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O43592 (XPOT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Exportin-T
Alternative name(s):
Exportin(tRNA)
tRNA exportin
Gene names
Name:XPOT
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length962 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mediates the nuclear export of aminoacylated tRNAs. In the nucleus binds to tRNA and to the GTPase Ran in its active GTP-bound form. Docking of this trimeric 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 tRNA from the export receptor. XPOT then return to the nuclear compartment and mediate another round of transport. 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. Ref.1 Ref.2 Ref.7

Subunit structure

Found in a complex with XPOT, Ran and tRNA. Probably found in a complex with nucleoporins. Interacts with Ran and tRNA in a GTP-dependent manner. Ref.1 Ref.2 Ref.7

Subcellular location

Nucleus. Cytoplasm. Note: Nuclear, once bound to tRNA and Ran the complex translocates to the cytoplasm. Shuttles between the nucleus and the cytoplasm. Ref.1 Ref.2 Ref.7

Sequence similarities

Belongs to the exportin family.

Ontologies

Keywords
   Biological processTransport
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityPolymorphism
   LigandRNA-binding
tRNA-binding
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processintracellular protein transport

Inferred from electronic annotation. Source: InterPro

tRNA export from nucleus

Inferred from direct assay Ref.1. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay Ref.1. Source: UniProtKB

nucleoplasm

Inferred from direct assay Ref.1. Source: UniProtKB

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functiontRNA binding

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 962962Exportin-T
PRO_0000204716

Regions

Region1 – 385385Necessary for interaction with Ran, nuclear localization and nuclear import
Region443 – 962520Necessary for tRNA-binding, cytoplasmic localization and nuclear export

Amino acid modifications

Modified residue11N-acetylmethionine Ref.8 Ref.11 Ref.12
Modified residue6341N6-acetyllysine Ref.9

Natural variations

Natural variant5261A → V. Ref.4
Corresponds to variant rs17851795 [ dbSNP | Ensembl ].
VAR_026528
Natural variant7161E → D.
Corresponds to variant rs1051396 [ dbSNP | Ensembl ].
VAR_048962

Experimental info

Mutagenesis405 – 4095RKQLK → AAQLA: Abolishes binding to tRNA. Does not abolish shuttling behavior.
Mutagenesis539 – 5435KVRSR → AVRSA: Does not abolish binding to tRNA. Does not abolish shuttling behavior.
Mutagenesis547 – 5515LFSRF → AFSRA: Does not abolish binding to tRNA. Does not abolish shuttling behavior.
Mutagenesis548 – 5525FSRFV → ASRFA: Does not abolish binding to tRNA. Does not abolish shuttling behavior. Ref.7
Mutagenesis550 – 5578RFVKSLNK → AFVASLNA: Abolishes binding to tRNA. Does not abolish shuttling behavior. Ref.7
Sequence conflict3601Q → R in AAC39793. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O43592 [UniParc].

Last modified May 30, 2006. Version 2.
Checksum: 2F407EEDEC7C2996

FASTA962109,964
        10         20         30         40         50         60 
MDEQALLGLN PNADSDFRQR ALAYFEQLKI SPDAWQVCAE ALAQRTYSDD HVKFFCFQVL 

        70         80         90        100        110        120 
EHQVKYKYSE LTTVQQQLIR ETLISWLQAQ MLNPQPEKTF IRNKAAQVFA LLFVTEYLTK 

       130        140        150        160        170        180 
WPKFFFDILS VVDLNPRGVD LYLRILMAID SELVDRDVVH TSEEARRNTL IKDTMREQCI 

       190        200        210        220        230        240 
PNLVESWYQI LQNYQFTNSE VTCQCLEVVG AYVSWIDLSL IANDRFINML LGHMSIEVLR 

       250        260        270        280        290        300 
EEACDCLFEV VNKGMDPVDK MKLVESLCQV LQSAGFFSID QEEDVDFLAR FSKLVNGMGQ 

       310        320        330        340        350        360 
SLIVSWSKLI KNGDIKNAQE ALQAIETKVA LMLQLLIHED DDISSNIIGF CYDYLHILKQ 

       370        380        390        400        410        420 
LTVLSDQQKA NVEAIMLAVM KKLTYDEEYN FENEGEDEAM FVEYRKQLKL LLDRLAQVSP 

       430        440        450        460        470        480 
ELLLASVRRV FSSTLQNWQT TRFMEVEVAI RLLYMLAEAL PVSHGAHFSG DVSKASALQD 

       490        500        510        520        530        540 
MMRTLVTSGV SSYQHTSVTL EFFETVVRYE KFFTVEPQHI PCVLMAFLDH RGLRHSSAKV 

       550        560        570        580        590        600 
RSRTAYLFSR FVKSLNKQMN PFIEDILNRI QDLLELSPPE NGHQSLLSSD DQLFIYETAG 

       610        620        630        640        650        660 
VLIVNSEYPA ERKQALMRNL LTPLMEKFKI LLEKLMLAQD EERQASLADC LNHAVGFASR 

       670        680        690        700        710        720 
TSKAFSNKQT VKQCGCSEVY LDCLQTFLPA LSCPLQKDIL RSGVRTFLHR MIICLEEEVL 

       730        740        750        760        770        780 
PFIPSASEHM LKDCEAKDLQ EFIPLINQIT AKFKIQVSPF LQQMFMPLLH AIFEVLLRPA 

       790        800        810        820        830        840 
EENDQSAALE KQMLRRSYFA FLQTVTGSGM SEVIANQGAE NVERVLVTVI QGAVEYPDPI 

       850        860        870        880        890        900 
AQKTCFIILS KLVELWGGKD GPVGFADFVY KHIVPACFLA PLKQTFDLAD AQTVLALSEC 

       910        920        930        940        950        960 
AVTLKTIHLK RGPECVQYLQ QEYLPSLQVA PEIIQEFCQA LQQPDAKVFK NYLKVFFQRA 


KP 

« Hide

References

« Hide 'large scale' references
[1]"Identification of a tRNA-specific nuclear export receptor."
Kutay U., Lipowsky G., Izaurralde E., Bischoff F.R., Schwarzmaier P., Hartmann E., Goerlich D.
Mol. Biol. Cell 1:359-369(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 431-440 AND 739-752, FUNCTION IN TRNA EXPORT, IDENTIFICATION IN A COMPLEX WITH RAN AND TRNA, TRNA-BINDING, SUBCELLULAR LOCATION.
Tissue: Cervix carcinoma.
[2]"Identification of a nuclear export receptor for tRNA."
Arts G.-J., Fornerod M., Mattaj I.W.
Curr. Biol. 8:305-314(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN TRNA EXPORT, IDENTIFICATION IN A COMPLEX WITH RAN AND TRNA, TRNA-BINDING, SUBCELLULAR LOCATION.
Tissue: Cervix carcinoma.
[3]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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], VARIANT VAL-526.
Tissue: Lymph and Placenta.
[5]Bienvenut W.V.
Submitted (JUN-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 21-29; 54-65; 317-328; 360-369 AND 825-851, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[6]"The role of exportin-t in selective nuclear export of mature tRNAs."
Arts G.-J., Kuersten S., Romby P., Ehresmann B., Mattaj I.W.
EMBO J. 17:7430-7441(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: TRNA-BINDING.
[7]"Steady-state nuclear localization of exportin-t involves RanGTP binding and two distinct nuclear pore complex interaction domains."
Kuersten S., Arts G.-J., Walther T.C., Englmeier L., Mattaj I.W.
Mol. Cell. Biol. 22:5708-5720(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN TRNA EXPORT, MUTAGENESIS OF 405-ARG--LYS-409; 539-LYS--ARG-543; 547-LEU--PHE-551; 548-PHE--VAL-552 AND 550-ARG--LYS-557, IDENTIFICATION IN COMPLEX WITH RAN AND TRNA, IDENTIFICATION IN COMPLEX WITH EXPORTINS, TRNA-BINDING, SUBCELLULAR LOCATION.
[8]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"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-634, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF039022 mRNA. Translation: AAC39793.1.
Y16414 mRNA. Translation: CAA76202.1.
AC135279 Genomic DNA. No translation available.
BC000950 mRNA. Translation: AAH00950.1.
BC020569 mRNA. Translation: AAH20569.1.
RefSeqNP_009166.2. NM_007235.4.
UniGeneHs.85951.

3D structure databases

ProteinModelPortalO43592.
SMRO43592. Positions 8-961.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116420. 26 interactions.
IntActO43592. 9 interactions.
MINTMINT-1138512.
STRING9606.ENSP00000327821.

PTM databases

PhosphoSiteO43592.

Proteomic databases

PaxDbO43592.
PRIDEO43592.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000332707; ENSP00000327821; ENSG00000184575.
GeneID11260.
KEGGhsa:11260.
UCSCuc001ssb.3. human.

Organism-specific databases

CTD11260.
GeneCardsGC12P064798.
HGNCHGNC:12826. XPOT.
HPAHPA038660.
HPA048067.
MIM603180. gene.
neXtProtNX_O43592.
PharmGKBPA37419.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG270401.
HOGENOMHOG000007104.
HOVERGENHBG094163.
InParanoidO43592.
KOK14288.
OMAKMRYDET.
OrthoDBEOG7SN8BQ.
PhylomeDBO43592.
TreeFamTF314001.

Gene expression databases

ArrayExpressO43592.
BgeeO43592.
CleanExHS_XPOT.
GenevestigatorO43592.

Family and domain databases

Gene3D1.25.10.10. 2 hits.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR013598. Exportin-1/Importin-b-like.
IPR001494. Importin-beta_N.
[Graphical view]
PfamPF08389. Xpo1. 1 hit.
[Graphical view]
SMARTSM00913. IBN_N. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 2 hits.
ProtoNetSearch...

Other

ChiTaRSXPOT. human.
GeneWikiXPOT.
GenomeRNAi11260.
NextBio42852.
PROO43592.
SOURCESearch...

Entry information

Entry nameXPOT_HUMAN
AccessionPrimary (citable) accession number: O43592
Secondary accession number(s): A6NLH1 expand/collapse secondary AC list , O43784, Q8WUG2, Q9BVS7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: May 30, 2006
Last modified: April 16, 2014
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM