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Protein

Ran GTPase-activating protein 1

Gene

RANGAP1

Organism
Homo sapiens (Human)
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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei562Hydrophobic interaction with UBC9By similarity1
Sitei565Hydrophobic interaction with UBC9By similarity1

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • GTPase activator activity Source: ProtInc

GO - Biological processi

  • cellular response to vasopressin Source: Ensembl
  • negative regulation of protein export from nucleus Source: BHF-UCL
  • protein sumoylation Source: Reactome
  • response to axon injury Source: Ensembl
  • signal transduction Source: ProtInc
  • sister chromatid cohesion Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Enzyme and pathway databases

ReactomeiR-HSA-165054. Rev-mediated nuclear export of HIV RNA.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-4615885. SUMOylation of DNA replication proteins.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-68877. Mitotic Prometaphase.
SIGNORiP46060.

Protein family/group databases

TCDBi1.I.1.1.3. the nuclear pore complex (npc) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Ran GTPase-activating protein 1
Short name:
RanGAP1
Gene namesi
Name:RANGAP1
Synonyms:KIAA1835, SD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:9854. 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
Mutagenesisi524K → R: No association with mitotic spindles during mitosis. 1 Publication1

Organism-specific databases

DisGeNETi5905.
OpenTargetsiENSG00000100401.
PharmGKBiPA34216.

Polymorphism and mutation databases

BioMutaiRANGAP1.
DMDMi1172922.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000567372 – 587Ran GTPase-activating protein 1Add BLAST586

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanine1 Publication1
Cross-linki8Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)
Modified residuei24PhosphoserineCombined sources1
Modified residuei301PhosphoserineCombined sources1
Modified residuei358PhosphoserineCombined sources1
Modified residuei409Phosphothreonine; by CDK21 Publication1
Modified residuei428PhosphoserineCombined sources1 Publication1
Modified residuei435PhosphoserineCombined sources1
Modified residuei436PhosphothreonineCombined sources1
Modified residuei442PhosphoserineCombined sources1 Publication1
Modified residuei524N6-acetyllysine; alternateCombined sources1
Cross-linki524Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki524Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources

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 UBC9.2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP46060.
MaxQBiP46060.
PaxDbiP46060.
PeptideAtlasiP46060.
PRIDEiP46060.

PTM databases

iPTMnetiP46060.
PhosphoSitePlusiP46060.
SwissPalmiP46060.

Expressioni

Tissue specificityi

Highly expressed in brain, thymus and testis.1 Publication

Gene expression databases

BgeeiENSG00000100401.
CleanExiHS_RANGAP1.
ExpressionAtlasiP46060. baseline and differential.
GenevisibleiP46060. HS.

Organism-specific databases

HPAiCAB004293.
HPA050110.
HPA062034.

Interactioni

Subunit structurei

Homodimer. 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. Interacts with TRAF6.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SUMO1P631655EBI-396091,EBI-80140
UBE2IP632796EBI-396091,EBI-80168

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL

Protein-protein interaction databases

BioGridi111840. 131 interactors.
DIPiDIP-29079N.
IntActiP46060. 45 interactors.
MINTiMINT-3016328.
STRINGi9606.ENSP00000348577.

Structurei

Secondary structure

1587
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi434 – 439Combined sources6
Helixi443 – 448Combined sources6
Helixi450 – 452Combined sources3
Helixi453 – 459Combined sources7
Helixi466 – 477Combined sources12
Helixi484 – 502Combined sources19
Beta strandi503 – 507Combined sources5
Helixi509 – 519Combined sources11
Beta strandi522 – 526Combined sources5
Helixi536 – 545Combined sources10
Beta strandi548 – 551Combined sources4
Helixi553 – 555Combined sources3
Helixi556 – 564Combined sources9
Helixi568 – 571Combined sources4
Helixi574 – 586Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Z5SX-ray3.01C418-587[»]
2GRNX-ray1.80B419-587[»]
2GROX-ray1.70B419-587[»]
2GRPX-ray2.05B419-587[»]
2GRQX-ray1.70B419-587[»]
2GRRX-ray1.30B419-587[»]
2IO2X-ray2.90C418-587[»]
2IO3X-ray3.20C418-587[»]
2IY0X-ray2.77C432-587[»]
3UINX-ray2.60C419-587[»]
3UIOX-ray2.60C419-587[»]
3UIPX-ray2.29C419-587[»]
5D2MX-ray2.40C/F418-587[»]
ProteinModelPortaliP46060.
SMRiP46060.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46060.

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 – 319LRR 5Add BLAST28
Repeati320 – 343LRR 6Add BLAST24

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi523 – 526SUMO conjugation4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi359 – 399Asp/Glu-rich (highly acidic)Add BLAST41
Compositional biasi359 – 397Asp/Glu-rich (highly acidic)Add BLAST39

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.
HOGENOMiHOG000195026.
HOVERGENiHBG017720.
InParanoidiP46060.
KOiK14319.
OMAiHETTDAL.
OrthoDBiEOG091G02K4.
PhylomeDBiP46060.
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.
[Graphical view]
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.

P46060-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASEDIAKLA ETLAKTQVAG GQLSFKGKSL KLNTAEDAKD VIKEIEDFDS
60 70 80 90 100
LEALRLEGNT VGVEAARVIA KALEKKSELK RCHWSDMFTG RLRTEIPPAL
110 120 130 140 150
ISLGEGLITA GAQLVELDLS DNAFGPDGVQ GFEALLKSSA CFTLQELKLN
160 170 180 190 200
NCGMGIGGGK ILAAALTECH RKSSAQGKPL ALKVFVAGRN RLENDGATAL
210 220 230 240 250
AEAFRVIGTL EEVHMPQNGI NHPGITALAQ AFAVNPLLRV INLNDNTFTE
260 270 280 290 300
KGAVAMAETL KTLRQVEVIN FGDCLVRSKG AVAIADAIRG GLPKLKELNL
310 320 330 340 350
SFCEIKRDAA LAVAEAMADK AELEKLDLNG NTLGEEGCEQ LQEVLEGFNM
360 370 380 390 400
AKVLASLSDD EDEEEEEEGE EEEEEAEEEE EEDEEEEEEE EEEEEEEPQQ
410 420 430 440 450
RGQGEKSATP SRKILDPNTG EPAPVLSSPP PADVSTFLAF PSPEKLLRLG
460 470 480 490 500
PKSSVLIAQQ TDTSDPEKVV SAFLKVSSVF KDEATVRMAV QDAVDALMQK
510 520 530 540 550
AFNSSSFNSN TFLTRLLVHM GLLKSEDKVK AIANLYGPLM ALNHMVQQDY
560 570 580
FPKALAPLLL AFVTKPNSAL ESCSFARHSL LQTLYKV
Length:587
Mass (Da):63,542
Last modified:November 1, 1995 - v1
Checksum:i3C18068AAC06B98F
GO

Sequence cautioni

The sequence BAB47464 differs from that shown. Reason: Erroneous initiation.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_029240133E → Q.Corresponds to variant rs2229752dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82260 mRNA. Translation: CAA57714.1.
AB058738 mRNA. Translation: BAB47464.1. Different initiation.
CR456557 mRNA. Translation: CAG30443.1.
AL035681 Genomic DNA. Translation: CAB63073.1.
BC014044 mRNA. Translation: AAH14044.1.
BC041396 mRNA. Translation: AAH41396.1.
CCDSiCCDS14012.1.
PIRiJC5300.
RefSeqiNP_001265580.1. NM_001278651.1.
NP_001304859.1. NM_001317930.1.
NP_002874.1. NM_002883.3.
XP_006724352.1. XM_006724289.3.
XP_011528596.1. XM_011530294.2.
XP_011528597.1. XM_011530295.2.
XP_016884382.1. XM_017028893.1.
XP_016884383.1. XM_017028894.1.
XP_016884384.1. XM_017028895.1.
XP_016884385.1. XM_017028896.1.
XP_016884386.1. XM_017028897.1.
UniGeneiHs.183800.

Genome annotation databases

EnsembliENST00000356244; ENSP00000348577; ENSG00000100401.
ENST00000405486; ENSP00000385866; ENSG00000100401.
ENST00000455915; ENSP00000401470; ENSG00000100401.
GeneIDi5905.
KEGGihsa:5905.
UCSCiuc003azs.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82260 mRNA. Translation: CAA57714.1.
AB058738 mRNA. Translation: BAB47464.1. Different initiation.
CR456557 mRNA. Translation: CAG30443.1.
AL035681 Genomic DNA. Translation: CAB63073.1.
BC014044 mRNA. Translation: AAH14044.1.
BC041396 mRNA. Translation: AAH41396.1.
CCDSiCCDS14012.1.
PIRiJC5300.
RefSeqiNP_001265580.1. NM_001278651.1.
NP_001304859.1. NM_001317930.1.
NP_002874.1. NM_002883.3.
XP_006724352.1. XM_006724289.3.
XP_011528596.1. XM_011530294.2.
XP_011528597.1. XM_011530295.2.
XP_016884382.1. XM_017028893.1.
XP_016884383.1. XM_017028894.1.
XP_016884384.1. XM_017028895.1.
XP_016884385.1. XM_017028896.1.
XP_016884386.1. XM_017028897.1.
UniGeneiHs.183800.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Z5SX-ray3.01C418-587[»]
2GRNX-ray1.80B419-587[»]
2GROX-ray1.70B419-587[»]
2GRPX-ray2.05B419-587[»]
2GRQX-ray1.70B419-587[»]
2GRRX-ray1.30B419-587[»]
2IO2X-ray2.90C418-587[»]
2IO3X-ray3.20C418-587[»]
2IY0X-ray2.77C432-587[»]
3UINX-ray2.60C419-587[»]
3UIOX-ray2.60C419-587[»]
3UIPX-ray2.29C419-587[»]
5D2MX-ray2.40C/F418-587[»]
ProteinModelPortaliP46060.
SMRiP46060.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111840. 131 interactors.
DIPiDIP-29079N.
IntActiP46060. 45 interactors.
MINTiMINT-3016328.
STRINGi9606.ENSP00000348577.

Protein family/group databases

TCDBi1.I.1.1.3. the nuclear pore complex (npc) family.

PTM databases

iPTMnetiP46060.
PhosphoSitePlusiP46060.
SwissPalmiP46060.

Polymorphism and mutation databases

BioMutaiRANGAP1.
DMDMi1172922.

Proteomic databases

EPDiP46060.
MaxQBiP46060.
PaxDbiP46060.
PeptideAtlasiP46060.
PRIDEiP46060.

Protocols and materials databases

DNASUi5905.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000356244; ENSP00000348577; ENSG00000100401.
ENST00000405486; ENSP00000385866; ENSG00000100401.
ENST00000455915; ENSP00000401470; ENSG00000100401.
GeneIDi5905.
KEGGihsa:5905.
UCSCiuc003azs.5. human.

Organism-specific databases

CTDi5905.
DisGeNETi5905.
GeneCardsiRANGAP1.
HGNCiHGNC:9854. RANGAP1.
HPAiCAB004293.
HPA050110.
HPA062034.
MIMi602362. gene.
neXtProtiNX_P46060.
OpenTargetsiENSG00000100401.
PharmGKBiPA34216.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1909. Eukaryota.
COG5238. LUCA.
GeneTreeiENSGT00440000039203.
HOGENOMiHOG000195026.
HOVERGENiHBG017720.
InParanoidiP46060.
KOiK14319.
OMAiHETTDAL.
OrthoDBiEOG091G02K4.
PhylomeDBiP46060.
TreeFamiTF318283.

Enzyme and pathway databases

ReactomeiR-HSA-165054. Rev-mediated nuclear export of HIV RNA.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-4615885. SUMOylation of DNA replication proteins.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-68877. Mitotic Prometaphase.
SIGNORiP46060.

Miscellaneous databases

ChiTaRSiRANGAP1. human.
EvolutionaryTraceiP46060.
GeneWikiiRANGAP1.
GenomeRNAii5905.
PROiP46060.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000100401.
CleanExiHS_RANGAP1.
ExpressionAtlasiP46060. baseline and differential.
GenevisibleiP46060. HS.

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.
[Graphical view]
PfamiPF13516. LRR_6. 3 hits.
PF07834. RanGAP1_C. 1 hit.
[Graphical view]
SUPFAMiSSF69099. SSF69099. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRAGP1_HUMAN
AccessioniPrimary (citable) accession number: P46060
Secondary accession number(s): Q96JJ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 2, 2016
This is version 186 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.