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O14980

- XPO1_HUMAN

UniProt

O14980 - XPO1_HUMAN

Protein

Exportin-1

Gene

XPO1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      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 (Ran-GTP). 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. Several viruses, among them HIV-1, HTLV-1 and influenza A use it to export their unspliced or incompletely spliced RNAs out of the nucleus. Interacts with, and mediates the nuclear export of HIV-1 Rev and HTLV-1 Rex proteins. Involved in HTLV-1 Rex multimerization.6 Publications

    GO - Molecular functioni

    1. nucleocytoplasmic transporter activity Source: BHF-UCL
    2. protein binding Source: UniProtKB
    3. protein transporter activity Source: Ensembl
    4. RNA binding Source: UniProtKB-KW
    5. transporter activity Source: Reactome

    GO - Biological processi

    1. gene expression Source: Reactome
    2. intracellular transport of virus Source: Reactome
    3. mitotic cell cycle Source: Reactome
    4. mRNA metabolic process Source: Reactome
    5. mRNA transport Source: UniProtKB-KW
    6. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    7. negative regulation of transforming growth factor beta receptor signaling pathway Source: Reactome
    8. protein export from nucleus Source: BHF-UCL
    9. protein localization to nucleus Source: Ensembl
    10. regulation of centrosome duplication Source: Ensembl
    11. regulation of protein catabolic process Source: Ensembl
    12. regulation of protein export from nucleus Source: Ensembl
    13. response to drug Source: Ensembl
    14. ribosomal large subunit export from nucleus Source: BHF-UCL
    15. ribosomal small subunit export from nucleus Source: BHF-UCL
    16. RNA metabolic process Source: Reactome
    17. transforming growth factor beta receptor signaling pathway Source: Reactome
    18. viral life cycle Source: Reactome
    19. viral process Source: Reactome

    Keywords - Biological processi

    Host-virus interaction, mRNA transport, Protein transport, Transport

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_120727. Downregulation of TGF-beta receptor signaling.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_1857. Cyclin A/B1 associated events during G2/M transition.
    REACT_200731. deactivation of the beta-catenin transactivating complex.
    REACT_25218. HuR stabilizes mRNA.
    REACT_6179. NEP/NS2 Interacts with the Cellular Export Machinery.
    REACT_6190. Rev-mediated nuclear export of HIV RNA.
    REACT_682. Mitotic Prometaphase.
    SignaLinkiO14980.

    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:12825. XPO1.

    Subcellular locationi

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

    GO - Cellular componenti

    1. annulate lamellae Source: UniProtKB
    2. Cajal body Source: UniProtKB-SubCell
    3. cytoplasm Source: HPA
    4. cytosol Source: Reactome
    5. intracellular membrane-bounded organelle Source: HPA
    6. kinetochore Source: UniProtKB
    7. membrane Source: UniProtKB
    8. nuclear envelope Source: ProtInc
    9. nuclear membrane Source: HPA
    10. nucleolus Source: UniProtKB-SubCell
    11. nucleoplasm Source: Reactome
    12. nucleus Source: HPA
    13. ribonucleoprotein complex Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi191 – 1911S → A: Does not abolish Rex-mediated mRNA export. 1 Publication
    Mutagenesisi284 – 2841V → E: Does not abolish Rex-mediated mRNA export. 1 Publication
    Mutagenesisi334 – 3341D → G: Does not abolish Rex-mediated mRNA export. 1 Publication
    Mutagenesisi337 – 3371I → L: Does not abolish Rex-mediated mRNA export. 1 Publication
    Mutagenesisi346 – 3461T → A: Does not abolish Rex-mediated mRNA export. 1 Publication
    Mutagenesisi402 – 4021V → I: Does not abolish Rex-mediated mRNA export. 1 Publication
    Mutagenesisi411 – 4111P → T: Strongly abolishes interaction with Rex and RANBP3, abolishes Rex-mediated mRNA export. Does not abolish interaction with RANBP3; when associated with S-414. Abolishes Rex multimerization; when associated with S-414. 1 Publication
    Mutagenesisi412 – 4121M → V: Does not abolish interaction with Rex and RANBP3, and Rex-mediated mRNA export. 1 Publication
    Mutagenesisi414 – 4141F → S: Strongly abolishes interaction with Rex and RANBP3, abolishes Rex-mediated mRNA export. Does not abolish interaction with RANBP3; when associated with T-411. Abolishes Rex multimerization; when associated with T-411. 1 Publication
    Mutagenesisi428 – 44720EEVLV…EFMKD → QQVLVVQNNQGQVVRQFMKN: Abolishes Ran binding activity in absence of cargo and abolishes partially Ran binding activity in presence of cargo. Add
    BLAST
    Mutagenesisi430 – 44617VLVVE…REFMK → DEDEENDQGEDEEEDDD: Partially restores Ran binding activity in presence of cargo. Add
    BLAST
    Mutagenesisi430 – 4334VLVV → DEDE: Abolishes Ran binding activity both in absence or presence of cargo.
    Mutagenesisi454 – 4541Y → A: Does not abolish Ran binding activity and nuclear export complex formation. 1 Publication
    Mutagenesisi474 – 4741R → I: Strongly abolishes interaction with Rex and RANBP3, abolishes Rex-mediated mRNA export. 1 Publication
    Mutagenesisi481 – 4811H → Q: Strongly abolishes interaction with Rex and RANBP3, abolishes Rex-mediated mRNA export. 1 Publication
    Mutagenesisi513 – 5131E → A: Abolishes Ran binding activity and nuclear export complex formation. Abolishes Ran binding activity and nuclear export complex formation; when associated with A-553 and A-554. 1 Publication
    Mutagenesisi525 – 5251L → A: Enhances Ran binding activity and does not abolish nuclear export complex formation. Does not abolish Ran binding activity and partially abolish nuclear export complex formation; when associated with A-561. Does not abolish Ran binding activity and partially abolish nuclear export complex formation; when associated with A-568 and A-572. 1 Publication
    Mutagenesisi550 – 5501Q → A: Enhances Ran binding activity and does not abolish nuclear export complex formation; when associated with A-553 and A-590. 1 Publication
    Mutagenesisi553 – 5531R → A: Enhances Ran binding activity and does not abolish nuclear export complex formation; when associated with A-550 and A-590. Abolishes Ran binding activity and nuclear export complex formation; when associated with A-513 and A-554. 1 Publication
    Mutagenesisi554 – 5541F → A: Partially abolishes Ran binding activity and does not abolish nuclear export complex formation. Abolishes Ran binding activity and nuclear export complex formation; when associated with A-561. Abolishes Ran binding activity and nuclear export complex formation; when associated with A-553 and A-513. 1 Publication
    Mutagenesisi561 – 5611F → A: Abolishes Ran binding activity and nuclear export complex formation. Abolishes Ran binding activity and nuclear export complex formation; when associated with A-554. Does not abolish Ran binding activity and partially abolish nuclear export complex formation; when associated with A-525. 1 Publication
    Mutagenesisi568 – 5681K → A: Does not abolish Ran binding activity and partially abolish nuclear export complex formation; when associated with A-525 and A-572. 1 Publication
    Mutagenesisi572 – 5721F → A: Does not abolish Ran binding activity and partially abolish nuclear export complex formation; when associated with A-525 and A-568. 1 Publication
    Mutagenesisi583 – 5831M → A: Enhances Ran binding activity; when associated with A-590. 1 Publication
    Mutagenesisi590 – 5901K → A: Enhances Ran binding activity and does not abolish nuclear export complex formation. Enhances Ran binding activity and does not abolish nuclear export complex formation; when associated with A-583. Enhances Ran binding activity and does not abolish nuclear export complex formation; when associated with A-550 and A-553. 1 Publication

    Organism-specific databases

    PharmGKBiPA37418.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10711071Exportin-1PRO_0000204705Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei391 – 3911Phosphoserine1 Publication
    Modified residuei446 – 4461N6-acetyllysine1 Publication
    Modified residuei448 – 4481PhosphothreonineBy similarity
    Modified residuei450 – 4501PhosphoserineBy similarity
    Modified residuei454 – 4541PhosphotyrosineBy similarity
    Modified residuei693 – 6931N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO14980.
    PaxDbiO14980.
    PRIDEiO14980.

    PTM databases

    PhosphoSiteiO14980.

    Expressioni

    Tissue specificityi

    Expressed in heart, brain, placenta, lung, liver, skeletal muscle, pancreas, spleen, thymus, prostate, testis, ovary, small intestine, colon and peripheral blood leukocytes. Not expressed in the kidney.2 Publications

    Gene expression databases

    ArrayExpressiO14980.
    BgeeiO14980.
    CleanExiHS_XPO1.
    GenevestigatoriO14980.

    Organism-specific databases

    HPAiCAB010184.
    HPA042933.

    Interactioni

    Subunit structurei

    Found in a U snRNA export complex with RNUXA/PHAX, NCBP1, NCBP2, RAN, XPO1 and m7G-capped RNA By similarity. 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. Also found in complex with several viral proteins involved in RNAs' nuclear export like HIV-1 Rev and HTLV-1 Rex. Interacts presumably with influenza A nucleoprotein. Interacts with Epstein-Barr virus BMLF1. 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 similarity23 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BIRC5O153922EBI-355867,EBI-518823
    ERBB2P046262EBI-355867,EBI-641062
    PHBP352322EBI-355867,EBI-354213
    PKIAP619252EBI-355867,EBI-2682139

    Protein-protein interaction databases

    BioGridi113348. 156 interactions.
    DIPiDIP-33678N.
    IntActiO14980. 35 interactions.
    MINTiMINT-5002192.
    STRINGi9606.ENSP00000195419.

    Structurei

    Secondary structure

    1
    1071
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi63 – 686
    Helixi76 – 8914
    Helixi97 – 11317
    Helixi124 – 14118
    Turni142 – 1454
    Helixi149 – 1579
    Helixi161 – 17515
    Helixi188 – 19710
    Helixi199 – 21517
    Helixi219 – 23214
    Turni233 – 2353
    Helixi238 – 2425
    Beta strandi243 – 2453
    Helixi246 – 2538
    Turni254 – 2563
    Helixi258 – 2603
    Helixi261 – 27313
    Helixi280 – 29718
    Helixi304 – 3107
    Helixi313 – 33927
    Helixi341 – 3433
    Helixi344 – 35815
    Helixi363 – 38321
    Helixi404 – 42320
    Helixi448 – 46720
    Helixi469 – 48416
    Beta strandi485 – 4884
    Helixi491 – 50313
    Turni504 – 5063
    Helixi510 – 53021
    Helixi534 – 55017
    Helixi552 – 5576
    Helixi559 – 57214
    Helixi580 – 59516
    Helixi596 – 5983
    Beta strandi605 – 6084
    Helixi610 – 6156
    Helixi618 – 6225
    Helixi627 – 64216
    Helixi647 – 67428
    Helixi676 – 6805
    Helixi682 – 70221
    Helixi704 – 7063
    Helixi711 – 7133
    Helixi714 – 73522
    Helixi738 – 7414
    Helixi743 – 76422
    Helixi769 – 7757
    Helixi777 – 78913
    Helixi793 – 7953
    Helixi799 – 81113
    Helixi812 – 8187
    Helixi819 – 83416
    Turni837 – 8393
    Helixi842 – 85817
    Helixi862 – 8654
    Helixi868 – 88114
    Beta strandi884 – 8863
    Helixi887 – 90620
    Helixi908 – 93124
    Beta strandi932 – 9343
    Helixi939 – 95416
    Beta strandi964 – 9663
    Helixi970 – 98516
    Helixi991 – 100313
    Turni1004 – 10063
    Helixi1008 – 102316
    Turni1024 – 10263
    Turni1028 – 10303
    Helixi1031 – 105222
    Helixi1053 – 10553

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1W9CX-ray2.30A/B707-1027[»]
    2L1LNMR-B504-630[»]
    3GB8X-ray2.90A1-1071[»]
    4BSMX-ray4.50A1-1032[»]
    4BSNX-ray4.10A1-1032[»]
    ProteinModelPortaliO14980.
    SMRiO14980. Positions 53-1061.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO14980.

    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
    Regioni1 – 679679Necessary for HTLV-1 Rex-mediated mRNA exportAdd
    BLAST
    Regioni327 – 450124Interaction with Ran and nuclear export complex formationAdd
    BLAST
    Regioni411 – 48171Interaction with RANBP3Add
    BLAST
    Regioni411 – 4144Necessary for HTLV-1 Rex multimerization
    Regioni800 – 82021Interaction with HIV-1 RevAdd
    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.
    HOVERGENiHBG052817.
    InParanoidiO14980.
    KOiK14290.
    OMAiQTYFTDI.
    OrthoDBiEOG7CZK4S.
    PhylomeDBiO14980.
    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.

    O14980-1 [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 SKHLKDSMCN 200
    EFSQIFQLCQ FVMENSQNAP LVHATLETLL RFLNWIPLGY IFETKLISTL 250
    IYKFLNVPMF RNVSLKCLTE IAGVSVSQYE EQFVTLFTLT MMQLKQMLPL 300
    NTNIRLAYSN GKDDEQNFIQ NLSLFLCTFL KEHDQLIEKR LNLRETLMEA 350
    LHYMLLVSEV EETEIFKICL EYWNHLAAEL YRESPFSTSA SPLLSGSQHF 400
    DVPPRRQLYL PMLFKVRLLM VSRMAKPEEV LVVENDQGEV VREFMKDTDS 450
    INLYKNMRET LVYLTHLDYV DTERIMTEKL HNQVNGTEWS 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 PAFLAIPPTQ FKLVLDSIIW AFKHTMRNVA DTGLQILFTL 900
    LQNVAQEEAA AQSFYQTYFC DILQHIFSVV TDTSHTAGLT MHASILAYMF 950
    NLVEEGKIST SLNPGNPVNN QIFLQEYVAN LLKSAFPHLQ DAQVKLFVTG 1000
    LFSLNQDIPA FKEHLRDFLV QIKEFAGEDT SDLFLEEREI ALRQADEEKH 1050
    KRQMSVPGIF NPHEIPEEMC D 1071
    Length:1,071
    Mass (Da):123,386
    Last modified:January 1, 1998 - v1
    Checksum:iFDB00C065DA2FB1D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti406 – 4061R → G in CAH56174. (PubMed:17974005)Curated
    Sequence conflicti953 – 9531V → G in CAH18695. (PubMed:17974005)Curated
    Sequence conflicti989 – 9891L → I in CAH56174. (PubMed:17974005)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y08614 mRNA. Translation: CAA69905.2.
    D89729 mRNA. Translation: BAA23415.1.
    AK289920 mRNA. Translation: BAF82609.1.
    BX647758 mRNA. Translation: CAH56174.1.
    CR749840 mRNA. Translation: CAH18695.1.
    AC016727 Genomic DNA. Translation: AAY14949.1.
    CH471053 Genomic DNA. Translation: EAW99993.1.
    CH471053 Genomic DNA. Translation: EAW99994.1.
    BC032847 mRNA. Translation: AAH32847.1.
    CCDSiCCDS33205.1.
    RefSeqiNP_003391.1. NM_003400.3.
    XP_006712157.1. XM_006712094.1.
    UniGeneiHs.370770.

    Genome annotation databases

    EnsembliENST00000401558; ENSP00000384863; ENSG00000082898.
    ENST00000404992; ENSP00000385942; ENSG00000082898.
    ENST00000406957; ENSP00000385559; ENSG00000082898.
    GeneIDi7514.
    KEGGihsa:7514.
    UCSCiuc002sbh.3. human.

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y08614 mRNA. Translation: CAA69905.2 .
    D89729 mRNA. Translation: BAA23415.1 .
    AK289920 mRNA. Translation: BAF82609.1 .
    BX647758 mRNA. Translation: CAH56174.1 .
    CR749840 mRNA. Translation: CAH18695.1 .
    AC016727 Genomic DNA. Translation: AAY14949.1 .
    CH471053 Genomic DNA. Translation: EAW99993.1 .
    CH471053 Genomic DNA. Translation: EAW99994.1 .
    BC032847 mRNA. Translation: AAH32847.1 .
    CCDSi CCDS33205.1.
    RefSeqi NP_003391.1. NM_003400.3.
    XP_006712157.1. XM_006712094.1.
    UniGenei Hs.370770.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1W9C X-ray 2.30 A/B 707-1027 [» ]
    2L1L NMR - B 504-630 [» ]
    3GB8 X-ray 2.90 A 1-1071 [» ]
    4BSM X-ray 4.50 A 1-1032 [» ]
    4BSN X-ray 4.10 A 1-1032 [» ]
    ProteinModelPortali O14980.
    SMRi O14980. Positions 53-1061.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113348. 156 interactions.
    DIPi DIP-33678N.
    IntActi O14980. 35 interactions.
    MINTi MINT-5002192.
    STRINGi 9606.ENSP00000195419.

    Chemistry

    BindingDBi O14980.
    ChEMBLi CHEMBL5661.

    PTM databases

    PhosphoSitei O14980.

    Proteomic databases

    MaxQBi O14980.
    PaxDbi O14980.
    PRIDEi O14980.

    Protocols and materials databases

    DNASUi 7514.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000401558 ; ENSP00000384863 ; ENSG00000082898 .
    ENST00000404992 ; ENSP00000385942 ; ENSG00000082898 .
    ENST00000406957 ; ENSP00000385559 ; ENSG00000082898 .
    GeneIDi 7514.
    KEGGi hsa:7514.
    UCSCi uc002sbh.3. human.

    Organism-specific databases

    CTDi 7514.
    GeneCardsi GC02M061704.
    HGNCi HGNC:12825. XPO1.
    HPAi CAB010184.
    HPA042933.
    MIMi 602559. gene.
    neXtProti NX_O14980.
    PharmGKBi PA37418.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5101.
    HOVERGENi HBG052817.
    InParanoidi O14980.
    KOi K14290.
    OMAi QTYFTDI.
    OrthoDBi EOG7CZK4S.
    PhylomeDBi O14980.
    TreeFami TF105695.

    Enzyme and pathway databases

    Reactomei REACT_120727. Downregulation of TGF-beta receptor signaling.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_1857. Cyclin A/B1 associated events during G2/M transition.
    REACT_200731. deactivation of the beta-catenin transactivating complex.
    REACT_25218. HuR stabilizes mRNA.
    REACT_6179. NEP/NS2 Interacts with the Cellular Export Machinery.
    REACT_6190. Rev-mediated nuclear export of HIV RNA.
    REACT_682. Mitotic Prometaphase.
    SignaLinki O14980.

    Miscellaneous databases

    ChiTaRSi XPO1. human.
    EvolutionaryTracei O14980.
    GeneWikii XPO1.
    GenomeRNAii 7514.
    NextBioi 29403.
    PROi O14980.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O14980.
    Bgeei O14980.
    CleanExi HS_XPO1.
    Genevestigatori O14980.

    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 human homologue of yeast CRM1 is in a dynamic subcomplex with CAN/Nup214 and the novel nuclear pore component Nup88."
      Fornerod M., van Deursen J.M., van Baal S., Reynolds A., Davis D., Murti K.G., Fransen J., Grosveld G.
      EMBO J. 16:807-816(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 757-765, INTERACTION WITH NUP88 AND NUP214, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Placenta.
    2. "Molecular cloning and cell cycle-dependent expression of mammalian CRM1, a protein involved in nuclear export of proteins."
      Kudo N., Kohchbin S., Nishi K., Kitano K., Yanagida M., Yoshida M., Horinouchi S.
      J. Biol. Chem. 272:29742-29751(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Chronic myeloid leukemia cell.
    3. "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.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Testis.
    5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Testis.
    8. Bienvenut W.V.
      Submitted (JUN-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 45-54; 63-88; 105-112; 130-139; 159-190; 246-253; 296-305; 407-415; 424-442; 459-474; 480-492; 516-531; 538-553; 675-686; 701-722; 797-810; 873-883; 996-1012 AND 1017-1038, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma.
    9. "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: FUNCTION IN PROTEIN NUCLEAR EXPORT, IDENTIFICATION IN A NUCLEAR EXPORT COMPLEX WITH RAN.
    10. "Evidence for a role of CRM1 in signal-mediated nuclear protein export."
      Ossareh-Nazari B., Bachelerie F., Dargemont C.
      Science 278:141-144(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PROTEIN NUCLEAR EXPORT.
    11. "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: FUNCTION IN HIV-1 REV EXPORT, IDENTIFICATION IN A COMPLEX WITH HIV-1 REV; HIV-1 REV RESPONSE ELEMENT AND RAN, INTERACTION WITH HIV-1 REV.
    12. Cited for: IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX, INTERACTION WITH IPO7; KPNB1 AND SNUPN, IDENTIFICATION IN A TRIMERIC EXPORT COMPLEX WITH RAN AND SNUPN.
    13. "Association with the cellular export receptor CRM 1 mediates function and intracellular localization of Epstein-Barr virus SM protein, a regulator of gene expression."
      Boyle S.M., Ruvolo V., Gupta A.K., Swaminathan S.
      J. Virol. 73:6872-6881(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EBV BMLF1.
    14. "Leptomycin B inactivates CRM1/exportin 1 by covalent modification at a cysteine residue in the central conserved region."
      Kudo N., Matsumori N., Taoka H., Fujiwara D., Schreiner E.P., Wolff B., Yoshida M., Horinouchi S.
      Proc. Natl. Acad. Sci. U.S.A. 96:9112-9117(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INACTIVATION BY LMB.
    15. "A new nucleoporin-like protein interacts with both HIV-1 Rev nuclear export signal and CRM-1."
      Farjot G., Sergeant A., Mikaelian I.
      J. Biol. Chem. 274:17309-17317(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NUPL2.
    16. "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 RAN, INTERACTION WITH RANBP3.
    17. "Interaction of the influenza virus nucleoprotein with the cellular CRM1-mediated nuclear export pathway."
      Elton D., Simpson-Holley M., Archer K., Medcalf L., Hallam R., McCauley J., Digard P.
      J. Virol. 75:408-419(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH INFLUENZA A NUCLEOPROTEIN.
    18. "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 RAN, INTERACTION WITH RANBP3.
    19. "Ran-binding protein 3 links Crm1 to the Ran guanine nucleotide exchange factor."
      Nemergut M.E., Lindsay M.E., Brownawell A.M., Macara I.G.
      J. Biol. Chem. 277:17385-17388(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RANBP3.
    20. "The carboxy-terminal region of the human immunodeficiency virus type 1 protein Rev has multiple roles in mediating CRM1-related Rev functions."
      Hakata Y., Yamada M., Mabuchi N., Shida H.
      J. Virol. 76:8079-8089(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIV-1 REV.
    21. "Biogenesis and nuclear export of ribosomal subunits in higher eukaryotes depend on the CRM1 export pathway."
      Thomas F., Kutay U.
      J. Cell Sci. 116:2409-2419(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A 60S RIBOSOMAL SUBUNIT COMPLEX WITH RAN AND NMD3, INTERACTION WITH NMD3.
    22. "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.
    23. "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: FUNCTION IN HTLV-1 REX EXPORT, IDENTIFICATION IN A COMPLEX WITH HTLV-1 REX; RANBP3 AND RAN, INTERACTION WITH HTLV-1 REX AND RANBP3, MUTAGENESIS OF SER-191; VAL-284; ASP-334; ILE-337; THR-346; VAL-402; PRO-411; MET-412; PHE-414; ARG-474 AND HIS-481.
    24. "Requirement of DDX3 DEAD box RNA helicase for HIV-1 Rev-RRE export function."
      Yedavalli V.S., Neuveut C., Chi Y.-H., Kleiman L., Jeang K.-T.
      Cell 119:381-392(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DDX3X.
    25. "PHAX and CRM1 are required sequentially to transport U3 snoRNA to nucleoli."
      Boulon S., Verheggen C., Jady B.E., Girard C., Pescia C., Paul C., Ospina J.K., Kiss T., Matera A.G., Bordonne R., Bertrand E.
      Mol. Cell 16:777-787(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN U3 SNORNA TRANSPORT, SUBCELLULAR LOCATION, RNA-BINDING.
    26. "Kinetic and molecular analysis of nuclear export factor CRM1 association with its cargo in vivo."
      Daelemans D., Costes S.V., Lockett S., Pavlakis G.N.
      Mol. Cell. Biol. 25:728-739(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIV-1 REV, SUBCELLULAR LOCATION.
    27. "Drosophila caliban, a nuclear export mediator, can function as a tumor suppressor in human lung cancer cells."
      Bi X., Jones T., Abbasi F., Lee H., Stultz B., Hursh D.A., Mortin M.A.
      Oncogene 24:8229-8239(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NEMF.
    28. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    29. "CRM1-mediated nuclear export is required for 26 S proteasome-dependent degradation of the TRIP-Br2 proto-oncoprotein."
      Cheong J.K., Gunaratnam L., Hsu S.I.
      J. Biol. Chem. 283:11661-11676(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SERTAD2.
    30. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    31. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    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-446 AND LYS-693, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    33. "Acetylation directs survivin nuclear localization to repress STAT3 oncogenic activity."
      Wang H., Holloway M.P., Ma L., Cooper Z.A., Riolo M., Samkari A., Elenitoba-Johnson K.S., Chin Y.E., Altura R.A.
      J. Biol. Chem. 285:36129-36137(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BIRC5/SURVIVIN.
    34. "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.
    35. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    36. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    37. "POST, partner of stromal interaction molecule 1 (STIM1), targets STIM1 to multiple transporters."
      Krapivinsky G., Krapivinsky L., Stotz S.C., Manasian Y., Clapham D.E.
      Proc. Natl. Acad. Sci. U.S.A. 108:19234-19239(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SLC35G1 AND STIM1.
    38. "Critical role of N-terminal end-localized nuclear export signal in regulation of activating transcription factor 2 (ATF2) subcellular localization and transcriptional activity."
      Hsu C.C., Hu C.D.
      J. Biol. Chem. 287:8621-8632(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATF2.
    39. "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: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 707-1027, ELECTRON MICROSCOPY (22 ANGSTROMS), IDENTIFICATION IN A NUCLEAR EXPORT COMPLEX WITH RAN, MUTAGENESIS OF 428-GLU--ASP-447; 430-VAL--LYS-446; 430-VAL--VAL-433; TYR-454; GLU-513; LEU-525; GLN-550; ARG-553; PHE-554; PHE-561; LYS-568; PHE-572; MET-583 AND LYS-590.

    Entry informationi

    Entry nameiXPO1_HUMAN
    AccessioniPrimary (citable) accession number: O14980
    Secondary accession number(s): A6NL14
    , A8K1K5, D6W5E2, Q63HP8, Q68CP3, Q99433
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 21, 2005
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 142 of the entry and version 1 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

    Miscellaneous

    Cellular target of leptomycin B (LMB), a XPO1/CRM1 nuclear export inhibitor.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3