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Q9HAV4

- XPO5_HUMAN

UniProt

Q9HAV4 - XPO5_HUMAN

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Protein

Exportin-5

Gene

XPO5

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

Functioni

Mediates the nuclear export of proteins bearing a double-stranded RNA binding domain (dsRBD) and double-stranded RNAs (cargos). XPO5 in the nucleus binds cooperatively to the RNA and to the GTPase Ran in its active GTP-bound form. Proteins containing dsRBDs can associate with this trimeric complex through the RNA. 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, hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause disassembly of the complex and release of the cargo from the export receptor. XPO5 then returns to the nuclear compartment by diffusion through the nuclear pore complex, to 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. Overexpression may in some circumstances enhance RNA-mediated gene silencing (RNAi). Mediates nuclear export of isoform 5 of ADAR/ADAR1 in a RanGTP-dependent manner.
Mediates the nuclear export of micro-RNA precursors, which form short hairpins. Also mediates the nuclear export of synthetic short hairpin RNAs used for RNA interference, and adenovirus VA1 dsRNA. In some circumstances can also mediate the nuclear export of deacylated and aminoacylated tRNAs. Specifically recognizes dsRNAs that lack a 5'-overhang in a sequence-independent manner, have only a short 3'-overhang, and that have a double-stranded length of at least 15 base-pairs. Binding is dependent on Ran-GTP.

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. protein transporter activity Source: Ensembl
  3. RNA binding Source: Reactome
  4. tRNA binding Source: UniProtKB-KW

GO - Biological processi

  1. gene expression Source: Reactome
  2. gene silencing by RNA Source: UniProtKB-KW
  3. protein export from nucleus Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Protein transport, RNA-mediated gene silencing, Transport

Keywords - Ligandi

RNA-binding, tRNA-binding

Enzyme and pathway databases

ReactomeiREACT_12417. MicroRNA (miRNA) biogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Exportin-5
Short name:
Exp5
Alternative name(s):
Ran-binding protein 21
Gene namesi
Name:XPO5
Synonyms:KIAA1291, RANBP21
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:17675. XPO5.

Subcellular locationi

Nucleus 1 Publication. Cytoplasm 1 Publication
Note: Shuttles between the nucleus and the cytoplasm.

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. nucleoplasm Source: Reactome
  4. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134979214.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 12041203Exportin-5PRO_0000235299Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei396 – 3961N6-acetyllysine1 Publication
Modified residuei826 – 8261Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9HAV4.
PaxDbiQ9HAV4.
PRIDEiQ9HAV4.

PTM databases

PhosphoSiteiQ9HAV4.

Miscellaneous databases

PMAP-CutDBQ9HAV4.

Expressioni

Tissue specificityi

Expressed in heart, brain, placenta, lung, skeletal muscle, kidney and pancreas.1 Publication

Gene expression databases

BgeeiQ9HAV4.
ExpressionAtlasiQ9HAV4. baseline and differential.
GenevestigatoriQ9HAV4.

Organism-specific databases

HPAiCAB012357.
HPA018402.
HPA023959.
HPA029909.
HPA029910.

Interactioni

Subunit structurei

Component of a nuclear export receptor complex composed of XPO5, Ran, dsRNA-binding proteins and dsRNA. Found in a nuclear export complex with XPO5, Ran, EEF1A1, and aminoacylated tRNA. Found in a nuclear export complex with XPO5, Ran, ILF3 and dsRNA. Found in a nuclear export complex with XPO5, Ran and pre-miRNA. Found in a nuclear export complex with XPO5, Ran, ILF3 and minihelix VA1 dsRNA. Found in a nuclear export complex with XPO5, RAN, ILF3, ZNF346 and dsRNA. Interacts with EEF1A1, ILF3, NUP153, NUP214 and ZNF346. Interacts with Ran and cargo proteins in a GTP-dependent manner. Interacts with isoform 5 of ADAR/ADAR1 (via DRBM domains).8 Publications

Protein-protein interaction databases

BioGridi121574. 57 interactions.
DIPiDIP-34547N.
IntActiQ9HAV4. 15 interactions.
MINTiMINT-264827.

Structurei

Secondary structure

1
1204
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 2116
Helixi27 – 4317
Helixi47 – 548
Helixi61 – 7717
Helixi79 – 813
Helixi84 – 10017
Helixi110 – 12718
Turni129 – 1313
Helixi135 – 14410
Helixi147 – 16519
Helixi172 – 18413
Helixi186 – 20722
Helixi214 – 23219
Turni233 – 2375
Helixi240 – 2445
Turni245 – 2473
Helixi249 – 2568
Helixi257 – 2593
Turni261 – 2633
Helixi264 – 27512
Helixi281 – 2844
Helixi285 – 2917
Helixi293 – 30412
Helixi313 – 33826
Helixi349 – 36012
Helixi365 – 37915
Turni382 – 3865
Helixi388 – 40518
Helixi418 – 4258
Helixi429 – 45325
Helixi455 – 47016
Beta strandi495 – 4973
Helixi498 – 52023
Helixi528 – 54013
Helixi546 – 55914
Helixi560 – 5645
Helixi567 – 5693
Helixi570 – 58213
Helixi595 – 61420
Helixi616 – 6194
Helixi620 – 6223
Helixi623 – 63513
Helixi642 – 65615
Helixi657 – 6593
Helixi662 – 68019
Helixi683 – 6908
Helixi692 – 6998
Helixi713 – 73422
Helixi741 – 7466
Beta strandi750 – 7534
Beta strandi759 – 7613
Helixi766 – 7705
Helixi773 – 78513
Helixi789 – 7924
Helixi797 – 7993
Turni800 – 8034
Helixi807 – 8137
Helixi832 – 85827
Turni860 – 8645
Helixi868 – 8758
Turni880 – 8823
Helixi885 – 89410
Helixi896 – 9016
Helixi905 – 9073
Turni908 – 9114
Helixi912 – 93524
Helixi953 – 97725
Helixi1013 – 10197
Helixi1022 – 103514
Helixi1041 – 105010
Helixi1052 – 10565
Helixi1066 – 108217
Helixi1087 – 110317
Turni1105 – 11073
Helixi1111 – 11155
Beta strandi1118 – 11203
Helixi1123 – 113210

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3A6PX-ray2.92A/F1-1204[»]
ProteinModelPortaliQ9HAV4.
SMRiQ9HAV4. Positions 58-243.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9HAV4.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 108107Necessary for interaction with RanAdd
BLAST
Regioni533 – 640108Necessary for interaction with ILF3Add
BLAST

Sequence similaritiesi

Belongs to the exportin family.Curated

Phylogenomic databases

eggNOGiNOG296759.
GeneTreeiENSGT00390000013979.
HOVERGENiHBG056281.
InParanoidiQ9HAV4.
KOiK14289.
OMAiFADSVGH.
OrthoDBiEOG7MWGW1.
PhylomeDBiQ9HAV4.
TreeFamiTF323382.

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. 4 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9HAV4-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAMDQVNALC EQLVKAVTVM MDPNSTQRYR LEALKFCEEF KEKCPICVPC
60 70 80 90 100
GLRLAEKTQV AIVRHFGLQI LEHVVKFRWN GMSRLEKVYL KNSVMELIAN
110 120 130 140 150
GTLNILEEEN HIKDALSRIV VEMIKREWPQ HWPDMLIELD TLSKQGETQT
160 170 180 190 200
ELVMFILLRL AEDVVTFQTL PPQRRRDIQQ TLTQNMERIF SFLLNTLQEN
210 220 230 240 250
VNKYQQVKTD TSQESKAQAN CRVGVAALNT LAGYIDWVSM SHITAENCKL
260 270 280 290 300
LEILCLLLNE QELQLGAAEC LLIAVSRKGK LEDRKPLMVL FGDVAMHYIL
310 320 330 340 350
SAAQTADGGG LVEKHYVFLK RLCQVLCALG NQLCALLGAD SDVETPSNFG
360 370 380 390 400
KYLESFLAFT THPSQFLRSS TQMTWGALFR HEILSRDPLL LAIIPKYLRA
410 420 430 440 450
SMTNLVKMGF PSKTDSPSCE YSRFDFDSDE DFNAFFNSSR AQQGEVMRLA
460 470 480 490 500
CRLDPKTSFQ MAGEWLKYQL STFLDAGSVN SCSAVGTGEG SLCSVFSPSF
510 520 530 540 550
VQWEAMTLFL ESVITQMFRT LNREEIPVND GIELLQMVLN FDTKDPLILS
560 570 580 590 600
CVLTNVSALF PFVTYRPEFL PQVFSKLFSS VTFETVEESK APRTRAVRNV
610 620 630 640 650
RRHACSSIIK MCRDYPQLVL PNFDMLYNHV KQLLSNELLL TQMEKCALME
660 670 680 690 700
ALVLISNQFK NYERQKVFLE ELMAPVASIW LSQDMHRVLS DVDAFIAYVG
710 720 730 740 750
TDQKSCDPGL EDPCGLNRAR MSFCVYSILG VVKRTCWPTD LEEAKAGGFV
760 770 780 790 800
VGYTSSGNPI FRNPCTEQIL KLLDNLLALI RTHNTLYAPE MLAKMAEPFT
810 820 830 840 850
KALDMLDAEK SAILGLPQPL LELNDSPVFK TVLERMQRFF STLYENCFHI
860 870 880 890 900
LGKAGPSMQQ DFYTVEDLAT QLLSSAFVNL NNIPDYRLRP MLRVFVKPLV
910 920 930 940 950
LFCPPEHYEA LVSPILGPLF TYLHMRLSQK WQVINQRSLL CGEDEAADEN
960 970 980 990 1000
PESQEMLEEQ LVRMLTREVM DLITVCCVSK KGADHSSAPP ADGDDEEMMA
1010 1020 1030 1040 1050
TEVTPSAMAE LTDLGKCLMK HEDVCTALLI TAFNSLAWKD TLSCQRTTSQ
1060 1070 1080 1090 1100
LCWPLLKQVL SGTLLADAVT WLFTSVLKGL QMHGQHDGCM ASLVHLAFQI
1110 1120 1130 1140 1150
YEALRPRYLE IRAVMEQIPE IQKDSLDQFD CKLLNPSLQK VADKRRKDQF
1160 1170 1180 1190 1200
KRLIAGCIGK PLGEQFRKEV HIKNLPSLFK KTKPMLETEV LDNDGGGLAT

IFEP
Length:1,204
Mass (Da):136,311
Last modified:March 1, 2001 - v1
Checksum:i3295A17DF7C37602
GO

Sequence cautioni

The sequence BAA91547.1 differs from that shown. Reason: Frameshift at position 920.
The sequence AAH00129.1 differs from that shown. Reason: Erroneous initiation.
The sequence BAA86605.2 differs from that shown. Reason: Erroneous initiation.
The sequence CAI42640.1 differs from that shown. Reason: Erroneous gene model prediction.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti81 – 811G → S in AAG53603. (PubMed:12426392)Curated
Sequence conflicti697 – 6971A → V in BAA86605. (PubMed:10574462)Curated
Sequence conflicti988 – 9881A → T in BAB14200. (PubMed:14574404)Curated
Sequence conflicti1151 – 11511K → E in BAA91547. (PubMed:14574404)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti241 – 2411S → N.
Corresponds to variant rs34324334 [ dbSNP | Ensembl ].
VAR_048960
Natural varianti610 – 6101K → N.
Corresponds to variant rs12173786 [ dbSNP | Ensembl ].
VAR_028032

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF271159 mRNA. Translation: AAG53603.1.
AF298880 mRNA. Translation: AAG17907.1.
AB033117 mRNA. Translation: BAA86605.2. Different initiation.
AL355802 Genomic DNA. Translation: CAI42640.1. Sequence problems.
BC000129 mRNA. Translation: AAH00129.1. Different initiation.
BC008347 mRNA. Translation: AAH08347.1.
BC009969 mRNA. Translation: AAH09969.2.
BC062635 mRNA. Translation: AAH62635.1.
AL137467 mRNA. Translation: CAB70753.1.
AK001195 mRNA. Translation: BAA91547.1. Frameshift.
AK022718 mRNA. Translation: BAB14200.1.
CCDSiCCDS47430.1.
PIRiT46411.
RefSeqiNP_065801.1. NM_020750.2.
UniGeneiHs.203206.

Genome annotation databases

EnsembliENST00000265351; ENSP00000265351; ENSG00000124571.
GeneIDi57510.
KEGGihsa:57510.
UCSCiuc003ovp.3. human.

Polymorphism databases

DMDMi74734245.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF271159 mRNA. Translation: AAG53603.1 .
AF298880 mRNA. Translation: AAG17907.1 .
AB033117 mRNA. Translation: BAA86605.2 . Different initiation.
AL355802 Genomic DNA. Translation: CAI42640.1 . Sequence problems.
BC000129 mRNA. Translation: AAH00129.1 . Different initiation.
BC008347 mRNA. Translation: AAH08347.1 .
BC009969 mRNA. Translation: AAH09969.2 .
BC062635 mRNA. Translation: AAH62635.1 .
AL137467 mRNA. Translation: CAB70753.1 .
AK001195 mRNA. Translation: BAA91547.1 . Frameshift.
AK022718 mRNA. Translation: BAB14200.1 .
CCDSi CCDS47430.1.
PIRi T46411.
RefSeqi NP_065801.1. NM_020750.2.
UniGenei Hs.203206.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3A6P X-ray 2.92 A/F 1-1204 [» ]
ProteinModelPortali Q9HAV4.
SMRi Q9HAV4. Positions 58-243.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121574. 57 interactions.
DIPi DIP-34547N.
IntActi Q9HAV4. 15 interactions.
MINTi MINT-264827.

PTM databases

PhosphoSitei Q9HAV4.

Polymorphism databases

DMDMi 74734245.

Proteomic databases

MaxQBi Q9HAV4.
PaxDbi Q9HAV4.
PRIDEi Q9HAV4.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000265351 ; ENSP00000265351 ; ENSG00000124571 .
GeneIDi 57510.
KEGGi hsa:57510.
UCSCi uc003ovp.3. human.

Organism-specific databases

CTDi 57510.
GeneCardsi GC06M043490.
H-InvDB HIX0005908.
HGNCi HGNC:17675. XPO5.
HPAi CAB012357.
HPA018402.
HPA023959.
HPA029909.
HPA029910.
MIMi 607845. gene.
neXtProti NX_Q9HAV4.
PharmGKBi PA134979214.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG296759.
GeneTreei ENSGT00390000013979.
HOVERGENi HBG056281.
InParanoidi Q9HAV4.
KOi K14289.
OMAi FADSVGH.
OrthoDBi EOG7MWGW1.
PhylomeDBi Q9HAV4.
TreeFami TF323382.

Enzyme and pathway databases

Reactomei REACT_12417. MicroRNA (miRNA) biogenesis.

Miscellaneous databases

ChiTaRSi XPO5. human.
EvolutionaryTracei Q9HAV4.
GeneWikii XPO5.
GenomeRNAii 57510.
NextBioi 63866.
PMAP-CutDB Q9HAV4.
PROi Q9HAV4.
SOURCEi Search...

Gene expression databases

Bgeei Q9HAV4.
ExpressionAtlasi Q9HAV4. baseline and differential.
Genevestigatori Q9HAV4.

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. 4 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Exp5 exports eEF1A via tRNA from nuclei and synergizes with other transport pathways to confine translation to the cytoplasm."
    Bohnsack M.T., Regener K., Schwappach B., Saffrich R., Paraskeva E., Hartmann E., Goerlich D.
    EMBO J. 21:6205-6215(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN PROTEIN AND TRNA NUCLEAR EXPORT, IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH EEF1A1; RAN AND TRNA, INTERACTION WITH EEF1A1, RNA-BINDING.
  2. "Exportin-5, a novel karyopherin, mediates nuclear export of double-stranded RNA binding proteins."
    Brownawell A.M., Macara I.G.
    J. Cell Biol. 156:53-64(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN PROTEIN NUCLEAR EXPORT, IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH ILF3; RAN AND DOUBLE-STRANDED RNA, INTERACTION WITH ILF3; NUP153 AND NUP214, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Brain.
  3. "Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.
    DNA Res. 6:337-345(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  5. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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].
    Tissue: Ascites, Placenta, Retinoblastoma and Rhabdomyosarcoma.
  7. Bienvenut W.V.
    Submitted (JUN-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 189-203 AND 387-396, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma.
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 450-1204.
    Tissue: Testis.
  9. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 537-1204.
    Tissue: Teratocarcinoma.
  10. "Exportin-5-mediated nuclear export of eukaryotic elongation factor 1A and tRNA."
    Calado A., Treichel N., Mueller E.-C., Otto A., Kutay U.
    EMBO J. 21:6216-6224(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PROTEIN AND TRNA NUCLEAR EXPORT, IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH EEF1A1; RAN AND TRNA, INTERACTION WITH EEF1A1, IDENTIFICATION BY MASS SPECTROMETRY, RNA-BINDING.
  11. "Exportin-5 mediates the nuclear export of pre-microRNAs and short hairpin RNAs."
    Yi R., Qin Y., Macara I.G., Cullen B.R.
    Genes Dev. 17:3011-3016(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PRE-MIRNA EXPORT, RNA-BINDING.
  12. Cited for: FUNCTION IN ADENOVIRUS VA1 RNA EXPORT, RNA-BINDING.
  13. "Minihelix-containing RNAs mediate exportin-5-dependent nuclear export of the double-stranded RNA-binding protein ILF3."
    Gwizdek C., Ossareh-Nazari B., Brownawell A.M., Evers S., Macara I.G., Dargemont C.
    J. Biol. Chem. 279:884-891(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PROTEIN AND ADENOVIRUS VA1 RNA EXPORT, IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH ILF3; RAN AND VA1 RNA, RNA-BINDING.
  14. "Nucleocytoplasmic shuttling of JAZ, a new cargo protein for exportin-5."
    Chen T., Brownawell A.M., Macara I.G.
    Mol. Cell. Biol. 24:6608-6619(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PROTEIN AND DOUBLE-STRANDED RNA EXPORT, IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH RAN; ILF3; ZNF346 AND DOUBLE-STRANDED RNA, INTERACTION WITH ILF3 AND ZNF346.
  15. "Exportin 5 is a RanGTP-dependent dsRNA-binding protein that mediates nuclear export of pre-miRNAs."
    Bohnsack M.T., Czaplinski K., Goerlich D.
    RNA 10:185-191(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PRE-MIRNA EXPORT, IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH RAN AND PRE-MIRNA, RNA-BINDING.
  16. Cited for: FUNCTION IN PRE-MIRNA EXPORT, IDENTIFICATION IN A NUCLEAR EXPORT RECEPTOR COMPLEX WITH RAN AND PRE-MIRNA, RNA-BINDING.
  17. "Overexpression of exportin 5 enhances RNA interference mediated by short hairpin RNAs and microRNAs."
    Yi R., Doehle B.P., Qin Y., Macara I.G., Cullen B.R.
    RNA 11:220-226(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PRE-MIRNA EXPORT.
  18. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-826, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. "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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  20. "RNA-regulated interaction of transportin-1 and exportin-5 with the double-stranded RNA-binding domain regulates nucleocytoplasmic shuttling of ADAR1."
    Fritz J., Strehblow A., Taschner A., Schopoff S., Pasierbek P., Jantsch M.F.
    Mol. Cell. Biol. 29:1487-1497(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ADAR.
  21. "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-396, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiXPO5_HUMAN
AccessioniPrimary (citable) accession number: Q9HAV4
Secondary accession number(s): Q5JTE6
, Q96G48, Q96HN3, Q9BWM6, Q9BZV5, Q9H9M4, Q9NT89, Q9NW39, Q9ULC9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: March 1, 2001
Last modified: October 29, 2014
This is version 108 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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3