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Protein

Exportin-1

Gene

Xpo1

Organism
Mus musculus (Mouse)
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. 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 (By similarity).By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

  • mRNA transport Source: UniProtKB-KW
  • negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  • protein export from nucleus Source: MGI
  • protein localization to nucleus Source: MGI
  • regulation of centrosome duplication Source: MGI
  • regulation of protein catabolic process Source: MGI
  • regulation of protein export from nucleus Source: MGI
  • response to drug Source: Ensembl
  • ribosomal large subunit export from nucleus Source: MGI
  • ribosomal small subunit export from nucleus Source: MGI
Complete GO annotation...

Keywords - Biological processi

mRNA transport, Protein transport, Transport

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2500257. Resolution of Sister Chromatid Cohesion.
R-MMU-3769402. Deactivation of the beta-catenin transactivating complex.
R-MMU-450520. HuR (ELAVL1) binds and stabilizes mRNA.
R-MMU-5663220. RHO GTPases Activate Formins.
R-MMU-5687128. MAPK6/MAPK4 signaling.
R-MMU-68877. Mitotic Prometaphase.
R-MMU-69273. Cyclin A/B1 associated events during G2/M transition.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:2144013. Xpo1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002047061 – 1071Exportin-1Add BLAST1071

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei391PhosphoserineBy similarity1
Modified residuei446N6-acetyllysineCombined sources1
Modified residuei448PhosphothreonineBy similarity1
Modified residuei450PhosphoserineBy similarity1
Modified residuei454PhosphotyrosineBy similarity1
Modified residuei693N6-acetyllysineBy similarity1
Modified residuei1031PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ6P5F9.
MaxQBiQ6P5F9.
PaxDbiQ6P5F9.
PeptideAtlasiQ6P5F9.
PRIDEiQ6P5F9.

PTM databases

iPTMnetiQ6P5F9.
PhosphoSitePlusiQ6P5F9.
SwissPalmiQ6P5F9.

Expressioni

Gene expression databases

BgeeiENSMUSG00000020290.
CleanExiMM_XPO1.
ExpressionAtlasiQ6P5F9. baseline and differential.
GenevisibleiQ6P5F9. MM.

Interactioni

Subunit structurei

Found in a U snRNA export complex with PHAX/RNUXA, NCBP1/CBP80, NCBP2/CBP20, RAN, XPO1 and m7G-capped RNA (PubMed:10786834). 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. Interacts with NEMF (via its N-terminus). Interacts with the monomeric form of BIRC5/survivin deacetylated at 'Lys-129'. Interacts with SERTAD2; the interaction translocates SERTAD2 out of the nucleus. Interacts with ATF2. Interacts with SLC35G1 and STIM1. Interacts with DCAF8 (By similarity). Interacts with DTNBP1 and the interaction translocates DTNBP1 out of the nucleus (PubMed:20921223). Interacts with CPEB3 (By similarity). Interacts with HAX1 (By similarity). Interacts with BOK; translocates to the cytoplasm (By similarity).By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
arpc1bQ6GNU12EBI-2550236,EBI-11607516From a different organism.
LOC495502Q3B8L52EBI-2550236,EBI-11608794From a different organism.
NS2P0DJZ22EBI-2550236,EBI-9673535From a different organism.
sept2B7ZR202EBI-2550236,EBI-11608460From a different organism.
SUP35Q918552EBI-2550236,EBI-11606693From a different organism.

Protein-protein interaction databases

BioGridi222117. 18 interactors.
DIPiDIP-48612N.
IntActiQ6P5F9. 1780 interactors.
STRINGi10090.ENSMUSP00000020538.

Structurei

Secondary structure

11071
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi18 – 20Combined sources3
Helixi25 – 33Combined sources9
Turni34 – 36Combined sources3
Helixi40 – 51Combined sources12
Turni52 – 54Combined sources3
Beta strandi55 – 57Combined sources3
Helixi59 – 63Combined sources5
Helixi73 – 89Combined sources17
Helixi91 – 93Combined sources3
Helixi96 – 114Combined sources19
Helixi117 – 120Combined sources4
Helixi124 – 141Combined sources18
Turni142 – 145Combined sources4
Helixi149 – 159Combined sources11
Helixi161 – 178Combined sources18
Helixi182 – 185Combined sources4
Helixi188 – 200Combined sources13
Helixi203 – 215Combined sources13
Helixi219 – 232Combined sources14
Turni233 – 235Combined sources3
Helixi239 – 242Combined sources4
Beta strandi243 – 245Combined sources3
Helixi246 – 253Combined sources8
Beta strandi255 – 257Combined sources3
Helixi258 – 273Combined sources16
Helixi277 – 279Combined sources3
Helixi280 – 297Combined sources18
Beta strandi300 – 302Combined sources3
Helixi304 – 309Combined sources6
Helixi315 – 339Combined sources25
Helixi341 – 343Combined sources3
Helixi344 – 357Combined sources14
Helixi363 – 383Combined sources21
Helixi404 – 407Combined sources4
Helixi410 – 422Combined sources13
Beta strandi430 – 434Combined sources5
Beta strandi436 – 438Combined sources3
Beta strandi440 – 444Combined sources5
Helixi449 – 467Combined sources19
Helixi469 – 484Combined sources16
Helixi491 – 503Combined sources13
Turni504 – 506Combined sources3
Helixi510 – 530Combined sources21
Helixi534 – 550Combined sources17
Helixi552 – 557Combined sources6
Helixi559 – 572Combined sources14
Helixi580 – 594Combined sources15
Helixi596 – 599Combined sources4
Helixi610 – 615Combined sources6
Helixi618 – 622Combined sources5
Helixi627 – 641Combined sources15
Helixi647 – 657Combined sources11
Helixi659 – 674Combined sources16
Helixi676 – 680Combined sources5
Helixi682 – 702Combined sources21
Helixi704 – 706Combined sources3
Helixi707 – 735Combined sources29
Helixi737 – 740Combined sources4
Helixi743 – 763Combined sources21
Helixi769 – 775Combined sources7
Helixi778 – 783Combined sources6
Helixi785 – 790Combined sources6
Helixi793 – 795Combined sources3
Helixi799 – 811Combined sources13
Helixi812 – 814Combined sources3
Helixi816 – 818Combined sources3
Helixi819 – 834Combined sources16
Beta strandi838 – 840Combined sources3
Helixi842 – 858Combined sources17
Helixi860 – 862Combined sources3
Turni863 – 865Combined sources3
Helixi868 – 882Combined sources15
Helixi887 – 904Combined sources18
Helixi908 – 930Combined sources23
Helixi936 – 938Combined sources3
Helixi939 – 953Combined sources15
Turni954 – 956Combined sources3
Beta strandi961 – 963Combined sources3
Turni965 – 968Combined sources4
Helixi970 – 985Combined sources16
Beta strandi987 – 989Combined sources3
Helixi991 – 1003Combined sources13
Turni1004 – 1006Combined sources3
Helixi1008 – 1022Combined sources15
Turni1027 – 1029Combined sources3
Helixi1037 – 1052Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3GJXX-ray2.50A/D1-1071[»]
3NBYX-ray3.42A/D1-1071[»]
3NBZX-ray2.80A/D1-1071[»]
3NC0X-ray2.90A/D1-1071[»]
3NC1X-ray3.35A1-1071[»]
ProteinModelPortaliQ6P5F9.
SMRiQ6P5F9.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ6P5F9.

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
Regioni327 – 450Necessary for interaction with Ran and nuclear export complex formationBy similarityAdd BLAST124
Regioni411 – 481Necessary for interaction with RANBP3By similarityAdd BLAST71

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.
HOGENOMiHOG000209012.
HOVERGENiHBG052817.
InParanoidiQ6P5F9.
KOiK14290.
OMAiTFIKIAL.
OrthoDBiEOG091G013G.
PhylomeDBiQ6P5F9.
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.

Q6P5F9-1 [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 AKHLKDSMCN
210 220 230 240 250
EFSQIFQLCQ FVMENSQNAP LVHATLETLL RFLNWIPLGY IFETKLISTL
260 270 280 290 300
IYKFLNVPMF RNVSLKCLTE IAGVSVSQYE EQFETLFTLT MMQLKQMLPL
310 320 330 340 350
NTNIRLAYSN GKDDEQNFIQ NLSLFLCTFL KEHGQLLEKR LNLREALMEA
360 370 380 390 400
LHYMLLVSEV EETEIFKICL EYWNHLAAEL YRESPFSTSA SPLLSGSQHF
410 420 430 440 450
DIPPRRQLYL TVLSKVRLLM VSRMAKPEEV LVVENDQGEV VREFMKDTDS
460 470 480 490 500
INLYKNMRET LVYLTHLDYV DTEIIMTKKL QNQVNGTEWS 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 PAFLAIPPAQ FKLVLDSIIW AFKHTMRNVA DTGLQILFTL
910 920 930 940 950
LQNVAQEEAA AQSFYQTYFC DILQHIFSVV TDTSHTAGLT MHASILAYMF
960 970 980 990 1000
NLVEEGKIST PLNPGNPVNN QMFIQDYVAN LLKSAFPHLQ DAQVKLFVTG
1010 1020 1030 1040 1050
LFSLNQDIPA FKEHLRDFLV QIKEFAGEDT SDLFLEERET ALRQAQEEKH
1060 1070
KLQMSVPGIL NPHEIPEEMC D
Length:1,071
Mass (Da):123,093
Last modified:July 5, 2004 - v1
Checksum:iB451A19780024562
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC062912 mRNA. Translation: AAH62912.1.
CCDSiCCDS24475.1.
RefSeqiNP_001030303.1. NM_001035226.1.
NP_598775.2. NM_134014.3.
XP_006514493.1. XM_006514430.2.
UniGeneiMm.217547.

Genome annotation databases

EnsembliENSMUST00000020538; ENSMUSP00000020538; ENSMUSG00000020290.
ENSMUST00000102869; ENSMUSP00000099933; ENSMUSG00000020290.
ENSMUST00000102870; ENSMUSP00000099934; ENSMUSG00000020290.
ENSMUST00000109551; ENSMUSP00000105178; ENSMUSG00000020290.
GeneIDi103573.
KEGGimmu:103573.
UCSCiuc007iet.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC062912 mRNA. Translation: AAH62912.1.
CCDSiCCDS24475.1.
RefSeqiNP_001030303.1. NM_001035226.1.
NP_598775.2. NM_134014.3.
XP_006514493.1. XM_006514430.2.
UniGeneiMm.217547.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3GJXX-ray2.50A/D1-1071[»]
3NBYX-ray3.42A/D1-1071[»]
3NBZX-ray2.80A/D1-1071[»]
3NC0X-ray2.90A/D1-1071[»]
3NC1X-ray3.35A1-1071[»]
ProteinModelPortaliQ6P5F9.
SMRiQ6P5F9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi222117. 18 interactors.
DIPiDIP-48612N.
IntActiQ6P5F9. 1780 interactors.
STRINGi10090.ENSMUSP00000020538.

PTM databases

iPTMnetiQ6P5F9.
PhosphoSitePlusiQ6P5F9.
SwissPalmiQ6P5F9.

Proteomic databases

EPDiQ6P5F9.
MaxQBiQ6P5F9.
PaxDbiQ6P5F9.
PeptideAtlasiQ6P5F9.
PRIDEiQ6P5F9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000020538; ENSMUSP00000020538; ENSMUSG00000020290.
ENSMUST00000102869; ENSMUSP00000099933; ENSMUSG00000020290.
ENSMUST00000102870; ENSMUSP00000099934; ENSMUSG00000020290.
ENSMUST00000109551; ENSMUSP00000105178; ENSMUSG00000020290.
GeneIDi103573.
KEGGimmu:103573.
UCSCiuc007iet.1. mouse.

Organism-specific databases

CTDi7514.
MGIiMGI:2144013. Xpo1.

Phylogenomic databases

eggNOGiKOG2020. Eukaryota.
COG5101. LUCA.
GeneTreeiENSGT00390000000572.
HOGENOMiHOG000209012.
HOVERGENiHBG052817.
InParanoidiQ6P5F9.
KOiK14290.
OMAiTFIKIAL.
OrthoDBiEOG091G013G.
PhylomeDBiQ6P5F9.
TreeFamiTF105695.

Enzyme and pathway databases

ReactomeiR-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2500257. Resolution of Sister Chromatid Cohesion.
R-MMU-3769402. Deactivation of the beta-catenin transactivating complex.
R-MMU-450520. HuR (ELAVL1) binds and stabilizes mRNA.
R-MMU-5663220. RHO GTPases Activate Formins.
R-MMU-5687128. MAPK6/MAPK4 signaling.
R-MMU-68877. Mitotic Prometaphase.
R-MMU-69273. Cyclin A/B1 associated events during G2/M transition.

Miscellaneous databases

ChiTaRSiXpo1. mouse.
EvolutionaryTraceiQ6P5F9.
PROiQ6P5F9.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000020290.
CleanExiMM_XPO1.
ExpressionAtlasiQ6P5F9. baseline and differential.
GenevisibleiQ6P5F9. MM.

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_MOUSE
AccessioniPrimary (citable) accession number: Q6P5F9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: July 5, 2004
Last modified: November 30, 2016
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.