Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9HAV4

- XPO5_HUMAN

UniProt

Q9HAV4 - XPO5_HUMAN

Protein

Exportin-5

Gene

XPO5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Mediates the nuclear export of proteins bearing a double-stranded RNA binding domain (dsRBD) and double-stranded RNAs (cargos). XPO5 in the nucleus binds cooperatively to the RNA and to the GTPase Ran in its active GTP-bound form. Proteins containing dsRBDs can associate with this trimeric complex through the RNA. 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, hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause disassembly of the complex and release of the cargo from the export receptor. XPO5 then returns to the nuclear compartment by diffusion through the nuclear pore complex, to 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. Overexpression may in some circumstances enhance RNA-mediated gene silencing (RNAi). Mediates nuclear export of isoform 5 of ADAR/ADAR1 in a RanGTP-dependent manner.
    Mediates the nuclear export of micro-RNA precursors, which form short hairpins. Also mediates the nuclear export of synthetic short hairpin RNAs used for RNA interference, and adenovirus VA1 dsRNA. In some circumstances can also mediate the nuclear export of deacylated and aminoacylated tRNAs. Specifically recognizes dsRNAs that lack a 5'-overhang in a sequence-independent manner, have only a short 3'-overhang, and that have a double-stranded length of at least 15 base-pairs. Binding is dependent on Ran-GTP.

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. protein transporter activity Source: Ensembl
    4. RNA binding Source: Reactome
    5. tRNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. gene expression Source: Reactome
    2. gene silencing by RNA Source: UniProtKB-KW
    3. protein export from nucleus Source: Ensembl

    Keywords - Biological processi

    Protein transport, RNA-mediated gene silencing, Transport

    Keywords - Ligandi

    RNA-binding, tRNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_12417. MicroRNA (miRNA) biogenesis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Exportin-5
    Short name:
    Exp5
    Alternative name(s):
    Ran-binding protein 21
    Gene namesi
    Name:XPO5
    Synonyms:KIAA1291, RANBP21
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:17675. XPO5.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasm 1 Publication
    Note: Shuttles between the nucleus and the cytoplasm.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. nucleoplasm Source: Reactome
    4. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134979214.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 12041203Exportin-5PRO_0000235299Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei396 – 3961N6-acetyllysine1 Publication
    Modified residuei826 – 8261Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9HAV4.
    PaxDbiQ9HAV4.
    PRIDEiQ9HAV4.

    PTM databases

    PhosphoSiteiQ9HAV4.

    Miscellaneous databases

    PMAP-CutDBQ9HAV4.

    Expressioni

    Tissue specificityi

    Expressed in heart, brain, placenta, lung, skeletal muscle, kidney and pancreas.1 Publication

    Gene expression databases

    ArrayExpressiQ9HAV4.
    BgeeiQ9HAV4.
    GenevestigatoriQ9HAV4.

    Organism-specific databases

    HPAiCAB012357.
    HPA018402.
    HPA023959.
    HPA029909.
    HPA029910.

    Interactioni

    Subunit structurei

    Component of a nuclear export receptor complex composed of XPO5, Ran, dsRNA-binding proteins and dsRNA. Found in a nuclear export complex with XPO5, Ran, EEF1A1, and aminoacylated tRNA. Found in a nuclear export complex with XPO5, Ran, ILF3 and dsRNA. Found in a nuclear export complex with XPO5, Ran and pre-miRNA. Found in a nuclear export complex with XPO5, Ran, ILF3 and minihelix VA1 dsRNA. Found in a nuclear export complex with XPO5, RAN, ILF3, ZNF346 and dsRNA. Interacts with EEF1A1, ILF3, NUP153, NUP214 and ZNF346. Interacts with Ran and cargo proteins in a GTP-dependent manner. Interacts with isoform 5 of ADAR/ADAR1 (via DRBM domains).8 Publications

    Protein-protein interaction databases

    BioGridi121574. 53 interactions.
    DIPiDIP-34547N.
    IntActiQ9HAV4. 15 interactions.
    MINTiMINT-264827.

    Structurei

    Secondary structure

    1
    1204
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 2116
    Helixi27 – 4317
    Helixi47 – 548
    Helixi61 – 7717
    Helixi79 – 813
    Helixi84 – 10017
    Helixi110 – 12718
    Turni129 – 1313
    Helixi135 – 14410
    Helixi147 – 16519
    Helixi172 – 18413
    Helixi186 – 20722
    Helixi214 – 23219
    Turni233 – 2375
    Helixi240 – 2445
    Turni245 – 2473
    Helixi249 – 2568
    Helixi257 – 2593
    Turni261 – 2633
    Helixi264 – 27512
    Helixi281 – 2844
    Helixi285 – 2917
    Helixi293 – 30412
    Helixi313 – 33826
    Helixi349 – 36012
    Helixi365 – 37915
    Turni382 – 3865
    Helixi388 – 40518
    Helixi418 – 4258
    Helixi429 – 45325
    Helixi455 – 47016
    Beta strandi495 – 4973
    Helixi498 – 52023
    Helixi528 – 54013
    Helixi546 – 55914
    Helixi560 – 5645
    Helixi567 – 5693
    Helixi570 – 58213
    Helixi595 – 61420
    Helixi616 – 6194
    Helixi620 – 6223
    Helixi623 – 63513
    Helixi642 – 65615
    Helixi657 – 6593
    Helixi662 – 68019
    Helixi683 – 6908
    Helixi692 – 6998
    Helixi713 – 73422
    Helixi741 – 7466
    Beta strandi750 – 7534
    Beta strandi759 – 7613
    Helixi766 – 7705
    Helixi773 – 78513
    Helixi789 – 7924
    Helixi797 – 7993
    Turni800 – 8034
    Helixi807 – 8137
    Helixi832 – 85827
    Turni860 – 8645
    Helixi868 – 8758
    Turni880 – 8823
    Helixi885 – 89410
    Helixi896 – 9016
    Helixi905 – 9073
    Turni908 – 9114
    Helixi912 – 93524
    Helixi953 – 97725
    Helixi1013 – 10197
    Helixi1022 – 103514
    Helixi1041 – 105010
    Helixi1052 – 10565
    Helixi1066 – 108217
    Helixi1087 – 110317
    Turni1105 – 11073
    Helixi1111 – 11155
    Beta strandi1118 – 11203
    Helixi1123 – 113210

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3A6PX-ray2.92A/F1-1204[»]
    ProteinModelPortaliQ9HAV4.
    SMRiQ9HAV4. Positions 58-243.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9HAV4.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 108107Necessary for interaction with RanAdd
    BLAST
    Regioni533 – 640108Necessary for interaction with ILF3Add
    BLAST

    Sequence similaritiesi

    Belongs to the exportin family.Curated

    Phylogenomic databases

    eggNOGiNOG296759.
    HOVERGENiHBG056281.
    KOiK14289.
    OMAiFADSVGH.
    OrthoDBiEOG7MWGW1.
    PhylomeDBiQ9HAV4.
    TreeFamiTF323382.

    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. 4 hits.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9HAV4-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAMDQVNALC EQLVKAVTVM MDPNSTQRYR LEALKFCEEF KEKCPICVPC     50
    GLRLAEKTQV AIVRHFGLQI LEHVVKFRWN GMSRLEKVYL KNSVMELIAN 100
    GTLNILEEEN HIKDALSRIV VEMIKREWPQ HWPDMLIELD TLSKQGETQT 150
    ELVMFILLRL AEDVVTFQTL PPQRRRDIQQ TLTQNMERIF SFLLNTLQEN 200
    VNKYQQVKTD TSQESKAQAN CRVGVAALNT LAGYIDWVSM SHITAENCKL 250
    LEILCLLLNE QELQLGAAEC LLIAVSRKGK LEDRKPLMVL FGDVAMHYIL 300
    SAAQTADGGG LVEKHYVFLK RLCQVLCALG NQLCALLGAD SDVETPSNFG 350
    KYLESFLAFT THPSQFLRSS TQMTWGALFR HEILSRDPLL LAIIPKYLRA 400
    SMTNLVKMGF PSKTDSPSCE YSRFDFDSDE DFNAFFNSSR AQQGEVMRLA 450
    CRLDPKTSFQ MAGEWLKYQL STFLDAGSVN SCSAVGTGEG SLCSVFSPSF 500
    VQWEAMTLFL ESVITQMFRT LNREEIPVND GIELLQMVLN FDTKDPLILS 550
    CVLTNVSALF PFVTYRPEFL PQVFSKLFSS VTFETVEESK APRTRAVRNV 600
    RRHACSSIIK MCRDYPQLVL PNFDMLYNHV KQLLSNELLL TQMEKCALME 650
    ALVLISNQFK NYERQKVFLE ELMAPVASIW LSQDMHRVLS DVDAFIAYVG 700
    TDQKSCDPGL EDPCGLNRAR MSFCVYSILG VVKRTCWPTD LEEAKAGGFV 750
    VGYTSSGNPI FRNPCTEQIL KLLDNLLALI RTHNTLYAPE MLAKMAEPFT 800
    KALDMLDAEK SAILGLPQPL LELNDSPVFK TVLERMQRFF STLYENCFHI 850
    LGKAGPSMQQ DFYTVEDLAT QLLSSAFVNL NNIPDYRLRP MLRVFVKPLV 900
    LFCPPEHYEA LVSPILGPLF TYLHMRLSQK WQVINQRSLL CGEDEAADEN 950
    PESQEMLEEQ LVRMLTREVM DLITVCCVSK KGADHSSAPP ADGDDEEMMA 1000
    TEVTPSAMAE LTDLGKCLMK HEDVCTALLI TAFNSLAWKD TLSCQRTTSQ 1050
    LCWPLLKQVL SGTLLADAVT WLFTSVLKGL QMHGQHDGCM ASLVHLAFQI 1100
    YEALRPRYLE IRAVMEQIPE IQKDSLDQFD CKLLNPSLQK VADKRRKDQF 1150
    KRLIAGCIGK PLGEQFRKEV HIKNLPSLFK KTKPMLETEV LDNDGGGLAT 1200
    IFEP 1204
    Length:1,204
    Mass (Da):136,311
    Last modified:March 1, 2001 - v1
    Checksum:i3295A17DF7C37602
    GO

    Sequence cautioni

    The sequence BAA91547.1 differs from that shown. Reason: Frameshift at position 920.
    The sequence AAH00129.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAA86605.2 differs from that shown. Reason: Erroneous initiation.
    The sequence CAI42640.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti81 – 811G → S in AAG53603. (PubMed:12426392)Curated
    Sequence conflicti697 – 6971A → V in BAA86605. (PubMed:10574462)Curated
    Sequence conflicti988 – 9881A → T in BAB14200. (PubMed:14574404)Curated
    Sequence conflicti1151 – 11511K → E in BAA91547. (PubMed:14574404)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti241 – 2411S → N.
    Corresponds to variant rs34324334 [ dbSNP | Ensembl ].
    VAR_048960
    Natural varianti610 – 6101K → N.
    Corresponds to variant rs12173786 [ dbSNP | Ensembl ].
    VAR_028032

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF271159 mRNA. Translation: AAG53603.1.
    AF298880 mRNA. Translation: AAG17907.1.
    AB033117 mRNA. Translation: BAA86605.2. Different initiation.
    AL355802 Genomic DNA. Translation: CAI42640.1. Sequence problems.
    BC000129 mRNA. Translation: AAH00129.1. Different initiation.
    BC008347 mRNA. Translation: AAH08347.1.
    BC009969 mRNA. Translation: AAH09969.2.
    BC062635 mRNA. Translation: AAH62635.1.
    AL137467 mRNA. Translation: CAB70753.1.
    AK001195 mRNA. Translation: BAA91547.1. Frameshift.
    AK022718 mRNA. Translation: BAB14200.1.
    CCDSiCCDS47430.1.
    PIRiT46411.
    RefSeqiNP_065801.1. NM_020750.2.
    UniGeneiHs.203206.

    Genome annotation databases

    EnsembliENST00000265351; ENSP00000265351; ENSG00000124571.
    GeneIDi57510.
    KEGGihsa:57510.
    UCSCiuc003ovp.3. human.

    Polymorphism databases

    DMDMi74734245.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF271159 mRNA. Translation: AAG53603.1 .
    AF298880 mRNA. Translation: AAG17907.1 .
    AB033117 mRNA. Translation: BAA86605.2 . Different initiation.
    AL355802 Genomic DNA. Translation: CAI42640.1 . Sequence problems.
    BC000129 mRNA. Translation: AAH00129.1 . Different initiation.
    BC008347 mRNA. Translation: AAH08347.1 .
    BC009969 mRNA. Translation: AAH09969.2 .
    BC062635 mRNA. Translation: AAH62635.1 .
    AL137467 mRNA. Translation: CAB70753.1 .
    AK001195 mRNA. Translation: BAA91547.1 . Frameshift.
    AK022718 mRNA. Translation: BAB14200.1 .
    CCDSi CCDS47430.1.
    PIRi T46411.
    RefSeqi NP_065801.1. NM_020750.2.
    UniGenei Hs.203206.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3A6P X-ray 2.92 A/F 1-1204 [» ]
    ProteinModelPortali Q9HAV4.
    SMRi Q9HAV4. Positions 58-243.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121574. 53 interactions.
    DIPi DIP-34547N.
    IntActi Q9HAV4. 15 interactions.
    MINTi MINT-264827.

    PTM databases

    PhosphoSitei Q9HAV4.

    Polymorphism databases

    DMDMi 74734245.

    Proteomic databases

    MaxQBi Q9HAV4.
    PaxDbi Q9HAV4.
    PRIDEi Q9HAV4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265351 ; ENSP00000265351 ; ENSG00000124571 .
    GeneIDi 57510.
    KEGGi hsa:57510.
    UCSCi uc003ovp.3. human.

    Organism-specific databases

    CTDi 57510.
    GeneCardsi GC06M043490.
    H-InvDB HIX0005908.
    HGNCi HGNC:17675. XPO5.
    HPAi CAB012357.
    HPA018402.
    HPA023959.
    HPA029909.
    HPA029910.
    MIMi 607845. gene.
    neXtProti NX_Q9HAV4.
    PharmGKBi PA134979214.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG296759.
    HOVERGENi HBG056281.
    KOi K14289.
    OMAi FADSVGH.
    OrthoDBi EOG7MWGW1.
    PhylomeDBi Q9HAV4.
    TreeFami TF323382.

    Enzyme and pathway databases

    Reactomei REACT_12417. MicroRNA (miRNA) biogenesis.

    Miscellaneous databases

    ChiTaRSi XPO5. human.
    EvolutionaryTracei Q9HAV4.
    GeneWikii XPO5.
    GenomeRNAii 57510.
    NextBioi 63866.
    PMAP-CutDB Q9HAV4.
    PROi Q9HAV4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9HAV4.
    Bgeei Q9HAV4.
    Genevestigatori Q9HAV4.

    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. 4 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Exp5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasm."
      Bohnsack M.T., Regener K., Schwappach B., Saffrich R., Paraskeva E., Hartmann E., Goerlich D.
      EMBO J. 21:6205-6215(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN PROTEIN AND TRNA NUCLEAR EXPORT, IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH EEF1A1; RAN AND TRNA, INTERACTION WITH EEF1A1, RNA-BINDING.
    2. "Exportin-5, a novel karyopherin, mediates nuclear export of double-stranded RNA binding proteins."
      Brownawell A.M., Macara I.G.
      J. Cell Biol. 156:53-64(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN PROTEIN NUCLEAR EXPORT, IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH ILF3; RAN AND DOUBLE-STRANDED RNA, INTERACTION WITH ILF3; NUP153 AND NUP214, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Brain.
    3. "Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.
      DNA Res. 6:337-345(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    4. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    5. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Ascites, Placenta, Retinoblastoma and Rhabdomyosarcoma.
    7. Bienvenut W.V.
      Submitted (JUN-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 189-203 AND 387-396, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 450-1204.
      Tissue: Testis.
    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] OF 537-1204.
      Tissue: Teratocarcinoma.
    10. "Exportin-5-mediated nuclear export of eukaryotic elongation factor 1A and tRNA."
      Calado A., Treichel N., Mueller E.-C., Otto A., Kutay U.
      EMBO J. 21:6216-6224(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PROTEIN AND TRNA NUCLEAR EXPORT, IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH EEF1A1; RAN AND TRNA, INTERACTION WITH EEF1A1, IDENTIFICATION BY MASS SPECTROMETRY, RNA-BINDING.
    11. "Exportin-5 mediates the nuclear export of pre-microRNAs and short hairpin RNAs."
      Yi R., Qin Y., Macara I.G., Cullen B.R.
      Genes Dev. 17:3011-3016(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PRE-MIRNA EXPORT, RNA-BINDING.
    12. Cited for: FUNCTION IN ADENOVIRUS VA1 RNA EXPORT, RNA-BINDING.
    13. "Minihelix-containing RNAs mediate exportin-5-dependent nuclear export of the double-stranded RNA-binding protein ILF3."
      Gwizdek C., Ossareh-Nazari B., Brownawell A.M., Evers S., Macara I.G., Dargemont C.
      J. Biol. Chem. 279:884-891(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PROTEIN AND ADENOVIRUS VA1 RNA EXPORT, IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH ILF3; RAN AND VA1 RNA, RNA-BINDING.
    14. "Nucleocytoplasmic shuttling of JAZ, a new cargo protein for exportin-5."
      Chen T., Brownawell A.M., Macara I.G.
      Mol. Cell. Biol. 24:6608-6619(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PROTEIN AND DOUBLE-STRANDED RNA EXPORT, IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH RAN; ILF3; ZNF346 AND DOUBLE-STRANDED RNA, INTERACTION WITH ILF3 AND ZNF346.
    15. "Exportin 5 is a RanGTP-dependent dsRNA-binding protein that mediates nuclear export of pre-miRNAs."
      Bohnsack M.T., Czaplinski K., Goerlich D.
      RNA 10:185-191(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PRE-MIRNA EXPORT, IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH RAN AND PRE-MIRNA, RNA-BINDING.
    16. Cited for: FUNCTION IN PRE-MIRNA EXPORT, IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH RAN AND PRE-MIRNA, RNA-BINDING.
    17. "Overexpression of exportin 5 enhances RNA interference mediated by short hairpin RNAs and microRNAs."
      Yi R., Doehle B.P., Qin Y., Macara I.G., Cullen B.R.
      RNA 11:220-226(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PRE-MIRNA EXPORT.
    18. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-826, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. "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], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    20. "RNA-regulated interaction of transportin-1 and exportin-5 with the double-stranded RNA-binding domain regulates nucleocytoplasmic shuttling of ADAR1."
      Fritz J., Strehblow A., Taschner A., Schopoff S., Pasierbek P., Jantsch M.F.
      Mol. Cell. Biol. 29:1487-1497(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ADAR.
    21. "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-396, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "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].

    Entry informationi

    Entry nameiXPO5_HUMAN
    AccessioniPrimary (citable) accession number: Q9HAV4
    Secondary accession number(s): Q5JTE6
    , Q96G48, Q96HN3, Q9BWM6, Q9BZV5, Q9H9M4, Q9NT89, Q9NW39, Q9ULC9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 16, 2006
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 107 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

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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