Reviewed, UniProtKB/Swiss-Prot O14980 (XPO1_HUMAN)

Names and origin

Protein names

Recommended name:
    Exportin-1
      Short name=Exp1
Alternative name(s):
    Chromosome region maintenance 1 protein homolog

Gene names

Name:	XPO1
Synonyms:	CRM1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1071 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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 an 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.22 Ref.24
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 and RANBP3. 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.
Subcellular location	Cytoplasm. Nucleus › nucleoplasm. Nucleus › Cajal body. Nucleus › nucleolus. Note: Located in the nucleoplasm, Cajal bodies and nucleoli. Shuttles between the nucleus/nucleolus and the cytoplasm. Ref.24 Ref.1 Ref.2 Ref.25
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
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.26 Ref.27
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 process	Host-virus interaction Protein transport Transport mRNA transport
Cellular component	Cytoplasm Nucleus
Domain	Repeat
Ligand	RNA-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW mRNA transport Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	Cajal body Inferred from electronic annotation. Source: UniProtKB-SubCell annulate lamellae Inferred from direct assay. Source: UniProtKB cytosol Inferred from Experiment. Source: Reactome kinetochore Inferred from direct assay. Source: UniProtKB nuclear envelope Ref.2 Traceable author statement. Source: ProtInc nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell ribonucleoprotein complex Inferred from direct assay. Source: MGI
Molecular function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Ref.19 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PHB	P35232	1	EBI-355867,EBI-354213
RCC1	P18754	1	EBI-355867,EBI-992720

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1071

1071

Exportin-1

PRO_0000204705

Regions

Domain

46 – 112

67

Importin N-terminal

Repeat

217 – 240

24

HEAT 1

Repeat

241 – 277

37

HEAT 2

Repeat

354 – 472

119

HEAT 3

Repeat

515 – 553

39

HEAT 4

Repeat

560 – 597

38

HEAT 5

Repeat

602 – 639

38

HEAT 6

Repeat

775 – 813

39

HEAT 7

Repeat

885 – 916

32

HEAT 8

Repeat

917 – 954

38

HEAT 9

Repeat

1002 – 1039

38

HEAT 10

Region

1 – 679

679

Necessary for HTLV-1 Rex-mediated mRNA export

Region

327 – 450

124

Interaction with Ran and nuclear export complex formation

Region

411 – 481

71

Interaction with RANBP3

Region

411 – 414

4

Necessary for HTLV-1 Rex multimerization

Region

800 – 820

21

Interaction with HIV-1 Rev

Amino acid modifications

Modified residue

391

1

Phosphoserine Ref.27

Modified residue

397

1

Phosphoserine Ref.26

Modified residue

446

1

N6-acetyllysine Ref.29

Modified residue

455

1

N6-acetyllysine Ref.29

Modified residue

693

1

N6-acetyllysine Ref.29

Modified residue

1031

1

Phosphoserine Ref.27

Experimental info

Mutagenesis

191

1

S → A: Does not abolish Rex-mediated mRNA export. Ref.22

Mutagenesis

284

1

V → E: Does not abolish Rex-mediated mRNA export. Ref.22

Mutagenesis

334

1

D → G: Does not abolish Rex-mediated mRNA export. Ref.22

Mutagenesis

337

1

I → L: Does not abolish Rex-mediated mRNA export. Ref.22

Mutagenesis

346

1

T → A: Does not abolish Rex-mediated mRNA export. Ref.22

Mutagenesis

402

1

V → I: Does not abolish Rex-mediated mRNA export. Ref.22

Mutagenesis

411

1

P → 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.22

Mutagenesis

412

1

M → V: Does not abolish interaction with Rex and RANBP3, and Rex-mediated mRNA export. Ref.22

Mutagenesis

414

1

F → 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.22

Mutagenesis

428 – 447

20

EEVLV…EFMKD → QQVLVVQNNQGQVVRQFMKN: Abolishes Ran binding activity in absence of cargo and abolishes partially Ran binding activity in presence of cargo.

Mutagenesis

430 – 446

17

VLVVE…REFMK → DEDEENDQGEDEEEDDD: Partially restores Ran binding activity in presence of cargo.

Mutagenesis

430 – 433

4

VLVV → DEDE: Abolishes Ran binding activity both in absence or presence of cargo.

Mutagenesis

454

1

Y → A: Does not abolish Ran binding activity and nuclear export complex formation. Ref.30

Mutagenesis

474

1

R → I: Strongly abolishes interaction with Rex and RANBP3, abolishes Rex-mediated mRNA export. Ref.22

Mutagenesis

481

1

H → Q: Strongly abolishes interaction with Rex and RANBP3, abolishes Rex-mediated mRNA export. Ref.22

Mutagenesis

513

1

E → 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.30

Mutagenesis

525

1

L → 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.30

Mutagenesis

550

1

Q → A: Enhances Ran binding activity and does not abolish nuclear export complex formation; when associated with A-553 and A-590. Ref.30

Mutagenesis

553

1

R → 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.30

Mutagenesis

554

1

F → 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.30

Mutagenesis

561

1

F → 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.30

Mutagenesis

568

1

K → A: Does not abolish Ran binding activity and partially abolish nuclear export complex formation; when associated with A-525 and A-572. Ref.30

Mutagenesis

572

1

F → A: Does not abolish Ran binding activity and partially abolish nuclear export complex formation; when associated with A-525 and A-568. Ref.30

Mutagenesis

583

1

M → A: Enhances Ran binding activity; when associated with A-590. Ref.30

Mutagenesis

590

1

K → 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.30

Sequence conflict

406

1

R → G in CAH56174. Ref.4

Sequence conflict

953

1

V → G in CAH18695. Ref.4

Sequence conflict

989

1

L → I in CAH56174. Ref.4

Secondary structure

1

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1071

Helix Strand Turn

Details...

Helix

711 – 713

3

Helix

714 – 735

22

Helix

738 – 741

4

Helix

743 – 764

22

Helix

769 – 775

7

Helix

777 – 789

13

Helix

793 – 795

3

Helix

799 – 811

13

Helix

812 – 818

7

Helix

819 – 834

16

Turn

837 – 839

3

Helix

842 – 858

17

Helix

862 – 865

4

Helix

868 – 881

14

Helix

887 – 906

20

Helix

908 – 931

24

Beta strand

932 – 934

3

Helix

939 – 954

16

Beta strand

964 – 966

3

Helix

970 – 985

16

Helix

991 – 1003

13

Turn

1004 – 1006

3

Helix

1008 – 1023

16

Turn

1024 – 1026

3

Sequences

	Sequence		Length	Mass (Da)
	O14980-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: FDB00C065DA2FB1D	FASTA	1,071	123,386
	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

References

	« Hide 'large scale' referencesShow '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: 9049309] [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: 9368044] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Chronic myeloid leukemia cell.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [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: 17974005] [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. , 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: 15815621] [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. , 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: 15489334] [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, 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: 9323133] [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: 9311922] [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: 9837918] [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: 10209022] [Abstract] Cited for: IDENTIFICATION IN AN 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: 10400785] [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: 10430904] [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: 10358091] [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: 11571268] [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: 11119609] [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: 11425870] [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: 11932251] [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: 12134013] [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: 12724356] [Abstract] Cited for: IDENTIFICATION IN A 60S RIBOSOMAL SUBUNIT COMPLEX WITH RAN AND NMD3, INTERACTION WITH NMD3.
[22]	"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: 14612415] [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.
[23]	"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: 15507209] [Abstract] Cited for: INTERACTION WITH DDX3X.
[24]	"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: 15574332] [Abstract] Cited for: FUNCTION IN U3 SNORNA TRANSPORT, SUBCELLULAR LOCATION, RNA-BINDING.
[25]	"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: 15632073] [Abstract] Cited for: INTERACTION WITH HIV-1 REV, SUBCELLULAR LOCATION.
[26]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-397, MASS SPECTROMETRY.
[27]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391 AND SER-1031, MASS SPECTROMETRY.
[28]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[29]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-446; LYS-455 AND LYS-693, MASS SPECTROMETRY.
[30]	"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: 15574331] [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

EMBLGenBankDDBJ

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.
BC032847 mRNA. Translation: AAH32847.1.

IPI

IPI00298961.

RefSeq

NP_003391.1.

UniGene

Hs.370770

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1W9C	X-ray	2.30	A/B	707-1027	[»]
3GB8	X-ray	2.90	A	1-1071	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

O14980. 8 interactions.

STRING

O14980.

PTM databases

PhosphoSite

O14980.

Proteomic databases

PRIDE

O14980.

Genome annotation databases

Ensembl

ENST00000195419; ENSP00000195419; ENSG00000082898; Homo sapiens. [Genome view]
ENST00000403576; ENSP00000385257; ENSG00000082898; Homo sapiens. [Genome view]
ENST00000405115; ENSP00000384826; ENSG00000082898; Homo sapiens. [Genome view]
ENST00000406957; ENSP00000385559; ENSG00000082898; Homo sapiens. [Genome view]

GeneID

7514.

KEGG

hsa:7514.

UCSC

uc002sbi.1. human.

Organism-specific databases

CTD

7514.

GeneCards

GC02M061616.

H-InvDB

HIX0002083.

HGNC

HGNC:12825. XPO1.

HPA

CAB010184.

MIM

602559. gene.

PharmGKB

PA37418.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

O14980.

HOVERGEN

O14980.

OMA

SKVRLLM

OrthoDB

EOG9SJ801

Enzyme and pathway databases

Pathway_Interaction_DB

nfkappabcanonicalpathway. Canonical NF-kappaB pathway.
foxopathway. FoxO family signaling.
hedgehog_glipathway. Hedgehog signaling events mediated by Gli proteins.
nfat_3pathway. Role of Calcineurin-dependent NFAT signaling in lymphocytes.
hdac_classi_pathway. Signaling events mediated by HDAC Class I.
hdac_classii_pathway. Signaling events mediated by HDAC Class II.
ranbp2pathway. Sumoylation by RanBP2 regulates transcriptional repression.

Reactome

REACT_152. Cell Cycle, Mitotic.
REACT_6167. Influenza Infection.
REACT_6185. HIV Infection.

Gene expression databases

ArrayExpress

O14980.

Bgee

O14980.

CleanEx

HS_XPO1.

Genevestigator

O14980.

GermOnline

ENSG00000082898. Homo sapiens.

Family and domain databases

InterPro

IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR013598. Exportin-1/Importin-b-like.
IPR014877. Exportin-1_C.
IPR001494. Importin-b_N.
[Graphical view]

Gene3D

G3DSA:1.25.10.10. ARM-like. 1 hit.

Pfam

PF08767. CRM1_C. 1 hit.
PF03810. IBN_N. 1 hit.
PF08389. Xpo1. 1 hit.
[Graphical view]

PROSITE

PS50077. HEAT_REPEAT. False negative.
PS50166. IMPORTIN_B_NT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

29403.

SOURCE

Search...

Entry information

Entry name

XPO1_HUMAN

Accession

Primary (citable) accession number: O14980
Secondary accession number(s): A6NL14 , A8K1K5, Q63HP8, Q68CP3, Q99433

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 21, 2005
Last sequence update:	January 1, 1998
Last modified:	November 24, 2009
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.