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O43592

- XPOT_HUMAN

UniProt

O43592 - XPOT_HUMAN

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Protein

Exportin-T

Gene
XPOT
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.3 Publications

GO - Molecular functioni

  1. tRNA binding Source: UniProtKB

GO - Biological processi

  1. intracellular protein transport Source: InterPro
  2. tRNA export from nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

RNA-binding, tRNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Exportin-T
Alternative name(s):
Exportin(tRNA)
tRNA exportin
Gene namesi
Name:XPOT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:12826. XPOT.

Subcellular locationi

Nucleus. Cytoplasm
Note: Nuclear, once bound to tRNA and Ran the complex translocates to the cytoplasm. Shuttles between the nucleus and the cytoplasm.3 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleoplasm Source: UniProtKB
  3. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi405 – 4095RKQLK → AAQLA: Abolishes binding to tRNA. Does not abolish shuttling behavior.
Mutagenesisi539 – 5435KVRSR → AVRSA: Does not abolish binding to tRNA. Does not abolish shuttling behavior.
Mutagenesisi547 – 5515LFSRF → AFSRA: Does not abolish binding to tRNA. Does not abolish shuttling behavior.
Mutagenesisi548 – 5525FSRFV → ASRFA: Does not abolish binding to tRNA. Does not abolish shuttling behavior. 1 Publication
Mutagenesisi550 – 5578RFVKSLNK → AFVASLNA: Abolishes binding to tRNA. Does not abolish shuttling behavior. 1 Publication

Organism-specific databases

PharmGKBiPA37419.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 962962Exportin-TPRO_0000204716Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine3 Publications
Modified residuei634 – 6341N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO43592.
PaxDbiO43592.
PRIDEiO43592.

PTM databases

PhosphoSiteiO43592.

Expressioni

Gene expression databases

ArrayExpressiO43592.
BgeeiO43592.
CleanExiHS_XPOT.
GenevestigatoriO43592.

Organism-specific databases

HPAiHPA038660.
HPA048067.

Interactioni

Subunit structurei

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.3 Publications

Protein-protein interaction databases

BioGridi116420. 25 interactions.
IntActiO43592. 9 interactions.
MINTiMINT-1138512.
STRINGi9606.ENSP00000327821.

Structurei

3D structure databases

ProteinModelPortaliO43592.
SMRiO43592. Positions 8-961.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 385385Necessary for interaction with Ran, nuclear localization and nuclear importAdd
BLAST
Regioni443 – 962520Necessary for tRNA-binding, cytoplasmic localization and nuclear exportAdd
BLAST

Sequence similaritiesi

Belongs to the exportin family.

Phylogenomic databases

eggNOGiNOG270401.
HOGENOMiHOG000007104.
HOVERGENiHBG094163.
InParanoidiO43592.
KOiK14288.
OMAiKMRYDET.
OrthoDBiEOG7SN8BQ.
PhylomeDBiO43592.
TreeFamiTF314001.

Family and domain databases

Gene3Di1.25.10.10. 2 hits.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR013598. Exportin-1/Importin-b-like.
IPR001494. Importin-beta_N.
[Graphical view]
PfamiPF08389. Xpo1. 1 hit.
[Graphical view]
SMARTiSM00913. IBN_N. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.

Sequencei

Sequence statusi: Complete.

O43592-1 [UniParc]FASTAAdd to Basket

« Hide

MDEQALLGLN PNADSDFRQR ALAYFEQLKI SPDAWQVCAE ALAQRTYSDD    50
HVKFFCFQVL EHQVKYKYSE LTTVQQQLIR ETLISWLQAQ MLNPQPEKTF 100
IRNKAAQVFA LLFVTEYLTK WPKFFFDILS VVDLNPRGVD LYLRILMAID 150
SELVDRDVVH TSEEARRNTL IKDTMREQCI PNLVESWYQI LQNYQFTNSE 200
VTCQCLEVVG AYVSWIDLSL IANDRFINML LGHMSIEVLR EEACDCLFEV 250
VNKGMDPVDK MKLVESLCQV LQSAGFFSID QEEDVDFLAR FSKLVNGMGQ 300
SLIVSWSKLI KNGDIKNAQE ALQAIETKVA LMLQLLIHED DDISSNIIGF 350
CYDYLHILKQ LTVLSDQQKA NVEAIMLAVM KKLTYDEEYN FENEGEDEAM 400
FVEYRKQLKL LLDRLAQVSP ELLLASVRRV FSSTLQNWQT TRFMEVEVAI 450
RLLYMLAEAL PVSHGAHFSG DVSKASALQD MMRTLVTSGV SSYQHTSVTL 500
EFFETVVRYE KFFTVEPQHI PCVLMAFLDH RGLRHSSAKV RSRTAYLFSR 550
FVKSLNKQMN PFIEDILNRI QDLLELSPPE NGHQSLLSSD DQLFIYETAG 600
VLIVNSEYPA ERKQALMRNL LTPLMEKFKI LLEKLMLAQD EERQASLADC 650
LNHAVGFASR TSKAFSNKQT VKQCGCSEVY LDCLQTFLPA LSCPLQKDIL 700
RSGVRTFLHR MIICLEEEVL PFIPSASEHM LKDCEAKDLQ EFIPLINQIT 750
AKFKIQVSPF LQQMFMPLLH AIFEVLLRPA EENDQSAALE KQMLRRSYFA 800
FLQTVTGSGM SEVIANQGAE NVERVLVTVI QGAVEYPDPI AQKTCFIILS 850
KLVELWGGKD GPVGFADFVY KHIVPACFLA PLKQTFDLAD AQTVLALSEC 900
AVTLKTIHLK RGPECVQYLQ QEYLPSLQVA PEIIQEFCQA LQQPDAKVFK 950
NYLKVFFQRA KP 962
Length:962
Mass (Da):109,964
Last modified:May 30, 2006 - v2
Checksum:i2F407EEDEC7C2996
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti526 – 5261A → V.1 Publication
Corresponds to variant rs17851795 [ dbSNP | Ensembl ].
VAR_026528
Natural varianti716 – 7161E → D.
Corresponds to variant rs1051396 [ dbSNP | Ensembl ].
VAR_048962

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti360 – 3601Q → R in AAC39793. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS31852.1.
RefSeqiNP_009166.2. NM_007235.4.
UniGeneiHs.85951.

Genome annotation databases

EnsembliENST00000332707; ENSP00000327821; ENSG00000184575.
GeneIDi11260.
KEGGihsa:11260.
UCSCiuc001ssb.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS31852.1.
RefSeqi NP_009166.2. NM_007235.4.
UniGenei Hs.85951.

3D structure databases

ProteinModelPortali O43592.
SMRi O43592. Positions 8-961.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116420. 25 interactions.
IntActi O43592. 9 interactions.
MINTi MINT-1138512.
STRINGi 9606.ENSP00000327821.

PTM databases

PhosphoSitei O43592.

Proteomic databases

MaxQBi O43592.
PaxDbi O43592.
PRIDEi O43592.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000332707 ; ENSP00000327821 ; ENSG00000184575 .
GeneIDi 11260.
KEGGi hsa:11260.
UCSCi uc001ssb.3. human.

Organism-specific databases

CTDi 11260.
GeneCardsi GC12P064798.
HGNCi HGNC:12826. XPOT.
HPAi HPA038660.
HPA048067.
MIMi 603180. gene.
neXtProti NX_O43592.
PharmGKBi PA37419.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG270401.
HOGENOMi HOG000007104.
HOVERGENi HBG094163.
InParanoidi O43592.
KOi K14288.
OMAi KMRYDET.
OrthoDBi EOG7SN8BQ.
PhylomeDBi O43592.
TreeFami TF314001.

Miscellaneous databases

ChiTaRSi XPOT. human.
GeneWikii XPOT.
GenomeRNAii 11260.
NextBioi 42852.
PROi O43592.
SOURCEi Search...

Gene expression databases

ArrayExpressi O43592.
Bgeei O43592.
CleanExi HS_XPOT.
Genevestigatori O43592.

Family and domain databases

Gene3Di 1.25.10.10. 2 hits.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR013598. Exportin-1/Importin-b-like.
IPR001494. Importin-beta_N.
[Graphical view ]
Pfami PF08389. Xpo1. 1 hit.
[Graphical view ]
SMARTi SM00913. IBN_N. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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.
    , 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. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiXPOT_HUMAN
AccessioniPrimary (citable) accession number: O43592
Secondary accession number(s): A6NLH1
, O43784, Q8WUG2, Q9BVS7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 2, 2001
Last sequence update: May 30, 2006
Last modified: September 3, 2014
This is version 118 of the entry and version 2 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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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