Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O14980 (XPO1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Exportin-1

Short name=Exp1
Alternative name(s):
Chromosome region maintenance 1 protein homolog
Gene names
Name:XPO1
Synonyms:CRM1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1071 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9 Ref.10 Ref.11 Ref.23 Ref.25 Ref.34

Subunit structure

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. Ref.1 Ref.9 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.26 Ref.27 Ref.29 Ref.33 Ref.34 Ref.37 Ref.38

Subcellular location

Cytoplasm. Nucleusnucleoplasm. NucleusCajal body. Nucleusnucleolus. Note: Located in the nucleoplasm, Cajal bodies and nucleoli. Shuttles between the nucleus/nucleolus and the cytoplasm. Ref.1 Ref.2 Ref.25 Ref.26

Tissue specificity

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. Ref.1 Ref.2

Miscellaneous

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

Sequence similarities

Belongs to the exportin family.

Contains 10 HEAT repeats.

Contains 1 importin N-terminal domain.

Ontologies

Keywords
   Biological processHost-virus interaction
mRNA transport
Protein transport
Transport
   Cellular componentCytoplasm
Nucleus
   DomainRepeat
   LigandRNA-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

intracellular transport of virus

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

mRNA transport

Inferred from electronic annotation. Source: UniProtKB-KW

mitotic cell cycle

Traceable author statement. Source: Reactome

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

negative regulation of transforming growth factor beta receptor signaling pathway

Traceable author statement. Source: Reactome

protein export from nucleus

Inferred from electronic annotation. Source: Ensembl

protein localization to nucleus

Inferred from electronic annotation. Source: Ensembl

regulation of centrosome duplication

Inferred from electronic annotation. Source: Ensembl

regulation of protein catabolic process

Inferred from electronic annotation. Source: Ensembl

regulation of protein export from nucleus

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

transforming growth factor beta receptor signaling pathway

Traceable author statement. Source: Reactome

viral life cycle

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentCajal body

Inferred from electronic annotation. Source: UniProtKB-SubCell

annulate lamellae

Inferred from direct assay PubMed 12210765. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

kinetochore

Inferred from direct assay PubMed 17363900. Source: UniProtKB

nuclear envelope

Traceable author statement Ref.2. Source: ProtInc

nuclear membrane

Inferred from direct assay. Source: HPA

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

ribonucleoprotein complex

Inferred from direct assay PubMed 18809582. Source: MGI

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 11545741Ref.33Ref.34PubMed 22730302. Source: UniProtKB

protein transporter activity

Inferred from electronic annotation. Source: Ensembl

transporter activity

Traceable author statement. Source: Reactome

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10711071Exportin-1
PRO_0000204705

Regions

Domain46 – 11267Importin N-terminal
Repeat217 – 24024HEAT 1
Repeat241 – 27737HEAT 2
Repeat354 – 472119HEAT 3
Repeat515 – 55339HEAT 4
Repeat560 – 59738HEAT 5
Repeat602 – 63938HEAT 6
Repeat775 – 81339HEAT 7
Repeat885 – 91632HEAT 8
Repeat917 – 95438HEAT 9
Repeat1002 – 103938HEAT 10
Region1 – 679679Necessary for HTLV-1 Rex-mediated mRNA export
Region327 – 450124Interaction with Ran and nuclear export complex formation
Region411 – 48171Interaction with RANBP3
Region411 – 4144Necessary for HTLV-1 Rex multimerization
Region800 – 82021Interaction with HIV-1 Rev

Amino acid modifications

Modified residue3911Phosphoserine Ref.35
Modified residue4461N6-acetyllysine Ref.32
Modified residue4481Phosphothreonine By similarity
Modified residue4501Phosphoserine By similarity
Modified residue4541Phosphotyrosine By similarity
Modified residue6931N6-acetyllysine Ref.32

Experimental info

Mutagenesis1911S → A: Does not abolish Rex-mediated mRNA export. Ref.23
Mutagenesis2841V → E: Does not abolish Rex-mediated mRNA export. Ref.23
Mutagenesis3341D → G: Does not abolish Rex-mediated mRNA export. Ref.23
Mutagenesis3371I → L: Does not abolish Rex-mediated mRNA export. Ref.23
Mutagenesis3461T → A: Does not abolish Rex-mediated mRNA export. Ref.23
Mutagenesis4021V → I: Does not abolish Rex-mediated mRNA export. Ref.23
Mutagenesis4111P → 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. Ref.23
Mutagenesis4121M → V: Does not abolish interaction with Rex and RANBP3, and Rex-mediated mRNA export. Ref.23
Mutagenesis4141F → 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. Ref.23
Mutagenesis428 – 44720EEVLV…EFMKD → QQVLVVQNNQGQVVRQFMKN: Abolishes Ran binding activity in absence of cargo and abolishes partially Ran binding activity in presence of cargo. Ref.38
Mutagenesis430 – 44617VLVVE…REFMK → DEDEENDQGEDEEEDDD: Partially restores Ran binding activity in presence of cargo. Ref.38
Mutagenesis430 – 4334VLVV → DEDE: Abolishes Ran binding activity both in absence or presence of cargo. Ref.38
Mutagenesis4541Y → A: Does not abolish Ran binding activity and nuclear export complex formation. Ref.38
Mutagenesis4741R → I: Strongly abolishes interaction with Rex and RANBP3, abolishes Rex-mediated mRNA export. Ref.23
Mutagenesis4811H → Q: Strongly abolishes interaction with Rex and RANBP3, abolishes Rex-mediated mRNA export. Ref.23
Mutagenesis5131E → 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. Ref.38
Mutagenesis5251L → 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. Ref.38
Mutagenesis5501Q → A: Enhances Ran binding activity and does not abolish nuclear export complex formation; when associated with A-553 and A-590. Ref.38
Mutagenesis5531R → 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. Ref.38
Mutagenesis5541F → 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. Ref.38
Mutagenesis5611F → 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. Ref.38
Mutagenesis5681K → A: Does not abolish Ran binding activity and partially abolish nuclear export complex formation; when associated with A-525 and A-572. Ref.38
Mutagenesis5721F → A: Does not abolish Ran binding activity and partially abolish nuclear export complex formation; when associated with A-525 and A-568. Ref.38
Mutagenesis5831M → A: Enhances Ran binding activity; when associated with A-590. Ref.38
Mutagenesis5901K → 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. Ref.38
Sequence conflict4061R → G in CAH56174. Ref.4
Sequence conflict9531V → G in CAH18695. Ref.4
Sequence conflict9891L → I in CAH56174. Ref.4

Secondary structure

............................................................................................................................ 1071
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O14980 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: FDB00C065DA2FB1D

FASTA1,071123,386
        10         20         30         40         50         60 
MPAIMTMLAD HAARQLLDFS QKLDINLLDN VVNCLYHGEG AQQRMAQEVL THLKEHPDAW 

        70         80         90        100        110        120 
TRVDTILEFS QNMNTKYYGL QILENVIKTR WKILPRNQCE GIKKYVVGLI IKTSSDPTCV 

       130        140        150        160        170        180 
EKEKVYIGKL NMILVQILKQ EWPKHWPTFI SDIVGASRTS ESLCQNNMVI LKLLSEEVFD 

       190        200        210        220        230        240 
FSSGQITQVK SKHLKDSMCN EFSQIFQLCQ FVMENSQNAP LVHATLETLL RFLNWIPLGY 

       250        260        270        280        290        300 
IFETKLISTL IYKFLNVPMF RNVSLKCLTE IAGVSVSQYE EQFVTLFTLT MMQLKQMLPL 

       310        320        330        340        350        360 
NTNIRLAYSN GKDDEQNFIQ NLSLFLCTFL KEHDQLIEKR LNLRETLMEA LHYMLLVSEV 

       370        380        390        400        410        420 
EETEIFKICL EYWNHLAAEL YRESPFSTSA SPLLSGSQHF DVPPRRQLYL PMLFKVRLLM 

       430        440        450        460        470        480 
VSRMAKPEEV LVVENDQGEV VREFMKDTDS INLYKNMRET LVYLTHLDYV DTERIMTEKL 

       490        500        510        520        530        540 
HNQVNGTEWS WKNLNTLCWA IGSISGAMHE EDEKRFLVTV IKDLLGLCEQ KRGKDNKAII 

       550        560        570        580        590        600 
ASNIMYIVGQ YPRFLRAHWK FLKTVVNKLF EFMHETHDGV QDMACDTFIK IAQKCRRHFV 

       610        620        630        640        650        660 
QVQVGEVMPF IDEILNNINT IICDLQPQQV HTFYEAVGYM IGAQTDQTVQ EHLIEKYMLL 

       670        680        690        700        710        720 
PNQVWDSIIQ QATKNVDILK DPETVKQLGS ILKTNVRACK AVGHPFVIQL GRIYLDMLNV 

       730        740        750        760        770        780 
YKCLSENISA AIQANGEMVT KQPLIRSMRT VKRETLKLIS GWVSRSNDPQ MVAENFVPPL 

       790        800        810        820        830        840 
LDAVLIDYQR NVPAAREPEV LSTMAIIVNK LGGHITAEIP QIFDAVFECT LNMINKDFEE 

       850        860        870        880        890        900 
YPEHRTNFFL LLQAVNSHCF PAFLAIPPTQ FKLVLDSIIW AFKHTMRNVA DTGLQILFTL 

       910        920        930        940        950        960 
LQNVAQEEAA AQSFYQTYFC DILQHIFSVV TDTSHTAGLT MHASILAYMF NLVEEGKIST 

       970        980        990       1000       1010       1020 
SLNPGNPVNN QIFLQEYVAN LLKSAFPHLQ DAQVKLFVTG LFSLNQDIPA FKEHLRDFLV 

      1030       1040       1050       1060       1070 
QIKEFAGEDT SDLFLEEREI ALRQADEEKH KRQMSVPGIF NPHEIPEEMC D 

« Hide

References

« Hide 'large scale' references
[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. 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].
Tissue: Hippocampus.
[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].
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"CRM1-mediated recycling of snurportin 1 to the cytoplasm."
Paraskeva E., Izaurralde E., Bischoff F.R., Huber J., Kutay U., Hartmann E., Luehrmann R., Goerlich D.
J. Cell Biol. 145:255-264(1999) [PubMed] [Europe PMC] [Abstract]
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]"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: 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]"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].
[37]"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.
[38]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS33205.1.
RefSeqNP_003391.1. NM_003400.3.
XP_006712157.1. XM_006712094.1.
UniGeneHs.370770.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1W9CX-ray2.30A/B707-1027[»]
2L1LNMR-B504-630[»]
3GB8X-ray2.90A1-1071[»]
4BSMX-ray4.50A1-1032[»]
4BSNX-ray4.10A1-1032[»]
ProteinModelPortalO14980.
SMRO14980. Positions 53-1061.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113348. 157 interactions.
DIPDIP-33678N.
IntActO14980. 34 interactions.
MINTMINT-5002192.
STRING9606.ENSP00000195419.

Chemistry

BindingDBO14980.
ChEMBLCHEMBL5661.

PTM databases

PhosphoSiteO14980.

Proteomic databases

MaxQBO14980.
PaxDbO14980.
PRIDEO14980.

Protocols and materials databases

DNASU7514.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000401558; ENSP00000384863; ENSG00000082898.
ENST00000404992; ENSP00000385942; ENSG00000082898.
ENST00000406957; ENSP00000385559; ENSG00000082898.
GeneID7514.
KEGGhsa:7514.
UCSCuc002sbh.3. human.

Organism-specific databases

CTD7514.
GeneCardsGC02M061704.
HGNCHGNC:12825. XPO1.
HPACAB010184.
HPA042933.
MIM602559. gene.
neXtProtNX_O14980.
PharmGKBPA37418.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5101.
HOVERGENHBG052817.
InParanoidO14980.
KOK14290.
OMAQTYFTDI.
OrthoDBEOG7CZK4S.
PhylomeDBO14980.
TreeFamTF105695.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_21257. Metabolism of RNA.
REACT_21300. Mitotic M-M/G1 phases.
REACT_71. Gene Expression.
SignaLinkO14980.

Gene expression databases

ArrayExpressO14980.
BgeeO14980.
CleanExHS_XPO1.
GenevestigatorO14980.

Family and domain databases

Gene3D1.25.10.10. 3 hits.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR014877. CRM1_C_dom.
IPR013598. Exportin-1/Importin-b-like.
IPR001494. Importin-beta_N.
[Graphical view]
PfamPF08767. CRM1_C. 1 hit.
PF03810. IBN_N. 1 hit.
PF08389. Xpo1. 1 hit.
[Graphical view]
SMARTSM01102. CRM1_C. 1 hit.
SM00913. IBN_N. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 4 hits.
PROSITEPS50166. IMPORTIN_B_NT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSXPO1. human.
EvolutionaryTraceO14980.
GeneWikiXPO1.
GenomeRNAi7514.
NextBio29403.
PROO14980.
SOURCESearch...

Entry information

Entry nameXPO1_HUMAN
AccessionPrimary (citable) accession number: O14980
Secondary accession number(s): A6NL14 expand/collapse secondary AC list , A8K1K5, D6W5E2, Q63HP8, Q68CP3, Q99433
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 140 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM