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Protein

Exportin-1

Gene

XPO1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

  • nuclear export signal receptor activity Source: GO_Central
  • nucleocytoplasmic transporter activity Source: ParkinsonsUK-UCL
  • RNA binding Source: UniProtKB-KW
  • transporter activity Source: Reactome

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

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

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000082898-MONOMER.
ReactomeiR-HSA-165054. Rev-mediated nuclear export of HIV RNA.
R-HSA-168333. NEP/NS2 Interacts with the Cellular Export Machinery.
R-HSA-2173788. Downregulation of TGF-beta receptor signaling.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-3769402. Deactivation of the beta-catenin transactivating complex.
R-HSA-450520. HuR (ELAVL1) binds and stabilizes mRNA.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-5687128. MAPK6/MAPK4 signaling.
R-HSA-68877. Mitotic Prometaphase.
R-HSA-69273. Cyclin A/B1 associated events during G2/M transition.
SignaLinkiO14980.
SIGNORiO14980.

Protein family/group databases

TCDBi1.I.1.1.3. the nuclear pore complex (npc) family.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:12825. XPO1.

Subcellular locationi

GO - Cellular componenti

  • annulate lamellae Source: UniProtKB
  • Cajal body Source: UniProtKB-SubCell
  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • intracellular membrane-bounded organelle Source: HPA
  • intracellular ribonucleoprotein complex Source: MGI
  • kinetochore Source: UniProtKB
  • membrane Source: UniProtKB
  • nuclear envelope Source: ProtInc
  • nuclear membrane Source: HPA
  • nucleolus Source: UniProtKB-SubCell
  • nucleoplasm Source: Reactome
  • nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi191S → A: Does not abolish Rex-mediated mRNA export. 1 Publication1
Mutagenesisi284V → E: Does not abolish Rex-mediated mRNA export. 1 Publication1
Mutagenesisi334D → G: Does not abolish Rex-mediated mRNA export. 1 Publication1
Mutagenesisi337I → L: Does not abolish Rex-mediated mRNA export. 1 Publication1
Mutagenesisi346T → A: Does not abolish Rex-mediated mRNA export. 1 Publication1
Mutagenesisi402V → I: Does not abolish Rex-mediated mRNA export. 1 Publication1
Mutagenesisi411P → 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 Publication1
Mutagenesisi412M → V: Does not abolish interaction with Rex and RANBP3, and Rex-mediated mRNA export. 1 Publication1
Mutagenesisi414F → 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 Publication1
Mutagenesisi428 – 447EEVLV…EFMKD → QQVLVVQNNQGQVVRQFMKN: Abolishes Ran binding activity in absence of cargo and abolishes partially Ran binding activity in presence of cargo. 1 PublicationAdd BLAST20
Mutagenesisi430 – 446VLVVE…REFMK → DEDEENDQGEDEEEDDD: Partially restores Ran binding activity in presence of cargo. 1 PublicationAdd BLAST17
Mutagenesisi430 – 433VLVV → DEDE: Abolishes Ran binding activity both in absence or presence of cargo. 1 Publication4
Mutagenesisi454Y → A: Does not abolish Ran binding activity and nuclear export complex formation. 1 Publication1
Mutagenesisi474R → I: Strongly abolishes interaction with Rex and RANBP3, abolishes Rex-mediated mRNA export. 1 Publication1
Mutagenesisi481H → Q: Strongly abolishes interaction with Rex and RANBP3, abolishes Rex-mediated mRNA export. 1 Publication1
Mutagenesisi513E → 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 Publication1
Mutagenesisi525L → 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 Publication1
Mutagenesisi550Q → A: Enhances Ran binding activity and does not abolish nuclear export complex formation; when associated with A-553 and A-590. 1 Publication1
Mutagenesisi553R → 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 Publication1
Mutagenesisi554F → 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 Publication1
Mutagenesisi561F → 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 Publication1
Mutagenesisi568K → A: Does not abolish Ran binding activity and partially abolish nuclear export complex formation; when associated with A-525 and A-572. 1 Publication1
Mutagenesisi572F → A: Does not abolish Ran binding activity and partially abolish nuclear export complex formation; when associated with A-525 and A-568. 1 Publication1
Mutagenesisi583M → A: Enhances Ran binding activity; when associated with A-590. 1 Publication1
Mutagenesisi590K → 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 Publication1

Organism-specific databases

DisGeNETi7514.
OpenTargetsiENSG00000082898.
PharmGKBiPA37418.

Chemistry databases

ChEMBLiCHEMBL5661.

Polymorphism and mutation databases

BioMutaiXPO1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002047051 – 1071Exportin-1Add BLAST1071

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei391PhosphoserineCombined sources1
Modified residuei446N6-acetyllysineCombined sources1
Modified residuei448PhosphothreonineBy similarity1
Modified residuei450PhosphoserineBy similarity1
Modified residuei454PhosphotyrosineBy similarity1
Modified residuei693N6-acetyllysineCombined sources1
Modified residuei1031PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO14980.
MaxQBiO14980.
PaxDbiO14980.
PeptideAtlasiO14980.
PRIDEiO14980.

PTM databases

iPTMnetiO14980.
PhosphoSitePlusiO14980.
SwissPalmiO14980.

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

BgeeiENSG00000082898.
CleanExiHS_XPO1.
ExpressionAtlasiO14980. baseline and differential.
GenevisibleiO14980. HS.

Organism-specific databases

HPAiCAB010184.
HPA042933.

Interactioni

Subunit structurei

Found in a U snRNA export complex with PHAX/RNUXA, NCBP1/CBP80, NCBP2/CBP20, 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. Interacts with SLC35G1 and STIM1. Interacts with DCAF8. Interacts with CPEB3 (PubMed:22730302). Interacts with HAX1 (PubMed:23164465). Interacts with BOK; translocates to the cytoplasm (PubMed:16302269).By similarity27 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q9WMX23EBI-355867,EBI-710918From a different organism.
BIRC5O153922EBI-355867,EBI-518823
ERBB2P046262EBI-355867,EBI-641062
PHBP352322EBI-355867,EBI-354213
PKIAP619252EBI-355867,EBI-2682139
YWHAZP631042EBI-355867,EBI-347088

Protein-protein interaction databases

BioGridi113348. 1229 interactors.
DIPiDIP-33678N.
IntActiO14980. 56 interactors.
MINTiMINT-5002192.
STRINGi9606.ENSP00000384863.

Chemistry databases

BindingDBiO14980.

Structurei

Secondary structure

11071
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 16Combined sources11
Helixi25 – 37Combined sources13
Helixi40 – 55Combined sources16
Turni57 – 59Combined sources3
Helixi60 – 69Combined sources10
Helixi73 – 90Combined sources18
Helixi91 – 93Combined sources3
Helixi96 – 114Combined sources19
Helixi117 – 119Combined sources3
Turni120 – 123Combined sources4
Helixi124 – 141Combined sources18
Beta strandi142 – 145Combined sources4
Helixi149 – 156Combined sources8
Turni157 – 159Combined sources3
Helixi161 – 179Combined sources19
Turni183 – 185Combined sources3
Helixi188 – 200Combined sources13
Helixi202 – 215Combined sources14
Helixi219 – 235Combined sources17
Helixi239 – 242Combined sources4
Beta strandi243 – 245Combined sources3
Helixi246 – 253Combined sources8
Beta strandi255 – 257Combined sources3
Helixi258 – 273Combined sources16
Helixi277 – 279Combined sources3
Helixi280 – 297Combined sources18
Helixi304 – 310Combined sources7
Helixi313 – 338Combined sources26
Helixi341 – 343Combined sources3
Helixi344 – 358Combined sources15
Helixi363 – 383Combined sources21
Helixi404 – 423Combined sources20
Beta strandi429 – 434Combined sources6
Beta strandi436 – 438Combined sources3
Beta strandi440 – 445Combined sources6
Helixi449 – 467Combined sources19
Helixi469 – 484Combined sources16
Beta strandi485 – 488Combined sources4
Helixi491 – 503Combined sources13
Turni504 – 506Combined sources3
Helixi510 – 530Combined sources21
Helixi534 – 549Combined sources16
Helixi552 – 557Combined sources6
Helixi559 – 572Combined sources14
Helixi580 – 594Combined sources15
Helixi597 – 600Combined sources4
Beta strandi605 – 608Combined sources4
Helixi610 – 616Combined sources7
Helixi618 – 622Combined sources5
Helixi627 – 642Combined sources16
Helixi647 – 657Combined sources11
Helixi659 – 674Combined sources16
Helixi676 – 680Combined sources5
Helixi682 – 702Combined sources21
Helixi704 – 706Combined sources3
Helixi711 – 713Combined sources3
Helixi714 – 735Combined sources22
Helixi738 – 741Combined sources4
Helixi743 – 764Combined sources22
Helixi769 – 775Combined sources7
Helixi777 – 789Combined sources13
Helixi793 – 795Combined sources3
Helixi799 – 811Combined sources13
Helixi812 – 818Combined sources7
Helixi819 – 834Combined sources16
Turni837 – 839Combined sources3
Helixi842 – 858Combined sources17
Helixi862 – 865Combined sources4
Helixi868 – 881Combined sources14
Beta strandi884 – 886Combined sources3
Helixi887 – 906Combined sources20
Helixi908 – 931Combined sources24
Beta strandi932 – 934Combined sources3
Helixi939 – 954Combined sources16
Beta strandi961 – 963Combined sources3
Beta strandi964 – 966Combined sources3
Helixi970 – 985Combined sources16
Helixi991 – 1003Combined sources13
Turni1004 – 1006Combined sources3
Helixi1008 – 1023Combined sources16
Turni1024 – 1026Combined sources3
Turni1028 – 1030Combined sources3
Helixi1035 – 1047Combined sources13
Helixi1053 – 1055Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1W9CX-ray2.30A/B707-1027[»]
2L1LNMR-B504-630[»]
3GB8X-ray2.90A1-1071[»]
4BSMX-ray4.50A1-1032[»]
4BSNX-ray4.10A1-1032[»]
5DISX-ray2.85A5-1048[»]
ProteinModelPortaliO14980.
SMRiO14980.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO14980.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini46 – 112Importin N-terminalPROSITE-ProRule annotationAdd BLAST67
Repeati217 – 240HEAT 1Add BLAST24
Repeati241 – 277HEAT 2Add BLAST37
Repeati354 – 472HEAT 3Add BLAST119
Repeati515 – 553HEAT 4Add BLAST39
Repeati560 – 597HEAT 5Add BLAST38
Repeati602 – 639HEAT 6Add BLAST38
Repeati775 – 813HEAT 7Add BLAST39
Repeati885 – 916HEAT 8Add BLAST32
Repeati917 – 954HEAT 9Add BLAST38
Repeati1002 – 1039HEAT 10Add BLAST38

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 679Necessary for HTLV-1 Rex-mediated mRNA exportAdd BLAST679
Regioni327 – 450Interaction with Ran and nuclear export complex formationAdd BLAST124
Regioni411 – 481Interaction with RANBP3Add BLAST71
Regioni411 – 414Necessary for HTLV-1 Rex multimerization4
Regioni800 – 820Interaction with HIV-1 RevAdd BLAST21

Sequence similaritiesi

Belongs to the exportin family.Curated
Contains 10 HEAT repeats.Curated
Contains 1 importin N-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG2020. Eukaryota.
COG5101. LUCA.
GeneTreeiENSGT00390000000572.
HOVERGENiHBG052817.
InParanoidiO14980.
KOiK14290.
OMAiTFIKIAL.
OrthoDBiEOG091G013G.
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

        10         20         30         40         50
MPAIMTMLAD HAARQLLDFS QKLDINLLDN VVNCLYHGEG AQQRMAQEVL
60 70 80 90 100
THLKEHPDAW TRVDTILEFS QNMNTKYYGL QILENVIKTR WKILPRNQCE
110 120 130 140 150
GIKKYVVGLI IKTSSDPTCV EKEKVYIGKL NMILVQILKQ EWPKHWPTFI
160 170 180 190 200
SDIVGASRTS ESLCQNNMVI LKLLSEEVFD FSSGQITQVK SKHLKDSMCN
210 220 230 240 250
EFSQIFQLCQ FVMENSQNAP LVHATLETLL RFLNWIPLGY IFETKLISTL
260 270 280 290 300
IYKFLNVPMF RNVSLKCLTE IAGVSVSQYE EQFVTLFTLT MMQLKQMLPL
310 320 330 340 350
NTNIRLAYSN GKDDEQNFIQ NLSLFLCTFL KEHDQLIEKR LNLRETLMEA
360 370 380 390 400
LHYMLLVSEV EETEIFKICL EYWNHLAAEL YRESPFSTSA SPLLSGSQHF
410 420 430 440 450
DVPPRRQLYL PMLFKVRLLM VSRMAKPEEV LVVENDQGEV VREFMKDTDS
460 470 480 490 500
INLYKNMRET LVYLTHLDYV DTERIMTEKL HNQVNGTEWS WKNLNTLCWA
510 520 530 540 550
IGSISGAMHE EDEKRFLVTV IKDLLGLCEQ KRGKDNKAII ASNIMYIVGQ
560 570 580 590 600
YPRFLRAHWK FLKTVVNKLF EFMHETHDGV QDMACDTFIK IAQKCRRHFV
610 620 630 640 650
QVQVGEVMPF IDEILNNINT IICDLQPQQV HTFYEAVGYM IGAQTDQTVQ
660 670 680 690 700
EHLIEKYMLL PNQVWDSIIQ QATKNVDILK DPETVKQLGS ILKTNVRACK
710 720 730 740 750
AVGHPFVIQL GRIYLDMLNV YKCLSENISA AIQANGEMVT KQPLIRSMRT
760 770 780 790 800
VKRETLKLIS GWVSRSNDPQ MVAENFVPPL LDAVLIDYQR NVPAAREPEV
810 820 830 840 850
LSTMAIIVNK LGGHITAEIP QIFDAVFECT LNMINKDFEE YPEHRTNFFL
860 870 880 890 900
LLQAVNSHCF PAFLAIPPTQ FKLVLDSIIW AFKHTMRNVA DTGLQILFTL
910 920 930 940 950
LQNVAQEEAA AQSFYQTYFC DILQHIFSVV TDTSHTAGLT MHASILAYMF
960 970 980 990 1000
NLVEEGKIST SLNPGNPVNN QIFLQEYVAN LLKSAFPHLQ DAQVKLFVTG
1010 1020 1030 1040 1050
LFSLNQDIPA FKEHLRDFLV QIKEFAGEDT SDLFLEEREI ALRQADEEKH
1060 1070
KRQMSVPGIF NPHEIPEEMC D
Length:1,071
Mass (Da):123,386
Last modified:January 1, 1998 - v1
Checksum:iFDB00C065DA2FB1D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti406R → G in CAH56174 (PubMed:17974005).Curated1
Sequence conflicti953V → G in CAH18695 (PubMed:17974005).Curated1
Sequence conflicti989L → I in CAH56174 (PubMed:17974005).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_006712094.2.
XP_011531399.1. XM_011533097.1.
UniGeneiHs.370770.

Genome annotation databases

EnsembliENST00000401558; ENSP00000384863; ENSG00000082898.
ENST00000404992; ENSP00000385942; ENSG00000082898.
ENST00000406957; ENSP00000385559; ENSG00000082898.
GeneIDi7514.
KEGGihsa:7514.
UCSCiuc002sbj.4. human.

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_006712094.2.
XP_011531399.1. XM_011533097.1.
UniGeneiHs.370770.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1W9CX-ray2.30A/B707-1027[»]
2L1LNMR-B504-630[»]
3GB8X-ray2.90A1-1071[»]
4BSMX-ray4.50A1-1032[»]
4BSNX-ray4.10A1-1032[»]
5DISX-ray2.85A5-1048[»]
ProteinModelPortaliO14980.
SMRiO14980.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113348. 1229 interactors.
DIPiDIP-33678N.
IntActiO14980. 56 interactors.
MINTiMINT-5002192.
STRINGi9606.ENSP00000384863.

Chemistry databases

BindingDBiO14980.
ChEMBLiCHEMBL5661.

Protein family/group databases

TCDBi1.I.1.1.3. the nuclear pore complex (npc) family.

PTM databases

iPTMnetiO14980.
PhosphoSitePlusiO14980.
SwissPalmiO14980.

Polymorphism and mutation databases

BioMutaiXPO1.

Proteomic databases

EPDiO14980.
MaxQBiO14980.
PaxDbiO14980.
PeptideAtlasiO14980.
PRIDEiO14980.

Protocols and materials databases

DNASUi7514.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000401558; ENSP00000384863; ENSG00000082898.
ENST00000404992; ENSP00000385942; ENSG00000082898.
ENST00000406957; ENSP00000385559; ENSG00000082898.
GeneIDi7514.
KEGGihsa:7514.
UCSCiuc002sbj.4. human.

Organism-specific databases

CTDi7514.
DisGeNETi7514.
GeneCardsiXPO1.
HGNCiHGNC:12825. XPO1.
HPAiCAB010184.
HPA042933.
MIMi602559. gene.
neXtProtiNX_O14980.
OpenTargetsiENSG00000082898.
PharmGKBiPA37418.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2020. Eukaryota.
COG5101. LUCA.
GeneTreeiENSGT00390000000572.
HOVERGENiHBG052817.
InParanoidiO14980.
KOiK14290.
OMAiTFIKIAL.
OrthoDBiEOG091G013G.
PhylomeDBiO14980.
TreeFamiTF105695.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000082898-MONOMER.
ReactomeiR-HSA-165054. Rev-mediated nuclear export of HIV RNA.
R-HSA-168333. NEP/NS2 Interacts with the Cellular Export Machinery.
R-HSA-2173788. Downregulation of TGF-beta receptor signaling.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2500257. Resolution of Sister Chromatid Cohesion.
R-HSA-3769402. Deactivation of the beta-catenin transactivating complex.
R-HSA-450520. HuR (ELAVL1) binds and stabilizes mRNA.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-5687128. MAPK6/MAPK4 signaling.
R-HSA-68877. Mitotic Prometaphase.
R-HSA-69273. Cyclin A/B1 associated events during G2/M transition.
SignaLinkiO14980.
SIGNORiO14980.

Miscellaneous databases

ChiTaRSiXPO1. human.
EvolutionaryTraceiO14980.
GeneWikiiXPO1.
GenomeRNAii7514.
PROiO14980.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000082898.
CleanExiHS_XPO1.
ExpressionAtlasiO14980. baseline and differential.
GenevisibleiO14980. HS.

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]
ProtoNetiSearch...

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: November 30, 2016
This is version 167 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.