| IED ID | IndEnz0002013807 |
| Enzyme Type ID | protease013807 |
| Protein Name |
Ran GTPase-activating protein 1 RanGAP1 |
| Gene Name | Rangap1 Fug1 |
| Organism | Mus musculus (Mouse) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Euarchontoglires Glires (Rodents and rabbits) Rodentia Myomorpha (mice and others) Muroidea Muridae Murinae Mus Mus Mus musculus (Mouse) |
| Enzyme Sequence | MASEDIAKLAETLAKTQVAGGQLSFKGKGLKLNTAEDAKDVIKEIEEFDGLEALRLEGNTVGVEAARVIAKALEKKSELKRCHWSDMFTGRLRSEIPPALISLGEGLITAGAQLVELDLSDNAFGPDGVRGFEALLKSPACFTLQELKLNNCGMGIGGGKILAAALTECHRKSSAQGKPLALKVFVAGRNRLENDGATALAEAFGIIGTLEEVHMPQNGINHPGVTALAQAFAINPLLRVINLNDNTFTEKGGVAMAETLKTLRQVEVINFGDCLVRSKGAVAIADAVRGGLPKLKELNLSFCEIKRDAALVVAEAVADKAELEKLDLNGNALGEEGCEQLQEVMDSFNMAKVLASLSDDEGEDEDEEEEGEEDDEEEEDEEDEEDDDEEEEEQEEEEEPPQRGSGEEPATPSRKILDPNSGEPAPVLSSPTPTDLSTFLSFPSPEKLLRLGPKVSVLIVQQTDTSDPEKVVSAFLKVASVFRDDASVKTAVLDAIDALMKKAFSCSSFNSNTFLTRLLIHMGLLKSEDKIKAIPSLHGPLMVLNHVVRQDYFPKALAPLLLAFVTKPNGALETCSFARHNLLQTLYNI |
| Enzyme Length | 589 |
| Uniprot Accession Number | P46061 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: GTPase activator for RAN. Converts cytoplasmic GTP-bound RAN to GDP-bound RAN, which is essential for RAN-mediated nuclear import and export (PubMed:18305100). Mediates dissociation of cargo from nuclear export complexes containing XPO1, RAN and RANBP2 after nuclear export (By similarity). Required for postimplantation embryonic development (PubMed:8314081). {ECO:0000250|UniProtKB:P46060, ECO:0000269|PubMed:18305100, ECO:0000269|PubMed:8314081}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (1); Compositional bias (1); Cross-link (9); Helix (10); Initiator methionine (1); Modified residue (11); Motif (1); Mutagenesis (23); Region (2); Repeat (6); Sequence conflict (2); Site (2) |
| Keywords | 3D-structure;Acetylation;Centromere;Chromosome;Cytoplasm;Cytoskeleton;GTPase activation;Isopeptide bond;Kinetochore;Leucine-rich repeat;Nucleus;Phosphoprotein;Reference proteome;Repeat;Ubl conjugation |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26506250, ECO:0000269|PubMed:9442102, ECO:0000269|PubMed:9456312}. Nucleus, nucleoplasm {ECO:0000269|PubMed:26506250}. Nucleus envelope {ECO:0000269|PubMed:16469311, ECO:0000269|PubMed:18305100, ECO:0000269|PubMed:26506250, ECO:0000269|PubMed:9442102, ECO:0000269|PubMed:9456312}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:P46060}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P46060}. Note=Cytoplasmic during interphase (PubMed:26506250). Detected at the nuclear envelope during interphase (PubMed:9442102, PubMed:9456312, PubMed:26506250). Shuttles between nucleus and cytoplasm (PubMed:26506250). Targeted to the nuclear pores after sumoylation. During mitosis, associates with mitotic spindles, but is essentially not detected at the spindle poles. Association with kinetochores appears soon after nuclear envelope breakdown and persists until late anaphase. Mitotic location also requires sumoylation (By similarity). {ECO:0000250|UniProtKB:P46060, ECO:0000269|PubMed:26506250, ECO:0000269|PubMed:9442102, ECO:0000269|PubMed:9456312}. |
| Modified Residue | MOD_RES 2; /note="N-acetylalanine"; /evidence="ECO:0000250|UniProtKB:P46060"; MOD_RES 24; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P46060"; MOD_RES 301; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P46060"; MOD_RES 358; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P46060"; MOD_RES 411; /note="Phosphothreonine; by CDK2"; /evidence="ECO:0000250|UniProtKB:P46060"; MOD_RES 430; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P46060"; MOD_RES 437; /note="Phosphoserine"; /evidence="ECO:0000250|UniProtKB:P46060"; MOD_RES 438; /note="Phosphothreonine"; /evidence="ECO:0000250|UniProtKB:P46060"; MOD_RES 441; /note="Phosphoserine"; /evidence="ECO:0007744|PubMed:21183079"; MOD_RES 444; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:15037602, ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"; MOD_RES 526; /note="N6-acetyllysine; alternate"; /evidence="ECO:0000250|UniProtKB:P46060" |
| Post Translational Modification | PTM: Phosphorylation occurs before nuclear envelope breakdown and continues throughout mitosis. Phosphorylated by the M-phase kinase cyclin B/Cdk1, in vitro. Differential timimg of dephosphorylation occurs during phases of mitosis. The phosphorylated form remains associated with RANBP2/NUP358 and the SUMO E2-conjugating enzyme, UBE2I, on nuclear pore complex (NPC) diassembly and during mitosis. {ECO:0000269|PubMed:15037602}.; PTM: Sumoylated (PubMed:26506250, PubMed:11853669). Sumoylation is necessary for targeting to the nuclear envelope (NE) (PubMed:16469311). Sumoylation is necessary for association with mitotic spindles and kinetochores during mitosis (By similarity). Also required for interaction with RANBP2 and is mediated by UBE2I (PubMed:9456312, PubMed:11853669). Desumoylated by HINT1 (PubMed:31088288). {ECO:0000250|UniProtKB:P46060, ECO:0000269|PubMed:11853669, ECO:0000269|PubMed:16469311, ECO:0000269|PubMed:26506250, ECO:0000269|PubMed:31088288, ECO:0000269|PubMed:9456312}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1KPS; |
| Mapped Pubmed ID | 10491385; 10591541; 10725249; 11217851; 12466851; 12520002; 12904583; 1317320; 14610273; 15033168; 15569683; 15923632; 16602821; 16615898; 18799693; 18974875; 19033381; 19285941; 21267068; 21677750; 22155005; 23892456; 25299344; 26045162; 26321253; 27717094; 34110283; 7799964; 8851043; 9603515; 9811942; |
| Motif | MOTIF 525..528; /note=SUMO conjugation; /evidence=ECO:0000250 |
| Gene Encoded By | |
| Mass | 63,531 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |