NU159_YEAST
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 03-AUG-2022, entry version 194.
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}.
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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 SMR; P40477; -.
DR BioGRID; 34876; 246.
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 iPTMnet; P40477; -.
DR MaxQB; P40477; -.
DR PaxDb; P40477; -.
DR PRIDE; P40477; -.
DR DNASU; 854691; -.
DR EnsemblFungi; YIL115C_mRNA; YIL115C; YIL115C.
DR GeneID; 854691; -.
DR KEGG; sce:YIL115C; -.
DR SGD; S000001377; NUP159.
DR VEuPathDB; FungiDB:YIL115C; -.
DR eggNOG; KOG3630; Eukaryota.
DR HOGENOM; CLU_250354_0_0_1; -.
DR InParanoid; P40477; -.
DR OMA; QAFENDE; -.
DR BioCyc; YEAST:G3O-31369-MON; -.
DR EvolutionaryTrace; P40477; -.
DR PRO; PR:P40477; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P40477; protein.
DR GO; GO:0005635; C:nuclear envelope; IC: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: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; IC: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 GO; GO:0061912; P:selective autophagy; IDA:SGD.
DR DisProt; DP01078; -.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR039462; Nup159/Nup146_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR Pfam; PF16755; NUP214; 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
