2GRP
Crystal Structure of human RanGAP1-Ubc9-Y87A
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000122 | biological_process | negative regulation of transcription by RNA polymerase II |
| A | 0000166 | molecular_function | nucleotide binding |
| 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 | 0016604 | cellular_component | nuclear body |
| A | 0016605 | cellular_component | PML body |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016925 | biological_process | protein sumoylation |
| A | 0019789 | molecular_function | SUMO transferase activity |
| A | 0019899 | molecular_function | enzyme binding |
| A | 0030335 | biological_process | positive regulation of cell migration |
| A | 0036211 | biological_process | protein modification process |
| A | 0043123 | biological_process | positive regulation of canonical NF-kappaB signal transduction |
| A | 0043398 | molecular_function | HLH domain binding |
| 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 | 0050804 | biological_process | modulation of chemical synaptic transmission |
| 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 | 0098685 | cellular_component | Schaffer collateral - CA1 synapse |
| A | 0098978 | cellular_component | glutamatergic synapse |
| A | 0099523 | cellular_component | presynaptic cytosol |
| A | 0099524 | cellular_component | postsynaptic cytosol |
| A | 0106068 | cellular_component | SUMO ligase complex |
| 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. FHPNVaps.GtVCLsiL |
| Chain | Residue | Details |
| A | PHE82-LEU97 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 153 |
| Details | Domain: {"description":"UBC core","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | Region: {"description":"Interaction with SUMO1"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Glycyl thioester intermediate"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Site: {"description":"Interaction with RANBP2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Site: {"description":"Substrate binding"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| 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_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine; by CDK1","evidences":[{"source":"PubMed","id":"22509284","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 5 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"25755297","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"25114211","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25218447","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25755297","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25772364","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 3 |
| Details | Motif: {"description":"SUMO conjugation"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | Site: {"description":"Hydrophobic interaction with UBE2I","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"15037602","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17081983","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
