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Protein

GTP-binding nuclear protein Ran

Gene

RAN

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

GTPase involved in nucleocytoplasmic transport, participating both to the import and the export from the nucleus of proteins and RNAs. Switches between a cytoplasmic GDP- and a nuclear GTP-bound state by nucleotide exchange and GTP hydrolysis. Nuclear import receptors such as importin beta bind their substrates only in the absence of GTP-bound RAN and release them upon direct interaction with GTP-bound RAN while export receptors behave in the opposite way. Thereby, RAN controls cargo loading and release by transport receptors in the proper compartment and ensure the directionality of the transport.By similarity
The complex with BIRC5/survivin plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. Acts as a negative regulator of the kinase activity of VRK1 and VRK2. Enhances AR-mediated transactivation. Transactivation decreases as the poly-Gln length within AR increases.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei68GTP; via amide nitrogenCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi18 – 25GTPCombined sources3 Publications8
Nucleotide bindingi36 – 42GTPCombined sources1 Publication7
Nucleotide bindingi122 – 125GTPCombined sources3 Publications4
Nucleotide bindingi150 – 152GTPCombined sources3 Publications3

GO - Molecular functioni

  • GTPase activity Source: GO_Central
  • GTP binding Source: UniProtKB
  • nuclear export signal receptor activity Source: UniProtKB
  • pre-miRNA binding Source: UniProtKB
  • pre-miRNA transporter activity Source: UniProtKB

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • cell division Source: UniProtKB-KW
  • nucleocytoplasmic transport Source: UniProtKB
  • positive regulation of protein export from nucleus Source: UniProtKB
  • pre-miRNA export from nucleus Source: UniProtKB
  • protein import into nucleus Source: UniProtKB
  • ribosomal subunit export from nucleus Source: GO_Central

Keywordsi

Biological processCell cycle, Cell division, Mitosis, Protein transport, Transport
LigandGTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
GTP-binding nuclear protein Ran
Alternative name(s):
GTPase Ran
Ras-like protein TC4
Ras-related nuclear protein
Gene namesi
Name:RAN
OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
Taxonomic identifieri9615 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
Proteomesi
  • UP000002254 Componenti: Unplaced

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

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002086952 – 216GTP-binding nuclear protein RanAdd BLAST215

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei24PhosphothreonineBy similarity1
Modified residuei60N6-acetyllysineBy similarity1
Modified residuei71N6-acetyllysine; alternateBy similarity1
Cross-linki71Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki71Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei99N6-acetyllysineBy similarity1
Cross-linki152Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei159N6-acetyllysine; alternateBy similarity1
Modified residuei159N6-succinyllysine; alternateBy similarity1

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP62825.
PRIDEiP62825.

Interactioni

Subunit structurei

Monomer. Found in a nuclear export complex with RAN, XPO5 and pre-miRNA (PubMed:19965479). Interacts (GTP-bound form) with XPO5 (PubMed:19965479). Also forms a complex with CHC1 and interacts with the AR N-terminal poly-Gln region. The interaction with AR is inversely correlated with the poly-Gln length. Part of a complex consisting of RANBP9, RAN, DYRK1B and COPS5. Found in a nuclear export complex with RANBP3 and XPO1. Component of a nuclear export receptor complex composed of KPNB1, RAN, SNUPN and XPO1. Found in a trimeric export complex with SNUPN, RAN and XPO1. Interacts with RANBP10. Interacts in its GTP-bound form with BIRC5/survivin at S and M phases of the cell cycle. Interacts with TERT; the interaction requires hydrogen peroxide-mediated phosphorylation of TERT and transports TERT to the nucleus. Interacts with MAD2L2. Interacts with RANBP10 (By similarity). Interacts with VRK1, VRK2 and VRK3. Interacts with NEMP1 and KPNB1 (By similarity). Interacts (GDP-bound form) with NUTF2; regulates RAN nuclear import (PubMed:9533885). Interacts with CAPG; mediates CAPG nuclear import (By similarity).By similarity2 Publications

Protein-protein interaction databases

BioGridi1530947. 1 interactor.
IntActiP62825. 2 interactors.
STRINGi9615.ENSCAFP00000009963.

Structurei

Secondary structure

1216
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni3 – 5Combined sources3
Beta strandi9 – 18Combined sources10
Helixi23 – 32Combined sources10
Beta strandi38 – 40Combined sources3
Helixi41 – 43Combined sources3
Beta strandi44 – 54Combined sources11
Beta strandi57 – 66Combined sources10
Helixi70 – 72Combined sources3
Helixi76 – 80Combined sources5
Beta strandi85 – 91Combined sources7
Helixi95 – 99Combined sources5
Helixi101 – 111Combined sources11
Beta strandi112 – 114Combined sources3
Beta strandi117 – 122Combined sources6
Beta strandi126 – 128Combined sources3
Turni133 – 135Combined sources3
Helixi138 – 142Combined sources5
Beta strandi145 – 148Combined sources4
Turni151 – 153Combined sources3
Turni155 – 158Combined sources4
Helixi159 – 169Combined sources11
Beta strandi176 – 178Combined sources3
Helixi191 – 205Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A2KX-ray2.50C/D/E1-216[»]
1BYUX-ray2.15A/B1-216[»]
1QG2X-ray2.50A1-216[»]
1QG4X-ray2.50A/B1-216[»]
1WA5X-ray2.00A1-176[»]
2BKUX-ray2.70A/C1-177[»]
3A6PX-ray2.92C/H1-216[»]
3RANX-ray2.15A/B/C/D1-216[»]
3W3ZX-ray2.70B1-176[»]
5BXQX-ray2.50C/D/E1-216[»]
ProteinModelPortaliP62825.
SMRiP62825.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62825.

Family & Domainsi

Sequence similaritiesi

Belongs to the small GTPase superfamily. Ran family.Curated

Phylogenomic databases

eggNOGiKOG0096. Eukaryota.
ENOG410XNRS. LUCA.
HOVERGENiHBG107376.
InParanoidiP62825.
KOiK07936.

Family and domain databases

InterProiView protein in InterPro
IPR027417. P-loop_NTPase.
IPR002041. Ran_GTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
PfamiView protein in Pfam
PF00071. Ras. 1 hit.
PRINTSiPR00627. GTPRANTC4.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiView protein in PROSITE
PS51418. RAN. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P62825-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAQGEPQVQ FKLVLVGDGG TGKTTFVKRH LTGEFEKKYV ATLGVEVHPL
60 70 80 90 100
VFHTNRGPIK FNVWDTAGQE KFGGLRDGYY IQAQCAIIMF DVTSRVTYKN
110 120 130 140 150
VPNWHRDLVR VCENIPIVLC GNKVDIKDRK VKAKSIVFHR KKNLQYYDIS
160 170 180 190 200
AKSNYNFEKP FLWLARKLIG DPNLEFVAMP ALAPPEVVMD PALAAQYEHD
210
LEVAQTTALP DEDDDL
Length:216
Mass (Da):24,423
Last modified:January 23, 2007 - v3
Checksum:iD5C9B7275C34BCE0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11922 mRNA. Translation: CAA77980.1.
PIRiJC1455.
RefSeqiNP_001181913.1. NM_001194984.1.
UniGeneiCfa.50.

Genome annotation databases

GeneIDi100499482.
KEGGicfa:100499482.

Similar proteinsi

Entry informationi

Entry nameiRAN_CANLF
AccessioniPrimary (citable) accession number: P62825
Secondary accession number(s): P17080
, P28746, P28747, Q9CSP3, Q9CWI7, Q9CZA2, Q9UDJ5, Q9UEU9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: January 23, 2007
Last modified: October 25, 2017
This is version 116 of the entry and version 3 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

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families