O43592 (XPOT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Exportin-T

Alternative name(s):
Exportin(tRNA)
tRNA exportin

Gene names

Name:

XPOT

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	962 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
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 process	Transport
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Ligand	RNA-binding tRNA-binding
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	intracellular protein transport Inferred from electronic annotation. Source: InterPro tRNA export from nucleus Inferred from direct assay Ref.1. Source: UniProtKB
Cellular component	cytoplasm Inferred from direct assay Ref.1. Source: UniProtKB nucleoplasm Inferred from direct assay Ref.1. Source: UniProtKB
Molecular function	protein transporter activity Inferred from electronic annotation. Source: InterPro tRNA binding Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 962	962	Exportin-T		PRO_0000204716
Regions
	Region	1 – 385	385	Necessary for interaction with Ran, nuclear localization and nuclear import
	Region	443 – 962	520	Necessary for tRNA-binding, cytoplasmic localization and nuclear export
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine Ref.8
	Modified residue	634	1	N6-acetyllysine Ref.9
Natural variations
	Natural variant	526	1	A → V. Ref.4 Corresponds to variant rs17851795 [ dbSNP | Ensembl ].		VAR_026528
	Natural variant	716	1	E → D. Corresponds to variant rs1051396 [ dbSNP | Ensembl ].		VAR_048962
Experimental info
	Mutagenesis	405 – 409	5	RKQLK → AAQLA: Abolishes binding to tRNA. Does not abolish shuttling behavior.
	Mutagenesis	539 – 543	5	KVRSR → AVRSA: Does not abolish binding to tRNA. Does not abolish shuttling behavior.
	Mutagenesis	547 – 551	5	LFSRF → AFSRA: Does not abolish binding to tRNA. Does not abolish shuttling behavior.
	Mutagenesis	548 – 552	5	FSRFV → ASRFA: Does not abolish binding to tRNA. Does not abolish shuttling behavior. Ref.7
	Mutagenesis	550 – 557	8	RFVKSLNK → AFVASLNA: Abolishes binding to tRNA. Does not abolish shuttling behavior. Ref.7
	Sequence conflict	360	1	Q → R in AAC39793. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O43592 [UniParc]. Last modified May 30, 2006. Version 2. Checksum: 2F407EEDEC7C2996	FASTA	962	109,964
	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

References

	« Hide 'large scale' referencesShow '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: 9660920] [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: 9512417] [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: 16541075] [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: 15489334] [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, 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: 9857198] [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: 12138183] [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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[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., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-634, MASS SPECTROMETRY.
[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: 21269460] [Abstract] Cited for: 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.
IPI	IPI00306290.
RefSeq	NP_009166.2. NM_007235.4.
UniGene	Hs.85951.
3D structure databases
ProteinModelPortal	O43592.
SMR	O43592. Positions 2-962.
ModBase	Search...
Protein-protein interaction databases
IntAct	O43592. 7 interactions.
MINT	MINT-1138512.
STRING	O43592.
PTM databases
PhosphoSite	O43592.
Proteomic databases
PRIDE	O43592.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000332707; ENSP00000327821; ENSG00000184575.
GeneID	11260.
KEGG	hsa:11260.
UCSC	uc001ssb.1. human.
Organism-specific databases
CTD	11260.
GeneCards	GC12P064798.
H-InvDB	HIX0021887.
HGNC	HGNC:12826. XPOT.
MIM	603180. gene.
neXtProt	NX_O43592.
PharmGKB	PA37419.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG16010.
GeneTree	ENSGT00390000007890.
HOGENOM	HBG716487.
HOVERGEN	HBG094163.
InParanoid	O43592.
OMA	KDCEAKD.
OrthoDB	EOG42JNQQ.
PhylomeDB	O43592.
Gene expression databases
ArrayExpress	O43592.
Bgee	O43592.
CleanEx	HS_XPOT.
Genevestigator	O43592.
GermOnline	ENSG00000184575. Homo sapiens.
Family and domain databases
InterPro	IPR011989. ARM-like. IPR016024. ARM-type_fold. IPR013598. Exportin-1/Importin-b-like. IPR001494. Importin-beta_N. [Graphical view]
Gene3D	G3DSA:1.25.10.10. ARM-like. 2 hits.
KO	K14288.
Pfam	PF03810. IBN_N. 1 hit. PF08389. Xpo1. 1 hit. [Graphical view]
SMART	SM00913. IBN_N. 1 hit. [Graphical view]
SUPFAM	SSF48371. ARM-type_fold. 1 hit.
ProtoNet	Search...
Other
NextBio	42852.
SOURCE	Search...

Entry information

Entry name

XPOT_HUMAN

Accession

Primary (citable) accession number: O43592
Secondary accession number(s): A6NLH1 , O43784, Q8WUG2, Q9BVS7

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 2, 2001
Last sequence update:	May 30, 2006
Last modified:	January 25, 2012
This is version 94 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.