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P62826

- RAN_HUMAN

UniProt

P62826 - RAN_HUMAN

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Protein

GTP-binding nuclear protein Ran

Gene

RAN

Organism
Homo sapiens (Human)
Status
Reviewed - 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 similarity
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

  1. androgen receptor binding Source: UniProtKB
  2. chromatin binding Source: UniProtKB
  3. GTPase activity Source: UniProtKB
  4. GTP binding Source: UniProtKB
  5. poly(A) RNA binding Source: UniProtKB
  6. transcription coactivator activity Source: UniProtKB

GO - Biological processi

  1. actin cytoskeleton organization Source: Ensembl
  2. androgen receptor signaling pathway Source: UniProtKB
  3. cellular protein complex localization Source: Ensembl
  4. DNA metabolic process Source: UniProtKB
  5. gene expression Source: Reactome
  6. intracellular transport of virus Source: Reactome
  7. mitotic nuclear division Source: UniProtKB
  8. mitotic spindle organization Source: UniProtKB
  9. positive regulation of protein binding Source: BHF-UCL
  10. positive regulation of transcription, DNA-templated Source: UniProtKB
  11. protein export from nucleus Source: BHF-UCL
  12. protein import into nucleus Source: Ensembl
  13. ribosomal large subunit export from nucleus Source: BHF-UCL
  14. ribosomal small subunit export from nucleus Source: BHF-UCL
  15. signal transduction Source: UniProtKB
  16. small GTPase mediated signal transduction Source: InterPro
  17. small molecule metabolic process Source: Reactome
  18. viral life cycle Source: Reactome
  19. 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

ReactomeiREACT_12417. MicroRNA (miRNA) biogenesis.
REACT_147797. Regulation of cholesterol biosynthesis by SREBP (SREBF).
REACT_6179. NEP/NS2 Interacts with the Cellular Export Machinery.
REACT_6190. Rev-mediated nuclear export of HIV RNA.
REACT_9395. Nuclear import of Rev protein.
SignaLinkiP62826.

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
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:9846. RAN.

Subcellular locationi

Nucleus. Cytoplasm. Melanosome
Note: Predominantly nuclear during interphase (By similarity). Becomes dispersed throughout the cytoplasm during mitosis. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProt
  4. membrane Source: UniProtKB
  5. nuclear pore Source: UniProtKB
  6. nucleoplasm Source: Reactome
  7. nucleus Source: UniProt
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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed4 Publications
Chaini2 – 216215GTP-binding nuclear protein RanPRO_0000208696Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine4 Publications
Modified residuei60 – 601N6-acetyllysine1 Publication
Modified residuei71 – 711N6-acetyllysine; alternate1 Publication
Cross-linki71 – 71Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
Modified residuei99 – 991N6-acetyllysine1 Publication
Modified residuei159 – 1591N6-acetyllysine; alternate1 Publication
Modified residuei159 – 1591N6-succinyllysine; alternateBy similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP62826.
PaxDbiP62826.
PRIDEiP62826.

2D gel databases

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

PTM databases

PhosphoSiteiP62826.

Expressioni

Tissue specificityi

Expressed in a variety of tissues.1 Publication

Gene expression databases

BgeeiP62826.
ExpressionAtlasiP62826. baseline and differential.
GenevestigatoriP62826.

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.By similarity15 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BIRC5O153927EBI-286642,EBI-518823
IPO13O9482913EBI-286642,EBI-747310
RCC1P187546EBI-286642,EBI-992720
TNPO1Q929732EBI-286642,EBI-286693
VRK1Q9998612EBI-286642,EBI-1769146
VRK2Q86Y07-12EBI-286642,EBI-1207633
VRK2Q86Y07-52EBI-286642,EBI-1207649

Protein-protein interaction databases

BioGridi111837. 104 interactions.
DIPiDIP-5929N.
IntActiP62826. 43 interactions.
MINTiMINT-94188.

Structurei

Secondary structure

1
216
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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[»]
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[»]
ProteinModelPortaliP62826.
SMRiP62826. Positions 8-216.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62826.

Family & Domainsi

Sequence similaritiesi

Belongs to the small GTPase superfamily. Ran family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00750000117729.
HOVERGENiHBG107376.
InParanoidiP62826.
KOiK07936.
OrthoDBiEOG7C8GJ1.
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.
SMARTiSM00176. RAN. 1 hit.
[Graphical view]
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 BAB93486.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

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:
EMBL
GenBank
DDBJ
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_006316.1. NM_006325.4.
UniGeneiHs.10842.

Genome annotation databases

EnsembliENST00000392369; ENSP00000376176; ENSG00000132341.
ENST00000543796; ENSP00000446215; ENSG00000132341.
GeneIDi5901.
KEGGihsa:5901.
UCSCiuc001uir.3. human.

Polymorphism databases

DMDMi51338598.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
CCDSi CCDS9271.1.
PIRi A44393. TVHUC3.
RefSeqi NP_006316.1. NM_006325.4.
UniGenei Hs.10842.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1I2M X-ray 1.76 A/C 1-216 [» ]
1IBR X-ray 2.30 A/C 1-216 [» ]
1K5D X-ray 2.70 A/D/G/J 1-216 [» ]
1K5G X-ray 3.10 A/D/G/J 1-216 [» ]
1QBK X-ray 3.00 C 1-216 [» ]
1RRP X-ray 2.96 A/C 8-211 [» ]
3CH5 X-ray 2.10 A 1-216 [» ]
3EA5 X-ray 2.50 A/C 1-216 [» ]
3GJ0 X-ray 1.48 A/B 2-216 [» ]
3GJ3 X-ray 1.79 A 2-216 [» ]
3GJ4 X-ray 2.15 A/C 2-216 [» ]
3GJ5 X-ray 1.79 A/C 2-216 [» ]
3GJ6 X-ray 2.70 A 2-216 [» ]
3GJ7 X-ray 1.93 A/C 2-216 [» ]
3GJ8 X-ray 1.82 A/C 2-216 [» ]
3GJX X-ray 2.50 C/F 1-216 [» ]
3NBY X-ray 3.42 C/F 5-180 [» ]
3NBZ X-ray 2.80 C/F 5-180 [» ]
3NC0 X-ray 2.90 C/F 5-180 [» ]
3NC1 X-ray 3.35 C 1-180 [» ]
3ZJY X-ray 3.60 A/D/F 1-180 [» ]
4C0Q X-ray 3.42 C/D 2-216 [» ]
4GMX X-ray 2.10 A 1-216 [» ]
4GPT X-ray 2.22 A 1-216 [» ]
4HAT X-ray 1.78 A 1-216 [» ]
4HAU X-ray 2.00 A 1-216 [» ]
4HAV X-ray 2.00 A 1-216 [» ]
4HAW X-ray 1.90 A 1-216 [» ]
4HAX X-ray 2.28 A 1-216 [» ]
4HAY X-ray 2.30 A 1-216 [» ]
4HAZ X-ray 1.90 A 1-216 [» ]
4HB0 X-ray 2.20 A 1-216 [» ]
4HB2 X-ray 1.80 A 1-216 [» ]
4HB3 X-ray 2.80 A 1-216 [» ]
4HB4 X-ray 2.05 A 1-216 [» ]
4OL0 X-ray 2.90 A 1-216 [» ]
ProteinModelPortali P62826.
SMRi P62826. Positions 8-216.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111837. 104 interactions.
DIPi DIP-5929N.
IntActi P62826. 43 interactions.
MINTi MINT-94188.

Protein family/group databases

TCDBi 9.A.60.1.1. the small nuclear rna exporter (snrna-e).

PTM databases

PhosphoSitei P62826.

Polymorphism databases

DMDMi 51338598.

2D gel databases

OGPi P62826.
REPRODUCTION-2DPAGE P62826.
UCD-2DPAGE P62826.

Proteomic databases

MaxQBi P62826.
PaxDbi P62826.
PRIDEi P62826.

Protocols and materials databases

DNASUi 5901.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000392369 ; ENSP00000376176 ; ENSG00000132341 .
ENST00000543796 ; ENSP00000446215 ; ENSG00000132341 .
GeneIDi 5901.
KEGGi hsa:5901.
UCSCi uc001uir.3. human.

Organism-specific databases

CTDi 5901.
GeneCardsi GC12P131356.
HGNCi HGNC:9846. RAN.
MIMi 601179. gene.
neXtProti NX_P62826.
PharmGKBi PA34205.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1100.
GeneTreei ENSGT00750000117729.
HOVERGENi HBG107376.
InParanoidi P62826.
KOi K07936.
OrthoDBi EOG7C8GJ1.
PhylomeDBi P62826.
TreeFami TF106302.

Enzyme and pathway databases

Reactomei REACT_12417. MicroRNA (miRNA) biogenesis.
REACT_147797. Regulation of cholesterol biosynthesis by SREBP (SREBF).
REACT_6179. NEP/NS2 Interacts with the Cellular Export Machinery.
REACT_6190. Rev-mediated nuclear export of HIV RNA.
REACT_9395. Nuclear import of Rev protein.
SignaLinki P62826.

Miscellaneous databases

ChiTaRSi RAN. human.
EvolutionaryTracei P62826.
GeneWikii Ran_(biology).
GenomeRNAii 5901.
NextBioi 22956.
PROi P62826.
SOURCEi Search...

Gene expression databases

Bgeei P62826.
ExpressionAtlasi P62826. baseline and differential.
Genevestigatori P62826.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR027417. P-loop_NTPase.
IPR002041. Ran_GTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view ]
Pfami PF00071. Ras. 1 hit.
[Graphical view ]
PRINTSi PR00627. GTPRANTC4.
SMARTi SM00176. RAN. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00231. small_GTP. 1 hit.
PROSITEi PS51418. RAN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of four novel ras-like genes expressed in a human teratocarcinoma cell line."
    Drivas G.T., Shih A., Coutavas E., Rush M.G., D'Eustachio P.
    Mol. Cell. Biol. 10:1793-1798(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Teratocarcinoma.
  2. "Premature initiation of mitosis in yeast lacking RCC1 or an interacting GTPase."
    Matsumoto T., Beach D.H.
    Cell 66:347-360(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO C-TERMINUS.
  3. "Ran/TC4: a small nuclear GTP-binding protein that regulates DNA synthesis."
    Ren M., Drivas G.T., D'Eustachio P., Rush M.G.
    J. Cell Biol. 120:313-323(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, MUTAGENESIS OF GLY-19 AND GLN-69.
    Tissue: Brain.
  4. "The linkage of Kennedy's neuron disease to ARA24, the first identified androgen receptor polyglutamine region-associated coactivator."
    Hsiao P.-W., Lin D.-L., Nakao R., Chang C.
    J. Biol. Chem. 274:20229-20234(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH AR, FUNCTION.
    Tissue: Brain.
  5. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Umbilical cord blood.
  6. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
    Puhl H.L. III, Ikeda S.R., Aronstam R.S.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  7. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  8. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  9. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Hippocampus.
  10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lymph, Ovary, Skin and Uterus.
  12. Bienvenut W.V., Claeys D.
    Submitted (FEB-2006) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-23 AND 143-166, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Platelet.
  13. Lubec G., Afjehi-Sadat L.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 39-56 AND 153-166, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Cajal-Retzius cell.
  14. "Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
    Shichijo S., Itoh K.
    Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 65-216.
    Tissue: Colon adenocarcinoma.
  15. "Mitotic regulator protein RCC1 is complexed with a nuclear ras-related polypeptide."
    Bischoff F.R., Ponstingl H.
    Proc. Natl. Acad. Sci. U.S.A. 88:10830-10834(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 65-76; 90-125; 128-147 AND 154-216, INTERACTION WITH CHC1, SUBCELLULAR LOCATION.
    Tissue: Cervix carcinoma.
  16. "Nuclear protein import: Ran-GTP dissociates the karyopherin alphabeta heterodimer by displacing alpha from an overlapping binding site on beta."
    Moroianu J., Blobel G., Radu A.
    Proc. Natl. Acad. Sci. U.S.A. 93:7059-7062(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "CRM1 is an export receptor for leucine-rich nuclear export signals."
    Fornerod M., Ohno M., Yoshida M., Mattaj I.W.
    Cell 90:1051-1060(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A NUCLEAR EXPORT COMPLEX WITH XPO1.
  18. "The specificity of the CRM1-Rev nuclear export signal interaction is mediated by RanGTP."
    Askjaer P., Jensen T.H., Nilsson J., Englmeier L., Kjems J.
    J. Biol. Chem. 273:33414-33422(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH HIV-1 REV; HIV-1 REV RESPONSE ELEMENT AND XPO1.
  19. Cited for: IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX, IDENTIFICATION IN A TRIMERIC EXPORT COMPLEX WITH SNUPN AND XPO1.
  20. "RanBP3 influences interactions between CRM1 and its nuclear protein export substrates."
    Englmeier L., Fornerod M., Bischoff F.R., Petosa C., Mattaj I.W., Kutay U.
    EMBO Rep. 2:926-932(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A NUCLEAR EXPORT COMPLEX WITH RANBP3 AND XPO1.
  21. "Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein export."
    Lindsay M.E., Holaska J.M., Welch K., Paschal B.M., Macara I.G.
    J. Cell Biol. 153:1391-1402(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A NUCLEAR EXPORT COMPLEX WITH RANBP3 AND XPO1.
  22. "Serine/threonine kinase Mirk/Dyrk1B is an inhibitor of epithelial cell migration and is negatively regulated by the Met adaptor Ran-binding protein M."
    Zou Y., Lim S., Lee K., Deng X., Friedman E.
    J. Biol. Chem. 278:49573-49581(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH COPS5; RANBP9 AND DYRK1B.
  23. "Hydrogen peroxide triggers nuclear export of telomerase reverse transcriptase via Src kinase family-dependent phosphorylation of tyrosine 707."
    Haendeler J., Hoffmann J., Brandes R.P., Zeiher A.M., Dimmeler S.
    Mol. Cell. Biol. 23:4598-4610(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TERT.
  24. "A multifunctional domain in human CRM1 (exportin 1) mediates RanBP3 binding and multimerization of human T-cell leukemia virus type 1 Rex protein."
    Hakata Y., Yamada M., Shida H.
    Mol. Cell. Biol. 23:8751-8761(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH HTLV-1 REX; RANBP3 AND XPO1.
  25. "A novel MET-interacting protein shares high sequence similarity with RanBPM, but fails to stimulate MET-induced Ras/Erk signaling."
    Wang D., Li Z., Schoen S.R., Messing E.M., Wu G.
    Biochem. Biophys. Res. Commun. 313:320-326(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RANBP9 AND RANBP10.
  26. "Architecture of CRM1/Exportin1 suggests how cooperativity is achieved during formation of a nuclear export complex."
    Petosa C., Schoehn G., Askjaer P., Bauer U., Moulin M., Steuerwald U., Soler-Lopez M., Baudin F., Mattaj I.W., Mueller C.W.
    Mol. Cell 16:761-775(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A NUCLEAR EXPORT COMPLEX WITH XPO1.
  27. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Melanoma.
  28. "A survivin-ran complex regulates spindle formation in tumor cells."
    Xia F., Canovas P.M., Guadagno T.M., Altieri D.C.
    Mol. Cell. Biol. 28:5299-5311(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH BIRC5, MUTAGENESIS OF THR-24 AND GLN-69.
  29. "Proteomics identification of nuclear Ran GTPase as an inhibitor of human VRK1 and VRK2 (vaccinia-related kinase) activities."
    Sanz-Garcia M., Lopez-Sanchez I., Lazo P.A.
    Mol. Cell. Proteomics 7:2199-2214(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH VRK1; VRK2 AND VRK3.
  30. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  31. "The mitotic arrest deficient protein MAD2B interacts with the small GTPase RAN throughout the cell cycle."
    Medendorp K., van Groningen J.J., Vreede L., Hetterschijt L., van den Hurk W.H., de Bruijn D.R., Brugmans L., van Kessel A.G.
    PLoS ONE 4:E7020-E7020(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAD2L2, SUBCELLULAR LOCATION.
  32. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-60; LYS-71; LYS-99 AND LYS-159, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  33. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  34. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  35. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  36. "Crystal structure of the nuclear Ras-related protein Ran in its GDP-bound form."
    Scheffzek K., Klebe C., Fritz-Wolf K., Kabsch W., Wittinghofer A.
    Nature 374:378-381(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
  37. "Structure of the nuclear transport complex karyopherin-beta2-Ran x GppNHp."
    Chook Y.M., Blobel G.
    Nature 399:230-237(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF COMPLEX WITH KPNB2.
  38. "Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue: implications for nuclear transport."
    Vetter I.R., Nowak C., Nishimoto T., Kuhlmann J., Wittinghofer A.
    Nature 398:39-46(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.96 ANGSTROMS) OF COMPLEX WITH NUP358.

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: October 29, 2014
This is version 139 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

External Data

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