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 02-SEP-2026, entry version 226. 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; Q02199: NUP49; NbExp=3; IntAct=EBI-12265, EBI-12315; CC P14907; P48837: NUP57; NbExp=6; IntAct=EBI-12265, EBI-12324; CC P14907; P40368: NUP82; NbExp=8; 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}. 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; 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=496-608. 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 PDB; 8TJ5; EM; 6.60 A; A/D/G/J=1-823. DR AlphaFoldDB; P14907; -. DR BMRB; P14907; -. DR EMDB; EMD-24232; -. DR EMDB; EMD-24258; -. DR EMDB; EMD-32653; -. DR EMDB; EMD-32658; -. DR EMDB; EMD-41300; -. DR SASBDB; P14907; -. DR SMR; P14907; -. DR BioGRID; 33717; 152. DR ComplexPortal; CPX-824; Nuclear pore complex. DR DIP; DIP-1484N; -. DR FunCoup; P14907; 448. DR IntAct; P14907; 46. DR MINT; P14907; -. DR STRING; 4932.YJL041W; -. DR TCDB; 1.I.1.1.1; the nuclear pore complex (npc) family. DR CarbonylDB; P14907; -. DR GlyGen; P14907; 11 sites, 1 O-linked glycan (11 sites). DR iPTMnet; P14907; -. DR PaxDb; 4932-YJL041W; -. DR PeptideAtlas; P14907; -. DR GeneID; 853409; -. DR KEGG; sce:YJL041W; -. DR AGR; SGD:S000003577; -. 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 OrthoDB; 344345at2759; -. DR BioCyc; YEAST:G3O-31506-MONOMER; -. DR BioGRID-ORCS; 853409; 7 hits in 10 CRISPR screens. DR CD-CODE; 691A1FB1; Nuclear pore complex. DR EvolutionaryTrace; P14907; -. DR PRO; PR:P14907; -. DR Proteomes; UP000002311; Chromosome X. DR RNAct; P14907; protein. DR GO; GO:0005635; C:nuclear envelope; NAS: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:0006607; P:NLS-bearing protein import into nucleus; IGI:SGD. DR GO; GO:0006913; P:nucleocytoplasmic transport; NAS: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; IMP:SGD. DR GO; GO:0006409; P:tRNA export from nucleus; IMP:SGD. DR DisProt; DP01077; -. DR FunFam; 1.20.5.170:FF:000040; Nuclear pore glycoprotein p62; 1. DR Gene3D; 1.20.5.170; -; 1. DR IDEAL; IID50140; -. DR InterPro; IPR026010; NSP1/NUP62. DR InterPro; IPR007758; Nucleoporin_NSP1_C. DR PANTHER; PTHR12084:SF0; NUCLEAR PORE GLYCOPROTEIN P62; 1. DR PANTHER; PTHR12084; NUCLEAR PORE GLYCOPROTEIN P62-RELATED; 1. DR Pfam; PF05064; Nsp1_C; 1. DR PDBsum; 1O6O; -. DR PDBsum; 7N85; -. DR PDBsum; 7N9F; -. DR PDBsum; 7WOO; -. DR PDBsum; 7WOT; -. DR PDBsum; 8TJ5; -. 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..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 1..18 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 19..31 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 46..63 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 70..79 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 80..89 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 129..144 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 152..166 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 186..195 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 199..229 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 238..252 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 270..281 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 308..317 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 365..374 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 403..412 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 460..469 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 479..488 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 517..527 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 537..547 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 594..604 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 605..620 FT /note="Polar 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 //