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P62826

- RAN_HUMAN

UniProt

P62826 - RAN_HUMAN

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
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    7. transcription coactivator activity Source: UniProtKB

    GO - Biological processi

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

    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. melanosome Source: UniProtKB-SubCell
    5. membrane Source: UniProtKB
    6. nuclear pore Source: UniProtKB
    7. nucleoplasm Source: Reactome
    8. nucleus Source: UniProt

    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

    ArrayExpressiP62826.
    BgeeiP62826.
    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
    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. 102 interactions.
    DIPiDIP-5929N.
    IntActiP62826. 42 interactions.
    MINTiMINT-94188.

    Structurei

    Secondary structure

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

    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.
    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

    MAAQGEPQVQ FKLVLVGDGG TGKTTFVKRH LTGEFEKKYV ATLGVEVHPL    50
    VFHTNRGPIK FNVWDTAGQE KFGGLRDGYY IQAQCAIIMF DVTSRVTYKN 100
    VPNWHRDLVR VCENIPIVLC GNKVDIKDRK VKAKSIVFHR KKNLQYYDIS 150
    AKSNYNFEKP FLWLARKLIG DPNLEFVAMP ALAPPEVVMD PALAAQYEHD 200
    LEVAQTTALP DEDDDL 216
    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_006325.3.
    XP_005253649.1. XM_005253592.2.
    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_006325.3.
    XP_005253649.1. XM_005253592.2.
    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. 102 interactions.
    DIPi DIP-5929N.
    IntActi P62826. 42 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.
    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

    ArrayExpressi P62826.
    Bgeei P62826.
    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

    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 1, 2014
    This is version 138 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

    Dasty 3