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Q9C0E2 (XPO4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Exportin-4

Short name=Exp4
Gene names
Name:XPO4
Synonyms:KIAA1721
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1151 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5 Ref.7

Subunit structure

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. Ref.5 Ref.7

Subcellular location

Cytoplasm. Nucleus. Note: Shuttles between the nucleus and the cytoplasm. Ref.7

Sequence similarities

Belongs to the exportin family.

Sequence caution

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

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processpositive regulation of protein export from nucleus

Inferred from mutant phenotype Ref.7. Source: BHF-UCL

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay. Source: HPA

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11511151Exportin-4
PRO_0000204711

Amino acid modifications

Modified residue4641Phosphoserine Ref.8 Ref.9
Modified residue5211Phosphoserine Ref.6 Ref.8 Ref.10 Ref.11 Ref.13

Natural variations

Natural variant1491N → S.
Corresponds to variant rs17320607 [ dbSNP | Ensembl ].
VAR_048958
Natural variant4511T → A.
Corresponds to variant rs9552285 [ dbSNP | Ensembl ].
VAR_048959

Experimental info

Sequence conflict5111L → S in BAB14409. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9C0E2 [UniParc].

Last modified November 2, 2001. Version 2.
Checksum: 38E7EEFC938B07C5

FASTA1,151130,139
        10         20         30         40         50         60 
MMAAALGPPE VIAQLENAAK VLMAPPSMVN NEQRQHAEHI FLSFRKSKSP FAVCKHILET 

        70         80         90        100        110        120 
SKVDYVLFQA ATAIMEAVVR EWILLEKGSI ESLRTFLLTY VLQRPNLQKY VREQILLAVA 

       130        140        150        160        170        180 
VIVKRGSLDK SIDCKSIFHE VSQLISSGNP TVQTLACSIL TALLSEFSSS SKTSNIGLSM 

       190        200        210        220        230        240 
EFHGNCKRVF QEEDLRQIFM LTVEVLQEFS RRENLNAQMS SVFQRYLALA NQVLSWNFLP 

       250        260        270        280        290        300 
PNLGRHYIAM FESSQNVLLK PTESWRETLL DSRVMELFFT VHRKIREDSD MAQDSLQCLA 

       310        320        330        340        350        360 
QLASLHGPIF PDEGSQVDYL AHFIEGLLNT INGIEIEDSE AVGISSIISN LITVFPRNVL 

       370        380        390        400        410        420 
TAIPSELFSS FVNCLTHLTC SFGRSAALEE VLDKDDMVYM EAYDKLLESW LTLVQDDKHF 

       430        440        450        460        470        480 
HKGFFTQHAV QVFNSYIQCH LAAPDGTRNL TANGVASREE EEISELQEDD RDQFSDQLAS 

       490        500        510        520        530        540 
VGMLGRIAAE HCIPLLTSLL EERVTRLHGQ LQRHQQQLLA SPGSSTVDNK MLDDLYEDIH 

       550        560        570        580        590        600 
WLILVTGYLL ADDTQGETPL IPPEIMEYSI KHSSEVDINT TLQILGSPGE KASSIPGYNR 

       610        620        630        640        650        660 
TDSVIRLLSA ILRVSEVESR AIRADLTHLL SPQMGKDIVW FLKRWAKTYL LVDEKLYDQI 

       670        680        690        700        710        720 
SLPFSTAFGA DTEGSQWIIG YLLQKVISNL SVWSSEQDLA NDTVQLLVTL VERRERANLV 

       730        740        750        760        770        780 
IQCENWWNLA KQFASRSPPL NFLSSPVQRT LMKALVLGGF AHMDTETKQQ YWTEVLQPLQ 

       790        800        810        820        830        840 
QRFLRVINQE NFQQMCQQEE VKQEITATLE ALCGIAEATQ IDNVAILFNF LMDFLTNCIG 

       850        860        870        880        890        900 
LMEVYKNTPE TVNLIIEVFV EVAHKQICYL GESKAMNLYE ACLTLLQVYS KNNLGRQRID 

       910        920        930        940        950        960 
VTAEEEQYQD LLLIMELLTN LLSKEFIDFS DTDEVFRGHE PGQAANRSVS AADVVLYGVN 

       970        980        990       1000       1010       1020 
LILPLMSQDL LKFPTLCNQY YKLITFICEI FPEKIPQLPE DLFKSLMYSL ELGMTSMSSE 

      1030       1040       1050       1060       1070       1080 
VCQLCLEALT PLAEQCAKAQ ETDSPLFLAT RHFLKLVFDM LVLQKHNTEM TTAAGEAFYT 

      1090       1100       1110       1120       1130       1140 
LVCLHQAEYS ELVETLLSSQ QDPVIYQRLA DAFNKLTASS TPPTLDRKQK MAFLKSLEEF 

      1150 
MANVGGLLCV K 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_071904.4. NM_022459.4.
UniGeneHs.507452.

3D structure databases

ProteinModelPortalQ9C0E2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122138. 15 interactions.
IntActQ9C0E2. 1 interaction.
STRING9606.ENSP00000255305.

PTM databases

PhosphoSiteQ9C0E2.

Polymorphism databases

DMDM17368720.

Proteomic databases

PaxDbQ9C0E2.
PRIDEQ9C0E2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000255305; ENSP00000255305; ENSG00000132953.
GeneID64328.
KEGGhsa:64328.
UCSCuc001unq.4. human.

Organism-specific databases

CTD64328.
GeneCardsGC13M021351.
H-InvDBHIX0011162.
HGNCHGNC:17796. XPO4.
HPAHPA053768.
MIM611449. gene.
neXtProtNX_Q9C0E2.
PharmGKBPA134866468.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG273883.
HOGENOMHOG000154878.
HOVERGENHBG023214.
OrthoDBEOG7FJGZW.
PhylomeDBQ9C0E2.
TreeFamTF312991.

Gene expression databases

ArrayExpressQ9C0E2.
BgeeQ9C0E2.
CleanExHS_XPO4.
GenevestigatorQ9C0E2.

Family and domain databases

InterProIPR016024. ARM-type_fold.
IPR014877. CRM1_C_dom.
[Graphical view]
PfamPF08767. CRM1_C. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 5 hits.
ProtoNetSearch...

Other

GeneWikiXPO4.
GenomeRNAi64328.
NextBio66257.
PROQ9C0E2.
SOURCESearch...

Entry information

Entry nameXPO4_HUMAN
AccessionPrimary (citable) accession number: Q9C0E2
Secondary accession number(s): Q5VUZ5, Q8N3V6, Q9H934
Entry history
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: November 2, 2001
Last modified: April 16, 2014
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM