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Protein

Ran GTPase-activating protein 1

Gene

Rangap1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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).By similarity2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei564Hydrophobic interaction with UBE2IBy similarity1
Sitei567Hydrophobic interaction with UBE2IBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGTPase activation

Enzyme and pathway databases

ReactomeiR-MMU-141444 Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal
R-MMU-2467813 Separation of Sister Chromatids
R-MMU-2500257 Resolution of Sister Chromatid Cohesion
R-MMU-4615885 SUMOylation of DNA replication proteins
R-MMU-5663220 RHO GTPases Activate Formins
R-MMU-68877 Mitotic Prometaphase

Names & Taxonomyi

Protein namesi
Recommended name:
Ran GTPase-activating protein 1
Short name:
RanGAP1
Gene namesi
Name:Rangap1
Synonyms:Fug11 Publication
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:103071 Rangap1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Nucleus

Pathology & Biotechi

Disruption phenotypei

Embryonic development is arrested around 6 dpc.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi411T → D: Greatly reduced phosphorylation by CDK1 or CDK2. Completely abolished phosphorylation by CDK1 or CDK2; when associated with D-444. 1 Publication1
Mutagenesisi444S → D: Little change in phosphorylation by CDK1 or CDK2. Completely abolished phosphorylation by CDK1 or CDK2; when associated with D-411. 1 Publication1
Mutagenesisi512N → A: No effect on UBE2I binding nor on sumoylation. 1 Publication1
Mutagenesisi516T → A: No effect on UBE2I binding nor on sumoylation. 1 Publication1
Mutagenesisi517R → A: No effect on UBE2I binding nor on sumoylation. 1 Publication1
Mutagenesisi520I → A: No effect on UBE2I binding nor on sumoylation. 1 Publication1
Mutagenesisi521H → A: No effect on UBE2I binding nor on sumoylation. 1 Publication1
Mutagenesisi522M → A: No effect on UBE2I binding nor on sumoylation. 1 Publication1
Mutagenesisi524L → A: No sumoylation. 1 Publication1
Mutagenesisi525L → A: Disrupted binding to UBE2I, and no sumoylation. 1 Publication1
Mutagenesisi526K → A: No UBE2I binding nor sumoylation. 4 Publications1
Mutagenesisi526K → 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. 4 Publications1
Mutagenesisi528E → A: No UBE2I binding nor sumoylation. 1 Publication1
Mutagenesisi529D → A: No effect on UBE2I binding nor on sumoylation. 1 Publication1
Mutagenesisi531I → A: No effect on UBE2I binding nor on sumoylation. 1 Publication1
Mutagenesisi537L → A: No effect on UBE2I binding nor on sumoylation. 1 Publication1
Mutagenesisi541 – 589Missing : Abolishes accumulation in the nucleus. 1 PublicationAdd BLAST49
Mutagenesisi560L → A: No effect on UBE2I binding nor on sumoylation. 1 Publication1
Mutagenesisi563A → L: No effect on UBE2I binding nor on sumoylation. 1 Publication1
Mutagenesisi564F → A: No UBE2I binding nor sumoylation. Not targeted to nuclear pore complexes; when associated with R-526. 2 Publications1
Mutagenesisi567 – 589Missing : No effect on accumulation in the nucleus. 1 PublicationAdd BLAST23
Mutagenesisi567K → A: No UBE2I binding nor sumoylation. 1 Publication1
Mutagenesisi569N → A: No effect on UBE2I binding nor on sumoylation. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000567382 – 589Ran GTPase-activating protein 1Add BLAST588

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Cross-linki8Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki8Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki8Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki15Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei24PhosphoserineBy similarity1
Cross-linki279Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei301PhosphoserineBy similarity1
Modified residuei358PhosphoserineBy similarity1
Modified residuei411Phosphothreonine; by CDK2By similarity1
Modified residuei430PhosphoserineBy similarity1
Modified residuei437PhosphoserineBy similarity1
Modified residuei438PhosphothreonineBy similarity1
Modified residuei441PhosphoserineCombined sources1
Modified residuei444PhosphoserineCombined sources1 Publication1
Cross-linki454Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei526N6-acetyllysine; alternateBy similarity1
Cross-linki526Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Cross-linki526Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki526Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity

Post-translational modificationi

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.1 Publication
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).By similarity4 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP46061
MaxQBiP46061
PaxDbiP46061
PeptideAtlasiP46061
PRIDEiP46061

PTM databases

iPTMnetiP46061
PhosphoSitePlusiP46061
SwissPalmiP46061

Expressioni

Tissue specificityi

Detected in adult brain, liver, kidney, intestine, uterus and ovary.1 Publication

Developmental stagei

Detected in embryos at 7.5 dpc, but not at 6 dpc.1 Publication

Gene expression databases

BgeeiENSMUSG00000022391
CleanExiMM_RANGAP1
GenevisibleiP46061 MM

Interactioni

Subunit structurei

Homodimer (PubMed:7891706). Interacts with RAN (PubMed:7891706). Forms a complex with RANBP2/NUP358, NXF1 and NXT1 (By similarity). Forms a tight complex in association with RANBP2 and UBE2I/UBC9, the ubiquitin-conjugating enzyme E2 (PubMed:11853669). Interacts with UBE2I; the interaction conjugates SUMO1 to RANGAP1, and subsequently stabilizes interactions of sumoylated RANGAP1 with RANBP2 (PubMed:9456312, PubMed:18305100, PubMed:11853669). The complex composed of RANBP2, SUMO1, RANGAP1 and UBE2I associates with nuclear pore complexes (By similarity). Identified in a complex composed of RAN, RANBP2, sumoylated RANGAP1, UBE2I and XPO1 (By similarity). Interacts with TRAF6 (By similarity). Interacts with SUMO1 and SENP1 (By similarity).By similarity1 Publication3 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi202583, 11 interactors
DIPiDIP-17024N
ELMiP46061
IntActiP46061, 6 interactors
MINTiP46061
STRINGi10090.ENSMUSP00000057771

Structurei

Secondary structure

1589
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi436 – 441Combined sources6
Helixi445 – 450Combined sources6
Helixi455 – 461Combined sources7
Helixi468 – 480Combined sources13
Helixi486 – 505Combined sources20
Helixi511 – 521Combined sources11
Helixi538 – 549Combined sources12
Helixi555 – 557Combined sources3
Helixi558 – 565Combined sources8
Helixi577 – 588Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1KPSX-ray2.50B/D420-589[»]
ProteinModelPortaliP46061
SMRiP46061
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46061

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati48 – 71LRR 1Add BLAST24
Repeati111 – 134LRR 2Add BLAST24
Repeati207 – 230LRR 3Add BLAST24
Repeati235 – 258LRR 4Add BLAST24
Repeati292 – 315LRR 5Add BLAST24
Repeati320 – 343LRR 6Add BLAST24

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni541 – 566Important for accumulation in the nucleus1 PublicationAdd BLAST26

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi525 – 528SUMO conjugationBy similarity4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi359 – 399Asp/Glu-rich (highly acidic)Add BLAST41

Sequence similaritiesi

Belongs to the RNA1 family.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiKOG1909 Eukaryota
COG5238 LUCA
GeneTreeiENSGT00440000039203
HOVERGENiHBG017720
InParanoidiP46061
KOiK14319
OMAiDLETVIC
OrthoDBiEOG091G02K4
TreeFamiTF318283

Family and domain databases

Gene3Di1.25.40.200, 1 hit
3.80.10.10, 1 hit
InterProiView protein in InterPro
IPR001611 Leu-rich_rpt
IPR032675 LRR_dom_sf
IPR009109 Ran_GTPase_activating_1_C
IPR027038 RanGap
IPR036720 RanGAP1_C_sf
PANTHERiPTHR24113 PTHR24113, 1 hit
PfamiView protein in Pfam
PF13516 LRR_6, 3 hits
PF07834 RanGAP1_C, 1 hit
SUPFAMiSSF69099 SSF69099, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P46061-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASEDIAKLA ETLAKTQVAG GQLSFKGKGL KLNTAEDAKD VIKEIEEFDG
60 70 80 90 100
LEALRLEGNT VGVEAARVIA KALEKKSELK RCHWSDMFTG RLRSEIPPAL
110 120 130 140 150
ISLGEGLITA GAQLVELDLS DNAFGPDGVR GFEALLKSPA CFTLQELKLN
160 170 180 190 200
NCGMGIGGGK ILAAALTECH RKSSAQGKPL ALKVFVAGRN RLENDGATAL
210 220 230 240 250
AEAFGIIGTL EEVHMPQNGI NHPGVTALAQ AFAINPLLRV INLNDNTFTE
260 270 280 290 300
KGGVAMAETL KTLRQVEVIN FGDCLVRSKG AVAIADAVRG GLPKLKELNL
310 320 330 340 350
SFCEIKRDAA LVVAEAVADK AELEKLDLNG NALGEEGCEQ LQEVMDSFNM
360 370 380 390 400
AKVLASLSDD EGEDEDEEEE GEEDDEEEED EEDEEDDDEE EEEQEEEEEP
410 420 430 440 450
PQRGSGEEPA TPSRKILDPN SGEPAPVLSS PTPTDLSTFL SFPSPEKLLR
460 470 480 490 500
LGPKVSVLIV QQTDTSDPEK VVSAFLKVAS VFRDDASVKT AVLDAIDALM
510 520 530 540 550
KKAFSCSSFN SNTFLTRLLI HMGLLKSEDK IKAIPSLHGP LMVLNHVVRQ
560 570 580
DYFPKALAPL LLAFVTKPNG ALETCSFARH NLLQTLYNI
Length:589
Mass (Da):63,531
Last modified:July 27, 2011 - v2
Checksum:i775ADE3A53EFD558
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti181A → R in AAA17681 (PubMed:8314081).Curated1
Sequence conflicti413S → L in AAB60517 (PubMed:7891706).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U08110 mRNA Translation: AAA17681.1
U20857 Genomic RNA Translation: AAB60517.1
AK146670 mRNA Translation: BAE27347.1
AK159009 mRNA Translation: BAE34767.1
AK159525 mRNA Translation: BAE35154.1
BC066213 mRNA Translation: AAH66213.1
BC071200 mRNA Translation: AAH71200.1
CCDSiCCDS27670.1
PIRiA36983
T52070
RefSeqiNP_001139646.1, NM_001146174.1
NP_035371.4, NM_011241.4
UniGeneiMm.270975
Mm.475271

Genome annotation databases

EnsembliENSMUST00000052374; ENSMUSP00000057771; ENSMUSG00000022391
ENSMUST00000170134; ENSMUSP00000126849; ENSMUSG00000022391
ENSMUST00000171115; ENSMUSP00000130046; ENSMUSG00000022391
GeneIDi19387
KEGGimmu:19387
UCSCiuc007wxa.2 mouse

Similar proteinsi

Entry informationi

Entry nameiRAGP1_MOUSE
AccessioniPrimary (citable) accession number: P46061
Secondary accession number(s): Q60801, Q6NZB5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: July 27, 2011
Last modified: May 23, 2018
This is version 177 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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