLU502 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylmethionine => ECO:0007744|PubMed:19413330 |
Chain | Residue | Details |
A | MET1 | |
B | MET1 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | THR54 | |
B | THR54 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER301 | |
B | SER301 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
A | LYS544 | |
B | LYS544 | |
A | LYS664 | |
B | LYS664 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | ACT_SITE: Glycyl thioester intermediate => ECO:0000255|PROSITE-ProRule:PRU10132 |
Chain | Residue | Details |
A | ALA625 | |
B | ALA625 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648 |
Chain | Residue | Details |
A | THR793 | |
B | THR793 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231 |
Chain | Residue | Details |
A | SER810 | |
B | SER810 |
site_id | SWS_FT_FI12 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q02053 |
Chain | Residue | Details |
A | SER816 | |
B | SER816 |
site_id | SWS_FT_FI13 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER820 | |
B | SER820 |
site_id | SWS_FT_FI14 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | SER835 | |
B | SER835 |