NSP1_YEAST
ID NSP1_YEAST Reviewed; 823 AA.
AC P14907; D6VWE3;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Nucleoporin NSP1;
DE AltName: Full=Nuclear pore protein NSP1;
DE AltName: Full=Nucleoskeletal-like protein;
DE AltName: Full=p110;
GN Name=NSP1; OrderedLocusNames=YJL041W; ORFNames=J1207;
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=3072197; DOI=10.1002/j.1460-2075.1988.tb03331.x;
RA Hurt E.C.;
RT "A novel nucleoskeletal-like protein located at the nuclear periphery is
RT required for the life cycle of Saccharomyces cerevisiae.";
RL EMBO J. 7:4323-4334(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
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 DOMAINS.
RX PubMed=2112428; DOI=10.1016/0092-8674(90)90063-k;
RA Nehrbass U., Kern H., Mutvei A., Horstmann H., Marshallsay B., Hurt E.C.;
RT "NSP1: a yeast nuclear envelope protein localized at the nuclear pores
RT exerts its essential function by its carboxy-terminal domain.";
RL Cell 61:979-989(1990).
RN [5]
RP FUNCTION, AND NUP57 NPC SUBCOMPLEX.
RX PubMed=9017593; DOI=10.1091/mbc.8.1.33;
RA Schlaich N.L., Haener M., Lustig A., Aebi U., Hurt E.C.;
RT "In vitro reconstitution of a heterotrimeric nucleoporin complex consisting
RT of recombinant Nsp1p, Nup49p, and Nup57p.";
RL Mol. Biol. Cell 8:33-46(1997).
RN [6]
RP FUNCTION, AND INTERACTION WITH LOS1.
RX PubMed=9774653; DOI=10.1128/mcb.18.11.6374;
RA Hellmuth K., Lau D.M., Bischoff F.R., Kuenzler M., Hurt E.C., Simos G.;
RT "Yeast Los1p has properties of an exportin-like nucleocytoplasmic transport
RT factor for tRNA.";
RL Mol. Cell. Biol. 18:6374-6386(1998).
RN [7]
RP FUNCTION, AND INTERACTION WITH GSP1.
RX PubMed=9461539; DOI=10.1042/bj3300421;
RA Stochaj U., Hejazi M., Belhumeur P.;
RT "The small GTPase Gsp1p binds to the repeat domain of the nucleoporin
RT Nsp1p.";
RL Biochem. J. 330:421-427(1998).
RN [8]
RP FUNCTION, AND INTERACTION WITH NUP159.
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 [9]
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 [10]
RP FUNCTION, AND INTERACTION WITH NTF2.
RX PubMed=10889207; DOI=10.1074/jbc.m005055200;
RA Quimby B.B., Lamitina T., L'Hernault S.W., Corbett A.H.;
RT "The mechanism of ran import into the nucleus by nuclear transport factor
RT 2.";
RL J. Biol. Chem. 275:28575-28582(2000).
RN [11]
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 [12]
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 [13]
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 [14]
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 [15]
RP FUNCTION, AND NUCLEAR SRP EXPORT.
RX PubMed=11352936; DOI=10.1083/jcb.153.4.745;
RA Grosshans H., Deinert K., Hurt E.C., Simos G.;
RT "Biogenesis of the signal recognition particle (SRP) involves import of SRP
RT proteins into the nucleolus, assembly with the SRP-RNA, and Xpo1p-mediated
RT export.";
RL J. Cell Biol. 153:745-762(2001).
RN [16]
RP FUNCTION, SUBCOMPLEX ASSEMBLY, AND INTERACTION WITH NUP57 AND NUP82.
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 [17]
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 [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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238; SER-361 AND SER-456, AND
RP IDENTIFICATION BY MASS 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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-631, 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 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 [24]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 511-516 IN COMPLEX WITH HUMAN
RP IMPORTIN BETA-1 SUBUNIT, STRUCTURAL BASIS OF FG REPEAT INTERACTION, AND
RP INTERACTION WITH 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).
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). NSP1 plays an important role
CC in several nuclear transport pathways including poly(A)+ RNA, tRNA,
CC pre-ribosome, signal recognition particle (SRP), and protein transport.
CC {ECO:0000269|PubMed:10889207, ECO:0000269|PubMed:10952996,
CC ECO:0000269|PubMed:11352936, ECO:0000269|PubMed:11387327,
CC ECO:0000269|PubMed:11689687, ECO:0000269|PubMed:11739405,
CC ECO:0000269|PubMed:12604785, ECO:0000269|PubMed:15039779,
CC ECO:0000269|PubMed:9017593, ECO:0000269|PubMed:9461539,
CC ECO:0000269|PubMed:9774653, ECO:0000269|PubMed:9843582,
CC ECO:0000269|PubMed:9891088}.
CC -!- SUBUNIT: Component of the nuclear pore complex (NPC). NPC constitutes
CC the exclusive means of nucleocytoplasmic transport. NPCs allow the
CC passive diffusion of ions and small molecules and the active, nuclear
CC transport receptor-mediated bidirectional transport of macromolecules
CC such as proteins, RNAs, ribonucleoparticles (RNPs), and ribosomal
CC subunits across the nuclear envelope. Due to its 8-fold rotational
CC symmetry, all subunits are present with 8 copies or multiples thereof.
CC NSP1 interacts alternatively with NUP82 or NUP57 through its C-terminal
CC coiled coil in two distinct NPC subcomplexes, the NUP82 subcomplex and
CC the NUP57 subcomplex (NIC96, NSP1, NUP49, NUP57). The NUP82 subcomplex
CC is the base for interactions with NUP116 and GLE2 and with NUP42 and
CC GLE1. Interacts through its FG repeats with karyopherins, such as
CC KAP95, KAP123, PSE1, LOS1, NTF2, the heterodimeric mRNA transport
CC factor MEX67/MTR2, and GSP1. {ECO:0000269|PubMed:10889207,
CC ECO:0000269|PubMed:10952996, ECO:0000269|PubMed:11689687,
CC ECO:0000269|PubMed:12372823, ECO:0000269|PubMed:25646085,
CC ECO:0000269|PubMed:9461539, ECO:0000269|PubMed:9774653,
CC ECO:0000269|PubMed:9843582, ECO:0000269|PubMed:9891088}.
CC -!- INTERACTION:
CC P14907; Q06142: KAP95; NbExp=4; IntAct=EBI-12265, EBI-9145;
CC P14907; P48837: NUP57; NbExp=5; IntAct=EBI-12265, EBI-12324;
CC P14907; P40368: NUP82; NbExp=7; IntAct=EBI-12265, EBI-12331;
CC P14907; Q14974: KPNB1; Xeno; NbExp=2; IntAct=EBI-12265, EBI-286758;
CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex. Nucleus membrane;
CC Peripheral membrane protein; Cytoplasmic side. Nucleus membrane;
CC Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric
CC distribution.
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.
CC {ECO:0000269|PubMed:2112428}.
CC -!- MISCELLANEOUS: Present with 2400 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the nucleoporin NSP1/NUP62 family.
CC {ECO:0000305}.
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DR EMBL; M37160; AAA34821.1; -; Genomic_DNA.
DR EMBL; Z49316; CAA89332.1; -; Genomic_DNA.
DR EMBL; Z49314; CAA89331.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08759.1; -; Genomic_DNA.
DR PIR; S14055; S14055.
DR RefSeq; NP_012494.3; NM_001181474.3.
DR PDB; 1O6O; X-ray; 2.80 A; D/E/F=497-608.
DR PDB; 7N85; EM; 7.60 A; A/D/G/J=1-823.
DR PDB; 7N9F; EM; 37.00 A; A/D/G/J/y/z=1-823.
DR PDB; 7WOO; EM; 3.71 A; I/L=1-823.
DR PDB; 7WOT; EM; 3.73 A; I/L/U/X=1-823.
DR PDBsum; 1O6O; -.
DR PDBsum; 7N85; -.
DR PDBsum; 7N9F; -.
DR PDBsum; 7WOO; -.
DR PDBsum; 7WOT; -.
DR AlphaFoldDB; P14907; -.
DR BMRB; P14907; -.
DR SASBDB; P14907; -.
DR SMR; P14907; -.
DR BioGRID; 33717; 139.
DR ComplexPortal; CPX-824; Nuclear pore complex.
DR DIP; DIP-1484N; -.
DR IntAct; P14907; 38.
DR MINT; P14907; -.
DR STRING; 4932.YJL041W; -.
DR TCDB; 1.I.1.1.1; the nuclear pore complex (npc) family.
DR CarbonylDB; P14907; -.
DR iPTMnet; P14907; -.
DR MaxQB; P14907; -.
DR PaxDb; P14907; -.
DR PRIDE; P14907; -.
DR GeneID; 853409; -.
DR KEGG; sce:YJL041W; -.
DR SGD; S000003577; NSP1.
DR VEuPathDB; FungiDB:YJL041W; -.
DR eggNOG; KOG2196; Eukaryota.
DR eggNOG; KOG4719; Eukaryota.
DR HOGENOM; CLU_020542_0_0_1; -.
DR InParanoid; P14907; -.
DR OMA; EMMSKQV; -.
DR BioCyc; YEAST:G3O-31506-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; P14907; -.
DR PRO; PR:P14907; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P14907; protein.
DR GO; GO:0005635; C:nuclear envelope; IC:ComplexPortal.
DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034399; C:nuclear periphery; HDA:SGD.
DR GO; GO:0005643; C:nuclear pore; IDA:SGD.
DR GO; GO:0044613; C:nuclear pore central transport channel; IDA:SGD.
DR GO; GO:0044615; C:nuclear pore nuclear basket; IDA:SGD.
DR GO; GO:0005543; F:phospholipid binding; IDA:SGD.
DR GO; GO:0017056; F:structural constituent of nuclear pore; IDA:SGD.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
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:0006913; P:nucleocytoplasmic transport; IC:ComplexPortal.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IGI:SGD.
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:0000056; P:ribosomal small 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 DisProt; DP01077; -.
DR IDEAL; IID50140; -.
DR InterPro; IPR026010; NSP1/NUP62.
DR InterPro; IPR007758; Nucleoporin_NSP1_C.
DR PANTHER; PTHR12084; PTHR12084; 1.
DR Pfam; PF05064; Nsp1_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Coiled coil; Membrane; mRNA transport;
KW Nuclear pore complex; Nucleus; Phosphoprotein; Protein transport;
KW Reference proteome; Repeat; Translocation; Transport.
FT CHAIN 1..823
FT /note="Nucleoporin NSP1"
FT /id="PRO_0000204865"
FT REPEAT 13..16
FT /note="FSFG 1"
FT REPEAT 36..37
FT /note="FG 1"
FT REPEAT 43..44
FT /note="FG 2"
FT REPEAT 64..65
FT /note="FG 3"
FT REPEAT 74..75
FT /note="FG 4"
FT REPEAT 84..85
FT /note="FG 5"
FT REPEAT 94..95
FT /note="FG 6"
FT REPEAT 104..105
FT /note="FG 7"
FT REPEAT 123..124
FT /note="FG 8"
FT REPEAT 142..143
FT /note="FG 9"
FT REPEAT 147..148
FT /note="FG 10"
FT REPEAT 168..169
FT /note="FG 11"
FT REPEAT 179..182
FT /note="FSFG 2"
FT REPEAT 217..220
FT /note="FSFG 3"
FT REPEAT 239..240
FT /note="FG 12"
FT REPEAT 268..269
FT /note="FG 13"
FT REPEAT 284..287
FT /note="FSFG 4"
FT REPEAT 303..306
FT /note="FSFG 5"
FT REPEAT 322..325
FT /note="FSFG 6"
FT REPEAT 341..344
FT /note="FSFG 7"
FT REPEAT 360..363
FT /note="FSFG 8"
FT REPEAT 379..382
FT /note="FSFG 9"
FT REPEAT 398..401
FT /note="FSFG 10"
FT REPEAT 417..420
FT /note="FSFG 11"
FT REPEAT 436..439
FT /note="FSFG 12"
FT REPEAT 455..458
FT /note="FSFG 13"
FT REPEAT 474..477
FT /note="FSFG 14"
FT REPEAT 493..496
FT /note="FSFG 15"
FT REPEAT 512..515
FT /note="FSFG 16"
FT REPEAT 531..534
FT /note="FSFG 17"
FT REPEAT 550..553
FT /note="FSFG 18"
FT REPEAT 571..572
FT /note="FG 14"
FT REPEAT 588..591
FT /note="FSFG 19; approximate"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 673..738
FT /note="Competitive binding site of NUP57 and NUP82"
FT REGION 740..823
FT /note="Required for association with NUP57 subcomplex"
FT COILED 630..823
FT /evidence="ECO:0000255"
FT COMPBIAS 129..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..606
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
SQ SEQUENCE 823 AA; 86516 MW; A258003CB1917810 CRC64;
MNFNTPQQNK TPFSFGTANN NSNTTNQNSS TGAGAFGTGQ STFGFNNSAP NNTNNANSSI
TPAFGSNNTG NTAFGNSNPT SNVFGSNNST TNTFGSNSAG TSLFGSSSAQ QTKSNGTAGG
NTFGSSSLFN NSTNSNTTKP AFGGLNFGGG NNTTPSSTGN ANTSNNLFGA TANANKPAFS
FGATTNDDKK TEPDKPAFSF NSSVGNKTDA QAPTTGFSFG SQLGGNKTVN EAAKPSLSFG
SGSAGANPAG ASQPEPTTNE PAKPALSFGT ATSDNKTTNT TPSFSFGAKS DENKAGATSK
PAFSFGAKPE EKKDDNSSKP AFSFGAKSNE DKQDGTAKPA FSFGAKPAEK NNNETSKPAF
SFGAKSDEKK DGDASKPAFS FGAKPDENKA SATSKPAFSF GAKPEEKKDD NSSKPAFSFG
AKSNEDKQDG TAKPAFSFGA KPAEKNNNET SKPAFSFGAK SDEKKDGDAS KPAFSFGAKS
DEKKDSDSSK PAFSFGTKSN EKKDSGSSKP AFSFGAKPDE KKNDEVSKPA FSFGAKANEK
KESDESKSAF SFGSKPTGKE EGDGAKAAIS FGAKPEEQKS SDTSKPAFTF GAQKDNEKKT
EESSTGKSTA DVKSSDSLKL NSKPVELKPV SLDNKTLDDL VTKWTNQLTE SASHFEQYTK
KINSWDQVLV KGGEQISQLY SDAVMAEHSQ NKIDQSLQYI ERQQDELENF LDNFETKTEA
LLSDVVSTSS GAAANNNDQK RQQAYKTAQT LDENLNSLSS NLSSLIVEIN NVSNTFNKTT
NIDINNEDEN IQLIKILNSH FDALRSLDDN STSLEKQINS IKK
