Rangap1
entrez
19387
canonical
uniprot
P46061
canonical
ensembl
ENSMUSG00000022391
resolver
ensp
ENSMUSP00000057771
resolver
ensp
ENSMUSP00000126849
resolver
ensp
ENSMUSP00000130046
resolver
enst
ENSMUST00000052374
resolver
enst
ENSMUST00000170134
resolver
enst
ENSMUST00000171115
resolver
genesymbol
Rangap1
resolver
genesymbol_syn
Fug1
resolver
uniprot
Q60801
resolver
uniprot
Q6NZB5
resolver
uniprot_entry
RAGP1_MOUSE
resolver
uniprot_sec
Q60801
resolver
uniprot_sec
Q6NZB5
resolver
amino_acid_sequence
MASEDIAKLAETLAKTQVAGGQLSFKGKGLKLNTAEDAKDVIKEIEEFDGLEALRLEGNTVGVEAARVIAKALEKKSELKRCHWSDMFTGRLRSEIPPALISLGEGLITAGAQLVELDLSDNAFGPDGVRGFEALLKSPACFTLQELKLNNCGMGIGGGKILAAALTECHRKSSAQGKPLALKVFVAGRNRLENDGATALAEAFGIIGTLEEVHMPQNGINHPGVTALAQAFAINPLLRVINLNDNTFTEKGGVAMAETLKTLRQVEVINFGDCLVRSKGAVAIADAVRGGLPKLKELNLSFCEIKRDAALVVAEAVADKAELEKLDLNGNALGEEGCEQLQEVMDSFNMAKVLASLSDDEGEDEDEEEEGEEDDEEEEDEEDEEDDDEEEEEQEEEEEPPQRGSGEEPATPSRKILDPNSGEPAPVLSSPTPTDLSTFLSFPSPEKLLRLGPKVSVLIVQQTDTSDPEKVVSAFLKVASVFRDDASVKTAVLDAIDALMKKAFSCSSFNSNTFLTRLLIHMGLLKSEDKIKAIPSLHGPLMVLNHVVRQDYFPKALAPLLLAFVTKPNGALETCSFARHNLLQTLYNI
uniprot
proteins
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}.
uniprot
proteins
mass_dalton
63531
uniprot
proteins
mutagenesis
MUTAGEN 411; /note="T->D: Greatly reduced phosphorylation by CDK1 or CDK2. Completely abolished phosphorylation by CDK1 or CDK2; when associated with D-444."; /evidence="ECO:0000269|PubMed:15037602"; MUTAGEN 444; /note="S->D: Little change in phosphorylation by CDK1 or CDK2. Completely abolished phosphorylation by CDK1 or CDK2; when associated with D-411."; /evidence="ECO:0000269|PubMed:15037602"; MUTAGEN 512; /note="N->A: No effect on UBE2I binding nor on sumoylation."; /evidence="ECO:0000269|PubMed:11853669"; MUTAGEN 516; /note="T->A: No effect on UBE2I binding nor on sumoylation."; /evidence="ECO:0000269|PubMed:11853669"; MUTAGEN 517; /note="R->A: No effect on UBE2I binding nor on sumoylation."; /evidence="ECO:0000269|PubMed:11853669"; MUTAGEN 520; /note="I->A: No effect on UBE2I binding nor on sumoylation."; /evidence="ECO:0000269|PubMed:11853669"; MUTAGEN 521; /note="H->A: No effect on UBE2I binding nor on sumoylation."; /evidence="ECO:0000269|PubMed:11853669"; MUTAGEN 522; /note="M->A: No effect on UBE2I binding nor on sumoylation."; /evidence="ECO:0000269|PubMed:11853669"; MUTAGEN 524; /note="L->A: No sumoylation."; /evidence="ECO:0000269|PubMed:11853669"; MUTAGEN 525; /note="L->A: Disrupted binding to UBE2I, and no sumoylation."; /evidence="ECO:0000269|PubMed:11853669"; MUTAGEN 526; /note="K->A: No UBE2I binding nor sumoylation."; /evidence="ECO:0000269|PubMed:11853669, ECO:0000269|PubMed:16469311, ECO:0000269|PubMed:9442102, ECO:0000269|PubMed:9456312"; MUTAGEN 526; /note="K->R: Absence of sumoylation. Not targeted to the nuclear envelope rim nor to nuclear pore complexes. Disrupted sumoylation. No interaction with SUMO1; when associated with A-564 and with or without SUMO1 A-97."; /evidence="ECO:0000269|PubMed:11853669, ECO:0000269|PubMed:16469311, ECO:0000269|PubMed:9442102, ECO:0000269|PubMed:9456312"; MUTAGEN 528; /note="E->A: No UBE2I binding nor sumoylation."; /evidence="ECO:0000269|PubMed:11853669"; MUTAGEN 529; /note="D->A: No effect on UBE2I binding nor on sumoylation."; /evidence="ECO:0000269|PubMed:11853669"; MUTAGEN 531; /note="I->A: No effect on UBE2I binding nor on sumoylation."; /evidence="ECO:0000269|PubMed:11853669"; MUTAGEN 537; /note="L->A: No effect on UBE2I binding nor on sumoylation."; /evidence="ECO:0000269|PubMed:11853669"; MUTAGEN 541..589; /note="Missing: Abolishes accumulation in the nucleus."; /evidence="ECO:0000269|PubMed:26506250"; MUTAGEN 560; /note="L->A: No effect on UBE2I binding nor on sumoylation."; /evidence="ECO:0000269|PubMed:11853669"; MUTAGEN 563; /note="A->L: No effect on UBE2I binding nor on sumoylation."; /evidence="ECO:0000269|PubMed:11853669"; MUTAGEN 564; /note="F->A: No UBE2I binding nor sumoylation. Not targeted to nuclear pore complexes; when associated with R-526."; /evidence="ECO:0000269|PubMed:11853669, ECO:0000269|PubMed:9456312"; MUTAGEN 567..589; /note="Missing: No effect on accumulation in the nucleus."; /evidence="ECO:0000269|PubMed:26506250"; MUTAGEN 567; /note="K->A: No UBE2I binding nor sumoylation."; /evidence="ECO:0000269|PubMed:11853669"; MUTAGEN 569; /note="N->A: No effect on UBE2I binding nor on sumoylation."; /evidence="ECO:0000269|PubMed:11853669
uniprot
proteins
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) disassembly and during mitosis. {ECO:0000269|PubMed:15037602}.; PTM: Sumoylated (PubMed:11853669, PubMed:26506250). 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:11853669, PubMed:9456312). 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}.
uniprot
proteins
protein_family
RNA1 family
uniprot
proteins
pubmed
11853669
uniprot
proteins
pubmed
15037602
uniprot
proteins
pubmed
15345747
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16469311
uniprot
proteins
pubmed
18305100
uniprot
proteins
pubmed
19131326
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
26304119
uniprot
proteins
pubmed
26506250
uniprot
proteins
pubmed
31088288
uniprot
proteins
pubmed
7891706
uniprot
proteins
pubmed
8314081
uniprot
proteins
pubmed
9442102
uniprot
proteins
pubmed
9456312
uniprot
proteins
sequence_length
589
uniprot
proteins
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:26506250, PubMed:9442102, PubMed:9456312). 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}.
uniprot
proteins