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Exportin-5 (Exp5) (Ran-binding protein 21)

 XPO5_HUMAN              Reviewed;        1204 AA.
Q9HAV4; Q5JTE6; Q96G48; Q96HN3; Q9BWM6; Q9BZV5; Q9H9M4; Q9NT89;
Q9NW39; Q9ULC9;
16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
25-OCT-2017, entry version 140.
RecName: Full=Exportin-5;
Short=Exp5;
AltName: Full=Ran-binding protein 21;
Name=XPO5; Synonyms=KIAA1291, RANBP21;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
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, AND RNA-BINDING.
PubMed=12426392; DOI=10.1093/emboj/cdf613;
Bohnsack M.T., Regener K., Schwappach B., Saffrich R., Paraskeva E.,
Hartmann E., Goerlich D.;
"Exp5 exports eEF1A via tRNA from nuclei and synergizes with other
transport pathways to confine translation to the cytoplasm.";
EMBO J. 21:6205-6215(2002).
[2]
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, AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=11777942; DOI=10.1083/jcb.200110082;
Brownawell A.M., Macara I.G.;
"Exportin-5, a novel karyopherin, mediates nuclear export of double-
stranded RNA binding proteins.";
J. Cell Biol. 156:53-64(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=10574462; DOI=10.1093/dnares/6.5.337;
Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
"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.";
DNA Res. 6:337-345(1999).
[4]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
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.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Ascites, Placenta, Retinoblastoma, and Rhabdomyosarcoma;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 189-203 AND 387-396, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (JUN-2005) to UniProtKB.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 450-1204.
TISSUE=Testis;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 537-1204.
TISSUE=Teratocarcinoma;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[10]
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, AND RNA-BINDING.
PubMed=12426393; DOI=10.1093/emboj/cdf620;
Calado A., Treichel N., Mueller E.-C., Otto A., Kutay U.;
"Exportin-5-mediated nuclear export of eukaryotic elongation factor 1A
and tRNA.";
EMBO J. 21:6216-6224(2002).
[11]
FUNCTION IN PRE-MIRNA EXPORT, AND RNA-BINDING.
PubMed=14681208; DOI=10.1101/gad.1158803;
Yi R., Qin Y., Macara I.G., Cullen B.R.;
"Exportin-5 mediates the nuclear export of pre-microRNAs and short
hairpin RNAs.";
Genes Dev. 17:3011-3016(2003).
[12]
FUNCTION IN ADENOVIRUS VA1 RNA EXPORT (MICROBIAL INFECTION), AND
RNA-BINDING (MICROBIAL INFECTION).
PubMed=12509441; DOI=10.1074/jbc.C200668200;
Gwizdek C., Ossareh-Nazari B., Brownawell A.M., Doglio A.,
Bertrand E., Macara I.G., Dargemont C.;
"Exportin-5 mediates nuclear export of minihelix-containing RNAs.";
J. Biol. Chem. 278:5505-5508(2003).
[13]
FUNCTION IN PROTEIN AND ADENOVIRUS VA1 RNA EXPORT, IDENTIFICATION IN A
NUCLEAR EXPORT RECEPTOR COMPLEX WITH ILF3; RAN AND VA1 RNA, AND
RNA-BINDING.
PubMed=14570900; DOI=10.1074/jbc.M306808200;
Gwizdek C., Ossareh-Nazari B., Brownawell A.M., Evers S., Macara I.G.,
Dargemont C.;
"Minihelix-containing RNAs mediate exportin-5-dependent nuclear export
of the double-stranded RNA-binding protein ILF3.";
J. Biol. Chem. 279:884-891(2004).
[14]
FUNCTION IN PROTEIN AND DOUBLE-STRANDED RNA EXPORT, IDENTIFICATION IN
A NUCLEAR EXPORT RECEPTOR COMPLEX WITH RAN; ILF3; ZNF346 AND
DOUBLE-STRANDED RNA, AND INTERACTION WITH ILF3 AND ZNF346.
PubMed=15254228; DOI=10.1128/MCB.24.15.6608-6619.2004;
Chen T., Brownawell A.M., Macara I.G.;
"Nucleocytoplasmic shuttling of JAZ, a new cargo protein for exportin-
5.";
Mol. Cell. Biol. 24:6608-6619(2004).
[15]
FUNCTION IN PRE-MIRNA EXPORT, IDENTIFICATION IN A NUCLEAR EXPORT
RECEPTOR COMPLEX WITH RAN AND PRE-MIRNA, AND RNA-BINDING.
PubMed=14730017; DOI=10.1261/rna.5167604;
Bohnsack M.T., Czaplinski K., Goerlich D.;
"Exportin 5 is a RanGTP-dependent dsRNA-binding protein that mediates
nuclear export of pre-miRNAs.";
RNA 10:185-191(2004).
[16]
FUNCTION IN PRE-MIRNA EXPORT, IDENTIFICATION IN A NUCLEAR EXPORT
RECEPTOR COMPLEX WITH RAN AND PRE-MIRNA, AND RNA-BINDING.
PubMed=14631048; DOI=10.1126/science.1090599;
Lund E., Guettinger S., Calado A., Dahlberg J.E., Kutay U.;
"Nuclear export of microRNA precursors.";
Science 303:95-98(2004).
[17]
FUNCTION IN PRE-MIRNA EXPORT.
PubMed=15613540; DOI=10.1261/rna.7233305;
Yi R., Doehle B.P., Qin Y., Macara I.G., Cullen B.R.;
"Overexpression of exportin 5 enhances RNA interference mediated by
short hairpin RNAs and microRNAs.";
RNA 11:220-226(2005).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-826, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[20]
FUNCTION, AND INTERACTION WITH ADAR.
PubMed=19124606; DOI=10.1128/MCB.01519-08;
Fritz J., Strehblow A., Taschner A., Schopoff S., Pasierbek P.,
Jantsch M.F.;
"RNA-regulated interaction of transportin-1 and exportin-5 with the
double-stranded RNA-binding domain regulates nucleocytoplasmic
shuttling of ADAR1.";
Mol. Cell. Biol. 29:1487-1497(2009).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-396, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[22]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[23]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[24]
X-RAY CRYSTALLOGRAPHY (2.92 ANGSTROMS) IN COMPLEX WITH DOG RAN;
PRE-MIRNA; GTP, AND INTERACTION WITH DOG RAN.
PubMed=19965479; DOI=10.1126/science.1178705;
Okada C., Yamashita E., Lee S.J., Shibata S., Katahira J.,
Nakagawa A., Yoneda Y., Tsukihara T.;
"A high-resolution structure of the pre-microRNA nuclear export
machinery.";
Science 326:1275-1279(2009).
[25]
VARIANT ILE-552, AND INTERACTION WITH SMAD4.
PubMed=26878725; DOI=10.1038/ng.3512;
Braun D.A., Sadowski C.E., Kohl S., Lovric S., Astrinidis S.A.,
Pabst W.L., Gee H.Y., Ashraf S., Lawson J.A., Shril S., Airik M.,
Tan W., Schapiro D., Rao J., Choi W.I., Hermle T., Kemper M.J.,
Pohl M., Ozaltin F., Konrad M., Bogdanovic R., Buescher R.,
Helmchen U., Serdaroglu E., Lifton R.P., Antonin W., Hildebrandt F.;
"Mutations in nuclear pore genes NUP93, NUP205 and XPO5 cause steroid-
resistant nephrotic syndrome.";
Nat. Genet. 48:457-465(2016).
-!- FUNCTION: 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.
-!- FUNCTION: Mediates the nuclear export of micro-RNA precursors,
which form short hairpins (PubMed:14681208, PubMed:14631048,
PubMed:15613540). Also mediates the nuclear export of synthetic
short hairpin RNAs used for RNA interference. 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 (PubMed:19965479). Binding is dependent on Ran-GTP
(PubMed:19965479). {ECO:0000269|PubMed:14631048,
ECO:0000269|PubMed:14681208, ECO:0000269|PubMed:15613540,
ECO:0000269|PubMed:19965479}.
-!- FUNCTION: (Microbial infection) Mediates the nuclear export of
adenovirus VA1 dsRNA. {ECO:0000269|PubMed:12509441}.
-!- SUBUNIT: 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
(PubMed:19965479). 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). Interacts with SMAD4; mediates
nuclear export of SMAD4 (PubMed:26878725). Interacts with RAN
(GTP-bound form) (PubMed:19965479). {ECO:0000269|PubMed:11777942,
ECO:0000269|PubMed:12426392, ECO:0000269|PubMed:12426393,
ECO:0000269|PubMed:14570900, ECO:0000269|PubMed:14631048,
ECO:0000269|PubMed:14730017, ECO:0000269|PubMed:15254228,
ECO:0000269|PubMed:19124606, ECO:0000269|PubMed:19965479,
ECO:0000269|PubMed:26878725}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11777942}.
Cytoplasm {ECO:0000269|PubMed:11777942}. Note=Shuttles between the
nucleus and the cytoplasm.
-!- TISSUE SPECIFICITY: Expressed in heart, brain, placenta, lung,
skeletal muscle, kidney and pancreas.
{ECO:0000269|PubMed:11777942}.
-!- SIMILARITY: Belongs to the exportin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH00129.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAA86605.2; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAA91547.1; Type=Frameshift; Positions=920; Evidence={ECO:0000305};
Sequence=CAI42640.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AF271159; AAG53603.1; -; mRNA.
EMBL; AF298880; AAG17907.1; -; mRNA.
EMBL; AB033117; BAA86605.2; ALT_INIT; mRNA.
EMBL; AL355802; CAI42640.1; ALT_SEQ; Genomic_DNA.
EMBL; BC000129; AAH00129.1; ALT_INIT; mRNA.
EMBL; BC008347; AAH08347.1; -; mRNA.
EMBL; BC009969; AAH09969.2; -; mRNA.
EMBL; BC062635; AAH62635.1; -; mRNA.
EMBL; AL137467; CAB70753.1; -; mRNA.
EMBL; AK001195; BAA91547.1; ALT_FRAME; mRNA.
EMBL; AK022718; BAB14200.1; -; mRNA.
CCDS; CCDS47430.1; -.
PIR; T46411; T46411.
RefSeq; NP_065801.1; NM_020750.2.
UniGene; Hs.203206; -.
PDB; 3A6P; X-ray; 2.92 A; A/F=1-1204.
PDBsum; 3A6P; -.
ProteinModelPortal; Q9HAV4; -.
SMR; Q9HAV4; -.
BioGrid; 121574; 79.
CORUM; Q9HAV4; -.
DIP; DIP-34547N; -.
IntAct; Q9HAV4; 25.
MINT; MINT-264827; -.
STRING; 9606.ENSP00000265351; -.
TCDB; 1.I.1.1.3; the eukaryotic nuclear pore complex (e-npc) family.
iPTMnet; Q9HAV4; -.
PhosphoSitePlus; Q9HAV4; -.
BioMuta; XPO5; -.
DMDM; 74734245; -.
EPD; Q9HAV4; -.
MaxQB; Q9HAV4; -.
PaxDb; Q9HAV4; -.
PeptideAtlas; Q9HAV4; -.
PRIDE; Q9HAV4; -.
Ensembl; ENST00000265351; ENSP00000265351; ENSG00000124571.
GeneID; 57510; -.
KEGG; hsa:57510; -.
UCSC; uc003ovp.3; human.
CTD; 57510; -.
DisGeNET; 57510; -.
EuPathDB; HostDB:ENSG00000124571.17; -.
GeneCards; XPO5; -.
H-InvDB; HIX0005908; -.
HGNC; HGNC:17675; XPO5.
HPA; CAB012357; -.
HPA; HPA018402; -.
HPA; HPA023959; -.
HPA; HPA029909; -.
HPA; HPA029910; -.
MalaCards; XPO5; -.
MIM; 607845; gene.
neXtProt; NX_Q9HAV4; -.
OpenTargets; ENSG00000124571; -.
PharmGKB; PA134979214; -.
eggNOG; KOG2020; Eukaryota.
eggNOG; COG5101; LUCA.
GeneTree; ENSGT00390000013979; -.
HOVERGEN; HBG056281; -.
InParanoid; Q9HAV4; -.
KO; K14289; -.
OMA; PERHAFL; -.
OrthoDB; EOG091G0154; -.
PhylomeDB; Q9HAV4; -.
TreeFam; TF323382; -.
Reactome; R-HSA-203927; MicroRNA (miRNA) biogenesis.
ChiTaRS; XPO5; human.
EvolutionaryTrace; Q9HAV4; -.
GeneWiki; XPO5; -.
GenomeRNAi; 57510; -.
PMAP-CutDB; Q9HAV4; -.
PRO; PR:Q9HAV4; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000124571; -.
ExpressionAtlas; Q9HAV4; baseline and differential.
Genevisible; Q9HAV4; HS.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0035068; C:micro-ribonucleoprotein complex; IDA:UniProtKB.
GO; GO:0042272; C:nuclear RNA export factor complex; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0042565; C:RNA nuclear export complex; IDA:BHF-UCL.
GO; GO:0003729; F:mRNA binding; IDA:BHF-UCL.
GO; GO:0005049; F:nuclear export signal receptor activity; IBA:GO_Central.
GO; GO:0070883; F:pre-miRNA binding; IDA:BHF-UCL.
GO; GO:0090631; F:pre-miRNA transporter activity; IMP:BHF-UCL.
GO; GO:0008536; F:Ran GTPase binding; IDA:BHF-UCL.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
GO; GO:0010586; P:miRNA metabolic process; TAS:Reactome.
GO; GO:1900370; P:positive regulation of RNA interference; IDA:BHF-UCL.
GO; GO:0035281; P:pre-miRNA export from nucleus; IDA:BHF-UCL.
GO; GO:0006611; P:protein export from nucleus; IDA:UniProtKB.
GO; GO:0046825; P:regulation of protein export from nucleus; IBA:GO_Central.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR013598; Exportin-1/Importin-b-like.
InterPro; IPR001494; Importin-beta_N.
Pfam; PF08389; Xpo1; 1.
SMART; SM00913; IBN_N; 1.
SUPFAM; SSF48371; SSF48371; 4.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Nucleus; Phosphoprotein; Polymorphism;
Protein transport; Reference proteome; RNA-binding;
RNA-mediated gene silencing; Transport; tRNA-binding.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895}.
CHAIN 2 1204 Exportin-5.
/FTId=PRO_0000235299.
REGION 2 108 Necessary for interaction with Ran.
REGION 533 640 Necessary for interaction with ILF3.
REGION 641 642 Pre-miRNA binding.
{ECO:0000269|PubMed:19965479}.
SITE 441 441 Pre-miRNA binding.
{ECO:0000269|PubMed:19965479}.
SITE 448 448 Pre-miRNA binding.
{ECO:0000269|PubMed:19965479}.
SITE 718 718 Pre-miRNA binding.
{ECO:0000269|PubMed:19965479}.
SITE 1045 1045 Pre-miRNA binding.
{ECO:0000269|PubMed:19965479}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895}.
MOD_RES 396 396 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 826 826 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
VARIANT 241 241 S -> N (in dbSNP:rs34324334).
/FTId=VAR_048960.
VARIANT 552 552 V -> I (found in a patient with nephrotic
syndrome; unknown pathological
significance).
{ECO:0000269|PubMed:26878725}.
/FTId=VAR_076472.
VARIANT 610 610 K -> N (in dbSNP:rs12173786).
/FTId=VAR_028032.
CONFLICT 81 81 G -> S (in Ref. 1; AAG53603).
{ECO:0000305}.
CONFLICT 697 697 A -> V (in Ref. 3; BAA86605).
{ECO:0000305}.
CONFLICT 988 988 A -> T (in Ref. 5; BAB14200).
{ECO:0000305}.
CONFLICT 1151 1151 K -> E (in Ref. 5; BAA91547).
{ECO:0000305}.
HELIX 6 21 {ECO:0000244|PDB:3A6P}.
HELIX 27 43 {ECO:0000244|PDB:3A6P}.
HELIX 47 54 {ECO:0000244|PDB:3A6P}.
HELIX 61 77 {ECO:0000244|PDB:3A6P}.
HELIX 79 81 {ECO:0000244|PDB:3A6P}.
HELIX 84 100 {ECO:0000244|PDB:3A6P}.
HELIX 110 127 {ECO:0000244|PDB:3A6P}.
TURN 129 131 {ECO:0000244|PDB:3A6P}.
HELIX 135 144 {ECO:0000244|PDB:3A6P}.
HELIX 147 165 {ECO:0000244|PDB:3A6P}.
HELIX 172 184 {ECO:0000244|PDB:3A6P}.
HELIX 186 207 {ECO:0000244|PDB:3A6P}.
HELIX 214 232 {ECO:0000244|PDB:3A6P}.
TURN 233 237 {ECO:0000244|PDB:3A6P}.
HELIX 240 244 {ECO:0000244|PDB:3A6P}.
TURN 245 247 {ECO:0000244|PDB:3A6P}.
HELIX 249 256 {ECO:0000244|PDB:3A6P}.
HELIX 257 259 {ECO:0000244|PDB:3A6P}.
TURN 261 263 {ECO:0000244|PDB:3A6P}.
HELIX 264 275 {ECO:0000244|PDB:3A6P}.
HELIX 281 284 {ECO:0000244|PDB:3A6P}.
HELIX 285 291 {ECO:0000244|PDB:3A6P}.
HELIX 293 304 {ECO:0000244|PDB:3A6P}.
HELIX 313 338 {ECO:0000244|PDB:3A6P}.
HELIX 349 360 {ECO:0000244|PDB:3A6P}.
HELIX 365 379 {ECO:0000244|PDB:3A6P}.
TURN 382 386 {ECO:0000244|PDB:3A6P}.
HELIX 388 405 {ECO:0000244|PDB:3A6P}.
HELIX 418 425 {ECO:0000244|PDB:3A6P}.
HELIX 429 453 {ECO:0000244|PDB:3A6P}.
HELIX 455 470 {ECO:0000244|PDB:3A6P}.
STRAND 495 497 {ECO:0000244|PDB:3A6P}.
HELIX 498 520 {ECO:0000244|PDB:3A6P}.
HELIX 528 540 {ECO:0000244|PDB:3A6P}.
HELIX 546 559 {ECO:0000244|PDB:3A6P}.
HELIX 560 564 {ECO:0000244|PDB:3A6P}.
HELIX 567 569 {ECO:0000244|PDB:3A6P}.
HELIX 570 582 {ECO:0000244|PDB:3A6P}.
HELIX 595 614 {ECO:0000244|PDB:3A6P}.
HELIX 616 619 {ECO:0000244|PDB:3A6P}.
HELIX 620 622 {ECO:0000244|PDB:3A6P}.
HELIX 623 635 {ECO:0000244|PDB:3A6P}.
HELIX 642 656 {ECO:0000244|PDB:3A6P}.
HELIX 657 659 {ECO:0000244|PDB:3A6P}.
HELIX 662 680 {ECO:0000244|PDB:3A6P}.
HELIX 683 690 {ECO:0000244|PDB:3A6P}.
HELIX 692 699 {ECO:0000244|PDB:3A6P}.
HELIX 713 734 {ECO:0000244|PDB:3A6P}.
HELIX 741 746 {ECO:0000244|PDB:3A6P}.
STRAND 750 753 {ECO:0000244|PDB:3A6P}.
STRAND 759 761 {ECO:0000244|PDB:3A6P}.
HELIX 766 770 {ECO:0000244|PDB:3A6P}.
HELIX 773 785 {ECO:0000244|PDB:3A6P}.
HELIX 789 792 {ECO:0000244|PDB:3A6P}.
HELIX 797 799 {ECO:0000244|PDB:3A6P}.
TURN 800 803 {ECO:0000244|PDB:3A6P}.
HELIX 807 813 {ECO:0000244|PDB:3A6P}.
HELIX 832 858 {ECO:0000244|PDB:3A6P}.
TURN 860 864 {ECO:0000244|PDB:3A6P}.
HELIX 868 875 {ECO:0000244|PDB:3A6P}.
TURN 880 882 {ECO:0000244|PDB:3A6P}.
HELIX 885 894 {ECO:0000244|PDB:3A6P}.
HELIX 896 901 {ECO:0000244|PDB:3A6P}.
HELIX 905 907 {ECO:0000244|PDB:3A6P}.
TURN 908 911 {ECO:0000244|PDB:3A6P}.
HELIX 912 935 {ECO:0000244|PDB:3A6P}.
HELIX 953 977 {ECO:0000244|PDB:3A6P}.
HELIX 1013 1019 {ECO:0000244|PDB:3A6P}.
HELIX 1022 1035 {ECO:0000244|PDB:3A6P}.
HELIX 1041 1050 {ECO:0000244|PDB:3A6P}.
HELIX 1052 1056 {ECO:0000244|PDB:3A6P}.
HELIX 1066 1082 {ECO:0000244|PDB:3A6P}.
HELIX 1087 1103 {ECO:0000244|PDB:3A6P}.
TURN 1105 1107 {ECO:0000244|PDB:3A6P}.
HELIX 1111 1115 {ECO:0000244|PDB:3A6P}.
STRAND 1118 1120 {ECO:0000244|PDB:3A6P}.
HELIX 1123 1132 {ECO:0000244|PDB:3A6P}.
SEQUENCE 1204 AA; 136311 MW; 3295A17DF7C37602 CRC64;
MAMDQVNALC EQLVKAVTVM MDPNSTQRYR LEALKFCEEF KEKCPICVPC GLRLAEKTQV
AIVRHFGLQI LEHVVKFRWN GMSRLEKVYL KNSVMELIAN GTLNILEEEN HIKDALSRIV
VEMIKREWPQ HWPDMLIELD TLSKQGETQT ELVMFILLRL AEDVVTFQTL PPQRRRDIQQ
TLTQNMERIF SFLLNTLQEN VNKYQQVKTD TSQESKAQAN CRVGVAALNT LAGYIDWVSM
SHITAENCKL LEILCLLLNE QELQLGAAEC LLIAVSRKGK LEDRKPLMVL FGDVAMHYIL
SAAQTADGGG LVEKHYVFLK RLCQVLCALG NQLCALLGAD SDVETPSNFG KYLESFLAFT
THPSQFLRSS TQMTWGALFR HEILSRDPLL LAIIPKYLRA SMTNLVKMGF PSKTDSPSCE
YSRFDFDSDE DFNAFFNSSR AQQGEVMRLA CRLDPKTSFQ MAGEWLKYQL STFLDAGSVN
SCSAVGTGEG SLCSVFSPSF VQWEAMTLFL ESVITQMFRT LNREEIPVND GIELLQMVLN
FDTKDPLILS CVLTNVSALF PFVTYRPEFL PQVFSKLFSS VTFETVEESK APRTRAVRNV
RRHACSSIIK MCRDYPQLVL PNFDMLYNHV KQLLSNELLL TQMEKCALME ALVLISNQFK
NYERQKVFLE ELMAPVASIW LSQDMHRVLS DVDAFIAYVG TDQKSCDPGL EDPCGLNRAR
MSFCVYSILG VVKRTCWPTD LEEAKAGGFV VGYTSSGNPI FRNPCTEQIL KLLDNLLALI
RTHNTLYAPE MLAKMAEPFT KALDMLDAEK SAILGLPQPL LELNDSPVFK TVLERMQRFF
STLYENCFHI LGKAGPSMQQ DFYTVEDLAT QLLSSAFVNL NNIPDYRLRP MLRVFVKPLV
LFCPPEHYEA LVSPILGPLF TYLHMRLSQK WQVINQRSLL CGEDEAADEN PESQEMLEEQ
LVRMLTREVM DLITVCCVSK KGADHSSAPP ADGDDEEMMA TEVTPSAMAE LTDLGKCLMK
HEDVCTALLI TAFNSLAWKD TLSCQRTTSQ LCWPLLKQVL SGTLLADAVT WLFTSVLKGL
QMHGQHDGCM ASLVHLAFQI YEALRPRYLE IRAVMEQIPE IQKDSLDQFD CKLLNPSLQK
VADKRRKDQF KRLIAGCIGK PLGEQFRKEV HIKNLPSLFK KTKPMLETEV LDNDGGGLAT
IFEP


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