2GRQ
Crystal Structure of human RanGAP1-Ubc9-D127A
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000122 | biological_process | negative regulation of transcription by RNA polymerase II |
A | 0000795 | cellular_component | synaptonemal complex |
A | 0001221 | molecular_function | transcription coregulator binding |
A | 0003723 | molecular_function | RNA binding |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005634 | cellular_component | nucleus |
A | 0005635 | cellular_component | nuclear envelope |
A | 0005643 | cellular_component | nuclear pore |
A | 0005654 | cellular_component | nucleoplasm |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006511 | biological_process | ubiquitin-dependent protein catabolic process |
A | 0007059 | biological_process | chromosome segregation |
A | 0007084 | biological_process | mitotic nuclear membrane reassembly |
A | 0008134 | molecular_function | transcription factor binding |
A | 0016605 | cellular_component | PML body |
A | 0016740 | molecular_function | transferase activity |
A | 0016925 | biological_process | protein sumoylation |
A | 0019787 | molecular_function | ubiquitin-like protein transferase activity |
A | 0019789 | molecular_function | SUMO transferase activity |
A | 0019899 | molecular_function | enzyme binding |
A | 0030335 | biological_process | positive regulation of cell migration |
A | 0032446 | biological_process | protein modification by small protein conjugation |
A | 0036211 | biological_process | protein modification process |
A | 0044388 | molecular_function | small protein activating enzyme binding |
A | 0045892 | biological_process | negative regulation of DNA-templated transcription |
A | 0048471 | cellular_component | perinuclear region of cytoplasm |
A | 0051168 | biological_process | nuclear export |
A | 0051301 | biological_process | cell division |
A | 0061656 | molecular_function | SUMO conjugating enzyme activity |
A | 0071535 | molecular_function | RING-like zinc finger domain binding |
A | 0106068 | cellular_component | SUMO ligase complex |
A | 1903755 | biological_process | positive regulation of SUMO transferase activity |
A | 1990234 | cellular_component | transferase complex |
B | 0005096 | molecular_function | GTPase activator activity |
B | 0007165 | biological_process | signal transduction |
Functional Information from PROSITE/UniProt
site_id | PS00183 |
Number of Residues | 16 |
Details | UBC_1 Ubiquitin-conjugating (UBC) active site signature. FHPNVyps.GtVCLsiL |
Chain | Residue | Details |
A | PHE82-LEU97 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | SITE: Hydrophobic interaction with UBE2I => ECO:0000250 |
Chain | Residue | Details |
B | PHE562 | |
B | LYS565 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:15037602, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231 |
Chain | Residue | Details |
B | SER428 | |
A | VAL25 | |
A | LEU57 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:19690332 |
Chain | Residue | Details |
B | SER435 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332 |
Chain | Residue | Details |
B | THR436 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:15037602, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
B | SER442 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 |
Chain | Residue | Details |
B | LYS524 |
site_id | SWS_FT_FI7 |
Number of Residues | 3 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
B | LYS452 | |
B | LYS586 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25114211, ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
B | LYS524 | |
A | LYS101 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
A | LYS48 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25114211, ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733 |
Chain | Residue | Details |
A | LYS49 |