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O43592

- XPOT_HUMAN

UniProt

O43592 - XPOT_HUMAN

Protein

Exportin-T

Gene

XPOT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 2 (30 May 2006)
      Previous versions | rss
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    Functioni

    Mediates the nuclear export of aminoacylated tRNAs. In the nucleus binds to tRNA and to the GTPase Ran in its active GTP-bound form. Docking of this trimeric complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of a nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the tRNA from the export receptor. XPOT then return to the nuclear compartment and mediate another round of transport. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus.3 Publications

    GO - Molecular functioni

    1. tRNA binding Source: UniProtKB

    GO - Biological processi

    1. intracellular protein transport Source: InterPro
    2. tRNA export from nucleus Source: UniProtKB

    Keywords - Biological processi

    Transport

    Keywords - Ligandi

    RNA-binding, tRNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Exportin-T
    Alternative name(s):
    Exportin(tRNA)
    tRNA exportin
    Gene namesi
    Name:XPOT
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:12826. XPOT.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: Nuclear, once bound to tRNA and Ran the complex translocates to the cytoplasm. Shuttles between the nucleus and the cytoplasm.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nucleoplasm Source: UniProtKB
    3. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi405 – 4095RKQLK → AAQLA: Abolishes binding to tRNA. Does not abolish shuttling behavior. 1 Publication
    Mutagenesisi539 – 5435KVRSR → AVRSA: Does not abolish binding to tRNA. Does not abolish shuttling behavior. 1 Publication
    Mutagenesisi547 – 5515LFSRF → AFSRA: Does not abolish binding to tRNA. Does not abolish shuttling behavior. 1 Publication
    Mutagenesisi548 – 5525FSRFV → ASRFA: Does not abolish binding to tRNA. Does not abolish shuttling behavior. 1 Publication
    Mutagenesisi550 – 5578RFVKSLNK → AFVASLNA: Abolishes binding to tRNA. Does not abolish shuttling behavior. 1 Publication

    Organism-specific databases

    PharmGKBiPA37419.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 962962Exportin-TPRO_0000204716Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine3 Publications
    Modified residuei634 – 6341N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiO43592.
    PaxDbiO43592.
    PRIDEiO43592.

    PTM databases

    PhosphoSiteiO43592.

    Expressioni

    Gene expression databases

    ArrayExpressiO43592.
    BgeeiO43592.
    CleanExiHS_XPOT.
    GenevestigatoriO43592.

    Organism-specific databases

    HPAiHPA038660.
    HPA048067.

    Interactioni

    Subunit structurei

    Found in a complex with XPOT, Ran and tRNA. Probably found in a complex with nucleoporins. Interacts with Ran and tRNA in a GTP-dependent manner.3 Publications

    Protein-protein interaction databases

    BioGridi116420. 25 interactions.
    IntActiO43592. 9 interactions.
    MINTiMINT-1138512.
    STRINGi9606.ENSP00000327821.

    Structurei

    3D structure databases

    ProteinModelPortaliO43592.
    SMRiO43592. Positions 8-961.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 385385Necessary for interaction with Ran, nuclear localization and nuclear importAdd
    BLAST
    Regioni443 – 962520Necessary for tRNA-binding, cytoplasmic localization and nuclear exportAdd
    BLAST

    Sequence similaritiesi

    Belongs to the exportin family.Curated

    Phylogenomic databases

    eggNOGiNOG270401.
    HOGENOMiHOG000007104.
    HOVERGENiHBG094163.
    InParanoidiO43592.
    KOiK14288.
    OMAiKMRYDET.
    OrthoDBiEOG7SN8BQ.
    PhylomeDBiO43592.
    TreeFamiTF314001.

    Family and domain databases

    Gene3Di1.25.10.10. 2 hits.
    InterProiIPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR013598. Exportin-1/Importin-b-like.
    IPR001494. Importin-beta_N.
    [Graphical view]
    PfamiPF08389. Xpo1. 1 hit.
    [Graphical view]
    SMARTiSM00913. IBN_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    O43592-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDEQALLGLN PNADSDFRQR ALAYFEQLKI SPDAWQVCAE ALAQRTYSDD    50
    HVKFFCFQVL EHQVKYKYSE LTTVQQQLIR ETLISWLQAQ MLNPQPEKTF 100
    IRNKAAQVFA LLFVTEYLTK WPKFFFDILS VVDLNPRGVD LYLRILMAID 150
    SELVDRDVVH TSEEARRNTL IKDTMREQCI PNLVESWYQI LQNYQFTNSE 200
    VTCQCLEVVG AYVSWIDLSL IANDRFINML LGHMSIEVLR EEACDCLFEV 250
    VNKGMDPVDK MKLVESLCQV LQSAGFFSID QEEDVDFLAR FSKLVNGMGQ 300
    SLIVSWSKLI KNGDIKNAQE ALQAIETKVA LMLQLLIHED DDISSNIIGF 350
    CYDYLHILKQ LTVLSDQQKA NVEAIMLAVM KKLTYDEEYN FENEGEDEAM 400
    FVEYRKQLKL LLDRLAQVSP ELLLASVRRV FSSTLQNWQT TRFMEVEVAI 450
    RLLYMLAEAL PVSHGAHFSG DVSKASALQD MMRTLVTSGV SSYQHTSVTL 500
    EFFETVVRYE KFFTVEPQHI PCVLMAFLDH RGLRHSSAKV RSRTAYLFSR 550
    FVKSLNKQMN PFIEDILNRI QDLLELSPPE NGHQSLLSSD DQLFIYETAG 600
    VLIVNSEYPA ERKQALMRNL LTPLMEKFKI LLEKLMLAQD EERQASLADC 650
    LNHAVGFASR TSKAFSNKQT VKQCGCSEVY LDCLQTFLPA LSCPLQKDIL 700
    RSGVRTFLHR MIICLEEEVL PFIPSASEHM LKDCEAKDLQ EFIPLINQIT 750
    AKFKIQVSPF LQQMFMPLLH AIFEVLLRPA EENDQSAALE KQMLRRSYFA 800
    FLQTVTGSGM SEVIANQGAE NVERVLVTVI QGAVEYPDPI AQKTCFIILS 850
    KLVELWGGKD GPVGFADFVY KHIVPACFLA PLKQTFDLAD AQTVLALSEC 900
    AVTLKTIHLK RGPECVQYLQ QEYLPSLQVA PEIIQEFCQA LQQPDAKVFK 950
    NYLKVFFQRA KP 962
    Length:962
    Mass (Da):109,964
    Last modified:May 30, 2006 - v2
    Checksum:i2F407EEDEC7C2996
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti360 – 3601Q → R in AAC39793. (PubMed:9660920)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti526 – 5261A → V.1 Publication
    Corresponds to variant rs17851795 [ dbSNP | Ensembl ].
    VAR_026528
    Natural varianti716 – 7161E → D.
    Corresponds to variant rs1051396 [ dbSNP | Ensembl ].
    VAR_048962

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF039022 mRNA. Translation: AAC39793.1.
    Y16414 mRNA. Translation: CAA76202.1.
    AC135279 Genomic DNA. No translation available.
    BC000950 mRNA. Translation: AAH00950.1.
    BC020569 mRNA. Translation: AAH20569.1.
    CCDSiCCDS31852.1.
    RefSeqiNP_009166.2. NM_007235.4.
    UniGeneiHs.85951.

    Genome annotation databases

    EnsembliENST00000332707; ENSP00000327821; ENSG00000184575.
    GeneIDi11260.
    KEGGihsa:11260.
    UCSCiuc001ssb.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF039022 mRNA. Translation: AAC39793.1 .
    Y16414 mRNA. Translation: CAA76202.1 .
    AC135279 Genomic DNA. No translation available.
    BC000950 mRNA. Translation: AAH00950.1 .
    BC020569 mRNA. Translation: AAH20569.1 .
    CCDSi CCDS31852.1.
    RefSeqi NP_009166.2. NM_007235.4.
    UniGenei Hs.85951.

    3D structure databases

    ProteinModelPortali O43592.
    SMRi O43592. Positions 8-961.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116420. 25 interactions.
    IntActi O43592. 9 interactions.
    MINTi MINT-1138512.
    STRINGi 9606.ENSP00000327821.

    PTM databases

    PhosphoSitei O43592.

    Proteomic databases

    MaxQBi O43592.
    PaxDbi O43592.
    PRIDEi O43592.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000332707 ; ENSP00000327821 ; ENSG00000184575 .
    GeneIDi 11260.
    KEGGi hsa:11260.
    UCSCi uc001ssb.3. human.

    Organism-specific databases

    CTDi 11260.
    GeneCardsi GC12P064798.
    HGNCi HGNC:12826. XPOT.
    HPAi HPA038660.
    HPA048067.
    MIMi 603180. gene.
    neXtProti NX_O43592.
    PharmGKBi PA37419.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG270401.
    HOGENOMi HOG000007104.
    HOVERGENi HBG094163.
    InParanoidi O43592.
    KOi K14288.
    OMAi KMRYDET.
    OrthoDBi EOG7SN8BQ.
    PhylomeDBi O43592.
    TreeFami TF314001.

    Miscellaneous databases

    ChiTaRSi XPOT. human.
    GeneWikii XPOT.
    GenomeRNAii 11260.
    NextBioi 42852.
    PROi O43592.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O43592.
    Bgeei O43592.
    CleanExi HS_XPOT.
    Genevestigatori O43592.

    Family and domain databases

    Gene3Di 1.25.10.10. 2 hits.
    InterProi IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR013598. Exportin-1/Importin-b-like.
    IPR001494. Importin-beta_N.
    [Graphical view ]
    Pfami PF08389. Xpo1. 1 hit.
    [Graphical view ]
    SMARTi SM00913. IBN_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 431-440 AND 739-752, FUNCTION IN TRNA EXPORT, IDENTIFICATION IN A COMPLEX WITH RAN AND TRNA, TRNA-BINDING, SUBCELLULAR LOCATION.
      Tissue: Cervix carcinoma.
    2. "Identification of a nuclear export receptor for tRNA."
      Arts G.-J., Fornerod M., Mattaj I.W.
      Curr. Biol. 8:305-314(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN TRNA EXPORT, IDENTIFICATION IN A COMPLEX WITH RAN AND TRNA, TRNA-BINDING, SUBCELLULAR LOCATION.
      Tissue: Cervix carcinoma.
    3. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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], VARIANT VAL-526.
      Tissue: Lymph and Placenta.
    5. Bienvenut W.V.
      Submitted (JUN-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 21-29; 54-65; 317-328; 360-369 AND 825-851, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma.
    6. "The role of exportin-t in selective nuclear export of mature tRNAs."
      Arts G.-J., Kuersten S., Romby P., Ehresmann B., Mattaj I.W.
      EMBO J. 17:7430-7441(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: TRNA-BINDING.
    7. "Steady-state nuclear localization of exportin-t involves RanGTP binding and two distinct nuclear pore complex interaction domains."
      Kuersten S., Arts G.-J., Walther T.C., Englmeier L., Mattaj I.W.
      Mol. Cell. Biol. 22:5708-5720(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TRNA EXPORT, MUTAGENESIS OF 405-ARG--LYS-409; 539-LYS--ARG-543; 547-LEU--PHE-551; 548-PHE--VAL-552 AND 550-ARG--LYS-557, IDENTIFICATION IN COMPLEX WITH RAN AND TRNA, IDENTIFICATION IN COMPLEX WITH EXPORTINS, TRNA-BINDING, SUBCELLULAR LOCATION.
    8. "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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    9. "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-634, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiXPOT_HUMAN
    AccessioniPrimary (citable) accession number: O43592
    Secondary accession number(s): A6NLH1
    , O43784, Q8WUG2, Q9BVS7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 2, 2001
    Last sequence update: May 30, 2006
    Last modified: October 1, 2014
    This is version 119 of the entry and version 2 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

    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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3