ID NUP2_YEAST Reviewed; 720 AA. AC P32499; D6VYX5; Q06130; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2003, sequence version 2. DT 02-SEP-2026, entry version 232. DE RecName: Full=Nucleoporin NUP2; DE AltName: Full=Nuclear pore protein NUP2; DE AltName: Full=p95; GN Name=NUP2; OrderedLocusNames=YLR335W; ORFNames=L8300.9; 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]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=8443417; DOI=10.1091/mbc.4.2.209; RA Loeb J.D.J., Davis L.I., Fink G.R.; RT "NUP2, a novel yeast nucleoporin, has functional overlap with other RT proteins of the nuclear pore complex."; RL Mol. Biol. Cell 4:209-222(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169871; DOI=10.1038/387s087; RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J., RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., RA Zollner A., Hani J., Hoheisel J.D.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."; RL Nature 387:87-90(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 INTERACTION WITH KAP122. RX PubMed=10525531; DOI=10.1083/jcb.147.2.235; RA Titov A.A., Blobel G.; RT "The karyopherin Kap122p/Pdr6p imports both subunits of the transcription RT factor IIA into the nucleus."; RL J. Cell Biol. 147:235-246(1999). RN [5] RP FUNCTION, IDENTIFICATION IN THE NUCLEAR PORE COMPLEX, AND SUBCELLULAR RP 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 [6] RP FUNCTION, AND SRP1 RECYCLING. RX PubMed=11046143; DOI=10.1128/mcb.20.22.8468-8479.2000; RA Solsbacher J., Maurer P., Vogel F., Schlenstedt G.; RT "Nup2p, a yeast nucleoporin, functions in bidirectional transport of RT importin alpha."; RL Mol. Cell. Biol. 20:8468-8479(2000). RN [7] RP FUNCTION, AND INTERACTION 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 [8] RP FUNCTION, AND ASSOCIATION WITH NPC. RX PubMed=11425876; DOI=10.1083/jcb.153.7.1465; RA Dilworth D.J., Suprapto A., Padovan J.C., Chait B.T., Wozniak R.W., RA Rout M.P., Aitchison J.D.; RT "Nup2p dynamically associates with the distal regions of the yeast nuclear RT pore complex."; RL J. Cell Biol. 153:1465-1478(2001). RN [9] RP FUNCTION, AND INTERACTION WITH NUP60. RX PubMed=11535617; DOI=10.1083/jcb.200101007; RA Denning D.P., Mykytka B., Allen N.P., Huang L., Burlingame A., Rexach M.; RT "The nucleoporin Nup60p functions as a Gsp1p-GTP-sensitive tether for Nup2p RT at the nuclear pore complex."; RL J. Cell Biol. 154:937-950(2001). RN [10] RP FUNCTION, AND STRUCTURAL BASIS OF FG REPEAT INTERACTION. 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 [11] RP FUNCTION, AND INTERACTION WITH KARYOPHERINS THROUGH FG REPEATS. 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 [12] RP FUNCTION, AND CHROMATIN BOUNDARY ACTIVITY. RX PubMed=12062099; DOI=10.1016/s0092-8674(02)00756-0; RA Ishii K., Arib G., Lin C., Van Houwe G., Laemmli U.K.; RT "Chromatin boundaries in budding yeast: the nuclear pore connection."; RL Cell 109:551-562(2002). RN [13] RP FUNCTION, AND SRP1-KAP95 NUCLEAR IMPORT COMPLEX DISASSEMBLY. RX PubMed=11867631; DOI=10.1074/jbc.m112306200; RA Gilchrist D., Mykytka B., Rexach M.; RT "Accelerating the rate of disassembly of karyopherin-cargo complexes."; RL J. Biol. Chem. 277:18161-18172(2002). RN [14] RP FUNCTION, AND FG REPEAT AFFINITY GRADIENT FOR KARYOPHERIN KAP95. RX PubMed=12917401; DOI=10.1074/jbc.m307135200; RA Pyhtila B., Rexach M.; RT "A gradient of affinity for the karyopherin Kap95p along the yeast nuclear RT pore complex."; RL J. Biol. Chem. 278:42699-42709(2003). 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 INTERACTION WITH SRP1. RX PubMed=14514698; DOI=10.1074/jbc.m307371200; RA Gilchrist D., Rexach M.; RT "Molecular basis for the rapid dissociation of nuclear localization signals RT from karyopherin alpha in the nucleoplasm."; RL J. Biol. Chem. 278:51937-51949(2003). RN [18] 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 [19] 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 [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-20; SER-165 AND RP SER-203, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-20; SER-203 AND RP SER-205, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=17287358; DOI=10.1073/pnas.0607084104; RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; RT "Analysis of phosphorylation sites on proteins from Saccharomyces RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry."; RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-20; SER-137; SER-203; RP SER-205 AND SER-351, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP 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 [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-20; SER-203; SER-348; RP THR-361; SER-581 AND THR-590, 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 [24] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 36-50 IN COMPLEX WITH SRP1. RX PubMed=14532109; DOI=10.1093/emboj/cdg538; RA Matsuura Y., Lange A., Harreman M.T., Corbett A.H., Stewart M.; RT "Structural basis for Nup2p function in cargo release and karyopherin RT recycling in nuclear import."; RL EMBO J. 22:5358-5369(2003). 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). As one of the FG repeat CC nucleoporins NUP2 is involved in interactions with and guidance of CC nuclear transport receptors such as SRP1-KAP95 (importin alpha and CC beta) through the NPC. Like the closely related NUP1 it also plays an CC important role in disassembling and recycling SRP1-KAP95 to the CC cytoplasm after nuclear import. Upon entry of the heterotrimeric SRP1- CC KAP95-cargo complex in the nucleus, NUP2 binds through its N-terminus CC to the SRP1 nuclear localization signal (NLS) binding site, thus CC accelerating the release of the NLS-cargo. SRP1 in turn is released CC from NUP2 by binding of the GSP1-GTP associated export factor CSE1. CC NUP2 may also have a chromatin boundary/insulator activity through CC indirect interaction with genomic DNA via CSE1 and blocking of CC heterochromatin spreading. {ECO:0000269|PubMed:10684247, CC ECO:0000269|PubMed:11046143, ECO:0000269|PubMed:11387327, CC ECO:0000269|PubMed:11425876, ECO:0000269|PubMed:11535617, CC ECO:0000269|PubMed:11867631, ECO:0000269|PubMed:12062099, CC ECO:0000269|PubMed:12372823, ECO:0000269|PubMed:12543930, CC ECO:0000269|PubMed:12604785, ECO:0000269|PubMed:12917401, CC ECO:0000269|PubMed:14514698, ECO:0000269|PubMed:15039779}. 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 Binds to the nuclear basket of the NPC through NUP60 in a (GSP1, GSP2) CC GTPase-GTP-dependent manner. Interacts through its FG repeats with CC nuclear transport factors. Interacts with KAP122. CC {ECO:0000269|PubMed:10525531, ECO:0000269|PubMed:10684247, CC ECO:0000269|PubMed:11387327, ECO:0000269|PubMed:11535617, CC ECO:0000269|PubMed:12543930, ECO:0000269|PubMed:14514698, CC ECO:0000269|PubMed:14532109}. CC -!- INTERACTION: CC P32499; Q06142: KAP95; NbExp=6; IntAct=EBI-12401, EBI-9145; CC P32499; P39705: NUP60; NbExp=3; IntAct=EBI-12401, EBI-20731; CC P32499; Q02821: SRP1; NbExp=5; IntAct=EBI-12401, EBI-1797; CC -!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex CC {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral membrane CC protein; Nucleoplasmic 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: FXFG repeats CC are especially abundant in NUPs on the nucleoplasmic side (in a highly CC charged environment and enriched in Ser and Thr). CC -!- MISCELLANEOUS: Present with 2960 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; X69964; CAA49587.1; -; Genomic_DNA. DR EMBL; U19028; AAB67259.1; -; Genomic_DNA. DR EMBL; BK006945; DAA09641.1; -; Genomic_DNA. DR PIR; S51340; S51340. DR RefSeq; NP_013439.1; NM_001182224.1. DR PDB; 1UN0; X-ray; 2.60 A; C/D=1-51. DR PDB; 2C1T; X-ray; 2.60 A; C/D=1-51. DR AlphaFoldDB; P32499; -. DR SMR; P32499; -. DR BioGRID; 31599; 235. DR ComplexPortal; CPX-824; Nuclear pore complex. DR DIP; DIP-859N; -. DR FunCoup; P32499; 286. DR IntAct; P32499; 31. DR MINT; P32499; -. DR STRING; 4932.YLR335W; -. DR TCDB; 1.I.1.1.1; the nuclear pore complex (npc) family. DR GlyGen; P32499; 16 sites, 1 O-linked glycan (16 sites). DR iPTMnet; P32499; -. DR PaxDb; 4932-YLR335W; -. DR PeptideAtlas; P32499; -. DR DNASU; 851048; -. DR EnsemblFungi; YLR335W_mRNA; YLR335W; YLR335W. DR GeneID; 851048; -. DR KEGG; sce:YLR335W; -. DR AGR; SGD:S000004327; -. DR SGD; S000004327; NUP2. DR VEuPathDB; FungiDB:YLR335W; -. DR eggNOG; KOG0864; Eukaryota. DR eggNOG; KOG4719; Eukaryota. DR HOGENOM; CLU_018357_0_0_1; -. DR InParanoid; P32499; -. DR OMA; SDGMGHI; -. DR OrthoDB; 185618at2759; -. DR BioCyc; YEAST:G3O-32414-MONOMER; -. DR BioGRID-ORCS; 851048; 0 hits in 10 CRISPR screens. DR EvolutionaryTrace; P32499; -. DR PRO; PR:P32499; -. DR Proteomes; UP000002311; Chromosome XII. DR RNAct; P32499; protein. DR GO; GO:0000781; C:chromosome, telomeric region; IEA:GOC. DR GO; GO:0005737; C:cytoplasm; IDA:CAFA. DR GO; GO:0005739; C:mitochondrion; HDA:SGD. DR GO; GO:0042564; C:NLS-dependent protein nuclear import complex; IMP:CAFA. 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; IBA:GO_Central. DR GO; GO:0044614; C:nuclear pore cytoplasmic filaments; IDA:SGD. DR GO; GO:0044615; C:nuclear pore nuclear basket; IDA:SGD. DR GO; GO:0061676; F:importin-alpha family protein binding; IPI:CAFA. DR GO; GO:0031267; F:small GTPase binding; IPI:SGD. DR GO; GO:0017056; F:structural constituent of nuclear pore; IGI:SGD. DR GO; GO:0031990; P:mRNA export from nucleus in response to heat stress; IMP:SGD. DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; IDA: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:0000973; P:post-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery; IMP:SGD. DR GO; GO:0006611; P:protein export from nucleus; IMP:SGD. DR GO; GO:0036228; P:protein localization to nuclear inner membrane; IMP:SGD. DR GO; GO:0030466; P:silent mating-type cassette heterochromatin formation; IMP:SGD. DR GO; GO:0031509; P:subtelomeric heterochromatin formation; IMP:SGD. DR GO; GO:0000972; P:transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery; IMP:SGD. DR DisProt; DP00222; -. DR FunFam; 2.30.29.30:FF:000623; Nucleoporin nup61; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1. DR IDEAL; IID50007; -. DR InterPro; IPR053074; NPC_Nucleoporin. DR InterPro; IPR015007; NUP2/50/61. DR InterPro; IPR011993; PH-like_dom_sf. DR InterPro; IPR000156; Ran_bind_dom. DR PANTHER; PTHR38697; NUCLEAR PORE COMPLEX PROTEIN SIMILAR TO S. CEREVISIAE NUP2 (EUROFUNG); 1. DR PANTHER; PTHR38697:SF1; NUCLEAR PORE COMPLEX PROTEIN SIMILAR TO S. CEREVISIAE NUP2 (EUROFUNG); 1. DR Pfam; PF08911; NUP50; 1. DR Pfam; PF00638; Ran_BP1; 1. DR SMART; SM00160; RanBD; 1. DR SUPFAM; SSF50729; PH domain-like; 1. DR PROSITE; PS50196; RANBD1; 1. DR PDBsum; 1UN0; -. DR PDBsum; 2C1T; -. 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..720 FT /note="Nucleoporin NUP2" FT /id="PRO_0000204903" FT REPEAT 67..69 FT /note="FXF 1" FT REPEAT 189..192 FT /note="FXFG 1" FT REPEAT 216..218 FT /note="FXF 2" FT REPEAT 247..249 FT /note="FXF 3" FT REPEAT 285..288 FT /note="FXFG 2" FT REPEAT 302..305 FT /note="FXFG 3" FT REPEAT 318..321 FT /note="FXFG 4" FT REPEAT 352..354 FT /note="FXF 4" FT REPEAT 369..372 FT /note="FXFG 5" FT REPEAT 386..389 FT /note="FXFG 6" FT REPEAT 438..441 FT /note="FXFG 7" FT REPEAT 474..477 FT /note="FXFG 8" FT REPEAT 493..496 FT /note="FXFG 9" FT REPEAT 511..514 FT /note="FXFG 10" FT REPEAT 524..527 FT /note="FXFG 11" FT REPEAT 550..552 FT /note="FXF 5" FT DOMAIN 583..720 FT /note="RanBD1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00164" FT REGION 1..33 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 35..50 FT /note="Interaction with SRP1 NLS binding site 1" FT REGION 52..92 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 136..278 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 315..604 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 81..92 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 147..159 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 193..202 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 243..278 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 315..324 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 345..360 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 373..384 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 424..435 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 479..495 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 513..533 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 534..548 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 574..584 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 17 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17287358, FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, FT ECO:0007744|PubMed:19779198" FT MOD_RES 20 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17287358, FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, FT ECO:0007744|PubMed:19779198" FT MOD_RES 137 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MOD_RES 165 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950" FT MOD_RES 203 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17287358, FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, FT ECO:0007744|PubMed:19779198" FT MOD_RES 205 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17287358, FT ECO:0007744|PubMed:18407956" FT MOD_RES 348 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 351 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MOD_RES 361 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 581 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" FT MOD_RES 590 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19779198" FT CONFLICT 137 FT /note="S -> F (in Ref. 1; CAA49587)" FT /evidence="ECO:0000305" FT CONFLICT 370 FT /note="S -> N (in Ref. 1; CAA49587)" FT /evidence="ECO:0000305" FT CONFLICT 418 FT /note="L -> F (in Ref. 1; CAA49587)" FT /evidence="ECO:0000305" FT TURN 12..14 FT /evidence="ECO:0007829|PDB:2C1T" FT HELIX 34..37 FT /evidence="ECO:0007829|PDB:2C1T" FT TURN 47..49 FT /evidence="ECO:0007829|PDB:1UN0" SQ SEQUENCE 720 AA; 77881 MW; 467210F14FA73311 CRC64; MAKRVADAQI QRETYDSNES DDDVTPSTKV ASSAVMNRRK IAMPKRRMAF KPFGSAKSDE TKQASSFSFL NRADGTGEAQ VDNSPTTESN SRLKALNLQF KAKVDDLVLG KPLADLRPLF TRYELYIKNI LEAPVKSIEN PTQTKGNDAK PAKVEDVQKS SDSSSEDEVK VEGPKFTIDA KPPISDSVFS FGPKKENRKK DESDSENDIE IKGPEFKFSG TVSSDVFKLN PSTDKNEKKT ETNAKPFSFS SATSTTEQTK SKNPLSLTEA TKTNVDNNSK AEASFTFGTK HAADSQNNKP SFVFGQAAAK PSLEKSSFTF GSTTIEKKND ENSTSNSKPE KSSDSNDSNP SFSFSIPSKN TPDASKPSFS FGVPNSSKNE TSKPVFSFGA ATPSAKEASQ EDDNNNVEKP SSKPAFNLIS NAGTEKEKES KKDSKPAFSF GISNGSESKD SDKPSLPSAV DGENDKKEAT KPAFSFGINT NTTKTADTKA PTFTFGSSAL ADNKEDVKKP FSFGTSQPNN TPSFSFGKTT ANLPANSSTS PAPSIPSTGF KFSLPFEQKG SQTTTNDSKE ESTTEATGNE SQDATKVDAT PEESKPINLQ NGEEDEVALF SQKAKLMTFN AETKSYDSRG VGEMKLLKKK DDPSKVRLLC RSDGMGNVLL NATVVDSFKY EPLAPGNDNL IKAPTVAADG KLVTYIVKFK QKEEGRSFTK AIEDAKKEMK //