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Protein

Ran GTPase-activating protein 1

Gene

Rangap1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

GTPase activator for the nuclear Ras-related regulatory protein Ran, converting it to the putatively inactive GDP-bound state. Required for postimplantation development.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei564Hydrophobic interaction with UBC9By similarity1
Sitei567Hydrophobic interaction with UBC9By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Enzyme and pathway databases

ReactomeiR-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:Fug1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:103071. Rangap1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm, Cytoskeleton, Kinetochore, Membrane, Nucleus

Pathology & Biotechi

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 UBC9 binding nor on sumoylation. 1 Publication1
Mutagenesisi516T → A: No effect on UBC9 binding nor on sumoylation. 1 Publication1
Mutagenesisi517R → A: No effect on UBC9 binding nor on sumoylation. 1 Publication1
Mutagenesisi520I → A: No effect on UBC9 binding nor on sumoylation. 1
Mutagenesisi521H → A: No effect on UBC9 binding nor on sumoylation. 1 Publication1
Mutagenesisi522M → A: No effect on UBC9 binding nor on sumoylation. 1 Publication1
Mutagenesisi524L → A: No sumoylation. 1 Publication1
Mutagenesisi525L → A: Disrupted binding of UCB9, and no sumoylation. 1 Publication1
Mutagenesisi526K → A: No UBC9 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 UBC9 binding nor sumoylation. 1 Publication1
Mutagenesisi529D → A: No effect on UBC9 binding nor on sumoylation. 1 Publication1
Mutagenesisi531I → A: No effect on UBC9 binding nor on sumoylation. 1 Publication1
Mutagenesisi537L → A: No effect on UBC9 binding nor on sumoylation. 1 Publication1
Mutagenesisi560L → A: No effect on UBC9 binding nor on sumoylation. 1 Publication1
Mutagenesisi563A → L: No effect on UBC9 binding nor on sumoylation. 1 Publication1
Mutagenesisi564F → A: No UBC9 binding nor sumoylation. Not targeted to nuclear core complexes; when associated with R-526. 2 Publications1
Mutagenesisi567K → A: No UBC9 binding nor sumoylation. 1 Publication1
Mutagenesisi569N → A: No effect on UBC9 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
Modified residuei24PhosphoserineBy similarity1
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
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

Phosphorylated 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, UBC9, on nuclear pore complex (NPC) diassembly and during mitosis.1 Publication
Sumoylated with SUMO1. Sumoylation is necessary for targeting to the nuclear envelope (NE), and for association with mitotic spindles and kinetochores during mitosis. Also required for interaction with RANBP2 and is mediated by UBC9 (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP46061.
MaxQBiP46061.
PaxDbiP46061.
PeptideAtlasiP46061.
PRIDEiP46061.

PTM databases

iPTMnetiP46061.
PhosphoSitePlusiP46061.
SwissPalmiP46061.

Expressioni

Gene expression databases

BgeeiENSMUSG00000022391.
CleanExiMM_RANGAP1.
GenevisibleiP46061. MM.

Interactioni

Subunit structurei

Homodimer. Interacts with TRAF6 (By similarity). Forms a tight complex in association with RANBP2/NUP358 and UBE2I/UBC9, the ubiquitin-conjugating enzyme E2. Interacts with UBE2I; the interaction conjugates SUMO1 to RANGAP1, and subsequently stabilizes interactions of sumoylated RANGAP1 with RANBP2/NUP358. The SUMO1/RANGAP1/UBC9/NUP358 complex associates with nuclear pore complexes.By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi202583. 10 interactors.
DIPiDIP-17024N.
IntActiP46061. 4 interactors.
MINTiMINT-4132270.
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

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
Contains 6 LRR (leucine-rich) repeats.Curated

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiKOG1909. Eukaryota.
COG5238. LUCA.
GeneTreeiENSGT00440000039203.
HOVERGENiHBG017720.
InParanoidiP46061.
KOiK14319.
OMAiHETTDAL.
OrthoDBiEOG091G02K4.
TreeFamiTF318283.

Family and domain databases

Gene3Di1.25.40.200. 1 hit.
3.80.10.10. 1 hit.
InterProiIPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR009109. Ran_GTPase_activating_1_C.
IPR027038. RanGap.
[Graphical view]
PANTHERiPTHR24113. PTHR24113. 1 hit.
PfamiPF13516. LRR_6. 3 hits.
PF07834. RanGAP1_C. 1 hit.
[Graphical view]
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.

Cross-referencesi

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.

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...

Protein-protein interaction databases

BioGridi202583. 10 interactors.
DIPiDIP-17024N.
IntActiP46061. 4 interactors.
MINTiMINT-4132270.
STRINGi10090.ENSMUSP00000057771.

PTM databases

iPTMnetiP46061.
PhosphoSitePlusiP46061.
SwissPalmiP46061.

Proteomic databases

EPDiP46061.
MaxQBiP46061.
PaxDbiP46061.
PeptideAtlasiP46061.
PRIDEiP46061.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5905.
MGIiMGI:103071. Rangap1.

Phylogenomic databases

eggNOGiKOG1909. Eukaryota.
COG5238. LUCA.
GeneTreeiENSGT00440000039203.
HOVERGENiHBG017720.
InParanoidiP46061.
KOiK14319.
OMAiHETTDAL.
OrthoDBiEOG091G02K4.
TreeFamiTF318283.

Enzyme and pathway databases

ReactomeiR-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.

Miscellaneous databases

ChiTaRSiRangap1. mouse.
EvolutionaryTraceiP46061.
PROiP46061.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000022391.
CleanExiMM_RANGAP1.
GenevisibleiP46061. MM.

Family and domain databases

Gene3Di1.25.40.200. 1 hit.
3.80.10.10. 1 hit.
InterProiIPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR009109. Ran_GTPase_activating_1_C.
IPR027038. RanGap.
[Graphical view]
PANTHERiPTHR24113. PTHR24113. 1 hit.
PfamiPF13516. LRR_6. 3 hits.
PF07834. RanGAP1_C. 1 hit.
[Graphical view]
SUPFAMiSSF69099. SSF69099. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRAGP1_MOUSE
AccessioniPrimary (citable) accession number: P46061
Secondary accession number(s): Q60801, Q6NZB5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: July 27, 2011
Last modified: November 2, 2016
This is version 163 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.