NU116_YEAST
ID NU116_YEAST Reviewed; 1113 AA.
AC Q02630; D6VZM2;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Nucleoporin NUP116/NSP116;
DE AltName: Full=Nuclear pore protein NUP116/NSP116;
GN Name=NUP116; Synonyms=NSP116; OrderedLocusNames=YMR047C;
GN ORFNames=YM9532.12C;
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=1385442; DOI=10.1083/jcb.119.4.705;
RA Wente S.R., Rout M.P., Blobel G.;
RT "A new family of yeast nuclear pore complex proteins.";
RL J. Cell Biol. 119:705-723(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1464327; DOI=10.1002/j.1460-2075.1992.tb05612.x;
RA Wimmer C., Doye V., Grandi P., Nehrbass U., Hurt E.C.;
RT "A new subclass of nucleoporins that functionally interact with nuclear
RT pore protein NSP1.";
RL EMBO J. 11:5051-5061(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [4]
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 [5]
RP FUNCTION, AND HOMOPOLYMERIC RNA-BINDING.
RX PubMed=8044840; DOI=10.1016/0092-8674(94)90297-6;
RA Fabre E., Boelens W.C., Wimmer C., Mattaj I.W., Hurt E.C.;
RT "Nup145p is required for nuclear export of mRNA and binds homopolymeric RNA
RT in vitro via a novel conserved motif.";
RL Cell 78:275-289(1994).
RN [6]
RP FUNCTION IN TRNA EXPORT.
RX PubMed=8524308; DOI=10.1128/mcb.16.1.294;
RA Sharma K., Fabre E., Tekotte H., Hurt E.C., Tollervey D.;
RT "Yeast nucleoporin mutants are defective in pre-tRNA splicing.";
RL Mol. Cell. Biol. 16:294-301(1996).
RN [7]
RP FUNCTION, AND INTERACTION WITH GLE2.
RX PubMed=9463388; DOI=10.1093/emboj/17.4.1107;
RA Bailer S.M., Siniossoglou S., Podtelejnikov A., Hellwig A., Mann M.,
RA Hurt E.C.;
RT "Nup116p and nup100p are interchangeable through a conserved motif which
RT constitutes a docking site for the mRNA transport factor gle2p.";
RL EMBO J. 17:1107-1119(1998).
RN [8]
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 [9]
RP FUNCTION, IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, AND INTERACTION WITH
RP NUP82.
RX PubMed=10891509; DOI=10.1128/mcb.20.15.5736-5748.2000;
RA Ho A.K., Shen T.X., Ryan K.J., Kiseleva E., Levy M.A., Allen T.D.,
RA Wente S.R.;
RT "Assembly and preferential localization of Nup116p on the cytoplasmic face
RT of the nuclear pore complex by interaction with Nup82p.";
RL Mol. Cell. Biol. 20:5736-5748(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 PRE-RIBOSOME EXPORT.
RX PubMed=11071906; DOI=10.1091/mbc.11.11.3777;
RA Stage-Zimmermann T., Schmidt U., Silver P.A.;
RT "Factors affecting nuclear export of the 60S ribosomal subunit in vivo.";
RL Mol. Biol. Cell 11:3777-3789(2000).
RN [12]
RP FUNCTION, AND INTERACTION WITH 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 [13]
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 [14]
RP FUNCTION, AND NUCLEOPORIN INTERACTING PROTEINS.
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 [15]
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 [16]
RP FUNCTION, AND INTERACTION WITH MEX67 AND KAP95.
RX PubMed=11104765; DOI=10.1074/jbc.m008311200;
RA Strawn L.A., Shen T.X., Wente S.R.;
RT "The GLFG regions of Nup116p and Nup100p serve as binding sites for both
RT Kap95p and Mex67p at the nuclear pore complex.";
RL J. Biol. Chem. 276:6445-6452(2001).
RN [17]
RP FUNCTION, STRUCTURAL BASIS OF FG REPEAT INTERACTION, AND INTERACTION WITH
RP KAP95.
RX PubMed=12372823; DOI=10.1074/jbc.m209037200;
RA Bayliss R., Littlewood T., Strawn L.A., Wente S.R., Stewart M.;
RT "GLFG and FxFG nucleoporins bind to overlapping sites on importin-beta.";
RL J. Biol. Chem. 277:50597-50606(2002).
RN [18]
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 [19]
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 [20]
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 [21]
RP INTERACTION WITH CEX1.
RX PubMed=17203074; DOI=10.1038/sj.emboj.7601493;
RA McGuire A.T., Mangroo D.;
RT "Cex1p is a novel cytoplasmic component of the Saccharomyces cerevisiae
RT nuclear tRNA export machinery.";
RL EMBO J. 26:288-300(2007).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-886, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [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 [23]
RP FUNCTION, INTERACTION WITH AFG2, AND MUTAGENESIS OF 92-SER--THR-1113;
RP 110-VAL--LYS-166 AND 173-GLY--THR-1113.
RX PubMed=23185031; DOI=10.1083/jcb.201205021;
RA Kappel L., Loibl M., Zisser G., Klein I., Fruhmann G., Gruber C.,
RA Unterweger S., Rechberger G., Pertschy B., Bergler H.;
RT "Rlp24 activates the AAA-ATPase Drg1 to initiate cytoplasmic pre-60S
RT maturation.";
RL J. Cell Biol. 199:771-782(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). Plays an important role in
CC several nuclear export and import pathways including poly(A)+ RNA,
CC tRNA, pre-ribosome, and protein transport. By binding ATPase AFG2,
CC promotes AFG2-mediated release of shuttling protein RLP24 from pre-60S
CC ribosomal particles (PubMed:23185031). {ECO:0000269|PubMed:10801828,
CC ECO:0000269|PubMed:10891509, ECO:0000269|PubMed:10952996,
CC ECO:0000269|PubMed:11071906, ECO:0000269|PubMed:11104765,
CC ECO:0000269|PubMed:11387327, ECO:0000269|PubMed:11689687,
CC ECO:0000269|PubMed:12372823, ECO:0000269|PubMed:12604785,
CC ECO:0000269|PubMed:15039779, ECO:0000269|PubMed:23185031,
CC ECO:0000269|PubMed:8044840, ECO:0000269|PubMed:8524308,
CC ECO:0000269|PubMed:9463388, ECO:0000269|PubMed:9891088}.
CC -!- SUBUNIT: Component of the nuclear pore complex (NPC). NPC constitutes
CC the exclusive means of nucleocytoplasmic transport (PubMed:10891509).
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 (PubMed:10891509). NUP116 interacts with the NUP82
CC subcomplex and GLE2 (PubMed:10801828, PubMed:9463388, PubMed:10891509).
CC Through its FG repeats it interacts with numerous karyopherins
CC including KAP95, PSE1 (GSP1-GDP dependent), MEX67, and to homomeric RNA
CC (PubMed:9891088, PubMed:10952996, PubMed:11104765, PubMed:12372823).
CC Interacts with CEX1 (PubMed:17203074). Interacts (via N-terminus) with
CC AFG2 (via N-terminus) (PubMed:23185031). {ECO:0000269|PubMed:10801828,
CC ECO:0000269|PubMed:10891509, ECO:0000269|PubMed:10952996,
CC ECO:0000269|PubMed:11104765, ECO:0000269|PubMed:12372823,
CC ECO:0000269|PubMed:17203074, ECO:0000269|PubMed:23185031,
CC ECO:0000269|PubMed:9463388, ECO:0000269|PubMed:9891088}.
CC -!- INTERACTION:
CC Q02630; Q12453: CEX1; NbExp=4; IntAct=EBI-11703, EBI-31271;
CC Q02630; P40066: GLE2; NbExp=5; IntAct=EBI-11703, EBI-22648;
CC Q02630; Q06142: KAP95; NbExp=4; IntAct=EBI-11703, EBI-9145;
CC Q02630; Q99257: MEX67; NbExp=5; IntAct=EBI-11703, EBI-11642;
CC Q02630; Q02629: NUP100; NbExp=4; IntAct=EBI-11703, EBI-11698;
CC Q02630; Q02630: NUP116; NbExp=2; IntAct=EBI-11703, EBI-11703;
CC Q02630; P47054: NUP192; NbExp=2; IntAct=EBI-11703, EBI-25846;
CC Q02630; P49686: NUP42; NbExp=2; IntAct=EBI-11703, EBI-12310;
CC Q02630; P48837: NUP57; NbExp=4; IntAct=EBI-11703, EBI-12324;
CC Q02630; P40368: NUP82; NbExp=3; IntAct=EBI-11703, EBI-12331;
CC Q02630; P46673: NUP85; NbExp=3; IntAct=EBI-11703, EBI-12345;
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:10891509}. Nucleus membrane; Peripheral membrane
CC protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane
CC protein; Nucleoplasmic side. Note=Biased towards 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: GLFG repeats
CC are especially abundant in NUPs in the central region (lacking a
CC charged environment but are enriched in Ser, Thr, Gln, and Asn).
CC -!- SIMILARITY: Belongs to the nucleoporin GLFG family. {ECO:0000305}.
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DR EMBL; Z15036; CAA78754.1; -; Genomic_DNA.
DR EMBL; X68108; CAA48228.1; -; Genomic_DNA.
DR EMBL; Z48502; CAA88413.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09946.1; -; Genomic_DNA.
DR PIR; S28925; S28925.
DR RefSeq; NP_013762.1; NM_001182544.1.
DR PDB; 1O6P; X-ray; 2.80 A; C/D/E/F=602-609.
DR PDB; 2AIV; NMR; -; A=967-1113.
DR PDB; 3PBP; X-ray; 2.60 A; B/E/H/K=967-1113.
DR PDBsum; 1O6P; -.
DR PDBsum; 2AIV; -.
DR PDBsum; 3PBP; -.
DR AlphaFoldDB; Q02630; -.
DR SMR; Q02630; -.
DR BioGRID; 35221; 496.
DR ComplexPortal; CPX-824; Nuclear pore complex.
DR DIP; DIP-2389N; -.
DR ELM; Q02630; -.
DR IntAct; Q02630; 40.
DR MINT; Q02630; -.
DR STRING; 4932.YMR047C; -.
DR MEROPS; S59.951; -.
DR TCDB; 1.I.1.1.1; the nuclear pore complex (npc) family.
DR iPTMnet; Q02630; -.
DR MaxQB; Q02630; -.
DR PaxDb; Q02630; -.
DR PRIDE; Q02630; -.
DR DNASU; 855066; -.
DR EnsemblFungi; YMR047C_mRNA; YMR047C; YMR047C.
DR GeneID; 855066; -.
DR KEGG; sce:YMR047C; -.
DR SGD; S000004650; NUP116.
DR VEuPathDB; FungiDB:YMR047C; -.
DR eggNOG; KOG0845; Eukaryota.
DR GeneTree; ENSGT00550000074799; -.
DR HOGENOM; CLU_011051_0_0_1; -.
DR InParanoid; Q02630; -.
DR OMA; VIITFEP; -.
DR BioCyc; YEAST:G3O-32752-MON; -.
DR Reactome; R-SCE-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-SCE-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-SCE-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-SCE-4570464; SUMOylation of RNA binding proteins.
DR EvolutionaryTrace; Q02630; -.
DR PRO; PR:Q02630; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q02630; 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:0051117; F:ATPase binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IMP:SGD.
DR GO; GO:0006406; P:mRNA export from nucleus; IPI:SGD.
DR GO; GO:0006999; P:nuclear pore organization; 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:0000973; P:post-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery; IBA:GO_Central.
DR GO; GO:0006606; P:protein import into nucleus; IMP:SGD.
DR GO; GO:0000055; P:ribosomal large subunit export from nucleus; IMP:SGD.
DR GO; GO:0006405; P:RNA export from nucleus; IBA:GO_Central.
DR GO; GO:0006409; P:tRNA export from nucleus; IMP:SGD.
DR Gene3D; 3.30.1610.10; -; 1.
DR InterPro; IPR025574; Nucleoporin_FG_rpt.
DR InterPro; IPR037665; Nucleoporin_S59-like.
DR InterPro; IPR037637; NUP98-NUP96.
DR InterPro; IPR007230; Nup98_auto-Pept-S59_dom.
DR InterPro; IPR036903; Nup98_auto-Pept-S59_dom_sf.
DR PANTHER; PTHR23198; PTHR23198; 2.
DR PANTHER; PTHR23198:SF17; PTHR23198:SF17; 2.
DR Pfam; PF04096; Nucleoporin2; 1.
DR Pfam; PF13634; Nucleoporin_FG; 6.
DR SUPFAM; SSF82215; SSF82215; 1.
DR PROSITE; PS51434; NUP_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Membrane; mRNA transport; Nuclear pore complex; Nucleus;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat;
KW Translocation; Transport.
FT CHAIN 1..1113
FT /note="Nucleoporin NUP116/NSP116"
FT /id="PRO_0000204835"
FT REPEAT 2..3
FT /note="FG 1"
FT REPEAT 17..18
FT /note="FG 2"
FT REPEAT 24..25
FT /note="FG 3"
FT REPEAT 40..41
FT /note="FG 4"
FT REPEAT 55..58
FT /note="GLFG 1; approximate"
FT REPEAT 66..67
FT /note="FG 5"
FT REPEAT 79..80
FT /note="FG 6"
FT REPEAT 94..95
FT /note="FG 7"
FT REPEAT 167..168
FT /note="FG 8"
FT REPEAT 189..190
FT /note="FG 9"
FT REPEAT 205..208
FT /note="GLFG 2"
FT REPEAT 214..217
FT /note="GLFG 3; approximate"
FT REPEAT 224..227
FT /note="GLFG 4; approximate"
FT REPEAT 235..238
FT /note="GLFG 5"
FT REPEAT 249..250
FT /note="FG 10"
FT REPEAT 259..262
FT /note="GLFG 6"
FT REPEAT 276..279
FT /note="GLFG 7"
FT REPEAT 288..291
FT /note="GLFG 8"
FT REPEAT 297..298
FT /note="FG 11"
FT REPEAT 306..309
FT /note="GLFG 9; approximate"
FT REPEAT 327..330
FT /note="GLFG 10; approximate"
FT REPEAT 339..342
FT /note="GLFG 11; approximate"
FT REPEAT 351..352
FT /note="FG 12"
FT REPEAT 359..362
FT /note="GLFG 12"
FT REPEAT 370..371
FT /note="FG 13"
FT REPEAT 382..385
FT /note="GLFG 13"
FT REPEAT 395..398
FT /note="GLFG 14"
FT REPEAT 407..410
FT /note="GLFG 15"
FT REPEAT 420..423
FT /note="GLFG 16"
FT REPEAT 431..432
FT /note="FG 14"
FT REPEAT 439..442
FT /note="GLFG 17"
FT REPEAT 448..451
FT /note="GLFG 18"
FT REPEAT 470..471
FT /note="FG 15"
FT REPEAT 482..485
FT /note="GLFG 19"
FT REPEAT 497..500
FT /note="GLFG 20"
FT REPEAT 510..511
FT /note="FG 16"
FT REPEAT 525..526
FT /note="FG 17"
FT REPEAT 532..533
FT /note="FG 18"
FT REPEAT 572..575
FT /note="GLFG 21"
FT REPEAT 585..588
FT /note="GLFG 22"
FT REPEAT 604..607
FT /note="GLFG 23"
FT REPEAT 616..617
FT /note="FG 19"
FT REPEAT 630..633
FT /note="GLFG 24; approximate"
FT REPEAT 648..651
FT /note="GLFG 25"
FT REPEAT 665..668
FT /note="GLFG 26"
FT REPEAT 683..686
FT /note="GLFG 27"
FT DOMAIN 967..1109
FT /note="Peptidase S59"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00765"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..172
FT /note="Interaction with AFG2"
FT /evidence="ECO:0000269|PubMed:23185031"
FT REGION 110..166
FT /note="GLE2 binding sequence (GLEBS)"
FT REGION 160..362
FT /note="Interaction with MEX67, not KAP95"
FT /evidence="ECO:0000269|PubMed:11104765"
FT REGION 265..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..535
FT /note="Sufficient for interaction with MEX67 and KAP95"
FT /evidence="ECO:0000269|PubMed:11104765"
FT REGION 371..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..732
FT /note="Interaction with KAP95, not MEX67"
FT REGION 678..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 967..1113
FT /note="Interaction with NUP82 NPC subcomplex"
FT REGION 969..1108
FT /note="Nucleoporin RNA-binding motif (NRM)"
FT COMPBIAS 8..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..882
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..906
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 913..939
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 886
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 92..1113
FT /note="Missing: Loss of interaction with AFG2."
FT /evidence="ECO:0000269|PubMed:23185031"
FT MUTAGEN 110..166
FT /note="Missing: Prevents the release of AFG2, RLP24 and
FT NOG1 from pre-60S ribosomal particles. Enhances growth
FT defect in an AFG2 (drg1-18) mutant background."
FT /evidence="ECO:0000269|PubMed:23185031"
FT MUTAGEN 173..1113
FT /note="Missing: No effect on the interaction with AFG2."
FT /evidence="ECO:0000269|PubMed:23185031"
FT CONFLICT 26
FT /note="G -> A (in Ref. 1; CAA78754)"
FT /evidence="ECO:0000305"
FT CONFLICT 536
FT /note="S -> G (in Ref. 1; CAA78754)"
FT /evidence="ECO:0000305"
FT CONFLICT 720
FT /note="S -> P (in Ref. 1; CAA78754)"
FT /evidence="ECO:0000305"
FT CONFLICT 1018
FT /note="S -> Y (in Ref. 1; CAA78754)"
FT /evidence="ECO:0000305"
FT CONFLICT 1023
FT /note="I -> Y (in Ref. 1; CAA78754)"
FT /evidence="ECO:0000305"
FT STRAND 970..974
FT /evidence="ECO:0007829|PDB:3PBP"
FT HELIX 976..981
FT /evidence="ECO:0007829|PDB:3PBP"
FT STRAND 988..990
FT /evidence="ECO:0007829|PDB:3PBP"
FT STRAND 994..997
FT /evidence="ECO:0007829|PDB:3PBP"
FT TURN 998..1000
FT /evidence="ECO:0007829|PDB:3PBP"
FT STRAND 1001..1007
FT /evidence="ECO:0007829|PDB:3PBP"
FT TURN 1019..1022
FT /evidence="ECO:0007829|PDB:3PBP"
FT STRAND 1023..1027
FT /evidence="ECO:0007829|PDB:3PBP"
FT STRAND 1030..1034
FT /evidence="ECO:0007829|PDB:3PBP"
FT STRAND 1042..1044
FT /evidence="ECO:0007829|PDB:2AIV"
FT STRAND 1051..1056
FT /evidence="ECO:0007829|PDB:3PBP"
FT TURN 1063..1065
FT /evidence="ECO:0007829|PDB:3PBP"
FT HELIX 1075..1084
FT /evidence="ECO:0007829|PDB:3PBP"
FT STRAND 1088..1095
FT /evidence="ECO:0007829|PDB:3PBP"
FT TURN 1097..1099
FT /evidence="ECO:0007829|PDB:3PBP"
FT STRAND 1102..1107
FT /evidence="ECO:0007829|PDB:3PBP"
SQ SEQUENCE 1113 AA; 116234 MW; FBAB0B9AEA958213 CRC64;
MFGVSRGAFP SATTQPFGST GSTFGGQQQQ QQPVANTSAF GLSQQTNTTQ APAFGNFGNQ
TSNSPFGMSG STTANGTPFG QSQLTNNNAS GSIFGGMGNN TALSAGSASV VPNSTAGTSI
KPFTTFEEKD PTTGVINVFQ SITCMPEYRN FSFEELRFQD YQAGRKFGTS QNGTGTTFNN
PQGTTNTGFG IMGNNNSTTS ATTGGLFGQK PATGMFGTGT GSGGGFGSGA TNSTGLFGSS
TNLSGNSAFG ANKPATSGGL FGNTTNNPTN GTNNTGLFGQ QNSNTNGGLF GQQQNSFGAN
NVSNGGAFGQ VNRGAFPQQQ TQQGSGGIFG QSNANANGGA FGQQQGTGAL FGAKPASGGL
FGQSAGSKAF GMNTNPTGTT GGLFGQTNQQ QSGGGLFGQQ QNSNAGGLFG QNNQSQNQSG
LFGQQNSSNA FGQPQQQGGL FGSKPAGGLF GQQQGASTFA SGNAQNNSIF GQNNQQQQST
GGLFGQQNNQ SQSQPGGLFG QTNQNNNQPF GQNGLQQPQQ NNSLFGAKPT GFGNTSLFSN
STTNQSNGIS GNNLQQQSGG LFQNKQQPAS GGLFGSKPSN TVGGGLFGNN QVANQNNPAS
TSGGLFGSKP ATGSLFGGTN STAPNASSGG IFGSNNASNT AATTNSTGLF GNKPVGAGAS
TSAGGLFGNN NNSSLNNSNG STGLFGSNNT SQSTNAGGLF QNNTSTNTSG GGLFSQPSQS
MAQSQNALQQ QQQQQRLQIQ NNNPYGTNEL FSKATVTNTV SYPIQPSATK IKADERKKAS
LTNAYKMIPK TLFTAKLKTN NSVMDKAQIK VDPKLSISID KKNNQIAISN QQEENLDESI
LKASELLFNP DKRSFKNLIN NRKMLIASEE KNNGSQNNDM NFKSKSEEQE TILGKPKMDE
KETANGGERM VLSSKNDGED SATKHHSRNM DEENKENVAD LQKQEYSEDD KKAVFADVAE
KDASFINENY YISPSLDTLS SYSLLQLRKV PHLVVGHKSY GKIEFLEPVD LAGIPLTSLG
GVIITFEPKT CIIYANLPNR PKRGEGINVR ARITCFNCYP VDKSTRKPIK DPNHQLVKRH
IERLKKNPNS KFESYDADSG TYVFIVNHAA EQT
