NXF1_HUMAN
ID NXF1_HUMAN Reviewed; 619 AA.
AC Q9UBU9; B4E269; Q99799; Q9UQL2;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 229.
DE RecName: Full=Nuclear RNA export factor 1;
DE AltName: Full=Tip-associated protein;
DE AltName: Full=Tip-associating protein;
DE AltName: Full=mRNA export factor TAP;
GN Name=NXF1; Synonyms=TAP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND MUTAGENESIS.
RC TISSUE=Cervix carcinoma;
RX PubMed=10202158; DOI=10.1093/emboj/18.7.1953;
RA Braun I.C., Rohrbach E., Schmitt C., Izaurralde E.;
RT "TAP binds to the constitutive transport element (CTE) through a novel RNA-
RT binding motif that is sufficient to promote CTE-dependent RNA export from
RT the nucleus.";
RL EMBO J. 18:1953-1965(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10323864; DOI=10.1101/gad.13.9.1126;
RA Kang Y., Cullen B.R.;
RT "The human Tap protein is a nuclear mRNA export factor that contains novel
RT RNA-binding and nucleocytoplasmic transport sequences.";
RL Genes Dev. 13:1126-1139(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10454577; DOI=10.1128/mcb.19.9.6306;
RA Bear J., Tan W., Zolotukhin A.S., Tabernero C., Hudson E.A., Felber B.K.;
RT "Identification of novel import and export signals of human TAP, the
RT protein that binds to the constitutive transport element of the type D
RT retrovirus mRNAs.";
RL Mol. Cell. Biol. 19:6306-6317(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 61-619, AND INTERACTION WITH SAIMIRIINE
RP HERPESVIRUS 2 TIP (MICROBIAL INFECTION).
RC TISSUE=Lymphocyte;
RX PubMed=9175835; DOI=10.1016/s1074-7613(00)80345-3;
RA Yoon D.-W., Lee H., Seol W., DeMaria M., Rosenzweig M., Jung J.U.;
RT "Tap: a novel cellular protein that interacts with tip of herpesvirus
RT saimiri and induces lymphocyte aggregation.";
RL Immunity 6:571-582(1997).
RN [9]
RP FUNCTION.
RX PubMed=9660949; DOI=10.1016/s1097-2765(00)80065-9;
RA Grueter P., Tabernero C., von Kobbe C., Schmitt C., Saavedra C., Bachi A.,
RA Wilm M., Felber B.K., Izaurralde E.;
RT "TAP, the human homolog of Mex67p, mediates CTE-dependent RNA export from
RT the nucleus.";
RL Mol. Cell 1:649-659(1998).
RN [10]
RP INTERACTION WITH NUP42.
RX PubMed=10228171; DOI=10.1093/emboj/18.9.2593;
RA Katahira J., Straesser K., Podtelejnikov A., Mann M., Jung J.U., Hurt E.;
RT "The Mex67p-mediated nuclear mRNA export pathway is conserved from yeast to
RT human.";
RL EMBO J. 18:2593-2609(1999).
RN [11]
RP FUNCTION, INTERACTION WITH DHX9, AND SUBCELLULAR LOCATION.
RX PubMed=10924507; DOI=10.1074/jbc.m003933200;
RA Tang H., Wong-Staal F.;
RT "Specific interaction between RNA helicase A and Tap, two cellular proteins
RT that bind to the constitutive transport element of type D retrovirus.";
RL J. Biol. Chem. 275:32694-32700(2000).
RN [12]
RP CHARACTERIZATION.
RX PubMed=11259411; DOI=10.1074/jbc.m100400200;
RA Braun I.C., Herold A., Rode M., Conti E., Izaurralde E.;
RT "Overexpression of TAP/p15 heterodimers bypasses nuclear retention and
RT stimulates nuclear mRNA export.";
RL J. Biol. Chem. 276:20536-20543(2001).
RN [13]
RP CHARACTERIZATION.
RX PubMed=10668806; DOI=10.1017/s1355838200991994;
RA Bachi A., Braun I.C., Rodrigues J.P., Pante N., Ribbeck K., von Kobbe C.,
RA Kutay U., Wilm M., Goerlich D., Carmo-Fonseca M., Izaurralde E.;
RT "The C-terminal domain of TAP interacts with the nuclear pore complex and
RT promotes export of specific CTE-bearing RNA substrates.";
RL RNA 6:136-158(2000).
RN [14]
RP MUTAGENESIS.
RX PubMed=11256625; DOI=10.1093/embo-reports/kvd009;
RA Suyama M., Doerks T., Braun I.C., Sattler M., Izaurralde E., Bork P.;
RT "Prediction of structural domains of TAP reveals details of its interaction
RT with p15 and nucleoporins.";
RL EMBO Rep. 1:53-58(2000).
RN [15]
RP INTERACTION WITH ALYREF/THOC4 AND THE EXON JUNCTION COMPLEX.
RX PubMed=11707413; DOI=10.1093/emboj/20.22.6424;
RA Kataoka N., Diem M.D., Kim V.N., Yong J., Dreyfuss G.;
RT "Magoh, a human homolog of Drosophila mago nashi protein, is a component of
RT the splicing-dependent exon-exon junction complex.";
RL EMBO J. 20:6424-6433(2001).
RN [16]
RP IDENTIFICATION IN A MRNP COMPLEX WITH UPF3A AND UPF3B.
RX PubMed=11546873; DOI=10.1126/science.1062829;
RA Kim V.N., Kataoka N., Dreyfuss G.;
RT "Role of the nonsense-mediated decay factor hUpf3 in the splicing-dependent
RT exon-exon junction complex.";
RL Science 293:1832-1836(2001).
RN [17]
RP IDENTIFICATION IN A POST-SPLICING COMPLEX WITH RBM8A; UPF1; UPF2; UPF3A;
RP UPF3B AND RNPS1.
RX PubMed=11546874; DOI=10.1126/science.1062786;
RA Lykke-Andersen J., Shu M.-D., Steitz J.A.;
RT "Communication of the position of exon-exon junctions to the mRNA
RT surveillance machinery by the protein RNPS1.";
RL Science 293:1836-1839(2001).
RN [18]
RP IDENTIFICATION IN A COMPLEX WITH RANBP2; RANGAP1 AND NXT1.
RX PubMed=14729961; DOI=10.1128/mcb.24.3.1155-1167.2004;
RA Forler D., Rabut G., Ciccarelli F.D., Herold A., Koecher T., Niggeweg R.,
RA Bork P., Ellenberg J., Izaurralde E.;
RT "RanBP2/Nup358 provides a major binding site for NXF1-p15 dimers at the
RT nuclear pore complex and functions in nuclear mRNA export.";
RL Mol. Cell. Biol. 24:1155-1167(2004).
RN [19]
RP INTERACTION WITH EIF4A3 AND ALYREF/THOC4.
RX PubMed=14730019; DOI=10.1261/rna.5230104;
RA Chan C.C., Dostie J., Diem M.D., Feng W., Mann M., Rappsilber J.,
RA Dreyfuss G.;
RT "eIF4A3 is a novel component of the exon junction complex.";
RL RNA 10:200-209(2004).
RN [20]
RP INTERACTION WITH RBM15.
RX PubMed=17001072; DOI=10.1074/jbc.m608745200;
RA Lindtner S., Zolotukhin A.S., Uranishi H., Bear J., Kulkarni V.,
RA Smulevitch S., Samiotaki M., Panayotou G., Felber B.K., Pavlakis G.N.;
RT "RNA-binding motif protein 15 binds to the RNA transport element RTE and
RT provides a direct link to the NXF1 export pathway.";
RL J. Biol. Chem. 281:36915-36928(2006).
RN [21]
RP INTERACTION WITH DDX3X AND PABPC1, AND SUBCELLULAR LOCATION.
RX PubMed=18596238; DOI=10.1091/mbc.e07-12-1264;
RA Lai M.C., Lee Y.H., Tarn W.Y.;
RT "The DEAD-box RNA helicase DDX3 associates with export messenger
RT ribonucleoproteins as well as tip-associated protein and participates in
RT translational control.";
RL Mol. Biol. Cell 19:3847-3858(2008).
RN [22]
RP FUNCTION, AND MUTAGENESIS OF ARG-71; ARG-78; ARG-81; ARG-82; ARG-89;
RP ARG-91; ARG-97; ARG-98; ARG-100 AND ARG-105.
RX PubMed=18364396; DOI=10.1073/pnas.0709167105;
RA Hautbergue G.M., Hung M.L., Golovanov A.P., Lian L.Y., Wilson S.A.;
RT "Mutually exclusive interactions drive handover of mRNA from export
RT adaptors to TAP.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:5154-5159(2008).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [24]
RP INTERACTION WITH FYTTD1.
RX PubMed=19836239; DOI=10.1016/j.cub.2009.09.041;
RA Hautbergue G.M., Hung M.L., Walsh M.J., Snijders A.P., Chang C.T.,
RA Jones R., Ponting C.P., Dickman M.J., Wilson S.A.;
RT "UIF, a new mRNA export adaptor that works together with REF/ALY, requires
RT FACT for recruitment to mRNA.";
RL Curr. Biol. 19:1918-1924(2009).
RN [25]
RP FUNCTION, AND INTERACTION WITH ALYREF/THOC4 AND THOC5.
RX PubMed=19165146; DOI=10.1038/emboj.2009.5;
RA Katahira J., Inoue H., Hurt E., Yoneda Y.;
RT "Adaptor Aly and co-adaptor Thoc5 function in the Tap-p15-mediated nuclear
RT export of HSP70 mRNA.";
RL EMBO J. 28:556-567(2009).
RN [26]
RP INTERACTION WITH RBM15B.
RX PubMed=19586903; DOI=10.1074/jbc.m109.040113;
RA Uranishi H., Zolotukhin A.S., Lindtner S., Warming S., Zhang G.M., Bear J.,
RA Copeland N.G., Jenkins N.A., Pavlakis G.N., Felber B.K.;
RT "The RNA-binding motif protein 15B (RBM15B/OTT3) acts as cofactor of the
RT nuclear export receptor NXF1.";
RL J. Biol. Chem. 284:26106-26116(2009).
RN [27]
RP INTERACTION WITH CPSF6, AND SUBCELLULAR LOCATION.
RX PubMed=19864460; DOI=10.1091/mbc.e09-05-0389;
RA Ruepp M.D., Aringhieri C., Vivarelli S., Cardinale S., Paro S.,
RA Schuemperli D., Barabino S.M.;
RT "Mammalian pre-mRNA 3' end processing factor CF I m 68 functions in mRNA
RT export.";
RL Mol. Biol. Cell 20:5211-5223(2009).
RN [28]
RP INTERACTION WITH FMR1.
RX PubMed=18936162; DOI=10.1128/mcb.01377-08;
RA Kim M., Bellini M., Ceman S.;
RT "Fragile X mental retardation protein FMRP binds mRNAs in the nucleus.";
RL Mol. Cell. Biol. 29:214-228(2009).
RN [29]
RP SUBCELLULAR LOCATION.
RX PubMed=19324961; DOI=10.1261/rna.1387009;
RA Schmidt U., Im K.-B., Benzing C., Janjetovic S., Rippe K., Lichter P.,
RA Wachsmuth M.;
RT "Assembly and mobility of exon-exon junction complexes in living cells.";
RL RNA 15:862-876(2009).
RN [30]
RP INTERACTION WITH HUMAN HERPES VIRUS 1 ICP27 (MICROBIAL INFECTION).
RX PubMed=19369354; DOI=10.1128/jvi.00375-09;
RA Johnson L.A., Li L., Sandri-Goldin R.M.;
RT "The cellular RNA export receptor TAP/NXF1 is required for ICP27-mediated
RT export of herpes simplex virus 1 RNA, but the TREX complex adaptor protein
RT Aly/REF appears to be dispensable.";
RL J. Virol. 83:6335-6346(2009).
RN [31]
RP INTERACTION WITH MCM3AP.
RX PubMed=20005110; DOI=10.1016/j.cub.2009.10.078;
RA Wickramasinghe V.O., McMurtrie P.I., Mills A.D., Takei Y., Penrhyn-Lowe S.,
RA Amagase Y., Main S., Marr J., Stewart M., Laskey R.A.;
RT "mRNA export from mammalian cell nuclei is dependent on GANP.";
RL Curr. Biol. 20:25-31(2010).
RN [32]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [33]
RP INTERACTION WITH FRG1.
RX PubMed=21699900; DOI=10.1016/j.jmb.2011.06.014;
RA Sun C.Y., van Koningsbruggen S., Long S.W., Straasheijm K., Klooster R.,
RA Jones T.I., Bellini M., Levesque L., Brieher W.M., van der Maarel S.M.,
RA Jones P.L.;
RT "Facioscapulohumeral muscular dystrophy region gene 1 is a dynamic RNA-
RT associated and actin-bundling protein.";
RL J. Mol. Biol. 411:397-416(2011).
RN [34]
RP ASSOCIATION WITH THE TREX COMPLEX, RNA-BINDING, AND MUTAGENESIS OF ARG-453
RP AND 456-LYS--ARG-459.
RX PubMed=22893130; DOI=10.1038/ncomms2005;
RA Viphakone N., Hautbergue G.M., Walsh M., Chang C.T., Holland A.,
RA Folco E.G., Reed R., Wilson S.A.;
RT "TREX exposes the RNA-binding domain of Nxf1 to enable mRNA export.";
RL Nat. Commun. 3:1006-1006(2012).
RN [35]
RP INTERACTION WITH CHTOP; THOC5 AND ALYREF, AND MUTAGENESIS OF
RP 450-LEU--ARG-453 AND 456-LYS--ARG-459.
RX PubMed=23299939; DOI=10.1038/emboj.2012.342;
RA Chang C.T., Hautbergue G.M., Walsh M.J., Viphakone N., van Dijk T.B.,
RA Philipsen S., Wilson S.A.;
RT "Chtop is a component of the dynamic TREX mRNA export complex.";
RL EMBO J. 32:473-486(2013).
RN [36]
RP SUBCELLULAR LOCATION.
RX PubMed=23591820; DOI=10.1242/jcs.118000;
RA Umlauf D., Bonnet J., Waharte F., Fournier M., Stierle M., Fischer B.,
RA Brino L., Devys D., Tora L.;
RT "The human TREX-2 complex is stably associated with the nuclear pore
RT basket.";
RL J. Cell Sci. 126:2656-2667(2013).
RN [37]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [38]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CHTOP.
RX PubMed=23826332; DOI=10.1371/journal.pone.0067676;
RA Teng I.F., Wilson S.A.;
RT "Mapping interactions between mRNA export factors in living cells.";
RL PLoS ONE 8:E67676-E67676(2013).
RN [39]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH LUZP4.
RX PubMed=25662211; DOI=10.1093/nar/gkv070;
RA Viphakone N., Cumberbatch M.G., Livingstone M.J., Heath P.R., Dickman M.J.,
RA Catto J.W., Wilson S.A.;
RT "Luzp4 defines a new mRNA export pathway in cancer cells.";
RL Nucleic Acids Res. 43:2353-2366(2015).
RN [40]
RP FUNCTION.
RX PubMed=28984244; DOI=10.7554/elife.31311;
RA Roundtree I.A., Luo G.Z., Zhang Z., Wang X., Zhou T., Cui Y., Sha J.,
RA Huang X., Guerrero L., Xie P., He E., Shen B., He C.;
RT "YTHDC1 mediates nuclear export of N6-methyladenosine methylated mRNAs.";
RL Elife 6:0-0(2017).
RN [41]
RP INTERACTION WITH EBOLAVIRUS NUCLEOPROTEIN (MICROBIAL INFECTION).
RX PubMed=31940815; DOI=10.3390/cells9010187;
RA Wendt L., Brandt J., Bodmer B.S., Reiche S., Schmidt M.L., Traeger S.,
RA Hoenen T.;
RT "The Ebola Virus Nucleoprotein Recruits the Nuclear RNA Export Factor NXF1
RT into Inclusion Bodies to Facilitate Viral Protein Expression.";
RL Cells 9:0-0(2020).
RN [42]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 102-372.
RX PubMed=11060011; DOI=10.1093/emboj/19.21.5587;
RA Liker E., Fernandez E., Izaurralde E., Conti E.;
RT "The structure of the mRNA export factor TAP reveals a cis arrangement of a
RT non-canonical RNP domain and an LRR domain.";
RL EMBO J. 19:5587-5598(2000).
RN [43]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NXT1, X-RAY
RP CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH NXT1-FG-REPEAT, SUBUNIT,
RP DOMAINS, AND MUTAGENESIS OF LEU-383; LEU-386; ASP-399; ASP-482; ILE-518;
RP PRO-521 AND TRP-594.
RX PubMed=11583626; DOI=10.1016/s1097-2765(01)00348-3;
RA Fribourg S., Braun I.C., Izaurralde E., Conti E.;
RT "Structural basis for the recognition of a nucleoporin FG repeat by the
RT NTF2-like domain of the TAP/p15 mRNA nuclear export factor.";
RL Mol. Cell 8:645-656(2001).
RN [44]
RP X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF 561-619 IN COMPLEX WITH RANBP3.
RX PubMed=12581645; DOI=10.1016/s0022-2836(02)01474-2;
RA Grant R.P., Neuhaus D., Stewart M.;
RT "Structural basis for the interaction between the Tap/NXF1 UBA domain and
RT FG nucleoporins at 1A resolution.";
RL J. Mol. Biol. 326:849-858(2003).
RN [45]
RP STRUCTURE BY NMR OF 551-619, AND MUTAGENESIS OF PHE-617.
RX PubMed=11875519; DOI=10.1038/nsb773;
RA Grant R.P., Hurt E., Neuhaus D., Stewart M.;
RT "Structure of the C-terminal FG-nucleoporin binding domain of Tap/NXF1.";
RL Nat. Struct. Biol. 9:247-251(2002).
CC -!- FUNCTION: Involved in the nuclear export of mRNA species bearing
CC retroviral constitutive transport elements (CTE) and in the export of
CC mRNA from the nucleus to the cytoplasm (TAP/NFX1 pathway)
CC (PubMed:10924507). The NXF1-NXT1 heterodimer is involved in the export
CC of HSP70 mRNA in conjunction with ALYREF/THOC4 and THOC5 components of
CC the TREX complex (PubMed:18364396, PubMed:19165146, PubMed:9660949).
CC ALYREF/THOC4-bound mRNA is thought to be transferred to the NXF1-NXT1
CC heterodimer for export (PubMed:18364396, PubMed:19165146,
CC PubMed:9660949). Also involved in nuclear export of m6A-containing
CC mRNAs: interaction between SRSF3 and YTHDC1 facilitates m6A-containing
CC mRNA-binding to both SRSF3 and NXF1, promoting mRNA nuclear export
CC (PubMed:28984244). {ECO:0000269|PubMed:10924507,
CC ECO:0000269|PubMed:18364396, ECO:0000269|PubMed:19165146,
CC ECO:0000269|PubMed:28984244, ECO:0000269|PubMed:9660949}.
CC -!- SUBUNIT: Heterodimer (via NTF2 domain) with NXT1 (PubMed:11583626). The
CC formation of NXF1-NXT1 heterodimers is required for the NXF1-mediated
CC nuclear mRNA export (PubMed:11583626). Forms a complex with
CC RANBP2/NUP358, NXT1 and RANGAP1 (PubMed:14729961). Associates with the
CC exon junction complex (EJC) and with the transcription/export (TREX)
CC complex (PubMed:11707413, PubMed:22893130). Found in a mRNA complex
CC with UPF3A and UPF3B (PubMed:11546873). Found in a post-splicing
CC complex with RBM8A, UPF1, UPF2, UPF3A, UPF3B and RNPS1
CC (PubMed:11546874). Interacts (via N-terminus) with DHX9 (via N-
CC terminus); this interaction is direct and negatively regulates NXF1-
CC mediated nuclear export of constitutive transport element (CTE)-
CC containing cellular mRNAs (PubMed:10924507). Interacts with
CC ALYREF/THOC4 (PubMed:11707413, PubMed:14730019, PubMed:19165146,
CC PubMed:23299939). Interacts with FYTTD1/UIF (PubMed:19836239).
CC Interacts with EIF4A3 (PubMed:14730019). Interacts with NUP42
CC (PubMed:10228171). Interacts with THOC5 (PubMed:19165146,
CC PubMed:23299939). Interacts with CHTOP (PubMed:23299939,
CC PubMed:23826332). Interacts with FRG1 (via N-terminus)
CC (PubMed:21699900). Interacts with LUZP4 (PubMed:25662211). Interacts
CC with FMR1; the interaction occurs in a mRNA-dependent and
CC polyribosomes-independent manner in the nucleus (PubMed:18936162).
CC Interacts with CPSF6 (via N-terminus); this interaction is direct
CC (PubMed:19864460). Interacts with RBM15 (PubMed:17001072). Interacts
CC with RBM15B (PubMed:19586903). Interacts with MCM3AP isoform GANP; this
CC interaction is not mediated by RNA (PubMed:20005110). Interacts with
CC DDX3X (via C-terminus); this interaction may be partly involved in
CC DDX3X nuclear export and in NXF1 localization to stress granules
CC (PubMed:18596238). Interacts with PABPC1/PABP1 (PubMed:18596238).
CC {ECO:0000269|PubMed:10228171, ECO:0000269|PubMed:10924507,
CC ECO:0000269|PubMed:11546873, ECO:0000269|PubMed:11546874,
CC ECO:0000269|PubMed:11583626, ECO:0000269|PubMed:11707413,
CC ECO:0000269|PubMed:12581645, ECO:0000269|PubMed:14729961,
CC ECO:0000269|PubMed:14730019, ECO:0000269|PubMed:17001072,
CC ECO:0000269|PubMed:18596238, ECO:0000269|PubMed:18936162,
CC ECO:0000269|PubMed:19165146, ECO:0000269|PubMed:19369354,
CC ECO:0000269|PubMed:19586903, ECO:0000269|PubMed:19836239,
CC ECO:0000269|PubMed:19864460, ECO:0000269|PubMed:20005110,
CC ECO:0000269|PubMed:21699900, ECO:0000269|PubMed:22893130,
CC ECO:0000269|PubMed:23299939, ECO:0000269|PubMed:23826332,
CC ECO:0000269|PubMed:25662211, ECO:0000269|PubMed:9175835}.
CC -!- SUBUNIT: (Microbial infection) Interacts with Saimiriine herpesvirus 2
CC TIP protein. {ECO:0000269|PubMed:9175835}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human herpes virus 1
CC (HHV-1) ICP27 protein; this interaction allows efficient export of HHV-
CC 1 early and late transcripts. {ECO:0000269|PubMed:19369354}.
CC -!- SUBUNIT: (Microbial infection) Interacts (via RNA-binding domain) with
CC Ebolavirus nucleoprotein; this interaction recruits NXF1 to the
CC inclusion bodies were viral replication takes place, probably to export
CC viral mRNA-NXF1 complexes from these sites.
CC {ECO:0000269|PubMed:31940815}.
CC -!- INTERACTION:
CC Q9UBU9; Q86V81: ALYREF; NbExp=4; IntAct=EBI-398874, EBI-347640;
CC Q9UBU9; Q9H7T9: AUNIP; NbExp=3; IntAct=EBI-398874, EBI-10693257;
CC Q9UBU9; Q9BYV9: BACH2; NbExp=3; IntAct=EBI-398874, EBI-1642333;
CC Q9UBU9; Q14457: BECN1; NbExp=3; IntAct=EBI-398874, EBI-949378;
CC Q9UBU9; Q9NQY0: BIN3; NbExp=3; IntAct=EBI-398874, EBI-2653038;
CC Q9UBU9; Q13490: BIRC2; NbExp=3; IntAct=EBI-398874, EBI-514538;
CC Q9UBU9; Q13867: BLMH; NbExp=3; IntAct=EBI-398874, EBI-718504;
CC Q9UBU9; B2RXH4: BTBD18; NbExp=3; IntAct=EBI-398874, EBI-18298734;
CC Q9UBU9; Q5SWW7: C10orf55; NbExp=3; IntAct=EBI-398874, EBI-12809220;
CC Q9UBU9; Q86WS4: C12orf40; NbExp=3; IntAct=EBI-398874, EBI-10286004;
CC Q9UBU9; Q13555-5: CAMK2G; NbExp=3; IntAct=EBI-398874, EBI-12020154;
CC Q9UBU9; Q96HB5: CCDC120; NbExp=3; IntAct=EBI-398874, EBI-744556;
CC Q9UBU9; A0A1B0GWI1: CCDC196; NbExp=3; IntAct=EBI-398874, EBI-10181422;
CC Q9UBU9; Q8NCU1: CCDC197; NbExp=3; IntAct=EBI-398874, EBI-750686;
CC Q9UBU9; Q96M83-3: CCDC7; NbExp=3; IntAct=EBI-398874, EBI-18211613;
CC Q9UBU9; Q8N8U2: CDYL2; NbExp=3; IntAct=EBI-398874, EBI-8467076;
CC Q9UBU9; Q9Y3Y2: CHTOP; NbExp=9; IntAct=EBI-398874, EBI-347794;
CC Q9UBU9; P49760: CLK2; NbExp=3; IntAct=EBI-398874, EBI-750020;
CC Q9UBU9; P49761: CLK3; NbExp=3; IntAct=EBI-398874, EBI-745579;
CC Q9UBU9; O00571: DDX3X; NbExp=5; IntAct=EBI-398874, EBI-353779;
CC Q9UBU9; Q08211: DHX9; NbExp=8; IntAct=EBI-398874, EBI-352022;
CC Q9UBU9; Q92997: DVL3; NbExp=3; IntAct=EBI-398874, EBI-739789;
CC Q9UBU9; Q9BQ95: ECSIT; NbExp=3; IntAct=EBI-398874, EBI-712452;
CC Q9UBU9; Q96DF8: ESS2; NbExp=3; IntAct=EBI-398874, EBI-3928124;
CC Q9UBU9; Q8IZU1: FAM9A; NbExp=3; IntAct=EBI-398874, EBI-8468186;
CC Q9UBU9; Q9C0B1-2: FTO; NbExp=3; IntAct=EBI-398874, EBI-18138793;
CC Q9UBU9; P14136: GFAP; NbExp=7; IntAct=EBI-398874, EBI-744302;
CC Q9UBU9; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-398874, EBI-5916454;
CC Q9UBU9; Q86WP2: GPBP1; NbExp=3; IntAct=EBI-398874, EBI-2349758;
CC Q9UBU9; Q9BX10: GTPBP2; NbExp=3; IntAct=EBI-398874, EBI-6115579;
CC Q9UBU9; P49639: HOXA1; NbExp=3; IntAct=EBI-398874, EBI-740785;
CC Q9UBU9; O75031: HSF2BP; NbExp=3; IntAct=EBI-398874, EBI-7116203;
CC Q9UBU9; Q9ULR0-1: ISY1; NbExp=3; IntAct=EBI-398874, EBI-18398632;
CC Q9UBU9; Q9H079: KATNBL1; NbExp=5; IntAct=EBI-398874, EBI-715394;
CC Q9UBU9; Q96MP8-2: KCTD7; NbExp=3; IntAct=EBI-398874, EBI-11954971;
CC Q9UBU9; Q6A162: KRT40; NbExp=3; IntAct=EBI-398874, EBI-10171697;
CC Q9UBU9; Q5T5B0: LCE3E; NbExp=3; IntAct=EBI-398874, EBI-10245456;
CC Q9UBU9; O95751: LDOC1; NbExp=4; IntAct=EBI-398874, EBI-740738;
CC Q9UBU9; Q8WWY6: MBD3L1; NbExp=3; IntAct=EBI-398874, EBI-12516603;
CC Q9UBU9; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-398874, EBI-10172526;
CC Q9UBU9; Q6NTE8: MRNIP; NbExp=3; IntAct=EBI-398874, EBI-2857471;
CC Q9UBU9; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-398874, EBI-11522433;
CC Q9UBU9; Q6ZUT1: NKAPD1; NbExp=3; IntAct=EBI-398874, EBI-3920396;
CC Q9UBU9; O00746: NME4; NbExp=3; IntAct=EBI-398874, EBI-744871;
CC Q9UBU9; P37198: NUP62; NbExp=11; IntAct=EBI-398874, EBI-347978;
CC Q9UBU9; Q9UKK6: NXT1; NbExp=6; IntAct=EBI-398874, EBI-301889;
CC Q9UBU9; Q8WWB5: PIH1D2; NbExp=3; IntAct=EBI-398874, EBI-10232538;
CC Q9UBU9; Q9BZL4: PPP1R12C; NbExp=3; IntAct=EBI-398874, EBI-721802;
CC Q9UBU9; P31321: PRKAR1B; NbExp=3; IntAct=EBI-398874, EBI-2805516;
CC Q9UBU9; P41219: PRPH; NbExp=3; IntAct=EBI-398874, EBI-752074;
CC Q9UBU9; P79522: PRR3; NbExp=3; IntAct=EBI-398874, EBI-2803328;
CC Q9UBU9; Q96P16-3: RPRD1A; NbExp=3; IntAct=EBI-398874, EBI-12840198;
CC Q9UBU9; Q9NR46: SH3GLB2; NbExp=3; IntAct=EBI-398874, EBI-749607;
CC Q9UBU9; Q8ND83: SLAIN1; NbExp=3; IntAct=EBI-398874, EBI-10269374;
CC Q9UBU9; Q13573: SNW1; NbExp=3; IntAct=EBI-398874, EBI-632715;
CC Q9UBU9; Q9H0A9-2: SPATC1L; NbExp=3; IntAct=EBI-398874, EBI-11995806;
CC Q9UBU9; Q07955: SRSF1; NbExp=5; IntAct=EBI-398874, EBI-398920;
CC Q9UBU9; P84103: SRSF3; NbExp=4; IntAct=EBI-398874, EBI-372557;
CC Q9UBU9; Q16629: SRSF7; NbExp=4; IntAct=EBI-398874, EBI-398885;
CC Q9UBU9; Q8IZU3: SYCP3; NbExp=3; IntAct=EBI-398874, EBI-7574149;
CC Q9UBU9; Q9P2M4: TBC1D14; NbExp=3; IntAct=EBI-398874, EBI-2797718;
CC Q9UBU9; Q8TDR4: TCP10L; NbExp=3; IntAct=EBI-398874, EBI-3923210;
CC Q9UBU9; Q8N6V9: TEX9; NbExp=3; IntAct=EBI-398874, EBI-746341;
CC Q9UBU9; Q9Y2W1: THRAP3; NbExp=4; IntAct=EBI-398874, EBI-352039;
CC Q9UBU9; Q96CG3: TIFA; NbExp=6; IntAct=EBI-398874, EBI-740711;
CC Q9UBU9; Q13829: TNFAIP1; NbExp=3; IntAct=EBI-398874, EBI-2505861;
CC Q9UBU9; Q13625-3: TP53BP2; NbExp=3; IntAct=EBI-398874, EBI-10175039;
CC Q9UBU9; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-398874, EBI-741480;
CC Q9UBU9; Q9UK41-2: VPS28; NbExp=3; IntAct=EBI-398874, EBI-12146727;
CC Q9UBU9; P15622-3: ZNF250; NbExp=3; IntAct=EBI-398874, EBI-10177272;
CC Q9UBU9; Q6P1L6: ZNF343; NbExp=3; IntAct=EBI-398874, EBI-10252492;
CC Q9UBU9; Q7Z4V0: ZNF438; NbExp=3; IntAct=EBI-398874, EBI-11962468;
CC Q9UBU9; P10238: UL54; Xeno; NbExp=4; IntAct=EBI-398874, EBI-6883946;
CC Q9UBU9; P22575; Xeno; NbExp=6; IntAct=EBI-398874, EBI-866709;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10924507,
CC ECO:0000269|PubMed:18596238, ECO:0000269|PubMed:19864460,
CC ECO:0000269|PubMed:23591820, ECO:0000269|PubMed:25662211}. Nucleus,
CC nucleoplasm {ECO:0000269|PubMed:19324961, ECO:0000269|PubMed:23826332}.
CC Nucleus speckle {ECO:0000269|PubMed:19324961,
CC ECO:0000269|PubMed:23826332}. Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:23591820}. Nucleus envelope
CC {ECO:0000269|PubMed:18596238, ECO:0000269|PubMed:23591820}. Cytoplasm
CC {ECO:0000269|PubMed:10924507, ECO:0000269|PubMed:18596238,
CC ECO:0000269|PubMed:19324961, ECO:0000269|PubMed:19864460}. Cytoplasm,
CC Stress granule {ECO:0000269|PubMed:18596238}. Note=Localized
CC predominantly in the nucleoplasm and at both the nucleoplasmic and
CC cytoplasmic faces of the nuclear pore complex. Shuttles between the
CC nucleus and the cytoplasm. Travels to the cytoplasm as part of the exon
CC junction complex (EJC) bound to mRNA. The association with the TREX
CC complex seems to occur in regions surrounding nuclear speckles known as
CC perispeckles (PubMed:23826332). Nucleus; nuclear rim (PubMed:25662211).
CC {ECO:0000269|PubMed:23826332, ECO:0000269|PubMed:25662211}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UBU9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UBU9-2; Sequence=VSP_041427, VSP_041428;
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously.
CC -!- DOMAIN: The minimal CTE binding domain consists of an RNP-type RNA
CC binding domain (RBD) and leucine-rich repeats.
CC {ECO:0000269|PubMed:11583626}.
CC -!- DOMAIN: The nucleoporin binding domain consists of a NTF2 domain (also
CC called NTF2-like domain) and a TAP-C domain (also called UBA-like
CC domain). It has 2 nucleoporin-FG-repeats binding sites (one in the NTF2
CC and the other in the TAP-C domain) which contribute to nucleoporin
CC association and act synergistically to export cellular mRNAs.
CC {ECO:0000269|PubMed:11583626}.
CC -!- DOMAIN: The NTF2 domain is functional only in the presence of NXT1 and
CC is essential for the export of mRNA from the nucleus. It inhibits RNA
CC binding activity through an intramolecular interaction with the N-
CC terminal RNA binding domain (RBD); the inhibition is removed by an
CC association with the TREX complex, specifically involving ALYREF/THOC4
CC and THOC5. {ECO:0000269|PubMed:11583626}.
CC -!- DOMAIN: The TAP-C domain mediates direct interactions with nucleoporin-
CC FG-repeats and is necessary and sufficient for localization of NXF1 to
CC the nuclear rim. The conserved loop 594-NWD-596 of the TAP-C domain has
CC a critical role in the interaction with nucleoporins.
CC {ECO:0000269|PubMed:11583626}.
CC -!- DOMAIN: The leucine-rich repeats are essential for the export of mRNA
CC from the nucleus. {ECO:0000269|PubMed:11583626}.
CC -!- DOMAIN: The RNA-binding domain is a non-canonical RNP-type domain.
CC {ECO:0000269|PubMed:11583626}.
CC -!- SIMILARITY: Belongs to the NXF family. {ECO:0000305}.
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DR EMBL; AJ132712; CAA10753.1; -; mRNA.
DR EMBL; AF112880; AAD39102.1; -; mRNA.
DR EMBL; AF126246; AAD20016.1; -; mRNA.
DR EMBL; AK304137; BAG65031.1; -; mRNA.
DR EMBL; AK027192; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AP001160; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471076; EAW74105.1; -; Genomic_DNA.
DR EMBL; BC004904; AAH04904.1; -; mRNA.
DR EMBL; BC028041; AAH28041.1; -; mRNA.
DR EMBL; U80073; AAB81111.1; -; mRNA.
DR CCDS; CCDS44629.1; -. [Q9UBU9-2]
DR CCDS; CCDS8037.1; -. [Q9UBU9-1]
DR RefSeq; NP_001074960.1; NM_001081491.1. [Q9UBU9-2]
DR RefSeq; NP_006353.2; NM_006362.4. [Q9UBU9-1]
DR PDB; 1FO1; X-ray; 2.90 A; A/B=102-372.
DR PDB; 1FT8; X-ray; 3.15 A; A/B/C/D/E=102-372.
DR PDB; 1GO5; NMR; -; A=551-619.
DR PDB; 1JKG; X-ray; 1.90 A; B=371-619.
DR PDB; 1JN5; X-ray; 2.80 A; B=371-619.
DR PDB; 1KOH; X-ray; 3.80 A; A/B/C/D=96-372.
DR PDB; 1KOO; X-ray; 3.80 A; A/B/C/D=96-372.
DR PDB; 1OAI; X-ray; 1.00 A; A=561-619.
DR PDB; 2Z5K; X-ray; 2.60 A; B=53-82.
DR PDB; 2Z5M; X-ray; 3.00 A; B=53-82.
DR PDB; 3RW6; X-ray; 2.30 A; A/B=96-362.
DR PDB; 3RW7; X-ray; 3.00 A; A/B/C/D=96-362.
DR PDB; 4WYK; X-ray; 3.40 A; A/C=96-555.
DR PDB; 6E5U; X-ray; 3.80 A; A/C/E/G=116-619.
DR PDBsum; 1FO1; -.
DR PDBsum; 1FT8; -.
DR PDBsum; 1GO5; -.
DR PDBsum; 1JKG; -.
DR PDBsum; 1JN5; -.
DR PDBsum; 1KOH; -.
DR PDBsum; 1KOO; -.
DR PDBsum; 1OAI; -.
DR PDBsum; 2Z5K; -.
DR PDBsum; 2Z5M; -.
DR PDBsum; 3RW6; -.
DR PDBsum; 3RW7; -.
DR PDBsum; 4WYK; -.
DR PDBsum; 6E5U; -.
DR AlphaFoldDB; Q9UBU9; -.
DR BMRB; Q9UBU9; -.
DR SMR; Q9UBU9; -.
DR BioGRID; 115745; 1332.
DR ComplexPortal; CPX-2435; mRNA nuclear export factor NXF1-NXT2.
DR ComplexPortal; CPX-725; mRNA nuclear export factor NXF1-NXT1.
DR CORUM; Q9UBU9; -.
DR DIP; DIP-31789N; -.
DR IntAct; Q9UBU9; 164.
DR MINT; Q9UBU9; -.
DR STRING; 9606.ENSP00000436679; -.
DR TCDB; 3.A.18.1.1; the nuclear mrna exporter (mrna-e) family.
DR GlyGen; Q9UBU9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UBU9; -.
DR MetOSite; Q9UBU9; -.
DR PhosphoSitePlus; Q9UBU9; -.
DR SwissPalm; Q9UBU9; -.
DR BioMuta; NXF1; -.
DR DMDM; 20139282; -.
DR EPD; Q9UBU9; -.
DR jPOST; Q9UBU9; -.
DR MassIVE; Q9UBU9; -.
DR MaxQB; Q9UBU9; -.
DR PaxDb; Q9UBU9; -.
DR PeptideAtlas; Q9UBU9; -.
DR PRIDE; Q9UBU9; -.
DR ProteomicsDB; 84075; -. [Q9UBU9-1]
DR ProteomicsDB; 84076; -. [Q9UBU9-2]
DR Antibodypedia; 4277; 308 antibodies from 36 providers.
DR DNASU; 10482; -.
DR Ensembl; ENST00000294172.7; ENSP00000294172.2; ENSG00000162231.14. [Q9UBU9-1]
DR Ensembl; ENST00000531709.6; ENSP00000453885.1; ENSG00000162231.14. [Q9UBU9-2]
DR Ensembl; ENST00000532297.5; ENSP00000436679.1; ENSG00000162231.14. [Q9UBU9-1]
DR GeneID; 10482; -.
DR KEGG; hsa:10482; -.
DR MANE-Select; ENST00000294172.7; ENSP00000294172.2; NM_006362.5; NP_006353.2.
DR UCSC; uc001nvf.1; human. [Q9UBU9-1]
DR CTD; 10482; -.
DR DisGeNET; 10482; -.
DR GeneCards; NXF1; -.
DR HGNC; HGNC:8071; NXF1.
DR HPA; ENSG00000162231; Low tissue specificity.
DR MIM; 602647; gene.
DR neXtProt; NX_Q9UBU9; -.
DR OpenTargets; ENSG00000162231; -.
DR PharmGKB; PA31858; -.
DR VEuPathDB; HostDB:ENSG00000162231; -.
DR eggNOG; KOG3763; Eukaryota.
DR GeneTree; ENSGT00390000007539; -.
DR HOGENOM; CLU_066652_0_0_1; -.
DR InParanoid; Q9UBU9; -.
DR OMA; YGGHEAW; -.
DR OrthoDB; 1051093at2759; -.
DR PhylomeDB; Q9UBU9; -.
DR TreeFam; TF314566; -.
DR PathwayCommons; Q9UBU9; -.
DR Reactome; R-HSA-159227; Transport of the SLBP independent Mature mRNA.
DR Reactome; R-HSA-159230; Transport of the SLBP Dependant Mature mRNA.
DR Reactome; R-HSA-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
DR Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR SignaLink; Q9UBU9; -.
DR SIGNOR; Q9UBU9; -.
DR BioGRID-ORCS; 10482; 501 hits in 1086 CRISPR screens.
DR ChiTaRS; NXF1; human.
DR EvolutionaryTrace; Q9UBU9; -.
DR GeneWiki; NXF1; -.
DR GenomeRNAi; 10482; -.
DR Pharos; Q9UBU9; Tbio.
DR PRO; PR:Q9UBU9; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9UBU9; protein.
DR Bgee; ENSG00000162231; Expressed in granulocyte and 91 other tissues.
DR ExpressionAtlas; Q9UBU9; baseline and differential.
DR Genevisible; Q9UBU9; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0042405; C:nuclear inclusion body; IEA:Ensembl.
DR GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR GO; GO:0042272; C:nuclear RNA export factor complex; IPI:ComplexPortal.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006406; P:mRNA export from nucleus; IDA:UniProtKB.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd00780; NTF2; 1.
DR CDD; cd14342; UBA_TAP-C; 1.
DR DisProt; DP01451; -.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR IDEAL; IID00225; -.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR002075; NTF2_dom.
DR InterPro; IPR018222; Nuclear_transport_factor_2_euk.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR030217; NXF_fam.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR005637; TAP_C_dom.
DR InterPro; IPR015245; Tap_RNA-bd.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR10662; PTHR10662; 1.
DR Pfam; PF02136; NTF2; 1.
DR Pfam; PF09162; Tap-RNA_bind; 1.
DR Pfam; PF03943; TAP_C; 1.
DR SMART; SM00804; TAP_C; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS51450; LRR; 3.
DR PROSITE; PS50177; NTF2_DOMAIN; 1.
DR PROSITE; PS51281; TAP_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Host-virus interaction; Leucine-rich repeat; Methylation; mRNA transport;
KW Nitration; Nuclear pore complex; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; RNA-binding; Translocation;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..619
FT /note="Nuclear RNA export factor 1"
FT /id="PRO_0000220529"
FT DOMAIN 119..198
FT /note="RRM"
FT REPEAT 266..291
FT /note="LRR 1"
FT REPEAT 292..315
FT /note="LRR 2"
FT REPEAT 316..343
FT /note="LRR 3"
FT REPEAT 344..371
FT /note="LRR 4"
FT DOMAIN 386..536
FT /note="NTF2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00137"
FT DOMAIN 565..619
FT /note="TAP-C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00611"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2..198
FT /note="Interaction with ALYREF/THOC4 and LUZP4"
FT /evidence="ECO:0000269|PubMed:25662211"
FT REGION 2..118
FT /note="RNA-binding (RBD)"
FT REGION 2..60
FT /note="Minor non-specific RNA-binding"
FT REGION 61..118
FT /note="Major non-specific RNA-binding"
FT MOTIF 67..100
FT /note="Nuclear localization signal"
FT MOTIF 83..110
FT /note="Nuclear export signal"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 42
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99JX7"
FT MOD_RES 42
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99JX7"
FT MOD_RES 126
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q99JX7"
FT VAR_SEQ 339..356
FT /note="SAIRERFPKLLRLDGHEL -> RSVVACVSPPGDLHPLGG (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041427"
FT VAR_SEQ 357..619
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041428"
FT MUTAGEN 71
FT /note="R->A: Greatly reduces RNA binding and no effect on
FT interaction with ALYREF/THOC4; when associated with A-78,
FT A-81, A-82, A-89, A-91, A-97, A-98, A-100 and A-105."
FT /evidence="ECO:0000269|PubMed:18364396"
FT MUTAGEN 78
FT /note="R->A: Greatly reduces RNA binding and no effect on
FT interaction with ALYREF/THOC4; when associated with A-71,
FT A-81, A-82, A-89, A-91, A-97, A-98, A-100 and A-105."
FT /evidence="ECO:0000269|PubMed:18364396"
FT MUTAGEN 81
FT /note="R->A: Greatly reduces RNA binding and no effect on
FT interaction with ALYREF/THOC4; when associated with A-71,
FT A-78, A-82, A-89, A-91, A-97, A-98, A-100 and A-105."
FT /evidence="ECO:0000269|PubMed:18364396"
FT MUTAGEN 82
FT /note="R->A: Greatly reduces RNA binding and no effect on
FT interaction with ALYREF/THOC4; when associated with A-71,
FT A-78, A-81, A-89, A-91, A-97, A-98, A-100 and A-105."
FT /evidence="ECO:0000269|PubMed:18364396"
FT MUTAGEN 89
FT /note="R->A: Greatly reduces RNA binding and no effect on
FT interaction with ALYREF/THOC4; when associated with A-71,
FT A-78, A-81, A-82, A-91, A-97, A-98, A-100 and A-105."
FT /evidence="ECO:0000269|PubMed:18364396"
FT MUTAGEN 91
FT /note="R->A: Greatly reduces RNA binding and no effect on
FT interaction with ALYREF/THOC4; when associated with A-71,
FT A-78, A-81, A-82, A-89, A-97, A-98, A-100 and A-105."
FT /evidence="ECO:0000269|PubMed:18364396"
FT MUTAGEN 97
FT /note="R->A: Greatly reduces RNA binding and no effect on
FT interaction with ALYREF/THOC4; when associated with A-71,
FT A-78, A-81, A-82, A-89, A-91, A-98, A-100 and A-105."
FT /evidence="ECO:0000269|PubMed:18364396"
FT MUTAGEN 98
FT /note="R->A: Greatly reduces RNA binding and no effect on
FT interaction with ALYREF/THOC4; when associated with A-71,
FT A-78, A-81, A-82, A-89, A-91, A-97, A-100 and A-105."
FT /evidence="ECO:0000269|PubMed:18364396"
FT MUTAGEN 100
FT /note="R->A: Greatly reduces RNA binding and no effect on
FT interaction with ALYREF/THOC4; when associated with A-71,
FT A-78, A-81, A-82, A-89, A-91, A-97, A-98 and A-105."
FT /evidence="ECO:0000269|PubMed:18364396"
FT MUTAGEN 105
FT /note="R->A: Greatly reduces RNA binding and no effect on
FT interaction with ALYREF/THOC4; when associated with A-71,
FT A-78, A-81, A-82, A-89, A-91, A-97, A-98 and A-100."
FT /evidence="ECO:0000269|PubMed:18364396"
FT MUTAGEN 306..308
FT /note="ERE->AAA: Decreases the export of mRNAs from the
FT nucleus."
FT MUTAGEN 383
FT /note="L->R: Diminishes nuclear rim staining and 80%
FT reduction in mRNA export activity; when associated with R-
FT 386. Complete loss of nuclear rim staining and mRNA export
FT activity; when associated with R-386 and A-594."
FT /evidence="ECO:0000269|PubMed:11583626"
FT MUTAGEN 386
FT /note="L->R: Diminishes nuclear rim staining and 80%
FT reduction in mRNA export activity; when associated with R-
FT 383. Complete loss of nuclear rim staining and mRNA export
FT activity; when associated with R-383 and A-594."
FT /evidence="ECO:0000269|PubMed:11583626"
FT MUTAGEN 399
FT /note="D->A: 60% reduction in mRNA export activity."
FT /evidence="ECO:0000269|PubMed:11583626"
FT MUTAGEN 450..453
FT /note="LRFR->AAAA: Abolishes interaction with THOC5 and
FT CHTOP."
FT /evidence="ECO:0000269|PubMed:23299939"
FT MUTAGEN 453
FT /note="R->A: Impairs intramolecular interaction between RBD
FT and NTF2."
FT /evidence="ECO:0000269|PubMed:22893130"
FT MUTAGEN 456..459
FT /note="KHTR->AAAA: Abolishes interaction with THOC5 and
FT CHTOP, no effect on interaction with NXT1; enhances
FT intramolecular interaction between RBD and NTF2, reduces
FT RNA binding and mRNA export."
FT /evidence="ECO:0000269|PubMed:22893130,
FT ECO:0000269|PubMed:23299939"
FT MUTAGEN 456
FT /note="K->D: Impairs intramolecular interaction between RBD
FT and NTF2; when associated with D-459."
FT MUTAGEN 459
FT /note="R->D: Impairs intramolecular interaction between RBD
FT and NTF2; when associated with D-456."
FT MUTAGEN 482
FT /note="D->R: 90% reduction in mRNA export activity."
FT /evidence="ECO:0000269|PubMed:11583626"
FT MUTAGEN 518
FT /note="I->R: 98% reduction in mRNA export activity."
FT /evidence="ECO:0000269|PubMed:11583626"
FT MUTAGEN 521
FT /note="P->Q: 35% reduction in mRNA export activity."
FT /evidence="ECO:0000269|PubMed:11583626"
FT MUTAGEN 594
FT /note="W->A: Suppresses FG-nucleoporin binding. Diminishes
FT nuclear rim staining and 88% reduction in mRNA export
FT activity. Complete loss of nuclear rim staining and mRNA
FT export activity; when associated with R-383 and R-386."
FT /evidence="ECO:0000269|PubMed:11583626"
FT MUTAGEN 595
FT /note="D->R: Suppresses FG-nucleoporin binding."
FT MUTAGEN 617
FT /note="F->A: Suppresses FG-nucleoporin binding."
FT /evidence="ECO:0000269|PubMed:11875519"
FT CONFLICT 119
FT /note="W -> C (in Ref. 8; AAB81111)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="T -> N (in Ref. 3; AAD20016)"
FT /evidence="ECO:0000305"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:3RW6"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:3RW6"
FT HELIX 132..141
FT /evidence="ECO:0007829|PDB:3RW6"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:3RW7"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:3RW6"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:3RW6"
FT HELIX 166..174
FT /evidence="ECO:0007829|PDB:3RW6"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:1FO1"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:3RW6"
FT HELIX 198..201
FT /evidence="ECO:0007829|PDB:3RW6"
FT HELIX 206..218
FT /evidence="ECO:0007829|PDB:3RW6"
FT TURN 222..225
FT /evidence="ECO:0007829|PDB:3RW6"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:3RW6"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:3RW6"
FT HELIX 236..240
FT /evidence="ECO:0007829|PDB:3RW6"
FT HELIX 250..263
FT /evidence="ECO:0007829|PDB:3RW6"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:3RW6"
FT HELIX 281..285
FT /evidence="ECO:0007829|PDB:3RW6"
FT HELIX 286..289
FT /evidence="ECO:0007829|PDB:3RW6"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:3RW6"
FT HELIX 306..312
FT /evidence="ECO:0007829|PDB:3RW6"
FT STRAND 318..321
FT /evidence="ECO:0007829|PDB:3RW6"
FT HELIX 328..330
FT /evidence="ECO:0007829|PDB:3RW6"
FT HELIX 334..344
FT /evidence="ECO:0007829|PDB:3RW6"
FT STRAND 350..353
FT /evidence="ECO:0007829|PDB:3RW6"
FT HELIX 381..398
FT /evidence="ECO:0007829|PDB:1JKG"
FT HELIX 403..408
FT /evidence="ECO:0007829|PDB:1JKG"
FT STRAND 410..419
FT /evidence="ECO:0007829|PDB:1JKG"
FT HELIX 433..436
FT /evidence="ECO:0007829|PDB:1JKG"
FT TURN 442..444
FT /evidence="ECO:0007829|PDB:1JKG"
FT HELIX 448..454
FT /evidence="ECO:0007829|PDB:1JKG"
FT STRAND 455..458
FT /evidence="ECO:0007829|PDB:1JKG"
FT HELIX 459..466
FT /evidence="ECO:0007829|PDB:1JKG"
FT STRAND 472..474
FT /evidence="ECO:0007829|PDB:1JKG"
FT HELIX 476..478
FT /evidence="ECO:0007829|PDB:1JKG"
FT STRAND 480..486
FT /evidence="ECO:0007829|PDB:1JKG"
FT STRAND 491..501
FT /evidence="ECO:0007829|PDB:1JKG"
FT TURN 505..508
FT /evidence="ECO:0007829|PDB:1JKG"
FT STRAND 510..521
FT /evidence="ECO:0007829|PDB:1JKG"
FT STRAND 525..538
FT /evidence="ECO:0007829|PDB:1JKG"
FT HELIX 541..548
FT /evidence="ECO:0007829|PDB:1JKG"
FT STRAND 553..557
FT /evidence="ECO:0007829|PDB:1GO5"
FT HELIX 565..578
FT /evidence="ECO:0007829|PDB:1OAI"
FT HELIX 582..591
FT /evidence="ECO:0007829|PDB:1OAI"
FT TURN 592..594
FT /evidence="ECO:0007829|PDB:1OAI"
FT HELIX 596..608
FT /evidence="ECO:0007829|PDB:1OAI"
FT HELIX 614..617
FT /evidence="ECO:0007829|PDB:1OAI"
SQ SEQUENCE 619 AA; 70182 MW; 338872AADA789FBF CRC64;
MADEGKSYSE HDDERVNFPQ RKKKGRGPFR WKYGEGNRRS GRGGSGIRSS RLEEDDGDVA
MSDAQDGPRV RYNPYTTRPN RRGDTWHDRD RIHVTVRRDR APPERGGAGT SQDGTSKNWF
KITIPYGRKY DKAWLLSMIQ SKCSVPFTPI EFHYENTRAQ FFVEDASTAS ALKAVNYKIL
DRENRRISII INSSAPPHTI LNELKPEQVE QLKLIMSKRY DGSQQALDLK GLRSDPDLVA
QNIDVVLNRR SCMAATLRII EENIPELLSL NLSNNRLYRL DDMSSIVQKA PNLKILNLSG
NELKSERELD KIKGLKLEEL WLDGNSLCDT FRDQSTYISA IRERFPKLLR LDGHELPPPI
AFDVEAPTTL PPCKGSYFGT ENLKSLVLHF LQQYYAIYDS GDRQGLLDAY HDGACCSLSI
PFIPQNPARS SLAEYFKDSR NVKKLKDPTL RFRLLKHTRL NVVAFLNELP KTQHDVNSFV
VDISAQTSTL LCFSVNGVFK EVDGKSRDSL RAFTRTFIAV PASNSGLCIV NDELFVRNAS
SEEIQRAFAM PAPTPSSSPV PTLSPEQQEM LQAFSTQSGM NLEWSQKCLQ DNNWDYTRSA
QAFTHLKAKG EIPEVAFMK
