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Protein

GTP-binding nuclear protein Ran

Gene

RAN

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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 (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.By similarity4 Publications
Enhances AR-mediated transactivation. Transactivation decreases as the poly-Gln length within AR increases.

Regions

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

GO - Molecular functioni

  • androgen receptor binding Source: UniProtKB
  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • chromatin binding Source: UniProtKB
  • GDP binding Source: UniProtKB
  • GTPase activity Source: UniProtKB
  • GTP binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • transcription coactivator activity Source: UniProtKB

GO - Biological processi

  • actin cytoskeleton organization Source: Ensembl
  • androgen receptor signaling pathway Source: UniProtKB
  • cell division Source: UniProtKB-KW
  • cellular protein complex localization Source: Ensembl
  • cellular response to mineralocorticoid stimulus Source: Ensembl
  • DNA metabolic process Source: UniProtKB
  • gene silencing by RNA Source: Reactome
  • hippocampus development Source: Ensembl
  • intracellular transport of virus Source: Reactome
  • mitotic nuclear division Source: UniProtKB
  • mitotic spindle organization Source: UniProtKB
  • positive regulation of protein binding Source: BHF-UCL
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • pre-miRNA export from nucleus Source: BHF-UCL
  • protein export from nucleus Source: BHF-UCL
  • protein import into nucleus, translocation Source: UniProtKB
  • protein localization to nucleolus Source: UniProtKB
  • ribosomal large subunit export from nucleus Source: ParkinsonsUK-UCL
  • ribosomal small subunit export from nucleus Source: ParkinsonsUK-UCL
  • signal transduction Source: UniProtKB
  • small GTPase mediated signal transduction Source: InterPro
  • spermatid development Source: Ensembl
  • tRNA export from nucleus Source: Reactome
  • viral process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Host-virus interaction, Mitosis, Protein transport, Transport

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-165054. Rev-mediated nuclear export of HIV RNA.
R-HSA-1655829. Regulation of cholesterol biosynthesis by SREBP (SREBF).
R-HSA-168333. NEP/NS2 Interacts with the Cellular Export Machinery.
R-HSA-180746. Nuclear import of Rev protein.
R-HSA-203927. MicroRNA (miRNA) biogenesis.
R-HSA-5578749. Transcriptional regulation by small RNAs.
R-HSA-6784531. tRNA processing in the nucleus.
SignaLinkiP62826.
SIGNORiP62826.

Protein family/group databases

TCDBi9.A.60.1.1. the small nuclear rna exporter (snrna-e).

Names & Taxonomyi

Protein namesi
Recommended name:
GTP-binding nuclear protein Ran
Alternative name(s):
Androgen receptor-associated protein 24
GTPase Ran
Ras-like protein TC4
Ras-related nuclear protein
Gene namesi
Name:RAN
Synonyms:ARA24
ORF Names:OK/SW-cl.81
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:9846. RAN.

Subcellular locationi

  • Nucleus
  • Cytoplasm
  • Melanosome
  • Nucleus envelope By similarity

  • Note: Predominantly nuclear during interphase. Becomes dispersed throughout the cytoplasm during mitosis. Colocalizes with NEMP1 at the nuclear envelope (By similarity). Identified by mass spectrometry in melanosome fractions from stage I to stage IV.By similarity

GO - Cellular componenti

  • cell-cell adherens junction Source: BHF-UCL
  • centriole Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: BHF-UCL
  • male germ cell nucleus Source: Ensembl
  • manchette Source: Ensembl
  • melanosome Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • midbody Source: UniProtKB
  • nuclear pore Source: UniProtKB
  • nucleolus Source: UniProtKB
  • nucleoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
  • recycling endosome Source: UniProtKB
  • RNA nuclear export complex Source: BHF-UCL
  • sperm flagellum Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi19 – 191G → V: Blocks DNA replication; when associated with L-69. 1 Publication
Mutagenesisi24 – 241T → L: Has low binding affinity for GTP and GDP. Almost completely abolishes interaction with BIRC5. 1 Publication
Mutagenesisi69 – 691Q → L: Blocks DNA replication; when associated with V-19. 2 Publications
Mutagenesisi69 – 691Q → N: Unable to hydrolyze GTP. Increases binding to BIRC5 and promotes exaggerated spindle formation. 2 Publications

Organism-specific databases

PharmGKBiPA34205.

Polymorphism and mutation databases

BioMutaiRAN.
DMDMi51338598.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources1 Publication
Chaini2 – 216215GTP-binding nuclear protein RanPRO_0000208696Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources1 Publication
Modified residuei24 – 241PhosphothreonineCombined sources
Modified residuei60 – 601N6-acetyllysineCombined sources
Modified residuei71 – 711N6-acetyllysine; alternateCombined sources
Cross-linki71 – 71Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
Modified residuei99 – 991N6-acetyllysineCombined sources
Modified residuei159 – 1591N6-acetyllysine; alternateCombined sources
Modified residuei159 – 1591N6-succinyllysine; alternateBy similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP62826.
MaxQBiP62826.
PaxDbiP62826.
PeptideAtlasiP62826.
PRIDEiP62826.
TopDownProteomicsiP62826.

2D gel databases

OGPiP62826.
REPRODUCTION-2DPAGEP62826.
UCD-2DPAGEP62826.

PTM databases

iPTMnetiP62826.
PhosphoSiteiP62826.
SwissPalmiP62826.

Expressioni

Tissue specificityi

Expressed in a variety of tissues.1 Publication

Gene expression databases

BgeeiENSG00000132341.
ExpressionAtlasiP62826. baseline and differential.
GenevisibleiP62826. HS.

Organism-specific databases

HPAiHPA063353.

Interactioni

Subunit structurei

Monomer. 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. In case of HIV-1 infection, found in a complex with HIV-1 Rev, RNAs containing a Rev response element (RRE) and XPO1. Found in a complex with HTLV-1 Rex, RANBP3 and XPO1. 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 and VRK3. Interacts with isoform 1 and isoform 2 of VRK2. Interacts with NEMP1 and KPNB1 (By similarity).By similarity15 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ANKRD49Q8WVL72EBI-286642,EBI-9381820
BIRC5O153927EBI-286642,EBI-518823
IPO13O9482913EBI-286642,EBI-747310
NUTF2P619704EBI-286642,EBI-591778
PPP1R13LQ8WUF59EBI-286642,EBI-5550163
RCC1P187546EBI-286642,EBI-992720
TNPO1Q929732EBI-286642,EBI-286693
TP53BP2Q136255EBI-286642,EBI-77642
VRK1Q9998612EBI-286642,EBI-1769146
VRK2Q86Y07-12EBI-286642,EBI-1207633
VRK2Q86Y07-52EBI-286642,EBI-1207649

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi111837. 146 interactions.
DIPiDIP-5929N.
IntActiP62826. 76 interactions.
MINTiMINT-94188.
STRINGi9606.ENSP00000376176.

Structurei

Secondary structure

1
216
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni2 – 54Combined sources
Beta strandi10 – 178Combined sources
Beta strandi18 – 225Combined sources
Helixi23 – 275Combined sources
Helixi31 – 355Combined sources
Beta strandi38 – 403Combined sources
Turni41 – 444Combined sources
Beta strandi45 – 5410Combined sources
Beta strandi57 – 6610Combined sources
Helixi69 – 713Combined sources
Helixi74 – 763Combined sources
Helixi77 – 804Combined sources
Beta strandi85 – 917Combined sources
Beta strandi92 – 943Combined sources
Helixi95 – 995Combined sources
Helixi101 – 11111Combined sources
Beta strandi112 – 1143Combined sources
Beta strandi117 – 1226Combined sources
Beta strandi126 – 1283Combined sources
Helixi133 – 1353Combined sources
Helixi138 – 1425Combined sources
Beta strandi145 – 1484Combined sources
Turni151 – 1544Combined sources
Turni156 – 1583Combined sources
Helixi159 – 16911Combined sources
Beta strandi176 – 1783Combined sources
Turni185 – 1873Combined sources
Helixi191 – 20515Combined sources
Helixi211 – 2155Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I2MX-ray1.76A/C1-216[»]
1IBRX-ray2.30A/C1-216[»]
1K5DX-ray2.70A/D/G/J1-216[»]
1K5GX-ray3.10A/D/G/J1-216[»]
1QBKX-ray3.00C1-216[»]
1RRPX-ray2.96A/C8-211[»]
2MMCNMR-A1-216[»]
2MMGNMR-A1-216[»]
2N1BNMR-A1-216[»]
3CH5X-ray2.10A1-216[»]
3EA5X-ray2.50A/C1-216[»]
3GJ0X-ray1.48A/B2-216[»]
3GJ3X-ray1.79A2-216[»]
3GJ4X-ray2.15A/C2-216[»]
3GJ5X-ray1.79A/C2-216[»]
3GJ6X-ray2.70A2-216[»]
3GJ7X-ray1.93A/C2-216[»]
3GJ8X-ray1.82A/C2-216[»]
3GJXX-ray2.50C/F1-216[»]
3NBYX-ray3.42C/F5-180[»]
3NBZX-ray2.80C/F5-180[»]
3NC0X-ray2.90C/F5-180[»]
3NC1X-ray3.35C1-180[»]
3ZJYX-ray3.60A/D/F1-180[»]
4C0QX-ray3.42C/D2-216[»]
4GMXX-ray2.10A1-216[»]
4GPTX-ray2.22A1-216[»]
4HATX-ray1.78A1-216[»]
4HAUX-ray2.00A1-216[»]
4HAVX-ray2.00A1-216[»]
4HAWX-ray1.90A1-216[»]
4HAXX-ray2.28A1-216[»]
4HAYX-ray2.30A1-216[»]
4HAZX-ray1.90A1-216[»]
4HB0X-ray2.20A1-216[»]
4HB2X-ray1.80A1-216[»]
4HB3X-ray2.80A1-216[»]
4HB4X-ray2.05A1-216[»]
4OL0X-ray2.90A1-216[»]
4WVFX-ray1.80A1-216[»]
5CIQX-ray1.65A/B1-216[»]
5CITX-ray1.75A/B1-216[»]
5CIWX-ray1.75A/B1-216[»]
5CJ2X-ray1.75A/B/C/D/E/F/G/H1-216[»]
5CLLX-ray2.45A/C1-191[»]
5CLQX-ray3.20A/C1-216[»]
5DH9X-ray2.55A1-216[»]
5DHAX-ray2.95A1-216[»]
5DHFX-ray2.29A1-216[»]
5DI9X-ray2.28A1-216[»]
5DIFX-ray2.09A1-216[»]
5DISX-ray2.85B8-179[»]
5DLQX-ray3.20C/D5-180[»]
5FYQX-ray3.00C/D31-43[»]
ProteinModelPortaliP62826.
SMRiP62826. Positions 2-207.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62826.

Family & Domainsi

Sequence similaritiesi

Belongs to the small GTPase superfamily. Ran family.Curated

Phylogenomic databases

eggNOGiKOG0096. Eukaryota.
ENOG410XNRS. LUCA.
GeneTreeiENSGT00840000129836.
HOVERGENiHBG107376.
InParanoidiP62826.
KOiK07936.
PhylomeDBiP62826.
TreeFamiTF106302.

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.

P62826-1 [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 cautioni

The sequence BAB93486 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21A → T in AAH72000 (PubMed:15489334).Curated
Sequence conflicti181 – 1811A → C in AAC99400 (PubMed:11042152).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti95 – 951R → I.
Corresponds to variant rs11546488 [ dbSNP | Ensembl ].
VAR_051900

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31469 mRNA. Translation: AAA36546.1.
AF052578 mRNA. Translation: AAC05840.1.
AF054183 mRNA. Translation: AAC99400.1.
AF501887 mRNA. Translation: AAM15923.1.
BT007271 mRNA. Translation: AAP35935.1.
CR450347 mRNA. Translation: CAG29343.1.
AK290763 mRNA. Translation: BAF83452.1.
AK312466 mRNA. Translation: BAG35373.1.
CH471054 Genomic DNA. Translation: EAW98516.1.
BC004272 mRNA. Translation: AAH04272.3.
BC014518 mRNA. Translation: AAH14518.1.
BC014901 mRNA. Translation: AAH14901.1.
BC016654 mRNA. Translation: AAH16654.1.
BC051908 mRNA. Translation: AAH51908.2.
BC072000 mRNA. Translation: AAH72000.1.
AB062399 mRNA. Translation: BAB93486.1. Different initiation.
CCDSiCCDS9271.1.
PIRiA44393. TVHUC3.
RefSeqiNP_001287725.1. NM_001300796.1.
NP_001287726.1. NM_001300797.1.
NP_006316.1. NM_006325.4.
UniGeneiHs.10842.

Genome annotation databases

EnsembliENST00000392369; ENSP00000376176; ENSG00000132341.
ENST00000543796; ENSP00000446215; ENSG00000132341.
GeneIDi5901.
KEGGihsa:5901.
UCSCiuc001uir.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31469 mRNA. Translation: AAA36546.1.
AF052578 mRNA. Translation: AAC05840.1.
AF054183 mRNA. Translation: AAC99400.1.
AF501887 mRNA. Translation: AAM15923.1.
BT007271 mRNA. Translation: AAP35935.1.
CR450347 mRNA. Translation: CAG29343.1.
AK290763 mRNA. Translation: BAF83452.1.
AK312466 mRNA. Translation: BAG35373.1.
CH471054 Genomic DNA. Translation: EAW98516.1.
BC004272 mRNA. Translation: AAH04272.3.
BC014518 mRNA. Translation: AAH14518.1.
BC014901 mRNA. Translation: AAH14901.1.
BC016654 mRNA. Translation: AAH16654.1.
BC051908 mRNA. Translation: AAH51908.2.
BC072000 mRNA. Translation: AAH72000.1.
AB062399 mRNA. Translation: BAB93486.1. Different initiation.
CCDSiCCDS9271.1.
PIRiA44393. TVHUC3.
RefSeqiNP_001287725.1. NM_001300796.1.
NP_001287726.1. NM_001300797.1.
NP_006316.1. NM_006325.4.
UniGeneiHs.10842.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I2MX-ray1.76A/C1-216[»]
1IBRX-ray2.30A/C1-216[»]
1K5DX-ray2.70A/D/G/J1-216[»]
1K5GX-ray3.10A/D/G/J1-216[»]
1QBKX-ray3.00C1-216[»]
1RRPX-ray2.96A/C8-211[»]
2MMCNMR-A1-216[»]
2MMGNMR-A1-216[»]
2N1BNMR-A1-216[»]
3CH5X-ray2.10A1-216[»]
3EA5X-ray2.50A/C1-216[»]
3GJ0X-ray1.48A/B2-216[»]
3GJ3X-ray1.79A2-216[»]
3GJ4X-ray2.15A/C2-216[»]
3GJ5X-ray1.79A/C2-216[»]
3GJ6X-ray2.70A2-216[»]
3GJ7X-ray1.93A/C2-216[»]
3GJ8X-ray1.82A/C2-216[»]
3GJXX-ray2.50C/F1-216[»]
3NBYX-ray3.42C/F5-180[»]
3NBZX-ray2.80C/F5-180[»]
3NC0X-ray2.90C/F5-180[»]
3NC1X-ray3.35C1-180[»]
3ZJYX-ray3.60A/D/F1-180[»]
4C0QX-ray3.42C/D2-216[»]
4GMXX-ray2.10A1-216[»]
4GPTX-ray2.22A1-216[»]
4HATX-ray1.78A1-216[»]
4HAUX-ray2.00A1-216[»]
4HAVX-ray2.00A1-216[»]
4HAWX-ray1.90A1-216[»]
4HAXX-ray2.28A1-216[»]
4HAYX-ray2.30A1-216[»]
4HAZX-ray1.90A1-216[»]
4HB0X-ray2.20A1-216[»]
4HB2X-ray1.80A1-216[»]
4HB3X-ray2.80A1-216[»]
4HB4X-ray2.05A1-216[»]
4OL0X-ray2.90A1-216[»]
4WVFX-ray1.80A1-216[»]
5CIQX-ray1.65A/B1-216[»]
5CITX-ray1.75A/B1-216[»]
5CIWX-ray1.75A/B1-216[»]
5CJ2X-ray1.75A/B/C/D/E/F/G/H1-216[»]
5CLLX-ray2.45A/C1-191[»]
5CLQX-ray3.20A/C1-216[»]
5DH9X-ray2.55A1-216[»]
5DHAX-ray2.95A1-216[»]
5DHFX-ray2.29A1-216[»]
5DI9X-ray2.28A1-216[»]
5DIFX-ray2.09A1-216[»]
5DISX-ray2.85B8-179[»]
5DLQX-ray3.20C/D5-180[»]
5FYQX-ray3.00C/D31-43[»]
ProteinModelPortaliP62826.
SMRiP62826. Positions 2-207.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111837. 146 interactions.
DIPiDIP-5929N.
IntActiP62826. 76 interactions.
MINTiMINT-94188.
STRINGi9606.ENSP00000376176.

Protein family/group databases

TCDBi9.A.60.1.1. the small nuclear rna exporter (snrna-e).

PTM databases

iPTMnetiP62826.
PhosphoSiteiP62826.
SwissPalmiP62826.

Polymorphism and mutation databases

BioMutaiRAN.
DMDMi51338598.

2D gel databases

OGPiP62826.
REPRODUCTION-2DPAGEP62826.
UCD-2DPAGEP62826.

Proteomic databases

EPDiP62826.
MaxQBiP62826.
PaxDbiP62826.
PeptideAtlasiP62826.
PRIDEiP62826.
TopDownProteomicsiP62826.

Protocols and materials databases

DNASUi5901.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000392369; ENSP00000376176; ENSG00000132341.
ENST00000543796; ENSP00000446215; ENSG00000132341.
GeneIDi5901.
KEGGihsa:5901.
UCSCiuc001uir.4. human.

Organism-specific databases

CTDi5901.
GeneCardsiRAN.
HGNCiHGNC:9846. RAN.
HPAiHPA063353.
MIMi601179. gene.
neXtProtiNX_P62826.
PharmGKBiPA34205.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0096. Eukaryota.
ENOG410XNRS. LUCA.
GeneTreeiENSGT00840000129836.
HOVERGENiHBG107376.
InParanoidiP62826.
KOiK07936.
PhylomeDBiP62826.
TreeFamiTF106302.

Enzyme and pathway databases

ReactomeiR-HSA-165054. Rev-mediated nuclear export of HIV RNA.
R-HSA-1655829. Regulation of cholesterol biosynthesis by SREBP (SREBF).
R-HSA-168333. NEP/NS2 Interacts with the Cellular Export Machinery.
R-HSA-180746. Nuclear import of Rev protein.
R-HSA-203927. MicroRNA (miRNA) biogenesis.
R-HSA-5578749. Transcriptional regulation by small RNAs.
R-HSA-6784531. tRNA processing in the nucleus.
SignaLinkiP62826.
SIGNORiP62826.

Miscellaneous databases

ChiTaRSiRAN. human.
EvolutionaryTraceiP62826.
GeneWikiiRan_(biology).
GenomeRNAii5901.
PROiP62826.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000132341.
ExpressionAtlasiP62826. baseline and differential.
GenevisibleiP62826. HS.

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...

Entry informationi

Entry nameiRAN_HUMAN
AccessioniPrimary (citable) accession number: P62826
Secondary accession number(s): A8K3Z8
, P17080, P28746, P28747, Q6IPB2, Q86V08, Q8NI90, Q9CSP3, Q9CWI7, Q9CZA2, Q9UDJ5, Q9UEU9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: January 23, 2007
Last modified: September 7, 2016
This is version 160 of the entry and version 3 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 12
    Human chromosome 12: 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.