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 27-MAR-2024, entry version 238. 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 EPSTEIN BARR VIRUS MRNA EXPORT FACTOR ICP27 HOMOLOG RP (MICROBIAL INFECTION). RX PubMed=19793817; DOI=10.1128/jvi.01276-09; RA Juillard F., Hiriart E., Sergeant N., Vingtdeux-Didier V., Drobecq H., RA Sergeant A., Manet E., Gruffat H.; RT "Epstein-Barr virus protein EB2 contains an N-terminal transferable nuclear RT export signal that promotes nucleocytoplasmic export by directly binding RT TAP/NXF1."; RL J. Virol. 83:12759-12768(2009). RN [32] 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 [33] 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 [34] 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 [35] 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 [36] 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 [37] 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 [38] 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 [39] 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 [40] 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 [41] 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 [42] 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 [43] 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 [44] 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 [45] 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 [46] 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 -!- SUBUNIT: (Microbial infection) Interacts with Epstein Barr virus (EBV) CC mRNA export factor ICP27 homolog; this interaction plays a role in mRNA CC export. {ECO:0000269|PubMed:19793817}. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 1363. 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; 168. DR MINT; Q9UBU9; -. DR STRING; 9606.ENSP00000436679; -. DR TCDB; 3.A.18.1.1; the nuclear mrna exporter (mrna-e) family. DR GlyGen; Q9UBU9; 2 sites, 1 O-linked glycan (2 sites). 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; 9606-ENSP00000436679; -. DR PeptideAtlas; Q9UBU9; -. DR ProteomicsDB; 84075; -. [Q9UBU9-1] DR ProteomicsDB; 84076; -. [Q9UBU9-2] DR Pumba; Q9UBU9; -. DR Antibodypedia; 4277; 346 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 AGR; HGNC:8071; -. 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; 21687at2759; -. 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; 537 hits in 1165 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 93 other cell types or tissues. DR ExpressionAtlas; Q9UBU9; baseline and differential. 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; 3.10.450.50; -; 1. DR Gene3D; 3.30.70.330; -; 1. DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1. DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 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; NUCLEAR RNA EXPORT FACTOR; 1. DR PANTHER; PTHR10662:SF27; NUCLEAR RNA EXPORT FACTOR 1; 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; SSF52058; L domain-like; 1. DR SUPFAM; SSF54427; NTF2-like; 1. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1. DR SUPFAM; SSF46934; UBA-like; 1. DR PROSITE; PS51450; LRR; 3. DR PROSITE; PS50177; NTF2_DOMAIN; 1. DR PROSITE; PS51281; TAP_C; 1. DR Genevisible; Q9UBU9; HS. 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 FT R-386. Complete loss of nuclear rim staining and mRNA FT export 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 FT R-383. Complete loss of nuclear rim staining and mRNA FT export 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 //