NXT1_HUMAN
ID NXT1_HUMAN Reviewed; 140 AA.
AC Q9UKK6;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=NTF2-related export protein 1;
DE AltName: Full=Protein p15;
GN Name=NXT1;
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], FUNCTION, AND INTERACTION WITH RANBP2.
RX PubMed=10567585; DOI=10.1128/mcb.19.12.8616;
RA Black B.E., Levesque L., Holaska J.M., Wood T.C., Paschal B.M.;
RT "Identification of an NTF2-related factor that binds Ran-GTP and regulates
RT nuclear protein export.";
RL Mol. Cell. Biol. 19:8616-8624(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, Placenta, and Uterus;
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 [4]
RP FUNCTION.
RX PubMed=10848583; DOI=10.1128/mcb.20.13.4562-4571.2000;
RA Ossareh-Nazari B., Maison C., Black B.E., Levesque L., Paschal B.M.,
RA Dargemont C.;
RT "RanGTP-binding protein NXT1 facilitates nuclear export of different
RT classes of RNA in vitro.";
RL Mol. Cell. Biol. 20:4562-4571(2000).
RN [5]
RP FUNCTION.
RX PubMed=11259602; DOI=10.1128/mcb.21.7.2545-2554.2001;
RA Guzik B.W., Levesque L., Prasad S., Bor Y.C., Black B.E., Paschal B.M.,
RA Rekosh D., Hammarskjold M.L.;
RT "NXT1 (p15) is a crucial cellular cofactor in TAP-dependent export of
RT intron-containing RNA in mammalian cells.";
RL Mol. Cell. Biol. 21:2545-2554(2001).
RN [6]
RP IDENTIFICATION IN A COMPLEX WITH RANGAP1; RANBP2 AND NXF1.
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 [7]
RP FUNCTION.
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 [8]
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=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), SUBUNIT, AND MUTAGENESIS OF ILE-114
RP AND ARG-134.
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).
CC -!- FUNCTION: Stimulator of protein export for NES-containing proteins
CC (PubMed:10567585). Also plays a role in the nuclear export of U1 snRNA,
CC tRNA, and mRNA (PubMed:10848583). The NXF1-NXT1 heterodimer is involved
CC in the export of HSP70 mRNA in conjunction with ALYREF/THOC4 and THOC5
CC (PubMed:19165146, PubMed:11259602). {ECO:0000269|PubMed:10567585,
CC ECO:0000269|PubMed:10848583, ECO:0000269|PubMed:11259602,
CC ECO:0000269|PubMed:19165146}.
CC -!- SUBUNIT: Heterodimer with NXF1 (PubMed:11583626). Forms a complex with
CC RANGAP1, RANBP2/NUP358 and NXF1 (PubMed:14729961). Interacts (via NTF2
CC domain) with NXF1 (PubMed:11583626). Stabilizes the NTF2 domain of NXF1
CC by heterodimerization (PubMed:11583626). The formation of NXF1-NXT1
CC heterodimers is required for the NXF1-mediated nuclear mRNA export
CC (PubMed:11583626). Preferentially binds Ran-GTP (PubMed:10567585).
CC Associates with NXF2, NXF3 and NXF5. Does not bind nucleoporins (NPC)
CC directly, its association to NPC is mediated by NXF1 (PubMed:11583626).
CC {ECO:0000269|PubMed:10567585, ECO:0000269|PubMed:11583626,
CC ECO:0000269|PubMed:14729961}.
CC -!- INTERACTION:
CC Q9UKK6; Q8IX29: FBXO16; NbExp=5; IntAct=EBI-301889, EBI-12063229;
CC Q9UKK6; Q9UBU9: NXF1; NbExp=6; IntAct=EBI-301889, EBI-398874;
CC Q9UKK6; Q9H4D5: NXF3; NbExp=16; IntAct=EBI-301889, EBI-750038;
CC Q9UKK6; Q6ZW49-2: PAXIP1; NbExp=3; IntAct=EBI-301889, EBI-10236271;
CC Q9UKK6; O95793: STAU1; NbExp=6; IntAct=EBI-301889, EBI-358174;
CC Q9UKK6; Q82506: NS; Xeno; NbExp=5; IntAct=EBI-301889, EBI-6149498;
CC Q9UKK6; Q9BP41: Ranbp21; Xeno; NbExp=2; IntAct=EBI-301889, EBI-301896;
CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus speckle {ECO:0000305}.
CC Cytoplasm. Note=Shuttles between the nucleus and the cytoplasm.
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DR EMBL; AF156957; AAD54942.1; -; mRNA.
DR EMBL; AL096677; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000759; AAH00759.1; -; mRNA.
DR EMBL; BC002687; AAH02687.1; -; mRNA.
DR EMBL; BC003029; AAH03029.1; -; mRNA.
DR EMBL; BC003410; AAH03410.1; -; mRNA.
DR CCDS; CCDS13150.1; -.
DR RefSeq; NP_037380.1; NM_013248.2.
DR RefSeq; XP_011527532.1; XM_011529230.2.
DR PDB; 1JKG; X-ray; 1.90 A; A=1-140.
DR PDB; 1JN5; X-ray; 2.80 A; A=1-140.
DR PDB; 4WYK; X-ray; 3.40 A; B/D=2-140.
DR PDB; 6E5U; X-ray; 3.80 A; B/D/F/H=1-140.
DR PDBsum; 1JKG; -.
DR PDBsum; 1JN5; -.
DR PDBsum; 4WYK; -.
DR PDBsum; 6E5U; -.
DR AlphaFoldDB; Q9UKK6; -.
DR SMR; Q9UKK6; -.
DR BioGRID; 118875; 33.
DR ComplexPortal; CPX-2433; mRNA nuclear export factor NXF5-NXT1.
DR ComplexPortal; CPX-2436; mRNA nuclear export factor complex, NXF3-NXT1.
DR ComplexPortal; CPX-725; mRNA nuclear export factor NXF1-NXT1.
DR ComplexPortal; CPX-925; mRNA nuclear export factor complex, NXF2-NXT1.
DR DIP; DIP-33075N; -.
DR IntAct; Q9UKK6; 17.
DR MINT; Q9UKK6; -.
DR STRING; 9606.ENSP00000254998; -.
DR GlyGen; Q9UKK6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UKK6; -.
DR PhosphoSitePlus; Q9UKK6; -.
DR BioMuta; NXT1; -.
DR DMDM; 18203504; -.
DR EPD; Q9UKK6; -.
DR jPOST; Q9UKK6; -.
DR MassIVE; Q9UKK6; -.
DR MaxQB; Q9UKK6; -.
DR PaxDb; Q9UKK6; -.
DR PeptideAtlas; Q9UKK6; -.
DR PRIDE; Q9UKK6; -.
DR ProteomicsDB; 84812; -.
DR TopDownProteomics; Q9UKK6; -.
DR Antibodypedia; 24862; 109 antibodies from 21 providers.
DR DNASU; 29107; -.
DR Ensembl; ENST00000254998.3; ENSP00000254998.2; ENSG00000132661.4.
DR GeneID; 29107; -.
DR KEGG; hsa:29107; -.
DR MANE-Select; ENST00000254998.3; ENSP00000254998.2; NM_013248.3; NP_037380.1.
DR UCSC; uc002wsx.2; human.
DR CTD; 29107; -.
DR DisGeNET; 29107; -.
DR GeneCards; NXT1; -.
DR HGNC; HGNC:15913; NXT1.
DR HPA; ENSG00000132661; Low tissue specificity.
DR MIM; 605811; gene.
DR neXtProt; NX_Q9UKK6; -.
DR OpenTargets; ENSG00000132661; -.
DR PharmGKB; PA31867; -.
DR VEuPathDB; HostDB:ENSG00000132661; -.
DR eggNOG; KOG4353; Eukaryota.
DR GeneTree; ENSGT00940000162041; -.
DR HOGENOM; CLU_122448_1_1_1; -.
DR InParanoid; Q9UKK6; -.
DR OMA; THAFTQT; -.
DR OrthoDB; 1450028at2759; -.
DR PhylomeDB; Q9UKK6; -.
DR TreeFam; TF318944; -.
DR PathwayCommons; Q9UKK6; -.
DR Reactome; R-HSA-159236; Transport of Mature mRNA derived from an Intron-Containing Transcript.
DR SignaLink; Q9UKK6; -.
DR BioGRID-ORCS; 29107; 277 hits in 1086 CRISPR screens.
DR ChiTaRS; NXT1; human.
DR EvolutionaryTrace; Q9UKK6; -.
DR GeneWiki; NXT1; -.
DR GenomeRNAi; 29107; -.
DR Pharos; Q9UKK6; Tbio.
DR PRO; PR:Q9UKK6; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9UKK6; protein.
DR Bgee; ENSG00000132661; Expressed in left uterine tube and 173 other tissues.
DR Genevisible; Q9UKK6; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005643; C:nuclear pore; TAS:ProtInc.
DR GO; GO:0044613; C:nuclear pore central transport channel; IBA:GO_Central.
DR GO; GO:0042272; C:nuclear RNA export factor complex; IPI:ComplexPortal.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0006406; P:mRNA export from nucleus; IDA:ComplexPortal.
DR GO; GO:0006913; P:nucleocytoplasmic transport; IBA:GO_Central.
DR GO; GO:0006611; P:protein export from nucleus; IEA:Ensembl.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR CDD; cd00780; NTF2; 1.
DR IDEAL; IID00399; -.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR045875; NTF2/Mtr2.
DR InterPro; IPR002075; NTF2_dom.
DR InterPro; IPR018222; Nuclear_transport_factor_2_euk.
DR PANTHER; PTHR12612; PTHR12612; 1.
DR Pfam; PF02136; NTF2; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
DR PROSITE; PS50177; NTF2_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Nucleus; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..140
FT /note="NTF2-related export protein 1"
FT /id="PRO_0000194793"
FT DOMAIN 16..135
FT /note="NTF2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00137"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MUTAGEN 114
FT /note="I->R: 70% reduction in mRNA export activity."
FT /evidence="ECO:0000269|PubMed:11583626"
FT MUTAGEN 134
FT /note="R->D: 57% reduction in mRNA export activity and loss
FT of nuclear rim staining."
FT /evidence="ECO:0000269|PubMed:11583626"
FT HELIX 6..30
FT /evidence="ECO:0007829|PDB:1JKG"
FT HELIX 32..38
FT /evidence="ECO:0007829|PDB:1JKG"
FT STRAND 39..47
FT /evidence="ECO:0007829|PDB:1JKG"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:1JKG"
FT HELIX 55..64
FT /evidence="ECO:0007829|PDB:1JKG"
FT STRAND 68..79
FT /evidence="ECO:0007829|PDB:1JKG"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:1JKG"
FT STRAND 90..101
FT /evidence="ECO:0007829|PDB:1JKG"
FT STRAND 107..118
FT /evidence="ECO:0007829|PDB:1JKG"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:1JKG"
FT STRAND 125..135
FT /evidence="ECO:0007829|PDB:1JKG"
FT TURN 136..139
FT /evidence="ECO:0007829|PDB:1JKG"
SQ SEQUENCE 140 AA; 15847 MW; 358FA86AC3944594 CRC64;
MASVDFKTYV DQACRAAEEF VNVYYTTMDK RRRLLSRLYM GTATLVWNGN AVSGQESLSE
FFEMLPSSEF QISVVDCQPV HDEATPSQTT VLVVICGSVK FEGNKQRDFN QNFILTAQAS
PSNTVWKIAS DCFRFQDWAS
