SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O14980

- XPO1_HUMAN

UniProt

O14980 - XPO1_HUMAN

(max 400 entries)x

Your basket is currently empty.

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

Protein
Exportin-1
Gene
XPO1, CRM1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.6 Publications

GO - Molecular functioni

  1. RNA binding Source: UniProtKB-KW
  2. nucleocytoplasmic transporter activity Source: BHF-UCL
  3. protein binding Source: UniProtKB
  4. protein transporter activity Source: Ensembl
  5. transporter activity Source: Reactome

GO - Biological processi

  1. RNA metabolic process Source: Reactome
  2. gene expression Source: Reactome
  3. intracellular transport of virus Source: Reactome
  4. mRNA metabolic process Source: Reactome
  5. mRNA transport Source: UniProtKB-KW
  6. mitotic cell cycle Source: Reactome
  7. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  8. negative regulation of transforming growth factor beta receptor signaling pathway Source: Reactome
  9. protein export from nucleus Source: BHF-UCL
  10. protein localization to nucleus Source: Ensembl
  11. regulation of centrosome duplication Source: Ensembl
  12. regulation of protein catabolic process Source: Ensembl
  13. regulation of protein export from nucleus Source: Ensembl
  14. response to drug Source: Ensembl
  15. ribosomal large subunit export from nucleus Source: BHF-UCL
  16. ribosomal small subunit export from nucleus Source: BHF-UCL
  17. transforming growth factor beta receptor signaling pathway Source: Reactome
  18. viral life cycle Source: Reactome
  19. viral process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, mRNA transport, Protein transport, Transport

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_120727. Downregulation of TGF-beta receptor signaling.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_1857. Cyclin A/B1 associated events during G2/M transition.
REACT_200731. deactivation of the beta-catenin transactivating complex.
REACT_25218. HuR stabilizes mRNA.
REACT_6179. NEP/NS2 Interacts with the Cellular Export Machinery.
REACT_6190. Rev-mediated nuclear export of HIV RNA.
REACT_682. Mitotic Prometaphase.
SignaLinkiO14980.

Names & Taxonomyi

Protein namesi
Recommended name:
Exportin-1
Short name:
Exp1
Alternative name(s):
Chromosome region maintenance 1 protein homolog
Gene namesi
Name:XPO1
Synonyms:CRM1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:12825. XPO1.

Subcellular locationi

Cytoplasm. Nucleusnucleoplasm. NucleusCajal body. Nucleusnucleolus
Note: Located in the nucleoplasm, Cajal bodies and nucleoli. Shuttles between the nucleus/nucleolus and the cytoplasm.4 Publications

GO - Cellular componenti

  1. Cajal body Source: UniProtKB-SubCell
  2. annulate lamellae Source: UniProtKB
  3. cytoplasm Source: HPA
  4. cytosol Source: Reactome
  5. intracellular membrane-bounded organelle Source: HPA
  6. kinetochore Source: UniProtKB
  7. nuclear envelope Source: ProtInc
  8. nuclear membrane Source: HPA
  9. nucleolus Source: UniProtKB-SubCell
  10. nucleoplasm Source: Reactome
  11. nucleus Source: HPA
  12. ribonucleoprotein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi191 – 1911S → A: Does not abolish Rex-mediated mRNA export. 1 Publication
Mutagenesisi284 – 2841V → E: Does not abolish Rex-mediated mRNA export. 1 Publication
Mutagenesisi334 – 3341D → G: Does not abolish Rex-mediated mRNA export. 1 Publication
Mutagenesisi337 – 3371I → L: Does not abolish Rex-mediated mRNA export. 1 Publication
Mutagenesisi346 – 3461T → A: Does not abolish Rex-mediated mRNA export. 1 Publication
Mutagenesisi402 – 4021V → I: Does not abolish Rex-mediated mRNA export. 1 Publication
Mutagenesisi411 – 4111P → 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. 1 Publication
Mutagenesisi412 – 4121M → V: Does not abolish interaction with Rex and RANBP3, and Rex-mediated mRNA export. 1 Publication
Mutagenesisi414 – 4141F → 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. 1 Publication
Mutagenesisi428 – 44720EEVLV…EFMKD → QQVLVVQNNQGQVVRQFMKN: Abolishes Ran binding activity in absence of cargo and abolishes partially Ran binding activity in presence of cargo. 1 Publication
Add
BLAST
Mutagenesisi430 – 44617VLVVE…REFMK → DEDEENDQGEDEEEDDD: Partially restores Ran binding activity in presence of cargo. 1 Publication
Add
BLAST
Mutagenesisi430 – 4334VLVV → DEDE: Abolishes Ran binding activity both in absence or presence of cargo. 1 Publication
Mutagenesisi454 – 4541Y → A: Does not abolish Ran binding activity and nuclear export complex formation. 1 Publication
Mutagenesisi474 – 4741R → I: Strongly abolishes interaction with Rex and RANBP3, abolishes Rex-mediated mRNA export. 1 Publication
Mutagenesisi481 – 4811H → Q: Strongly abolishes interaction with Rex and RANBP3, abolishes Rex-mediated mRNA export. 1 Publication
Mutagenesisi513 – 5131E → 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. 1 Publication
Mutagenesisi525 – 5251L → 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. 1 Publication
Mutagenesisi550 – 5501Q → A: Enhances Ran binding activity and does not abolish nuclear export complex formation; when associated with A-553 and A-590. 1 Publication
Mutagenesisi553 – 5531R → 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. 1 Publication
Mutagenesisi554 – 5541F → 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. 1 Publication
Mutagenesisi561 – 5611F → 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. 1 Publication
Mutagenesisi568 – 5681K → A: Does not abolish Ran binding activity and partially abolish nuclear export complex formation; when associated with A-525 and A-572. 1 Publication
Mutagenesisi572 – 5721F → A: Does not abolish Ran binding activity and partially abolish nuclear export complex formation; when associated with A-525 and A-568. 1 Publication
Mutagenesisi583 – 5831M → A: Enhances Ran binding activity; when associated with A-590. 1 Publication
Mutagenesisi590 – 5901K → 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. 1 Publication

Organism-specific databases

PharmGKBiPA37418.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10711071Exportin-1
PRO_0000204705Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei391 – 3911Phosphoserine1 Publication
Modified residuei446 – 4461N6-acetyllysine1 Publication
Modified residuei448 – 4481Phosphothreonine By similarity
Modified residuei450 – 4501Phosphoserine By similarity
Modified residuei454 – 4541Phosphotyrosine By similarity
Modified residuei693 – 6931N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO14980.
PaxDbiO14980.
PRIDEiO14980.

PTM databases

PhosphoSiteiO14980.

Expressioni

Tissue specificityi

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.2 Publications

Gene expression databases

ArrayExpressiO14980.
BgeeiO14980.
CleanExiHS_XPO1.
GenevestigatoriO14980.

Organism-specific databases

HPAiCAB010184.
HPA042933.

Interactioni

Subunit structurei

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 ATF2.22 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BIRC5O153922EBI-355867,EBI-518823
ERBB2P046262EBI-355867,EBI-641062
PHBP352322EBI-355867,EBI-354213
PKIAP619252EBI-355867,EBI-2682139

Protein-protein interaction databases

BioGridi113348. 156 interactions.
DIPiDIP-33678N.
IntActiO14980. 34 interactions.
MINTiMINT-5002192.
STRINGi9606.ENSP00000195419.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi63 – 686
Helixi76 – 8914
Helixi97 – 11317
Helixi124 – 14118
Turni142 – 1454
Helixi149 – 1579
Helixi161 – 17515
Helixi188 – 19710
Helixi199 – 21517
Helixi219 – 23214
Turni233 – 2353
Helixi238 – 2425
Beta strandi243 – 2453
Helixi246 – 2538
Turni254 – 2563
Helixi258 – 2603
Helixi261 – 27313
Helixi280 – 29718
Helixi304 – 3107
Helixi313 – 33927
Helixi341 – 3433
Helixi344 – 35815
Helixi363 – 38321
Helixi404 – 42320
Helixi448 – 46720
Helixi469 – 48416
Beta strandi485 – 4884
Helixi491 – 50313
Turni504 – 5063
Helixi510 – 53021
Helixi534 – 55017
Helixi552 – 5576
Helixi559 – 57214
Helixi580 – 59516
Helixi596 – 5983
Beta strandi605 – 6084
Helixi610 – 6156
Helixi618 – 6225
Helixi627 – 64216
Helixi647 – 67428
Helixi676 – 6805
Helixi682 – 70221
Helixi704 – 7063
Helixi711 – 7133
Helixi714 – 73522
Helixi738 – 7414
Helixi743 – 76422
Helixi769 – 7757
Helixi777 – 78913
Helixi793 – 7953
Helixi799 – 81113
Helixi812 – 8187
Helixi819 – 83416
Turni837 – 8393
Helixi842 – 85817
Helixi862 – 8654
Helixi868 – 88114
Beta strandi884 – 8863
Helixi887 – 90620
Helixi908 – 93124
Beta strandi932 – 9343
Helixi939 – 95416
Beta strandi964 – 9663
Helixi970 – 98516
Helixi991 – 100313
Turni1004 – 10063
Helixi1008 – 102316
Turni1024 – 10263
Turni1028 – 10303
Helixi1031 – 105222
Helixi1053 – 10553

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1W9CX-ray2.30A/B707-1027[»]
2L1LNMR-B504-630[»]
3GB8X-ray2.90A1-1071[»]
4BSMX-ray4.50A1-1032[»]
4BSNX-ray4.10A1-1032[»]
ProteinModelPortaliO14980.
SMRiO14980. Positions 53-1061.

Miscellaneous databases

EvolutionaryTraceiO14980.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini46 – 11267Importin N-terminal
Add
BLAST
Repeati217 – 24024HEAT 1
Add
BLAST
Repeati241 – 27737HEAT 2
Add
BLAST
Repeati354 – 472119HEAT 3
Add
BLAST
Repeati515 – 55339HEAT 4
Add
BLAST
Repeati560 – 59738HEAT 5
Add
BLAST
Repeati602 – 63938HEAT 6
Add
BLAST
Repeati775 – 81339HEAT 7
Add
BLAST
Repeati885 – 91632HEAT 8
Add
BLAST
Repeati917 – 95438HEAT 9
Add
BLAST
Repeati1002 – 103938HEAT 10
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 679679Necessary for HTLV-1 Rex-mediated mRNA export
Add
BLAST
Regioni327 – 450124Interaction with Ran and nuclear export complex formation
Add
BLAST
Regioni411 – 48171Interaction with RANBP3
Add
BLAST
Regioni411 – 4144Necessary for HTLV-1 Rex multimerization
Regioni800 – 82021Interaction with HIV-1 Rev
Add
BLAST

Sequence similaritiesi

Belongs to the exportin family.
Contains 10 HEAT repeats.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5101.
HOVERGENiHBG052817.
InParanoidiO14980.
KOiK14290.
OMAiQTYFTDI.
OrthoDBiEOG7CZK4S.
PhylomeDBiO14980.
TreeFamiTF105695.

Family and domain databases

Gene3Di1.25.10.10. 3 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR014877. CRM1_C_dom.
IPR013598. Exportin-1/Importin-b-like.
IPR001494. Importin-beta_N.
[Graphical view]
PfamiPF08767. CRM1_C. 1 hit.
PF03810. IBN_N. 1 hit.
PF08389. Xpo1. 1 hit.
[Graphical view]
SMARTiSM01102. CRM1_C. 1 hit.
SM00913. IBN_N. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 4 hits.
PROSITEiPS50166. IMPORTIN_B_NT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O14980-1 [UniParc]FASTAAdd to Basket

« Hide

MPAIMTMLAD HAARQLLDFS QKLDINLLDN VVNCLYHGEG AQQRMAQEVL     50
THLKEHPDAW TRVDTILEFS QNMNTKYYGL QILENVIKTR WKILPRNQCE 100
GIKKYVVGLI IKTSSDPTCV EKEKVYIGKL NMILVQILKQ EWPKHWPTFI 150
SDIVGASRTS ESLCQNNMVI LKLLSEEVFD FSSGQITQVK SKHLKDSMCN 200
EFSQIFQLCQ FVMENSQNAP LVHATLETLL RFLNWIPLGY IFETKLISTL 250
IYKFLNVPMF RNVSLKCLTE IAGVSVSQYE EQFVTLFTLT MMQLKQMLPL 300
NTNIRLAYSN GKDDEQNFIQ NLSLFLCTFL KEHDQLIEKR LNLRETLMEA 350
LHYMLLVSEV EETEIFKICL EYWNHLAAEL YRESPFSTSA SPLLSGSQHF 400
DVPPRRQLYL PMLFKVRLLM VSRMAKPEEV LVVENDQGEV VREFMKDTDS 450
INLYKNMRET LVYLTHLDYV DTERIMTEKL HNQVNGTEWS WKNLNTLCWA 500
IGSISGAMHE EDEKRFLVTV IKDLLGLCEQ KRGKDNKAII ASNIMYIVGQ 550
YPRFLRAHWK FLKTVVNKLF EFMHETHDGV QDMACDTFIK IAQKCRRHFV 600
QVQVGEVMPF IDEILNNINT IICDLQPQQV HTFYEAVGYM IGAQTDQTVQ 650
EHLIEKYMLL PNQVWDSIIQ QATKNVDILK DPETVKQLGS ILKTNVRACK 700
AVGHPFVIQL GRIYLDMLNV YKCLSENISA AIQANGEMVT KQPLIRSMRT 750
VKRETLKLIS GWVSRSNDPQ MVAENFVPPL LDAVLIDYQR NVPAAREPEV 800
LSTMAIIVNK LGGHITAEIP QIFDAVFECT LNMINKDFEE YPEHRTNFFL 850
LLQAVNSHCF PAFLAIPPTQ FKLVLDSIIW AFKHTMRNVA DTGLQILFTL 900
LQNVAQEEAA AQSFYQTYFC DILQHIFSVV TDTSHTAGLT MHASILAYMF 950
NLVEEGKIST SLNPGNPVNN QIFLQEYVAN LLKSAFPHLQ DAQVKLFVTG 1000
LFSLNQDIPA FKEHLRDFLV QIKEFAGEDT SDLFLEEREI ALRQADEEKH 1050
KRQMSVPGIF NPHEIPEEMC D 1071
Length:1,071
Mass (Da):123,386
Last modified:January 1, 1998 - v1
Checksum:iFDB00C065DA2FB1D
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti406 – 4061R → G in CAH56174. 1 Publication
Sequence conflicti953 – 9531V → G in CAH18695. 1 Publication
Sequence conflicti989 – 9891L → I in CAH56174. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS33205.1.
RefSeqiNP_003391.1. NM_003400.3.
XP_006712157.1. XM_006712094.1.
UniGeneiHs.370770.

Genome annotation databases

EnsembliENST00000401558; ENSP00000384863; ENSG00000082898.
ENST00000404992; ENSP00000385942; ENSG00000082898.
ENST00000406957; ENSP00000385559; ENSG00000082898.
GeneIDi7514.
KEGGihsa:7514.
UCSCiuc002sbh.3. human.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS33205.1.
RefSeqi NP_003391.1. NM_003400.3.
XP_006712157.1. XM_006712094.1.
UniGenei Hs.370770.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1W9C X-ray 2.30 A/B 707-1027 [» ]
2L1L NMR - B 504-630 [» ]
3GB8 X-ray 2.90 A 1-1071 [» ]
4BSM X-ray 4.50 A 1-1032 [» ]
4BSN X-ray 4.10 A 1-1032 [» ]
ProteinModelPortali O14980.
SMRi O14980. Positions 53-1061.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113348. 156 interactions.
DIPi DIP-33678N.
IntActi O14980. 34 interactions.
MINTi MINT-5002192.
STRINGi 9606.ENSP00000195419.

Chemistry

BindingDBi O14980.
ChEMBLi CHEMBL5661.

PTM databases

PhosphoSitei O14980.

Proteomic databases

MaxQBi O14980.
PaxDbi O14980.
PRIDEi O14980.

Protocols and materials databases

DNASUi 7514.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000401558 ; ENSP00000384863 ; ENSG00000082898 .
ENST00000404992 ; ENSP00000385942 ; ENSG00000082898 .
ENST00000406957 ; ENSP00000385559 ; ENSG00000082898 .
GeneIDi 7514.
KEGGi hsa:7514.
UCSCi uc002sbh.3. human.

Organism-specific databases

CTDi 7514.
GeneCardsi GC02M061704.
HGNCi HGNC:12825. XPO1.
HPAi CAB010184.
HPA042933.
MIMi 602559. gene.
neXtProti NX_O14980.
PharmGKBi PA37418.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5101.
HOVERGENi HBG052817.
InParanoidi O14980.
KOi K14290.
OMAi QTYFTDI.
OrthoDBi EOG7CZK4S.
PhylomeDBi O14980.
TreeFami TF105695.

Enzyme and pathway databases

Reactomei REACT_120727. Downregulation of TGF-beta receptor signaling.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_1857. Cyclin A/B1 associated events during G2/M transition.
REACT_200731. deactivation of the beta-catenin transactivating complex.
REACT_25218. HuR stabilizes mRNA.
REACT_6179. NEP/NS2 Interacts with the Cellular Export Machinery.
REACT_6190. Rev-mediated nuclear export of HIV RNA.
REACT_682. Mitotic Prometaphase.
SignaLinki O14980.

Miscellaneous databases

ChiTaRSi XPO1. human.
EvolutionaryTracei O14980.
GeneWikii XPO1.
GenomeRNAii 7514.
NextBioi 29403.
PROi O14980.
SOURCEi Search...

Gene expression databases

ArrayExpressi O14980.
Bgeei O14980.
CleanExi HS_XPO1.
Genevestigatori O14980.

Family and domain databases

Gene3Di 1.25.10.10. 3 hits.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR014877. CRM1_C_dom.
IPR013598. Exportin-1/Importin-b-like.
IPR001494. Importin-beta_N.
[Graphical view ]
Pfami PF08767. CRM1_C. 1 hit.
PF03810. IBN_N. 1 hit.
PF08389. Xpo1. 1 hit.
[Graphical view ]
SMARTi SM01102. CRM1_C. 1 hit.
SM00913. IBN_N. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 4 hits.
PROSITEi PS50166. IMPORTIN_B_NT. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. 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. 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. 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. 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.

Entry informationi

Entry nameiXPO1_HUMAN
AccessioniPrimary (citable) accession number: O14980
Secondary accession number(s): A6NL14
, A8K1K5, D6W5E2, Q63HP8, Q68CP3, Q99433
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: January 1, 1998
Last modified: September 3, 2014
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

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

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi