3UIN
Complex between human RanGAP1-SUMO2, UBC9 and the IR1 domain from RanBP2
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 | 
| C | 0005096 | molecular_function | GTPase activator activity | 
| C | 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 | 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 | 6 | 
| 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 | 2 | 
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)"} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI14 | 
| Number of Residues | 3 | 
| Details | Motif: {"description":"SUMO conjugation"} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI15 | 
| Number of Residues | 2 | 
| Details | Site: {"description":"Hydrophobic interaction with UBE2I","evidences":[{"evidenceCode":"ECO:0000250"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI16 | 
| Number of Residues | 1 | 
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI17 | 
| Number of Residues | 1 | 
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI18 | 
| 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_FI19 | 
| Number of Residues | 1 | 
| Details | Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI20 | 
| Number of Residues | 52 | 
| Details | Repeat: {"description":"1","evidences":[{"source":"PubMed","id":"22959972","evidenceCode":"ECO:0000269"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI21 | 
| Number of Residues | 4 | 
| Details | Region: {"description":"Interaction with sumoylated RANGAP1"} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI22 | 
| Number of Residues | 52 | 
| Details | Region: {"description":"Interaction with UBE2I"} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI23 | 
| Number of Residues | 1 | 
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI24 | 
| Number of Residues | 1 | 
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} | 
| Chain | Residue | Details | 











