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Nuclear RNA export factor 1 (Tip-associated protein) (Tip-associating protein) (mRNA export factor TAP)

 NXF1_HUMAN              Reviewed;         619 AA.
Q9UBU9; B4E269; Q99799; Q9UQL2;
27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
30-AUG-2017, entry version 193.
RecName: Full=Nuclear RNA export factor 1;
AltName: Full=Tip-associated protein;
AltName: Full=Tip-associating protein;
AltName: Full=mRNA export factor TAP;
Name=NXF1; Synonyms=TAP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND MUTAGENESIS.
TISSUE=Cervix carcinoma;
PubMed=10202158; DOI=10.1093/emboj/18.7.1953;
Braun I.C., Rohrbach E., Schmitt C., Izaurralde E.;
"TAP binds to the constitutive transport element (CTE) through a novel
RNA-binding motif that is sufficient to promote CTE-dependent RNA
export from the nucleus.";
EMBO J. 18:1953-1965(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=10323864; DOI=10.1101/gad.13.9.1126;
Kang Y., Cullen B.R.;
"The human Tap protein is a nuclear mRNA export factor that contains
novel RNA-binding and nucleocytoplasmic transport sequences.";
Genes Dev. 13:1126-1139(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=10454577; DOI=10.1128/MCB.19.9.6306;
Bear J., Tan W., Zolotukhin A.S., Tabernero C., Hudson E.A.,
Felber B.K.;
"Identification of novel import and export signals of human TAP, the
protein that binds to the constitutive transport element of the type D
retrovirus mRNAs.";
Mol. Cell. Biol. 19:6306-6317(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Lung, and Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 61-619, AND INTERACTION WITH SAIMIRIINE
HERPESVIRUS 2 TIP (MICROBIAL INFECTION).
TISSUE=Lymphocyte;
PubMed=9175835; DOI=10.1016/S1074-7613(00)80345-3;
Yoon D.-W., Lee H., Seol W., DeMaria M., Rosenzweig M., Jung J.U.;
"Tap: a novel cellular protein that interacts with tip of herpesvirus
saimiri and induces lymphocyte aggregation.";
Immunity 6:571-582(1997).
[9]
FUNCTION.
PubMed=9660949; DOI=10.1016/S1097-2765(00)80065-9;
Grueter P., Tabernero C., von Kobbe C., Schmitt C., Saavedra C.,
Bachi A., Wilm M., Felber B.K., Izaurralde E.;
"TAP, the human homolog of Mex67p, mediates CTE-dependent RNA export
from the nucleus.";
Mol. Cell 1:649-659(1998).
[10]
INTERACTION WITH NUPL2.
PubMed=10228171; DOI=10.1093/emboj/18.9.2593;
Katahira J., Straesser K., Podtelejnikov A., Mann M., Jung J.U.,
Hurt E.;
"The Mex67p-mediated nuclear mRNA export pathway is conserved from
yeast to human.";
EMBO J. 18:2593-2609(1999).
[11]
CHARACTERIZATION.
PubMed=11259411; DOI=10.1074/jbc.M100400200;
Braun I.C., Herold A., Rode M., Conti E., Izaurralde E.;
"Overexpression of TAP/p15 heterodimers bypasses nuclear retention and
stimulates nuclear mRNA export.";
J. Biol. Chem. 276:20536-20543(2001).
[12]
CHARACTERIZATION.
PubMed=10668806; DOI=10.1017/S1355838200991994;
Bachi A., Braun I.C., Rodrigues J.P., Pante N., Ribbeck K.,
von Kobbe C., Kutay U., Wilm M., Goerlich D., Carmo-Fonseca M.,
Izaurralde E.;
"The C-terminal domain of TAP interacts with the nuclear pore complex
and promotes export of specific CTE-bearing RNA substrates.";
RNA 6:136-158(2000).
[13]
MUTAGENESIS.
PubMed=11256625; DOI=10.1093/embo-reports/kvd009;
Suyama M., Doerks T., Braun I.C., Sattler M., Izaurralde E., Bork P.;
"Prediction of structural domains of TAP reveals details of its
interaction with p15 and nucleoporins.";
EMBO Rep. 1:53-58(2000).
[14]
INTERACTION WITH ALYREF/THOC4 AND THE EXON JUNCTION COMPLEX.
PubMed=11707413; DOI=10.1093/emboj/20.22.6424;
Kataoka N., Diem M.D., Kim V.N., Yong J., Dreyfuss G.;
"Magoh, a human homolog of Drosophila mago nashi protein, is a
component of the splicing-dependent exon-exon junction complex.";
EMBO J. 20:6424-6433(2001).
[15]
IDENTIFICATION IN A MRNP COMPLEX WITH UPF3A AND UPF3B.
PubMed=11546873; DOI=10.1126/science.1062829;
Kim V.N., Kataoka N., Dreyfuss G.;
"Role of the nonsense-mediated decay factor hUpf3 in the splicing-
dependent exon-exon junction complex.";
Science 293:1832-1836(2001).
[16]
IDENTIFICATION IN A POST-SPLICING COMPLEX WITH RBM8A; UPF1; UPF2;
UPF3A; UPF3B AND RNPS1.
PubMed=11546874; DOI=10.1126/science.1062786;
Lykke-Andersen J., Shu M.-D., Steitz J.A.;
"Communication of the position of exon-exon junctions to the mRNA
surveillance machinery by the protein RNPS1.";
Science 293:1836-1839(2001).
[17]
INTERACTION WITH EIF4A3 AND ALYREF/THOC4.
PubMed=14730019; DOI=10.1261/rna.5230104;
Chan C.C., Dostie J., Diem M.D., Feng W., Mann M., Rappsilber J.,
Dreyfuss G.;
"eIF4A3 is a novel component of the exon junction complex.";
RNA 10:200-209(2004).
[18]
FUNCTION, AND MUTAGENESIS OF ARG-71; ARG-78; ARG-81; ARG-82; ARG-89;
ARG-91; ARG-97; ARG-98; ARG-100 AND ARG-105.
PubMed=18364396; DOI=10.1073/pnas.0709167105;
Hautbergue G.M., Hung M.L., Golovanov A.P., Lian L.Y., Wilson S.A.;
"Mutually exclusive interactions drive handover of mRNA from export
adaptors to TAP.";
Proc. Natl. Acad. Sci. U.S.A. 105:5154-5159(2008).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[20]
INTERACTION WITH FYTTD1.
PubMed=19836239; DOI=10.1016/j.cub.2009.09.041;
Hautbergue G.M., Hung M.L., Walsh M.J., Snijders A.P., Chang C.T.,
Jones R., Ponting C.P., Dickman M.J., Wilson S.A.;
"UIF, a new mRNA export adaptor that works together with REF/ALY,
requires FACT for recruitment to mRNA.";
Curr. Biol. 19:1918-1924(2009).
[21]
FUNCTION, AND INTERACTION WITH ALYREF/THOC4 AND THOC5.
PubMed=19165146; DOI=10.1038/emboj.2009.5;
Katahira J., Inoue H., Hurt E., Yoneda Y.;
"Adaptor Aly and co-adaptor Thoc5 function in the Tap-p15-mediated
nuclear export of HSP70 mRNA.";
EMBO J. 28:556-567(2009).
[22]
INTERACTION WITH FMR1.
PubMed=18936162; DOI=10.1128/MCB.01377-08;
Kim M., Bellini M., Ceman S.;
"Fragile X mental retardation protein FMRP binds mRNAs in the
nucleus.";
Mol. Cell. Biol. 29:214-228(2009).
[23]
SUBCELLULAR LOCATION.
PubMed=19324961; DOI=10.1261/rna.1387009;
Schmidt U., Im K.-B., Benzing C., Janjetovic S., Rippe K., Lichter P.,
Wachsmuth M.;
"Assembly and mobility of exon-exon junction complexes in living
cells.";
RNA 15:862-876(2009).
[24]
INTERACTION WITH HUMAN HERPES VIRUS 1 ICP27 (MICROBIAL INFECTION).
PubMed=19369354; DOI=10.1128/JVI.00375-09;
Johnson L.A., Li L., Sandri-Goldin R.M.;
"The cellular RNA export receptor TAP/NXF1 is required for ICP27-
mediated export of herpes simplex virus 1 RNA, but the TREX complex
adaptor protein Aly/REF appears to be dispensable.";
J. Virol. 83:6335-6346(2009).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[26]
INTERACTION WITH FRG1.
PubMed=21699900; DOI=10.1016/j.jmb.2011.06.014;
Sun C.Y., van Koningsbruggen S., Long S.W., Straasheijm K.,
Klooster R., Jones T.I., Bellini M., Levesque L., Brieher W.M.,
van der Maarel S.M., Jones P.L.;
"Facioscapulohumeral muscular dystrophy region gene 1 is a dynamic
RNA-associated and actin-bundling protein.";
J. Mol. Biol. 411:397-416(2011).
[27]
ASSOCIATION WITH THE TREX COMPLEX, RNA-BINDING, AND MUTAGENESIS OF
ARG-453 AND 456-LYS--ARG-459.
PubMed=22893130; DOI=10.1038/ncomms2005;
Viphakone N., Hautbergue G.M., Walsh M., Chang C.T., Holland A.,
Folco E.G., Reed R., Wilson S.A.;
"TREX exposes the RNA-binding domain of Nxf1 to enable mRNA export.";
Nat. Commun. 3:1006-1006(2012).
[28]
INTERACTION WITH CHTOP; THOC5 AND ALYREF, AND MUTAGENESIS OF
450-LEU--ARG-453 AND 456-LYS--ARG-459.
PubMed=23299939; DOI=10.1038/emboj.2012.342;
Chang C.T., Hautbergue G.M., Walsh M.J., Viphakone N., van Dijk T.B.,
Philipsen S., Wilson S.A.;
"Chtop is a component of the dynamic TREX mRNA export complex.";
EMBO J. 32:473-486(2013).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[30]
SUBCELLULAR LOCATION, AND INTERACTION WITH CHTOP.
PubMed=23826332; DOI=10.1371/journal.pone.0067676;
Teng I.F., Wilson S.A.;
"Mapping interactions between mRNA export factors in living cells.";
PLoS ONE 8:E67676-E67676(2013).
[31]
SUBCELLULAR LOCATION, AND INTERACTION WITH LUZP4.
PubMed=25662211; DOI=10.1093/nar/gkv070;
Viphakone N., Cumberbatch M.G., Livingstone M.J., Heath P.R.,
Dickman M.J., Catto J.W., Wilson S.A.;
"Luzp4 defines a new mRNA export pathway in cancer cells.";
Nucleic Acids Res. 43:2353-2366(2015).
[32]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 102-372.
PubMed=11060011; DOI=10.1093/emboj/19.21.5587;
Liker E., Fernandez E., Izaurralde E., Conti E.;
"The structure of the mRNA export factor TAP reveals a cis arrangement
of a non-canonical RNP domain and an LRR domain.";
EMBO J. 19:5587-5598(2000).
[33]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NXT1, X-RAY
CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH NXT1-FG-REPEAT,
SUBUNIT, DOMAINS, AND MUTAGENESIS OF LEU-383; LEU-386; ASP-399;
ASP-482; ILE-518; PRO-521 AND TRP-594.
PubMed=11583626; DOI=10.1016/S1097-2765(01)00348-3;
Fribourg S., Braun I.C., Izaurralde E., Conti E.;
"Structural basis for the recognition of a nucleoporin FG repeat by
the NTF2-like domain of the TAP/p15 mRNA nuclear export factor.";
Mol. Cell 8:645-656(2001).
[34]
X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF 561-619 IN COMPLEX WITH
RANBP3.
PubMed=12581645; DOI=10.1016/S0022-2836(02)01474-2;
Grant R.P., Neuhaus D., Stewart M.;
"Structural basis for the interaction between the Tap/NXF1 UBA domain
and FG nucleoporins at 1A resolution.";
J. Mol. Biol. 326:849-858(2003).
[35]
STRUCTURE BY NMR OF 551-619, AND MUTAGENESIS OF PHE-617.
PubMed=11875519; DOI=10.1038/nsb773;
Grant R.P., Hurt E., Neuhaus D., Stewart M.;
"Structure of the C-terminal FG-nucleoporin binding domain of
Tap/NXF1.";
Nat. Struct. Biol. 9:247-251(2002).
-!- FUNCTION: Involved in the nuclear export of mRNA species bearing
retroviral constitutive transport elements (CTE) and in the export
of mRNA from the nucleus to the cytoplasm (TAP/NFX1 pathway). The
NXF1-NXT1 heterodimer is involved in the export of HSP70 mRNA in
conjunction with ALYREF/THOC4 and THOC5 components of the TREX
complex. ALYREF/THOC4-bound mRNA is thought to be transferred to
the NXF1-NXT1 heterodimer for export.
{ECO:0000269|PubMed:18364396, ECO:0000269|PubMed:19165146,
ECO:0000269|PubMed:9660949}.
-!- SUBUNIT: Heterodimer with NXT1 (PubMed:11583626). The formation of
NXF1-NXT1 heterodimers is required for the NXF1-mediated nuclear
mRNA export (PubMed:11583626). Found in a post-splicing complex
with RBM8A, UPF1, UPF2, UPF3A, UPF3B and RNPS1 (PubMed:11546874).
Interacts (via NTF2 domain) with NXT1 (PubMed:11583626). Interacts
with ALYREF/THOC4 (PubMed:11707413, PubMed:14730019,
PubMed:19165146, PubMed:23299939). Interacts with FYTTD1/UIF
(PubMed:19836239). Interacts with EIF4A3 (PubMed:14730019).
Interacts with NUPL2 (PubMed:10228171). Interacts with THOC5
(PubMed:19165146, PubMed:23299939). Interacts with CHTOP
(PubMed:23299939, PubMed:23826332). Interacts with FRG1 (via N-
terminus) (PubMed:21699900). Interacts with LUZP4
(PubMed:25662211). Interacts with FMR1; the interaction occurs in
a mRNA-dependent and polyribosomes-independent manner in the
nucleus (PubMed:18936162). Associates with the exon junction
complex (EJC) and with the transcription/export (TREX) complex
(PubMed:11707413, PubMed:22893130). Found in a mRNA complex with
UPF3A and UPF3B (PubMed:11546873). {ECO:0000269|PubMed:10228171,
ECO:0000269|PubMed:11546873, ECO:0000269|PubMed:11546874,
ECO:0000269|PubMed:11583626, ECO:0000269|PubMed:11707413,
ECO:0000269|PubMed:12581645, ECO:0000269|PubMed:14730019,
ECO:0000269|PubMed:18936162, ECO:0000269|PubMed:19165146,
ECO:0000269|PubMed:19369354, ECO:0000269|PubMed:19836239,
ECO:0000269|PubMed:21699900, ECO:0000269|PubMed:22893130,
ECO:0000269|PubMed:23299939, ECO:0000269|PubMed:23826332,
ECO:0000269|PubMed:25662211, ECO:0000269|PubMed:9175835}.
-!- SUBUNIT: (Microbial infection) Interacts with Saimiriine
herpesvirus 2 TIP protein. {ECO:0000269|PubMed:9175835}.
-!- SUBUNIT: (Microbial infection) Interacts with human herpes virus 1
(HHV-1) ICP27 protein; this interaction allows efficient export of
HHV-1 early and late transcripts. {ECO:0000269|PubMed:19369354}.
-!- INTERACTION:
P22575:- (xeno); NbExp=6; IntAct=EBI-398874, EBI-866709;
Q86V81:ALYREF; NbExp=4; IntAct=EBI-398874, EBI-347640;
Q9BYV9:BACH2; NbExp=4; IntAct=EBI-398874, EBI-1642333;
Q9Y3Y2:CHTOP; NbExp=9; IntAct=EBI-398874, EBI-347794;
O00571:DDX3X; NbExp=5; IntAct=EBI-398874, EBI-353779;
Q08211:DHX9; NbExp=8; IntAct=EBI-398874, EBI-352022;
Q92997:DVL3; NbExp=3; IntAct=EBI-398874, EBI-739789;
P14136:GFAP; NbExp=5; IntAct=EBI-398874, EBI-744302;
Q9H079:KATNBL1; NbExp=4; IntAct=EBI-398874, EBI-715394;
Q6A162:KRT40; NbExp=3; IntAct=EBI-398874, EBI-10171697;
O95751:LDOC1; NbExp=3; IntAct=EBI-398874, EBI-740738;
Q9UJV3-2:MID2; NbExp=3; IntAct=EBI-398874, EBI-10172526;
P37198:NUP62; NbExp=8; IntAct=EBI-398874, EBI-347978;
Q9UKK6:NXT1; NbExp=5; IntAct=EBI-398874, EBI-301889;
P31321:PRKAR1B; NbExp=4; IntAct=EBI-398874, EBI-2805516;
Q8IX06:REXO1L1P; NbExp=4; IntAct=EBI-398874, EBI-10262361;
Q07955:SRSF1; NbExp=5; IntAct=EBI-398874, EBI-398920;
P84103:SRSF3; NbExp=4; IntAct=EBI-398874, EBI-372557;
Q16629:SRSF7; NbExp=4; IntAct=EBI-398874, EBI-398885;
Q9Y2W1:THRAP3; NbExp=4; IntAct=EBI-398874, EBI-352039;
Q96CG3:TIFA; NbExp=5; IntAct=EBI-398874, EBI-740711;
Q13625-3:TP53BP2; NbExp=3; IntAct=EBI-398874, EBI-10175039;
Q9UMX0:UBQLN1; NbExp=4; IntAct=EBI-398874, EBI-741480;
P10238:UL54 (xeno); NbExp=4; IntAct=EBI-398874, EBI-6883946;
-!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
{ECO:0000269|PubMed:19324961, ECO:0000269|PubMed:23826332}.
Nucleus speckle {ECO:0000269|PubMed:19324961,
ECO:0000269|PubMed:23826332}. Cytoplasm
{ECO:0000269|PubMed:19324961}. Nucleus
{ECO:0000269|PubMed:25662211}. Note=Localized predominantly in the
nucleoplasm and at both the nucleoplasmic and cytoplasmic faces of
the nuclear pore complex. Shuttles between the nucleus and the
cytoplasm. Travels to the cytoplasm as part of the exon junction
complex (EJC) bound to mRNA. The association with the TREX complex
seems to occur in regions surrounding nuclear speckles known as
perispeckles (PubMed:23826332). Nucleus; nuclear rim
(PubMed:25662211). {ECO:0000269|PubMed:23826332,
ECO:0000269|PubMed:25662211}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9UBU9-1; Sequence=Displayed;
Name=2;
IsoId=Q9UBU9-2; Sequence=VSP_041427, VSP_041428;
-!- TISSUE SPECIFICITY: Expressed ubiquitously.
-!- DOMAIN: The minimal CTE binding domain consists of an RNP-type RNA
binding domain (RBD) and leucine-rich repeats.
{ECO:0000269|PubMed:11583626}.
-!- DOMAIN: The nucleoporin binding domain consists of a NTF2 domain
(also called NTF2-like domain) and a TAP-C domain (also called
UBA-like domain). It has 2 nucleoporin-FG-repeats binding sites
(one in the NTF2 and the other in the TAP-C domain) which
contribute to nucleoporin association and act synergistically to
export cellular mRNAs. {ECO:0000269|PubMed:11583626}.
-!- DOMAIN: The NTF2 domain is functional only in the presence of NXT1
and is essential for the export of mRNA from the nucleus. It
inhibits RNA binding activity through an intramolecular
interaction with the N-terminal RNA binding domain (RBD); the
inhibition is removed by an association with the TREX complex,
specifically involving ALYREF/THOC4 and THOC5.
{ECO:0000269|PubMed:11583626}.
-!- DOMAIN: The TAP-C domain mediates direct interactions with
nucleoporin-FG-repeats and is necessary and sufficient for
localization of NXF1 to the nuclear rim. The conserved loop 594-
NWD-596 of the TAP-C domain has a critical role in the interaction
with nucleoporins. {ECO:0000269|PubMed:11583626}.
-!- DOMAIN: The leucine-rich repeats are essential for the export of
mRNA from the nucleus. {ECO:0000269|PubMed:11583626}.
-!- DOMAIN: The RNA-binding domain is a non-canonical RNP-type domain.
{ECO:0000269|PubMed:11583626}.
-!- SIMILARITY: Belongs to the NXF family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AJ132712; CAA10753.1; -; mRNA.
EMBL; AF112880; AAD39102.1; -; mRNA.
EMBL; AF126246; AAD20016.1; -; mRNA.
EMBL; AK304137; BAG65031.1; -; mRNA.
EMBL; AK027192; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AP001160; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471076; EAW74105.1; -; Genomic_DNA.
EMBL; BC004904; AAH04904.1; -; mRNA.
EMBL; BC028041; AAH28041.1; -; mRNA.
EMBL; U80073; AAB81111.1; -; mRNA.
CCDS; CCDS44629.1; -. [Q9UBU9-2]
CCDS; CCDS8037.1; -. [Q9UBU9-1]
RefSeq; NP_001074960.1; NM_001081491.1. [Q9UBU9-2]
RefSeq; NP_006353.2; NM_006362.4. [Q9UBU9-1]
UniGene; Hs.523739; -.
UniGene; Hs.601546; -.
PDB; 1FO1; X-ray; 2.90 A; A/B=102-372.
PDB; 1FT8; X-ray; 3.15 A; A/B/C/D/E=102-372.
PDB; 1GO5; NMR; -; A=551-619.
PDB; 1JKG; X-ray; 1.90 A; B=371-619.
PDB; 1JN5; X-ray; 2.80 A; B=371-619.
PDB; 1KOH; X-ray; 3.80 A; A/B/C/D=96-372.
PDB; 1KOO; X-ray; 3.80 A; A/B/C/D=96-372.
PDB; 1OAI; X-ray; 1.00 A; A=561-619.
PDB; 2Z5K; X-ray; 2.60 A; B=53-82.
PDB; 2Z5M; X-ray; 3.00 A; B=53-82.
PDB; 3RW6; X-ray; 2.30 A; A/B=96-362.
PDB; 3RW7; X-ray; 3.00 A; A/B/C/D=96-362.
PDB; 4WYK; X-ray; 3.40 A; A/C=96-555.
PDBsum; 1FO1; -.
PDBsum; 1FT8; -.
PDBsum; 1GO5; -.
PDBsum; 1JKG; -.
PDBsum; 1JN5; -.
PDBsum; 1KOH; -.
PDBsum; 1KOO; -.
PDBsum; 1OAI; -.
PDBsum; 2Z5K; -.
PDBsum; 2Z5M; -.
PDBsum; 3RW6; -.
PDBsum; 3RW7; -.
PDBsum; 4WYK; -.
ProteinModelPortal; Q9UBU9; -.
SMR; Q9UBU9; -.
BioGrid; 115745; 1131.
DIP; DIP-31789N; -.
IntAct; Q9UBU9; 103.
MINT; MINT-121360; -.
STRING; 9606.ENSP00000294172; -.
TCDB; 3.A.18.1.1; the nuclear mrna exporter (mrna-e) family.
iPTMnet; Q9UBU9; -.
PhosphoSitePlus; Q9UBU9; -.
BioMuta; NXF1; -.
DMDM; 20139282; -.
EPD; Q9UBU9; -.
PaxDb; Q9UBU9; -.
PeptideAtlas; Q9UBU9; -.
PRIDE; Q9UBU9; -.
DNASU; 10482; -.
Ensembl; ENST00000294172; ENSP00000294172; ENSG00000162231. [Q9UBU9-1]
Ensembl; ENST00000531709; ENSP00000453885; ENSG00000162231. [Q9UBU9-2]
Ensembl; ENST00000532297; ENSP00000436679; ENSG00000162231. [Q9UBU9-1]
GeneID; 10482; -.
KEGG; hsa:10482; -.
UCSC; uc001nvf.1; human. [Q9UBU9-1]
CTD; 10482; -.
DisGeNET; 10482; -.
GeneCards; NXF1; -.
HGNC; HGNC:8071; NXF1.
HPA; CAB016327; -.
HPA; HPA061593; -.
MIM; 602647; gene.
neXtProt; NX_Q9UBU9; -.
OpenTargets; ENSG00000162231; -.
PharmGKB; PA31858; -.
eggNOG; KOG3763; Eukaryota.
eggNOG; ENOG410XR55; LUCA.
GeneTree; ENSGT00390000007539; -.
HOGENOM; HOG000236269; -.
HOVERGEN; HBG013199; -.
InParanoid; Q9UBU9; -.
KO; K14284; -.
OMA; SYFGTET; -.
OrthoDB; EOG091G04QA; -.
PhylomeDB; Q9UBU9; -.
TreeFam; TF314566; -.
Reactome; R-HSA-159227; Transport of the SLBP independent Mature mRNA.
Reactome; R-HSA-159230; Transport of the SLBP Dependant Mature mRNA.
Reactome; R-HSA-159231; Transport of Mature mRNA Derived from an Intronless Transcript.
Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
SIGNOR; Q9UBU9; -.
ChiTaRS; NXF1; human.
EvolutionaryTrace; Q9UBU9; -.
GeneWiki; NXF1; -.
GenomeRNAi; 10482; -.
PRO; PR:Q9UBU9; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000162231; -.
CleanEx; HS_NXF1; -.
ExpressionAtlas; Q9UBU9; baseline and differential.
Genevisible; Q9UBU9; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0042405; C:nuclear inclusion body; IEA:Ensembl.
GO; GO:0005643; C:nuclear pore; IEA:Ensembl.
GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003729; F:mRNA binding; IEA:Ensembl.
GO; GO:0005487; F:nucleocytoplasmic transporter activity; IEA:Ensembl.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0003727; F:single-stranded RNA binding; IDA:UniProtKB.
GO; GO:0006406; P:mRNA export from nucleus; IDA:UniProtKB.
GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IBA:GO_Central.
GO; GO:0006405; P:RNA export from nucleus; TAS:Reactome.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
CDD; cd00780; NTF2; 1.
CDD; cd14342; UBA_TAP-C; 1.
Gene3D; 3.80.10.10; -; 1.
InterPro; IPR032675; L_dom-like.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR002075; NTF2.
InterPro; IPR032710; NTF2-like_dom.
InterPro; IPR018222; Nuclear_transport_factor_2_euk.
InterPro; IPR030217; NXF_fam.
InterPro; IPR000504; RRM_dom.
InterPro; IPR005637; TAP_C_dom.
InterPro; IPR015245; Tap_RNA-bd.
InterPro; IPR009060; UBA-like.
PANTHER; PTHR10662; PTHR10662; 1.
Pfam; PF02136; NTF2; 1.
Pfam; PF09162; Tap-RNA_bind; 1.
Pfam; PF03943; TAP_C; 1.
ProDom; PD043466; Tap_RNA_bd; 1.
SMART; SM00804; TAP_C; 1.
SUPFAM; SSF46934; SSF46934; 1.
SUPFAM; SSF52058; SSF52058; 1.
SUPFAM; SSF54427; SSF54427; 1.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS51450; LRR; 3.
PROSITE; PS50177; NTF2_DOMAIN; 1.
PROSITE; PS51281; TAP_C; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; Host-virus interaction; Leucine-rich repeat; Methylation;
mRNA transport; Nitration; Nucleus; Phosphoprotein;
Reference proteome; Repeat; RNA-binding; Transport.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}.
CHAIN 2 619 Nuclear RNA export factor 1.
/FTId=PRO_0000220529.
DOMAIN 119 198 RRM.
REPEAT 266 291 LRR 1.
REPEAT 292 315 LRR 2.
REPEAT 316 343 LRR 3.
REPEAT 344 371 LRR 4.
DOMAIN 386 536 NTF2. {ECO:0000255|PROSITE-
ProRule:PRU00137}.
DOMAIN 565 619 TAP-C. {ECO:0000255|PROSITE-
ProRule:PRU00611}.
REGION 2 198 Interaction with ALYREF/THOC4 and LUZP4.
{ECO:0000269|PubMed:25662211}.
REGION 2 118 RNA-binding (RBD).
REGION 2 60 Minor non-specific RNA-binding.
REGION 61 118 Major non-specific RNA-binding.
MOTIF 67 100 Nuclear localization signal.
MOTIF 83 110 Nuclear export signal.
COMPBIAS 551 561 Pro-rich.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 9 9 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 42 42 Asymmetric dimethylarginine; alternate.
{ECO:0000250|UniProtKB:Q99JX7}.
MOD_RES 42 42 Omega-N-methylarginine; alternate.
{ECO:0000250|UniProtKB:Q99JX7}.
MOD_RES 126 126 Nitrated tyrosine.
{ECO:0000250|UniProtKB:Q99JX7}.
VAR_SEQ 339 356 SAIRERFPKLLRLDGHEL -> RSVVACVSPPGDLHPLGG
(in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_041427.
VAR_SEQ 357 619 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_041428.
MUTAGEN 71 71 R->A: Greatly reduces RNA binding and no
effect on interaction with ALYREF/THOC4;
when associated with A-78, A-81, A-82, A-
89, A-91, A-97, A-98, A-100 and A-105.
{ECO:0000269|PubMed:18364396}.
MUTAGEN 78 78 R->A: Greatly reduces RNA binding and no
effect on interaction with ALYREF/THOC4;
when associated with A-71, A-81, A-82, A-
89, A-91, A-97, A-98, A-100 and A-105.
{ECO:0000269|PubMed:18364396}.
MUTAGEN 81 81 R->A: Greatly reduces RNA binding and no
effect on interaction with ALYREF/THOC4;
when associated with A-71, A-78, A-82, A-
89, A-91, A-97, A-98, A-100 and A-105.
{ECO:0000269|PubMed:18364396}.
MUTAGEN 82 82 R->A: Greatly reduces RNA binding and no
effect on interaction with ALYREF/THOC4;
when associated with A-71, A-78, A-81, A-
89, A-91, A-97, A-98, A-100 and A-105.
{ECO:0000269|PubMed:18364396}.
MUTAGEN 89 89 R->A: Greatly reduces RNA binding and no
effect on interaction with ALYREF/THOC4;
when associated with A-71, A-78, A-81, A-
82, A-91, A-97, A-98, A-100 and A-105.
{ECO:0000269|PubMed:18364396}.
MUTAGEN 91 91 R->A: Greatly reduces RNA binding and no
effect on interaction with ALYREF/THOC4;
when associated with A-71, A-78, A-81, A-
82, A-89, A-97, A-98, A-100 and A-105.
{ECO:0000269|PubMed:18364396}.
MUTAGEN 97 97 R->A: Greatly reduces RNA binding and no
effect on interaction with ALYREF/THOC4;
when associated with A-71, A-78, A-81, A-
82, A-89, A-91, A-98, A-100 and A-105.
{ECO:0000269|PubMed:18364396}.
MUTAGEN 98 98 R->A: Greatly reduces RNA binding and no
effect on interaction with ALYREF/THOC4;
when associated with A-71, A-78, A-81, A-
82, A-89, A-91, A-97, A-100 and A-105.
{ECO:0000269|PubMed:18364396}.
MUTAGEN 100 100 R->A: Greatly reduces RNA binding and no
effect on interaction with ALYREF/THOC4;
when associated with A-71, A-78, A-81, A-
82, A-89, A-91, A-97, A-98 and A-105.
{ECO:0000269|PubMed:18364396}.
MUTAGEN 105 105 R->A: Greatly reduces RNA binding and no
effect on interaction with ALYREF/THOC4;
when associated with A-71, A-78, A-81, A-
82, A-89, A-91, A-97, A-98 and A-100.
{ECO:0000269|PubMed:18364396}.
MUTAGEN 306 308 ERE->AAA: Decreases the export of mRNAs
from the nucleus.
MUTAGEN 383 383 L->R: Diminishes nuclear rim staining and
80% reduction in mRNA export activity;
when associated with R-386. Complete loss
of nuclear rim staining and mRNA export
activity; when associated with R-386 and
A-594. {ECO:0000269|PubMed:11583626}.
MUTAGEN 386 386 L->R: Diminishes nuclear rim staining and
80% reduction in mRNA export activity;
when associated with R-383. Complete loss
of nuclear rim staining and mRNA export
activity; when associated with R-383 and
A-594. {ECO:0000269|PubMed:11583626}.
MUTAGEN 399 399 D->A: 60% reduction in mRNA export
activity. {ECO:0000269|PubMed:11583626}.
MUTAGEN 450 453 LRFR->AAAA: Abolishes interaction with
THOC5 and CHTOP.
{ECO:0000269|PubMed:23299939}.
MUTAGEN 453 453 R->A: Impairs intramolecular interaction
between RBD and NTF2.
{ECO:0000269|PubMed:22893130}.
MUTAGEN 456 459 KHTR->AAAA: Abolishes interaction with
THOC5 and CHTOP, no effect on interaction
with NXT1; enhances intramolecular
interaction between RBD and NTF2, reduces
RNA binding and mRNA export.
{ECO:0000269|PubMed:22893130,
ECO:0000269|PubMed:23299939}.
MUTAGEN 456 456 K->D: Impairs intramolecular interaction
between RBD and NTF2; when associated
with D-459.
MUTAGEN 459 459 R->D: Impairs intramolecular interaction
between RBD and NTF2; when associated
with D-456.
MUTAGEN 482 482 D->R: 90% reduction in mRNA export
activity. {ECO:0000269|PubMed:11583626}.
MUTAGEN 518 518 I->R: 98% reduction in mRNA export
activity. {ECO:0000269|PubMed:11583626}.
MUTAGEN 521 521 P->Q: 35% reduction in mRNA export
activity. {ECO:0000269|PubMed:11583626}.
MUTAGEN 594 594 W->A: Suppresses FG-nucleoporin binding.
Diminishes nuclear rim staining and 88%
reduction in mRNA export activity.
Complete loss of nuclear rim staining and
mRNA export activity; when associated
with R-383 and R-386.
{ECO:0000269|PubMed:11583626}.
MUTAGEN 595 595 D->R: Suppresses FG-nucleoporin binding.
MUTAGEN 617 617 F->A: Suppresses FG-nucleoporin binding.
{ECO:0000269|PubMed:11875519}.
CONFLICT 119 119 W -> C (in Ref. 8; AAB81111).
{ECO:0000305}.
CONFLICT 256 256 T -> N (in Ref. 3; AAD20016).
{ECO:0000305}.
STRAND 120 124 {ECO:0000244|PDB:3RW6}.
HELIX 127 129 {ECO:0000244|PDB:3RW6}.
HELIX 132 141 {ECO:0000244|PDB:3RW6}.
STRAND 143 145 {ECO:0000244|PDB:3RW7}.
STRAND 150 155 {ECO:0000244|PDB:3RW6}.
STRAND 158 164 {ECO:0000244|PDB:3RW6}.
HELIX 166 174 {ECO:0000244|PDB:3RW6}.
TURN 176 178 {ECO:0000244|PDB:1FO1}.
STRAND 190 193 {ECO:0000244|PDB:3RW6}.
HELIX 198 201 {ECO:0000244|PDB:3RW6}.
HELIX 206 218 {ECO:0000244|PDB:3RW6}.
TURN 222 225 {ECO:0000244|PDB:3RW6}.
STRAND 226 228 {ECO:0000244|PDB:3RW6}.
HELIX 232 234 {ECO:0000244|PDB:3RW6}.
HELIX 236 240 {ECO:0000244|PDB:3RW6}.
HELIX 250 263 {ECO:0000244|PDB:3RW6}.
STRAND 269 271 {ECO:0000244|PDB:3RW6}.
HELIX 281 285 {ECO:0000244|PDB:3RW6}.
HELIX 286 289 {ECO:0000244|PDB:3RW6}.
STRAND 295 297 {ECO:0000244|PDB:3RW6}.
HELIX 306 312 {ECO:0000244|PDB:3RW6}.
STRAND 318 321 {ECO:0000244|PDB:3RW6}.
HELIX 328 330 {ECO:0000244|PDB:3RW6}.
HELIX 334 344 {ECO:0000244|PDB:3RW6}.
STRAND 350 353 {ECO:0000244|PDB:3RW6}.
HELIX 381 398 {ECO:0000244|PDB:1JKG}.
HELIX 403 408 {ECO:0000244|PDB:1JKG}.
STRAND 410 419 {ECO:0000244|PDB:1JKG}.
HELIX 433 436 {ECO:0000244|PDB:1JKG}.
TURN 442 444 {ECO:0000244|PDB:1JKG}.
HELIX 448 454 {ECO:0000244|PDB:1JKG}.
STRAND 455 458 {ECO:0000244|PDB:1JKG}.
HELIX 459 466 {ECO:0000244|PDB:1JKG}.
STRAND 472 474 {ECO:0000244|PDB:1JKG}.
HELIX 476 478 {ECO:0000244|PDB:1JKG}.
STRAND 480 486 {ECO:0000244|PDB:1JKG}.
STRAND 491 501 {ECO:0000244|PDB:1JKG}.
TURN 505 508 {ECO:0000244|PDB:1JKG}.
STRAND 510 521 {ECO:0000244|PDB:1JKG}.
STRAND 525 538 {ECO:0000244|PDB:1JKG}.
HELIX 541 548 {ECO:0000244|PDB:1JKG}.
STRAND 553 557 {ECO:0000244|PDB:1GO5}.
HELIX 565 578 {ECO:0000244|PDB:1OAI}.
HELIX 582 591 {ECO:0000244|PDB:1OAI}.
TURN 592 594 {ECO:0000244|PDB:1OAI}.
HELIX 596 608 {ECO:0000244|PDB:1OAI}.
HELIX 614 617 {ECO:0000244|PDB:1OAI}.
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


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