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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: 4 out of 5-Experimental evidence at protein leveli

Functioni

GTP-binding protein involved in nucleocytoplasmic transport. Required for the import of protein into the nucleus and also for RNA export. Involved in chromatin condensation and control of cell cycle. 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 (By similarity).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi17 – 248GTPBy similarity
Nucleotide bindingi65 – 695GTPBy similarity
Nucleotide bindingi122 – 1254GTPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Protein transport, Transport

Keywords - Ligandi

GTP-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

  • Nucleus By similarity
  • Cytoplasm
  • Melanosome By similarity
  • Nucleus envelope By similarity

  • Note: Predominantly nuclear during interphase (By similarity). Becomes dispersed throughout the cytoplasm during mitosis. Colocalizes with NEMP1 at the nuclear envelope.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 216215GTP-binding nuclear protein RanPRO_0000208695Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei24 – 241PhosphothreonineBy similarity
Modified residuei60 – 601N6-acetyllysineBy similarity
Modified residuei71 – 711N6-acetyllysine; alternateBy similarity
Cross-linki71 – 71Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei99 – 991N6-acetyllysineBy similarity
Modified residuei159 – 1591N6-acetyllysine; alternateBy similarity
Modified residuei159 – 1591N6-succinyllysine; alternateBy similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP62825.
PRIDEiP62825.

Interactioni

Subunit structurei

Monomer (By similarity). Also forms a complex with CHC1. Found in a complex with nuclear export signal-cargo peptides, 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 (By similarity). Interacts with RANBP10 (By similarity). Interacts with VRK1, VRK2 and VRK3. Interacts with NEMP1 and KPNB1 (By similarity).By similarity

Protein-protein interaction databases

BioGridi1530947. 1 interaction.
IntActiP62825. 2 interactions.
STRINGi9615.ENSCAFP00000009963.

Structurei

Secondary structure

1
216
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni3 – 53Combined sources
Beta strandi9 – 1810Combined sources
Helixi23 – 3210Combined sources
Beta strandi38 – 403Combined sources
Helixi41 – 433Combined sources
Beta strandi44 – 5411Combined sources
Beta strandi57 – 6610Combined sources
Helixi70 – 723Combined sources
Helixi76 – 805Combined sources
Beta strandi85 – 917Combined sources
Helixi95 – 995Combined sources
Helixi101 – 11111Combined sources
Beta strandi112 – 1143Combined sources
Beta strandi117 – 1226Combined sources
Beta strandi126 – 1283Combined sources
Turni133 – 1353Combined sources
Helixi138 – 1425Combined sources
Beta strandi145 – 1484Combined sources
Turni151 – 1533Combined sources
Turni155 – 1584Combined sources
Helixi159 – 16911Combined sources
Beta strandi176 – 1783Combined sources
Helixi191 – 20515Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-207.
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

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR002041. Ran_GTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00627. GTPRANTC4.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51418. RAN. 1 hit.
[Graphical view]

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.

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-207.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi1530947. 1 interaction.
IntActiP62825. 2 interactions.
STRINGi9615.ENSCAFP00000009963.

Proteomic databases

PaxDbiP62825.
PRIDEiP62825.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi100499482.
KEGGicfa:100499482.

Phylogenomic databases

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

Miscellaneous databases

EvolutionaryTraceiP62825.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR002041. Ran_GTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00627. GTPRANTC4.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51418. RAN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Sequence of a canine cDNA clone encoding a Ran/TC4 GTP-binding protein."
    Dupree P., Olkkonen V.M., Chavrier P.
    Gene 120:325-326(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Cocker spaniel.
    Tissue: Kidney.
  2. "Structural basis for molecular recognition between nuclear transport factor 2 (NTF2) and the GDP-bound form of the Ras-family GTPase Ran."
    Stewart M., Kent H.M., McCoy A.J.
    J. Mol. Biol. 277:635-646(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF COMPLEX WITH NTF2.
  3. "The structure of the Q69L mutant of GDP-Ran shows a major conformational change in the switch II loop that accounts for its failure to bind nuclear transport factor 2 (NTF2)."
    Stewart M., Kent H.M., McCoy A.J.
    J. Mol. Biol. 284:1517-1527(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF MUTANT LEU-69.

Entry informationi

Entry nameiRAN_CANLF
AccessioniPrimary (citable) accession number: P62825
Secondary accession number(s): P17080
, P28746, P28747, Q9CSP3, Q9CWI7, Q9CZA2, Q9UDJ5, Q9UEU9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: January 23, 2007
Last modified: July 6, 2016
This is version 108 of the entry and version 3 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.