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Q6P5F9

- XPO1_MOUSE

UniProt

Q6P5F9 - XPO1_MOUSE

Protein

Exportin-1

Gene

Xpo1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    Mediates the nuclear export of cellular proteins (cargos) bearing a leucine-rich nuclear export signal (NES) and of RNAs. In the nucleus, in association with RANBP3, binds cooperatively to the NES on its target protein and to the GTPase Ran in its active GTP-bound form. Docking of this 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 cargo from the export receptor. 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. Involved in U3 snoRNA transport from Cajal bodies to nucleoli. Binds to late precursor U3 snoRNA bearing a TMG cap By similarity.By similarity

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. protein transporter activity Source: MGI
    3. RNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. mRNA transport Source: UniProtKB-KW
    2. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    3. protein export from nucleus Source: MGI
    4. protein localization to nucleus Source: MGI
    5. regulation of centrosome duplication Source: MGI
    6. regulation of protein catabolic process Source: MGI
    7. regulation of protein export from nucleus Source: MGI
    8. response to drug Source: Ensembl

    Keywords - Biological processi

    mRNA transport, Protein transport, Transport

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_198691. HuR stabilizes mRNA.
    REACT_198961. Resolution of Sister Chromatid Cohesion.
    REACT_206803. Cyclin A/B1 associated events during G2/M transition.
    REACT_207679. Separation of Sister Chromatids.
    REACT_215733. Downregulation of TGF-beta receptor signaling.
    REACT_219771. deactivation of the beta-catenin transactivating complex.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Exportin-1
    Short name:
    Exp1
    Alternative name(s):
    Chromosome region maintenance 1 protein homolog
    Gene namesi
    Name:Xpo1
    Synonyms:Crm1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:2144013. Xpo1.

    Subcellular locationi

    Cytoplasm By similarity. Nucleusnucleoplasm By similarity. NucleusCajal body By similarity. Nucleusnucleolus By similarity
    Note: Located in the nucleoplasm, Cajal bodies and nucleoli. Shuttles between the nucleus/nucleolus and the cytoplasm By similarity.By similarity

    GO - Cellular componenti

    1. annulate lamellae Source: Ensembl
    2. Cajal body Source: UniProtKB-SubCell
    3. cytoplasm Source: UniProtKB-SubCell
    4. kinetochore Source: UniProtKB
    5. nucleolus Source: UniProtKB-SubCell
    6. nucleus Source: MGI
    7. ribonucleoprotein complex Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10711071Exportin-1PRO_0000204706Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei391 – 3911PhosphoserineBy similarity
    Modified residuei446 – 4461N6-acetyllysine1 Publication
    Modified residuei448 – 4481PhosphothreonineBy similarity
    Modified residuei450 – 4501PhosphoserineBy similarity
    Modified residuei454 – 4541PhosphotyrosineBy similarity
    Modified residuei693 – 6931N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ6P5F9.
    PaxDbiQ6P5F9.
    PRIDEiQ6P5F9.

    PTM databases

    PhosphoSiteiQ6P5F9.

    Expressioni

    Gene expression databases

    ArrayExpressiQ6P5F9.
    BgeeiQ6P5F9.
    CleanExiMM_XPO1.
    GenevestigatoriQ6P5F9.

    Interactioni

    Subunit structurei

    Found in a U snRNA export complex with RNUXA/PHAX, NCBP1, NCBP2, RAN, XPO1 and m7G-capped RNA. 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. Found in a nuclear export complex with RANBP3 and RAN. Found in a 60S ribosomal subunit export complex with NMD3, RAN, XPO1. Interacts with DDX3X, NMD3, NUPL2, NUP88, NUP214, RANBP3 and TERT. Interacts with NEMF (via its N-terminus). Interacts with the monomeric form of BIRC5/survivin deacetylated at 'Lys-129'. Interacts with DTNBP1 and SERTAD2; the interactions translocate DTNBP1 and SERTAD2 out of the nucleus. Interacts with ATF2. Interacts with SLC35G1 and STIM1 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi222117. 10 interactions.
    DIPiDIP-48612N.
    IntActiQ6P5F9. 4 interactions.
    STRINGi10090.ENSMUSP00000099934.

    Structurei

    Secondary structure

    1
    1071
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi18 – 203
    Helixi25 – 339
    Turni34 – 363
    Helixi40 – 5112
    Turni52 – 543
    Beta strandi55 – 573
    Helixi59 – 635
    Helixi73 – 8917
    Helixi91 – 933
    Helixi96 – 11419
    Helixi117 – 1204
    Helixi124 – 14118
    Turni142 – 1454
    Helixi149 – 15911
    Helixi161 – 17818
    Helixi182 – 1854
    Helixi188 – 20013
    Helixi203 – 21513
    Helixi219 – 23214
    Turni233 – 2353
    Helixi239 – 2424
    Beta strandi243 – 2453
    Helixi246 – 2538
    Beta strandi255 – 2573
    Helixi258 – 27316
    Helixi277 – 2793
    Helixi280 – 29718
    Beta strandi300 – 3023
    Helixi304 – 3096
    Helixi315 – 33925
    Helixi341 – 3433
    Helixi344 – 35714
    Helixi363 – 38321
    Helixi404 – 4074
    Helixi410 – 42213
    Beta strandi430 – 4345
    Beta strandi436 – 4383
    Beta strandi440 – 4445
    Helixi449 – 46719
    Helixi469 – 48416
    Helixi491 – 50313
    Turni504 – 5063
    Helixi510 – 53021
    Helixi534 – 55017
    Helixi552 – 5576
    Helixi559 – 57214
    Helixi580 – 59415
    Helixi596 – 5994
    Helixi610 – 6156
    Helixi618 – 6225
    Helixi627 – 64115
    Helixi647 – 65711
    Helixi659 – 67416
    Helixi676 – 6805
    Helixi682 – 70221
    Helixi704 – 7063
    Helixi707 – 73529
    Helixi737 – 7404
    Helixi743 – 76321
    Helixi769 – 7757
    Helixi778 – 7836
    Helixi785 – 7906
    Helixi793 – 7953
    Helixi799 – 81113
    Helixi812 – 8143
    Helixi816 – 8183
    Helixi819 – 83416
    Beta strandi838 – 8403
    Helixi842 – 85817
    Helixi860 – 8623
    Turni863 – 8653
    Helixi868 – 88215
    Helixi887 – 90418
    Helixi908 – 93023
    Helixi936 – 9383
    Helixi939 – 95315
    Turni954 – 9563
    Beta strandi961 – 9633
    Turni965 – 9684
    Helixi970 – 98516
    Beta strandi987 – 9893
    Helixi991 – 100313
    Turni1004 – 10063
    Helixi1008 – 102215
    Turni1027 – 10293
    Helixi1037 – 105216

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3GJXX-ray2.50A/D1-1071[»]
    3NBYX-ray3.42A/D1-1071[»]
    3NBZX-ray2.80A/D1-1071[»]
    3NC0X-ray2.90A/D1-1071[»]
    3NC1X-ray3.35A1-1071[»]
    ProteinModelPortaliQ6P5F9.
    SMRiQ6P5F9. Positions 53-1061.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ6P5F9.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini46 – 11267Importin N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Repeati217 – 24024HEAT 1Add
    BLAST
    Repeati241 – 27737HEAT 2Add
    BLAST
    Repeati354 – 472119HEAT 3Add
    BLAST
    Repeati515 – 55339HEAT 4Add
    BLAST
    Repeati560 – 59738HEAT 5Add
    BLAST
    Repeati602 – 63938HEAT 6Add
    BLAST
    Repeati775 – 81339HEAT 7Add
    BLAST
    Repeati885 – 91632HEAT 8Add
    BLAST
    Repeati917 – 95438HEAT 9Add
    BLAST
    Repeati1002 – 103938HEAT 10Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni327 – 450124Necessary for interaction with Ran and nuclear export complex formationBy similarityAdd
    BLAST
    Regioni411 – 48171Necessary for interaction with RANBP3By similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the exportin family.Curated
    Contains 10 HEAT repeats.Curated
    Contains 1 importin N-terminal domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG5101.
    GeneTreeiENSGT00390000000572.
    HOGENOMiHOG000209012.
    HOVERGENiHBG052817.
    InParanoidiQ6P5F9.
    KOiK14290.
    OMAiQTYFTDI.
    OrthoDBiEOG7CZK4S.
    PhylomeDBiQ6P5F9.
    TreeFamiTF105695.

    Family and domain databases

    Gene3Di1.25.10.10. 3 hits.
    InterProiIPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR014877. CRM1_C_dom.
    IPR013598. Exportin-1/Importin-b-like.
    IPR001494. Importin-beta_N.
    [Graphical view]
    PfamiPF08767. CRM1_C. 1 hit.
    PF03810. IBN_N. 1 hit.
    PF08389. Xpo1. 1 hit.
    [Graphical view]
    SMARTiSM01102. CRM1_C. 1 hit.
    SM00913. IBN_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 4 hits.
    PROSITEiPS50166. IMPORTIN_B_NT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q6P5F9-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPAIMTMLAD HAARQLLDFS QKLDINLLDN VVNCLYHGEG AQQRMAQEVL     50
    THLKEHPDAW TRVDTILEFS QNMNTKYYGL QILENVIKTR WKILPRNQCE 100
    GIKKYVVGLI IKTSSDPTCV EKEKVYIGKL NMILVQILKQ EWPKHWPTFI 150
    SDIVGASRTS ESLCQNNMVI LKLLSEEVFD FSSGQITQVK AKHLKDSMCN 200
    EFSQIFQLCQ FVMENSQNAP LVHATLETLL RFLNWIPLGY IFETKLISTL 250
    IYKFLNVPMF RNVSLKCLTE IAGVSVSQYE EQFETLFTLT MMQLKQMLPL 300
    NTNIRLAYSN GKDDEQNFIQ NLSLFLCTFL KEHGQLLEKR LNLREALMEA 350
    LHYMLLVSEV EETEIFKICL EYWNHLAAEL YRESPFSTSA SPLLSGSQHF 400
    DIPPRRQLYL TVLSKVRLLM VSRMAKPEEV LVVENDQGEV VREFMKDTDS 450
    INLYKNMRET LVYLTHLDYV DTEIIMTKKL QNQVNGTEWS WKNLNTLCWA 500
    IGSISGAMHE EDEKRFLVTV IKDLLGLCEQ KRGKDNKAII ASNIMYIVGQ 550
    YPRFLRAHWK FLKTVVNKLF EFMHETHDGV QDMACDTFIK IAQKCRRHFV 600
    QVQVGEVMPF IDEILNNINT IICDLQPQQV HTFYEAVGYM IGAQTDQTVQ 650
    EHLIEKYMLL PNQVWDSIIQ QATKNVDILK DPETVKQLGS ILKTNVRACK 700
    AVGHPFVIQL GRIYLDMLNV YKCLSENISA AIQANGEMVT KQPLIRSMRT 750
    VKRETLKLIS GWVSRSNDPQ MVAENFVPPL LDAVLIDYQR NVPAAREPEV 800
    LSTMAIIVNK LGGHITAEIP QIFDAVFECT LNMINKDFEE YPEHRTNFFL 850
    LLQAVNSHCF PAFLAIPPAQ FKLVLDSIIW AFKHTMRNVA DTGLQILFTL 900
    LQNVAQEEAA AQSFYQTYFC DILQHIFSVV TDTSHTAGLT MHASILAYMF 950
    NLVEEGKIST PLNPGNPVNN QMFIQDYVAN LLKSAFPHLQ DAQVKLFVTG 1000
    LFSLNQDIPA FKEHLRDFLV QIKEFAGEDT SDLFLEERET ALRQAQEEKH 1050
    KLQMSVPGIL NPHEIPEEMC D 1071
    Length:1,071
    Mass (Da):123,093
    Last modified:July 5, 2004 - v1
    Checksum:iB451A19780024562
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC062912 mRNA. Translation: AAH62912.1.
    CCDSiCCDS24475.1.
    RefSeqiNP_001030303.1. NM_001035226.1.
    NP_598775.2. NM_134014.3.
    XP_006514493.1. XM_006514430.1.
    UniGeneiMm.217547.

    Genome annotation databases

    EnsembliENSMUST00000020538; ENSMUSP00000020538; ENSMUSG00000020290.
    ENSMUST00000102869; ENSMUSP00000099933; ENSMUSG00000020290.
    ENSMUST00000102870; ENSMUSP00000099934; ENSMUSG00000020290.
    ENSMUST00000109551; ENSMUSP00000105178; ENSMUSG00000020290.
    GeneIDi103573.
    KEGGimmu:103573.
    UCSCiuc007iet.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC062912 mRNA. Translation: AAH62912.1 .
    CCDSi CCDS24475.1.
    RefSeqi NP_001030303.1. NM_001035226.1.
    NP_598775.2. NM_134014.3.
    XP_006514493.1. XM_006514430.1.
    UniGenei Mm.217547.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3GJX X-ray 2.50 A/D 1-1071 [» ]
    3NBY X-ray 3.42 A/D 1-1071 [» ]
    3NBZ X-ray 2.80 A/D 1-1071 [» ]
    3NC0 X-ray 2.90 A/D 1-1071 [» ]
    3NC1 X-ray 3.35 A 1-1071 [» ]
    ProteinModelPortali Q6P5F9.
    SMRi Q6P5F9. Positions 53-1061.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 222117. 10 interactions.
    DIPi DIP-48612N.
    IntActi Q6P5F9. 4 interactions.
    STRINGi 10090.ENSMUSP00000099934.

    PTM databases

    PhosphoSitei Q6P5F9.

    Proteomic databases

    MaxQBi Q6P5F9.
    PaxDbi Q6P5F9.
    PRIDEi Q6P5F9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000020538 ; ENSMUSP00000020538 ; ENSMUSG00000020290 .
    ENSMUST00000102869 ; ENSMUSP00000099933 ; ENSMUSG00000020290 .
    ENSMUST00000102870 ; ENSMUSP00000099934 ; ENSMUSG00000020290 .
    ENSMUST00000109551 ; ENSMUSP00000105178 ; ENSMUSG00000020290 .
    GeneIDi 103573.
    KEGGi mmu:103573.
    UCSCi uc007iet.1. mouse.

    Organism-specific databases

    CTDi 7514.
    MGIi MGI:2144013. Xpo1.

    Phylogenomic databases

    eggNOGi COG5101.
    GeneTreei ENSGT00390000000572.
    HOGENOMi HOG000209012.
    HOVERGENi HBG052817.
    InParanoidi Q6P5F9.
    KOi K14290.
    OMAi QTYFTDI.
    OrthoDBi EOG7CZK4S.
    PhylomeDBi Q6P5F9.
    TreeFami TF105695.

    Enzyme and pathway databases

    Reactomei REACT_198691. HuR stabilizes mRNA.
    REACT_198961. Resolution of Sister Chromatid Cohesion.
    REACT_206803. Cyclin A/B1 associated events during G2/M transition.
    REACT_207679. Separation of Sister Chromatids.
    REACT_215733. Downregulation of TGF-beta receptor signaling.
    REACT_219771. deactivation of the beta-catenin transactivating complex.

    Miscellaneous databases

    ChiTaRSi XPO1. mouse.
    EvolutionaryTracei Q6P5F9.
    NextBioi 356011.
    PROi Q6P5F9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6P5F9.
    Bgeei Q6P5F9.
    CleanExi MM_XPO1.
    Genevestigatori Q6P5F9.

    Family and domain databases

    Gene3Di 1.25.10.10. 3 hits.
    InterProi IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR014877. CRM1_C_dom.
    IPR013598. Exportin-1/Importin-b-like.
    IPR001494. Importin-beta_N.
    [Graphical view ]
    Pfami PF08767. CRM1_C. 1 hit.
    PF03810. IBN_N. 1 hit.
    PF08389. Xpo1. 1 hit.
    [Graphical view ]
    SMARTi SM01102. CRM1_C. 1 hit.
    SM00913. IBN_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 4 hits.
    PROSITEi PS50166. IMPORTIN_B_NT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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].
      Strain: C57BL/6.
      Tissue: Brain.
    2. "PHAX, a mediator of U snRNA nuclear export whose activity is regulated by phosphorylation."
      Ohno M., Segref A., Bachi A., Wilm M., Mattaj I.W.
      Cell 101:187-198(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A U SNRNA EXPORT COMPLEX WITH NCBP1; NCBP2; RAN; RNUXA/PHAX AND M7G-CAPPED RNA.
    3. "Nucleocytoplasmic shuttling of dysbindin-1, a schizophrenia-related protein, regulates synapsin I expression."
      Fei E., Ma X., Zhu C., Xue T., Yan J., Xu Y., Zhou J., Wang G.
      J. Biol. Chem. 285:38630-38640(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DTNBP1, FUNCTION.
    4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiXPO1_MOUSE
    AccessioniPrimary (citable) accession number: Q6P5F9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 21, 2005
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 101 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3