ID NU159_YEAST Reviewed; 1460 AA. AC P40477; D6VVH2; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 27-MAR-2024, entry version 201. DE RecName: Full=Nucleoporin NUP159; DE AltName: Full=Nuclear pore protein NUP159; GN Name=NUP159; Synonyms=NUP158, RAT7; OrderedLocusNames=YIL115C; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=7744966; DOI=10.1083/jcb.129.4.939; RA Gorsch L.C., Dockendorff T.C., Cole C.N.; RT "A conditional allele of the novel repeat-containing yeast nucleoporin RT RAT7/NUP159 causes both rapid cessation of mRNA export and reversible RT clustering of nuclear pore complexes."; RL J. Cell Biol. 129:939-955(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169870; RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C., RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V., RA Walsh S.V., Whitehead S., Barrell B.G.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX."; RL Nature 387:84-87(1997). RN [3] RP GENOME REANNOTATION. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [4] RP FUNCTION, AND INTERACTION WITH NUP82. RX PubMed=9736720; DOI=10.1073/pnas.95.19.11241; RA Hurwitz M.E., Strambio-de-Castillia C., Blobel G.; RT "Two yeast nuclear pore complex proteins involved in mRNA export form a RT cytoplasmically oriented subcomplex."; RL Proc. Natl. Acad. Sci. U.S.A. 95:11241-11245(1998). RN [5] RP FUNCTION, AND INTERACTION WITH NSP1. RX PubMed=9843582; DOI=10.1091/mbc.9.12.3475; RA Belgareh N., Snay-Hodge C., Pasteau F., Dagher S., Cole C.N., Doye V.; RT "Functional characterization of a Nup159p-containing nuclear pore RT subcomplex."; RL Mol. Biol. Cell 9:3475-3492(1998). RN [6] RP FUNCTION, AND INTERACTION WITH PSE1. RX PubMed=9891088; DOI=10.1128/mcb.19.2.1547; RA Seedorf M., Damelin M., Kahana J., Taura T., Silver P.A.; RT "Interactions between a nuclear transporter and a subset of nuclear pore RT complex proteins depend on Ran GTPase."; RL Mol. Cell. Biol. 19:1547-1557(1999). RN [7] RP FUNCTION, AND INTERACTION WITH GLE1; CRM1 AND DBP5. RX PubMed=10523319; DOI=10.1093/emboj/18.20.5778; RA Hodge C.A., Colot H.V., Stafford P., Cole C.N.; RT "Rat8p/Dbp5p is a shuttling transport factor that interacts with RT Rat7p/Nup159p and Gle1p and suppresses the mRNA export defect of xpo1-1 RT cells."; RL EMBO J. 18:5778-5788(1999). RN [8] RP FUNCTION, AND NUP82 NPC SUBCOMPLEX. RX PubMed=10801828; DOI=10.1074/jbc.m001963200; RA Bailer S.M., Balduf C., Katahira J., Podtelejnikov A., Rollenhagen C., RA Mann M., Pante N., Hurt E.C.; RT "Nup116p associates with the Nup82p-Nsp1p-Nup159p nucleoporin complex."; RL J. Biol. Chem. 275:23540-23548(2000). RN [9] RP CHARACTERIZATION, AND NPC SUBUNIT LOCATION. RX PubMed=10684247; DOI=10.1083/jcb.148.4.635; RA Rout M.P., Aitchison J.D., Suprapto A., Hjertaas K., Zhao Y., Chait B.T.; RT "The yeast nuclear pore complex: composition, architecture, and transport RT mechanism."; RL J. Cell Biol. 148:635-651(2000). RN [10] RP FUNCTION, AND INTERACTION WITH MEX67/MTR2 HETERODIMER. RX PubMed=10952996; DOI=10.1083/jcb.150.4.695; RA Straesser K., Bassler J., Hurt E.C.; RT "Binding of the Mex67p/Mtr2p heterodimer to FXFG, GLFG, and FG repeat RT nucleoporins is essential for nuclear mRNA export."; RL J. Cell Biol. 150:695-706(2000). RN [11] RP FUNCTION, AND INTERACTION WITH KARYOPHERINS THROUGH FG REPEATS. RX PubMed=11387327; DOI=10.1074/jbc.m102629200; RA Allen N.P., Huang L., Burlingame A., Rexach M.; RT "Proteomic analysis of nucleoporin interacting proteins."; RL J. Biol. Chem. 276:29268-29274(2001). RN [12] RP FUNCTION, AND PRE-RIBOSOME EXPORT. RX PubMed=11739405; DOI=10.1083/jcb.200108142; RA Gleizes P.-E., Noaillac-Depeyre J., Leger-Silvestre I., Teulieres F., RA Dauxois J.-Y., Pommet D., Azum-Gelade M.-C., Gas N.; RT "Ultrastructural localization of rRNA shows defective nuclear export of RT preribosomes in mutants of the Nup82p complex."; RL J. Cell Biol. 155:923-936(2001). RN [13] RP FUNCTION, AND NPC ASSEMBLY. RX PubMed=11689687; DOI=10.1128/mcb.21.23.7944-7955.2001; RA Bailer S.M., Balduf C., Hurt E.C.; RT "The Nsp1p carboxy-terminal domain is organized into functionally distinct RT coiled-coil regions required for assembly of nucleoporin subcomplexes and RT nucleocytoplasmic transport."; RL Mol. Cell. Biol. 21:7944-7955(2001). RN [14] RP FUNCTION, AND INTERACTION WITH CRM1 AND RNA1. RX PubMed=12543930; DOI=10.1074/mcp.t200012-mcp200; RA Allen N.P., Patel S.S., Huang L., Chalkley R.J., Burlingame A., RA Lutzmann M., Hurt E.C., Rexach M.; RT "Deciphering networks of protein interactions at the nuclear pore RT complex."; RL Mol. Cell. Proteomics 1:930-946(2002). RN [15] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [16] RP FUNCTION, AND FG REPEAT STRUCTURE. RX PubMed=12604785; DOI=10.1073/pnas.0437902100; RA Denning D.P., Patel S.S., Uversky V., Fink A.L., Rexach M.; RT "Disorder in the nuclear pore complex: the FG repeat regions of RT nucleoporins are natively unfolded."; RL Proc. Natl. Acad. Sci. U.S.A. 100:2450-2455(2003). RN [17] RP FUNCTION, AND FG REPEATS IN NPC TRANSPORT. RX PubMed=15039779; DOI=10.1038/ncb1097; RA Strawn L.A., Shen T.X., Shulga N., Goldfarb D.S., Wente S.R.; RT "Minimal nuclear pore complexes define FG repeat domains essential for RT transport."; RL Nat. Cell Biol. 6:197-206(2004). RN [18] RP REVIEW. RX PubMed=12791264; DOI=10.1016/s1534-5807(03)00162-x; RA Suntharalingam M., Wente S.R.; RT "Peering through the pore: nuclear pore complex structure, assembly, and RT function."; RL Dev. Cell 4:775-789(2003). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-404; SER-735; THR-803; RP SER-805 AND SER-819, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC STRAIN=ADR376; RX PubMed=17330950; DOI=10.1021/pr060559j; RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., RA Elias J.E., Gygi S.P.; RT "Large-scale phosphorylation analysis of alpha-factor-arrested RT Saccharomyces cerevisiae."; RL J. Proteome Res. 6:1190-1197(2007). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-657; SER-724; SER-735; RP SER-745; SER-805; SER-819; SER-889 AND SER-940, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth phosphoproteome RT analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-404; SER-735; THR-803; RP SER-805; SER-819 AND SER-940, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=19779198; DOI=10.1126/science.1172867; RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.; RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights RT into evolution."; RL Science 325:1682-1686(2009). RN [22] RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH DYN2, AND REGION. RX PubMed=17546040; DOI=10.1038/ncb1604; RA Stelter P., Kunze R., Flemming D., Hoepfner D., Diepholz M., Philippsen P., RA Boettcher B., Hurt E.; RT "Molecular basis for the functional interaction of dynein light chain with RT the nuclear-pore complex."; RL Nat. Cell Biol. 9:788-796(2007). RN [23] RP INTERACTION WITH DYN2, SUBCELLULAR LOCATION, AND REGION. RX PubMed=23223634; DOI=10.1074/jbc.m112.432831; RA Nyarko A., Song Y., Novacek J., Zidek L., Barbar E.; RT "Multiple recognition motifs in nucleoporin Nup159 provide a stable and RT rigid Nup159-Dyn2 assembly."; RL J. Biol. Chem. 288:2614-2622(2013). RN [24] RP INTERACTION WITH DYN2, NUP82 NPC SUBCOMPLEX, AND SUBCELLULAR LOCATION. RX PubMed=25646085; DOI=10.1083/jcb.201411003; RA Gaik M., Flemming D., von Appen A., Kastritis P., Muecke N., Fischer J., RA Stelter P., Ori A., Bui K.H., Bassler J., Barbar E., Beck M., Hurt E.; RT "Structural basis for assembly and function of the Nup82 complex in the RT nuclear pore scaffold."; RL J. Cell Biol. 208:283-297(2015). RN [25] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-387, FUNCTION, AND INTERACTION RP WITH DBP5. RX PubMed=15574330; DOI=10.1016/j.molcel.2004.10.032; RA Weirich C.S., Erzberger J.P., Berger J.M., Weis K.; RT "The N-terminal domain of Nup159 forms a beta-propeller that functions in RT mRNA export by tethering the helicase Dbp5 to the nuclear pore."; RL Mol. Cell 16:749-760(2004). RN [26] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1425-1460 IN COMPLEX WITH NUP82 RP AND NUP116, AND SUBUNIT. RX PubMed=21930948; DOI=10.1073/pnas.1112846108; RA Yoshida K., Seo H.S., Debler E.W., Blobel G., Hoelz A.; RT "Structural and functional analysis of an essential nucleoporin RT heterotrimer on the cytoplasmic face of the nuclear pore complex."; RL Proc. Natl. Acad. Sci. U.S.A. 108:16571-16576(2011). RN [27] RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 1425-1460 IN COMPLEX WITH NUP82 RP AND THE MOUSE ORTHOLOG OF NUP145, AND SUBUNIT. RX PubMed=22480613; DOI=10.1016/j.jmb.2012.03.024; RA Stuwe T., von Borzyskowski L.S., Davenport A.M., Hoelz A.; RT "Molecular basis for the anchoring of proto-oncoprotein Nup98 to the RT cytoplasmic face of the nuclear pore complex."; RL J. Mol. Biol. 419:330-346(2012). CC -!- FUNCTION: Functions as a component of the nuclear pore complex (NPC). CC NPC components, collectively referred to as nucleoporins (NUPs), can CC play the role of both NPC structural components and of docking or CC interaction partners for transiently associated nuclear transport CC factors. Active directional transport is assured by both, a Phe-Gly CC (FG) repeat affinity gradient for these transport factors across the CC NPC and a transport cofactor concentration gradient across the nuclear CC envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in CC the nucleus, with GDP in the cytoplasm). NUP159 plays an important role CC in several nuclear export pathways including poly(A)+ RNA, pre- CC ribosome, and protein export. {ECO:0000269|PubMed:10523319, CC ECO:0000269|PubMed:10801828, ECO:0000269|PubMed:10952996, CC ECO:0000269|PubMed:11387327, ECO:0000269|PubMed:11689687, CC ECO:0000269|PubMed:11739405, ECO:0000269|PubMed:12543930, CC ECO:0000269|PubMed:12604785, ECO:0000269|PubMed:15039779, CC ECO:0000269|PubMed:15574330, ECO:0000269|PubMed:9736720, CC ECO:0000269|PubMed:9843582, ECO:0000269|PubMed:9891088}. CC -!- SUBUNIT: Component of the nuclear pore complex (NPC) (PubMed:17546040). CC NPC constitutes the exclusive means of nucleocytoplasmic transport. CC NPCs allow the passive diffusion of ions and small molecules and the CC active, nuclear transport receptor-mediated bidirectional transport of CC macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs), and CC ribosomal subunits across the nuclear envelope. Due to its 8-fold CC rotational symmetry, all subunits are present with 8 copies or CC multiples thereof. Part of the NUP82 subcomplex, interacts with NUP82 CC through its C-terminal coiled coil (PubMed:9736720, PubMed:17546040, CC PubMed:23223634, PubMed:25646085). This subcomplex is the base for CC interactions with NUP116 and GLE2, with NUP42 and GLE1 and with DYN2 CC (PubMed:17546040, PubMed:23223634). Interacts directly with DYN2 CC (PubMed:17546040, PubMed:23223634, PubMed:25646085). Interacts through CC its FG repeats with karyopherins, such as heterodimeric mRNA transport CC factor MEX67/MTR2, CRM1 (XPO1), and PSE1 (GSP1-GDP dependent). CC Interaction with CRM1 (XPO1) is GSP1-GTP dependent and stimulated by CC RNA1. NUP159 also interacts with GLE1 and the ATP-dependent RNA CC helicase DBP5. {ECO:0000269|PubMed:10523319, CC ECO:0000269|PubMed:10952996, ECO:0000269|PubMed:11387327, CC ECO:0000269|PubMed:12543930, ECO:0000269|PubMed:15574330, CC ECO:0000269|PubMed:17546040, ECO:0000269|PubMed:21930948, CC ECO:0000269|PubMed:22480613, ECO:0000269|PubMed:23223634, CC ECO:0000269|PubMed:25646085, ECO:0000269|PubMed:9736720, CC ECO:0000269|PubMed:9843582, ECO:0000269|PubMed:9891088}. CC -!- INTERACTION: CC P40477; Q06142: KAP95; NbExp=3; IntAct=EBI-11747, EBI-9145; CC P40477; P40368: NUP82; NbExp=5; IntAct=EBI-11747, EBI-12331; CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex CC {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:17546040, CC ECO:0000269|PubMed:23223634, ECO:0000269|PubMed:25646085}. Nucleus CC membrane; Peripheral membrane protein; Cytoplasmic side. CC -!- DOMAIN: Contains FG repeats. FG repeats are interaction sites for CC karyopherins (importins, exportins) and form probably an affinity CC gradient, guiding the transport proteins unidirectionally with their CC cargo through the NPC. FG repeat regions are highly flexible and lack CC ordered secondary structure. The overall conservation of FG repeats CC regarding exact sequence, spacing, and repeat unit length is limited. CC FG repeat types and their physico-chemical environment change across CC the NPC from the nucleoplasmic to the cytoplasmic side: SXFG/PXFG CC repeats are especially abundant in NUPs on the cytoplasmic side. CC -!- MISCELLANEOUS: Present with 1230 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. 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; L40634; AAC41652.1; -; Genomic_DNA. DR EMBL; Z38125; CAA86265.1; -; Genomic_DNA. DR EMBL; BK006942; DAA08438.1; -; Genomic_DNA. DR PIR; S48457; S48457. DR RefSeq; NP_012151.1; NM_001179463.1. DR PDB; 1XIP; X-ray; 2.50 A; A=2-387. DR PDB; 3PBP; X-ray; 2.60 A; C/F/I/L=1425-1460. DR PDB; 3RRM; X-ray; 2.88 A; C=2-387. DR PDB; 3TKN; X-ray; 3.40 A; B/E/H=1425-1460. DR PDB; 4DS1; X-ray; 1.85 A; B/D=1116-1126. DR PDB; 7N9F; EM; 37.00 A; w/x=1-1460. DR PDBsum; 1XIP; -. DR PDBsum; 3PBP; -. DR PDBsum; 3RRM; -. DR PDBsum; 3TKN; -. DR PDBsum; 4DS1; -. DR PDBsum; 7N9F; -. DR AlphaFoldDB; P40477; -. DR EMDB; EMD-24258; -. DR SMR; P40477; -. DR BioGRID; 34876; 255. DR ComplexPortal; CPX-824; Nuclear pore complex. DR DIP; DIP-2314N; -. DR IntAct; P40477; 18. DR MINT; P40477; -. DR STRING; 4932.YIL115C; -. DR TCDB; 1.I.1.1.1; the nuclear pore complex (npc) family. DR GlyGen; P40477; 23 sites, 1 O-linked glycan (23 sites). DR iPTMnet; P40477; -. DR MaxQB; P40477; -. DR PaxDb; 4932-YIL115C; -. DR PeptideAtlas; P40477; -. DR DNASU; 854691; -. DR EnsemblFungi; YIL115C_mRNA; YIL115C; YIL115C. DR GeneID; 854691; -. DR KEGG; sce:YIL115C; -. DR AGR; SGD:S000001377; -. DR SGD; S000001377; NUP159. DR VEuPathDB; FungiDB:YIL115C; -. DR eggNOG; KOG3630; Eukaryota. DR HOGENOM; CLU_250354_0_0_1; -. DR InParanoid; P40477; -. DR OMA; NIYTWRI; -. DR OrthoDB; 2015094at2759; -. DR BioCyc; YEAST:G3O-31369-MONOMER; -. DR BioGRID-ORCS; 854691; 8 hits in 10 CRISPR screens. DR EvolutionaryTrace; P40477; -. DR PRO; PR:P40477; -. DR Proteomes; UP000002311; Chromosome IX. DR RNAct; P40477; Protein. DR GO; GO:0005635; C:nuclear envelope; NAS:ComplexPortal. DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005643; C:nuclear pore; IDA:SGD. DR GO; GO:0044613; C:nuclear pore central transport channel; IDA:SGD. DR GO; GO:0044614; C:nuclear pore cytoplasmic filaments; IDA:SGD. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IDA:SGD. DR GO; GO:0060090; F:molecular adaptor activity; IDA:DisProt. DR GO; GO:0017056; F:structural constituent of nuclear pore; IPI:SGD. DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central. DR GO; GO:0097064; P:ncRNA export from nucleus; IMP:SGD. DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; IGI:SGD. DR GO; GO:0051664; P:nuclear pore localization; IMP:SGD. DR GO; GO:0006913; P:nucleocytoplasmic transport; NAS:ComplexPortal. DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:SGD. DR GO; GO:0006611; P:protein export from nucleus; IMP:SGD. DR GO; GO:0000055; P:ribosomal large subunit export from nucleus; IMP:SGD. DR GO; GO:0000056; P:ribosomal small subunit export from nucleus; IMP:SGD. DR DisProt; DP01078; -. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1. DR InterPro; IPR039462; Nup159/Nup146_N. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR PANTHER; PTHR21099:SF2; C3H1-TYPE DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR21099; RAD201; 1. DR Pfam; PF16755; NUP214; 1. DR SUPFAM; SSF117289; Nucleoporin domain; 1. PE 1: Evidence at protein level; KW 3D-structure; Coiled coil; Membrane; mRNA transport; Nuclear pore complex; KW Nucleus; Phosphoprotein; Protein transport; Reference proteome; Repeat; KW Translocation; Transport. FT CHAIN 1..1460 FT /note="Nucleoporin NUP159" FT /id="PRO_0000204849" FT REPEAT 228..231 FT /note="FG 1" FT REPEAT 267..270 FT /note="PXFG 1" FT REPEAT 462..470 FT /note="SXFGXPXFG 1" FT REPEAT 503..511 FT /note="SXFGXPXFG 2; approximate" FT REPEAT 522..530 FT /note="SXFGXPXFG 3; approximate" FT REPEAT 532..535 FT /note="PXFG 2" FT REPEAT 548..556 FT /note="SXFGXPXFG 4" FT REPEAT 558..561 FT /note="PXFG 3" FT REPEAT 574..582 FT /note="SXFGXPXFG 5" FT REPEAT 584..587 FT /note="PXFG 4" FT REPEAT 600..608 FT /note="SXFGXPXFG 6" FT REPEAT 610..613 FT /note="SXFG 1" FT REPEAT 624..632 FT /note="SXFGXPXFG 7; approximate" FT REPEAT 642..645 FT /note="FG 2" FT REPEAT 687..690 FT /note="FG 3" FT REPEAT 704..707 FT /note="FXFG 1" FT REPEAT 709..712 FT /note="SXFG 2" FT REPEAT 728..731 FT /note="FXFG 2" FT REPEAT 842..845 FT /note="PXFG 5" FT REPEAT 873..876 FT /note="FXFG 3" FT REGION 1..500 FT /note="Interaction with DBP5" FT REGION 401..435 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 483..504 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 497..701 FT /note="Interactions with CRM1 and GLE1" FT REGION 533..619 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 647..704 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 727..824 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 861..1092 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1086..1175 FT /note="Interaction with DYN2" FT /evidence="ECO:0000269|PubMed:17546040, FT ECO:0000269|PubMed:23223634" FT REGION 1223..1460 FT /note="Interaction with NUP82" FT /evidence="ECO:0000269|PubMed:9736720" FT COILED 1279..1320 FT COILED 1383..1418 FT COMPBIAS 413..427 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 483..497 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 533..571 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 578..619 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 647..673 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 683..704 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 727..766 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 778..802 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 861..893 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 914..937 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 942..963 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 964..999 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1016..1092 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 404 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:19779198" FT MOD_RES 657 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MOD_RES 724 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MOD_RES 735 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198" FT MOD_RES 745 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MOD_RES 803 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:19779198" FT MOD_RES 805 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198" FT MOD_RES 819 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198" FT MOD_RES 889 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MOD_RES 940 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956, FT ECO:0007744|PubMed:19779198" FT STRAND 10..15 FT /evidence="ECO:0007829|PDB:1XIP" FT STRAND 17..25 FT /evidence="ECO:0007829|PDB:1XIP" FT STRAND 42..45 FT /evidence="ECO:0007829|PDB:1XIP" FT TURN 46..49 FT /evidence="ECO:0007829|PDB:1XIP" FT STRAND 50..55 FT /evidence="ECO:0007829|PDB:1XIP" FT STRAND 58..63 FT /evidence="ECO:0007829|PDB:1XIP" FT HELIX 64..72 FT /evidence="ECO:0007829|PDB:1XIP" FT STRAND 73..75 FT /evidence="ECO:0007829|PDB:1XIP" FT STRAND 81..85 FT /evidence="ECO:0007829|PDB:1XIP" FT STRAND 89..95 FT /evidence="ECO:0007829|PDB:1XIP" FT STRAND 98..114 FT /evidence="ECO:0007829|PDB:1XIP" FT STRAND 118..123 FT /evidence="ECO:0007829|PDB:1XIP" FT STRAND 128..133 FT /evidence="ECO:0007829|PDB:1XIP" FT STRAND 135..142 FT /evidence="ECO:0007829|PDB:1XIP" FT STRAND 145..151 FT /evidence="ECO:0007829|PDB:1XIP" FT TURN 152..154 FT /evidence="ECO:0007829|PDB:1XIP" FT STRAND 157..169 FT /evidence="ECO:0007829|PDB:1XIP" FT STRAND 171..178 FT /evidence="ECO:0007829|PDB:1XIP" FT STRAND 183..189 FT /evidence="ECO:0007829|PDB:1XIP" FT STRAND 192..199 FT /evidence="ECO:0007829|PDB:1XIP" FT HELIX 203..206 FT /evidence="ECO:0007829|PDB:1XIP" FT TURN 210..212 FT /evidence="ECO:0007829|PDB:1XIP" FT STRAND 213..231 FT /evidence="ECO:0007829|PDB:1XIP" FT STRAND 245..253 FT /evidence="ECO:0007829|PDB:1XIP" FT STRAND 256..265 FT /evidence="ECO:0007829|PDB:1XIP" FT STRAND 278..284 FT /evidence="ECO:0007829|PDB:1XIP" FT STRAND 286..288 FT /evidence="ECO:0007829|PDB:1XIP" FT STRAND 292..298 FT /evidence="ECO:0007829|PDB:1XIP" FT STRAND 305..307 FT /evidence="ECO:0007829|PDB:1XIP" FT STRAND 309..317 FT /evidence="ECO:0007829|PDB:1XIP" FT HELIX 318..320 FT /evidence="ECO:0007829|PDB:1XIP" FT TURN 328..330 FT /evidence="ECO:0007829|PDB:1XIP" FT STRAND 336..342 FT /evidence="ECO:0007829|PDB:1XIP" FT STRAND 364..369 FT /evidence="ECO:0007829|PDB:1XIP" FT STRAND 372..380 FT /evidence="ECO:0007829|PDB:1XIP" FT STRAND 1118..1123 FT /evidence="ECO:0007829|PDB:4DS1" FT HELIX 1436..1454 FT /evidence="ECO:0007829|PDB:3PBP" SQ SEQUENCE 1460 AA; 158908 MW; A33FFA52378F8205 CRC64; MSSLKDEVPT ETSEDFGFKF LGQKQILPSF NEKLPFASLQ NLDISNSKSL FVAASGSKAV VGELQLLRDH ITSDSTPLTF KWEKEIPDVI FVCFHGDQVL VSTRNALYSL DLEELSEFRT VTSFEKPVFQ LKNVNNTLVI LNSVNDLSAL DLRTKSTKQL AQNVTSFDVT NSQLAVLLKD RSFQSFAWRN GEMEKQFEFS LPSELEELPV EEYSPLSVTI LSPQDFLAVF GNVISETDDE VSYDQKMYII KHIDGSASFQ ETFDITPPFG QIVRFPYMYK VTLSGLIEPD ANVNVLASSC SSEVSIWDSK QVIEPSQDSE RAVLPISEET DKDTNPIGVA VDVVTSGTIL EPCSGVDTIE RLPLVYILNN EGSLQIVGLF HVAAIKSGHY SINLESLEHE KSLSPTSEKI PIAGQEQEEK KKNNESSKAL SENPFTSANT SGFTFLKTQP AAANSLQSQS SSTFGAPSFG SSAFKIDLPS VSSTSTGVAS SEQDATDPAS AKPVFGKPAF GAIAKEPSTS EYAFGKPSFG APSFGSGKSS VESPASGSAF GKPSFGTPSF GSGNSSVEPP ASGSAFGKPS FGTPSFGSGN SSAEPPASGS AFGKPSFGTS AFGTASSNET NSGSIFGKAA FGSSSFAPAN NELFGSNFTI SKPTVDSPKE VDSTSPFPSS GDQSEDESKS DVDSSSTPFG TKPNTSTKPK TNAFDFGSSS FGSGFSKALE SVGSDTTFKF GTQASPFSSQ LGNKSPFSSF TKDDTENGSL SKGSTSEIND DNEEHESNGP NVSGNDLTDS TVEQTSSTRL PETPSDEDGE VVEEEAQKSP IGKLTETIKK SANIDMAGLK NPVFGNHVKA KSESPFSAFA TNITKPSSTT PAFSFGNSTM NKSNTSTVSP MEEADTKETS EKGPITLKSV ENPFLPAKEE RTGESSKKDH NDDPKDGYVS GSEISVRTSE SAFDTTANEE IPKSQDVNNH EKSETDPKYS QHAVVDHDNK SKEMNETSKN NERSGQPNHG VQGDGIALKK DNEKENFDSN MAIKQFEDHQ SSEEDASEKD SRQSSEVKES DDNMSLNSDR DESISESYDK LEDINTDELP HGGEAFKARE VSASADFDVQ TSLEDNYAES GIQTDLSESS KENEVQTDAI PVKHNSTQTV KKEAVDNGLQ TEPVETCNFS VQTFEGDENY LAEQCKPKQL KEYYTSAKVS NIPFVSQNST LRLIESTFQT VEAEFTVLME NIRNMDTFFT DQSSIPLVKR TVRSINNLYT WRIPEAEILL NIQNNIKCEQ MQITNANIQD LKEKVTDYVR KDIAQITEDV ANAKEEYLFL MHFDDASSGY VKDLSTHQFR MQKTLRQKLF DVSAKINHTE ELLNILKLFT VKNKRLDDNP LVAKLAKESL ARDGLLKEIK LLREQVSRLQ LEEKGKKASS FDASSSITKD MKGFKVVEVG LAMNTKKQIG DFFKNLNMAK //