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Q9C0E2

- XPO4_HUMAN

UniProt

Q9C0E2 - XPO4_HUMAN

Protein

Exportin-4

Gene

XPO4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 2 (02 Nov 2001)
      Previous versions | rss
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    Functioni

    Mediates the nuclear export of proteins (cargos) with broad substrate specificity. In the nucleus binds cooperatively to its cargo 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 cargo from the export receptor. XPO4 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.2 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. positive regulation of protein export from nucleus Source: BHF-UCL
    2. protein transport Source: UniProtKB-KW

    Keywords - Biological processi

    Protein transport, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Exportin-4
    Short name:
    Exp4
    Gene namesi
    Name:XPO4
    Synonyms:KIAA1721
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 13

    Organism-specific databases

    HGNCiHGNC:17796. XPO4.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134866468.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11511151Exportin-4PRO_0000204711Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei464 – 4641Phosphoserine2 Publications
    Modified residuei521 – 5211Phosphoserine5 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9C0E2.
    PaxDbiQ9C0E2.
    PRIDEiQ9C0E2.

    PTM databases

    PhosphoSiteiQ9C0E2.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9C0E2.
    BgeeiQ9C0E2.
    CleanExiHS_XPO4.
    GenevestigatoriQ9C0E2.

    Organism-specific databases

    HPAiHPA053768.

    Interactioni

    Subunit structurei

    Found in a complex with XPO4, Ran and EIF5A. Found in a complex with XPO4, Ran and SMAD3. Interacts with SMAD3. Interacts with Ran and cargo proteins in a GTP-dependent manner.2 Publications

    Protein-protein interaction databases

    BioGridi122138. 15 interactions.
    IntActiQ9C0E2. 1 interaction.
    STRINGi9606.ENSP00000255305.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9C0E2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the exportin family.Curated

    Phylogenomic databases

    eggNOGiNOG273883.
    HOGENOMiHOG000154878.
    HOVERGENiHBG023214.
    OrthoDBiEOG7FJGZW.
    PhylomeDBiQ9C0E2.
    TreeFamiTF312991.

    Family and domain databases

    InterProiIPR016024. ARM-type_fold.
    IPR014877. CRM1_C_dom.
    [Graphical view]
    PfamiPF08767. CRM1_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 5 hits.

    Sequencei

    Sequence statusi: Complete.

    Q9C0E2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MMAAALGPPE VIAQLENAAK VLMAPPSMVN NEQRQHAEHI FLSFRKSKSP     50
    FAVCKHILET SKVDYVLFQA ATAIMEAVVR EWILLEKGSI ESLRTFLLTY 100
    VLQRPNLQKY VREQILLAVA VIVKRGSLDK SIDCKSIFHE VSQLISSGNP 150
    TVQTLACSIL TALLSEFSSS SKTSNIGLSM EFHGNCKRVF QEEDLRQIFM 200
    LTVEVLQEFS RRENLNAQMS SVFQRYLALA NQVLSWNFLP PNLGRHYIAM 250
    FESSQNVLLK PTESWRETLL DSRVMELFFT VHRKIREDSD MAQDSLQCLA 300
    QLASLHGPIF PDEGSQVDYL AHFIEGLLNT INGIEIEDSE AVGISSIISN 350
    LITVFPRNVL TAIPSELFSS FVNCLTHLTC SFGRSAALEE VLDKDDMVYM 400
    EAYDKLLESW LTLVQDDKHF HKGFFTQHAV QVFNSYIQCH LAAPDGTRNL 450
    TANGVASREE EEISELQEDD RDQFSDQLAS VGMLGRIAAE HCIPLLTSLL 500
    EERVTRLHGQ LQRHQQQLLA SPGSSTVDNK MLDDLYEDIH WLILVTGYLL 550
    ADDTQGETPL IPPEIMEYSI KHSSEVDINT TLQILGSPGE KASSIPGYNR 600
    TDSVIRLLSA ILRVSEVESR AIRADLTHLL SPQMGKDIVW FLKRWAKTYL 650
    LVDEKLYDQI SLPFSTAFGA DTEGSQWIIG YLLQKVISNL SVWSSEQDLA 700
    NDTVQLLVTL VERRERANLV IQCENWWNLA KQFASRSPPL NFLSSPVQRT 750
    LMKALVLGGF AHMDTETKQQ YWTEVLQPLQ QRFLRVINQE NFQQMCQQEE 800
    VKQEITATLE ALCGIAEATQ IDNVAILFNF LMDFLTNCIG LMEVYKNTPE 850
    TVNLIIEVFV EVAHKQICYL GESKAMNLYE ACLTLLQVYS KNNLGRQRID 900
    VTAEEEQYQD LLLIMELLTN LLSKEFIDFS DTDEVFRGHE PGQAANRSVS 950
    AADVVLYGVN LILPLMSQDL LKFPTLCNQY YKLITFICEI FPEKIPQLPE 1000
    DLFKSLMYSL ELGMTSMSSE VCQLCLEALT PLAEQCAKAQ ETDSPLFLAT 1050
    RHFLKLVFDM LVLQKHNTEM TTAAGEAFYT LVCLHQAEYS ELVETLLSSQ 1100
    QDPVIYQRLA DAFNKLTASS TPPTLDRKQK MAFLKSLEEF MANVGGLLCV 1150
    K 1151
    Length:1,151
    Mass (Da):130,139
    Last modified:November 2, 2001 - v2
    Checksum:i38E7EEFC938B07C5
    GO

    Sequence cautioni

    The sequence BAB14409.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti511 – 5111L → S in BAB14409. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti149 – 1491N → S.
    Corresponds to variant rs17320607 [ dbSNP | Ensembl ].
    VAR_048958
    Natural varianti451 – 4511T → A.
    Corresponds to variant rs9552285 [ dbSNP | Ensembl ].
    VAR_048959

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB051508 mRNA. Translation: BAB21812.1.
    AL512652, AL356285 Genomic DNA. Translation: CAH71795.1.
    AL356285, AL512652 Genomic DNA. Translation: CAI15862.1.
    AK023108 mRNA. Translation: BAB14409.1. Different initiation.
    AL831819 mRNA. Translation: CAD38533.2.
    CCDSiCCDS41872.1.
    RefSeqiNP_071904.4. NM_022459.4.
    UniGeneiHs.507452.

    Genome annotation databases

    EnsembliENST00000255305; ENSP00000255305; ENSG00000132953.
    GeneIDi64328.
    KEGGihsa:64328.
    UCSCiuc001unq.4. human.

    Polymorphism databases

    DMDMi17368720.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB051508 mRNA. Translation: BAB21812.1 .
    AL512652 , AL356285 Genomic DNA. Translation: CAH71795.1 .
    AL356285 , AL512652 Genomic DNA. Translation: CAI15862.1 .
    AK023108 mRNA. Translation: BAB14409.1 . Different initiation.
    AL831819 mRNA. Translation: CAD38533.2 .
    CCDSi CCDS41872.1.
    RefSeqi NP_071904.4. NM_022459.4.
    UniGenei Hs.507452.

    3D structure databases

    ProteinModelPortali Q9C0E2.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122138. 15 interactions.
    IntActi Q9C0E2. 1 interaction.
    STRINGi 9606.ENSP00000255305.

    PTM databases

    PhosphoSitei Q9C0E2.

    Polymorphism databases

    DMDMi 17368720.

    Proteomic databases

    MaxQBi Q9C0E2.
    PaxDbi Q9C0E2.
    PRIDEi Q9C0E2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000255305 ; ENSP00000255305 ; ENSG00000132953 .
    GeneIDi 64328.
    KEGGi hsa:64328.
    UCSCi uc001unq.4. human.

    Organism-specific databases

    CTDi 64328.
    GeneCardsi GC13M021351.
    H-InvDB HIX0011162.
    HGNCi HGNC:17796. XPO4.
    HPAi HPA053768.
    MIMi 611449. gene.
    neXtProti NX_Q9C0E2.
    PharmGKBi PA134866468.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG273883.
    HOGENOMi HOG000154878.
    HOVERGENi HBG023214.
    OrthoDBi EOG7FJGZW.
    PhylomeDBi Q9C0E2.
    TreeFami TF312991.

    Miscellaneous databases

    GeneWikii XPO4.
    GenomeRNAii 64328.
    NextBioi 66257.
    PROi Q9C0E2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9C0E2.
    Bgeei Q9C0E2.
    CleanExi HS_XPO4.
    Genevestigatori Q9C0E2.

    Family and domain databases

    InterProi IPR016024. ARM-type_fold.
    IPR014877. CRM1_C_dom.
    [Graphical view ]
    Pfami PF08767. CRM1_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 5 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
      DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    2. "The DNA sequence and analysis of human chromosome 13."
      Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
      Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] OF 337-1151.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 888-1151.
      Tissue: Skeletal muscle.
    5. "Exportin 4: a mediator of a novel nuclear export pathway in higher eukaryotes."
      Lipowsky G., Bischoff F.R., Schwarzmaier P., Kraft R., Kostka S., Hartmann E., Kutay U., Goerlich D.
      EMBO J. 19:4362-4371(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, FUNCTION IN NUCLEAR PROTEIN EXPORT, IDENTIFICATION IN A COMPLEX WITH RAN AND EIF5A.
    6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "The mechanism of nuclear export of Smad3 involves exportin 4 and Ran."
      Kurisaki A., Kurisaki K., Kowanetz M., Sugino H., Yoneda Y., Heldin C.-H., Moustakas A.
      Mol. Cell. Biol. 26:1318-1332(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NUCLEAR PROTEIN EXPORT, IDENTIFICATION IN A COMPLEX WITH RAN AND SMAD3, INTERACTION WITH SMAD3, SUBCELLULAR LOCATION.
    8. "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-464 AND SER-521, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "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-521, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiXPO4_HUMAN
    AccessioniPrimary (citable) accession number: Q9C0E2
    Secondary accession number(s): Q5VUZ5, Q8N3V6, Q9H934
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 2, 2001
    Last sequence update: November 2, 2001
    Last modified: October 1, 2014
    This is version 108 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 13
      Human chromosome 13: 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