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 27-MAR-2024, entry version 222.
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;
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=5; IntAct=EBI-12401, EBI-9145;
CC P32499; P39705: NUP60; NbExp=2; IntAct=EBI-12401, EBI-20731;
CC P32499; Q02821: SRP1; NbExp=4; 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}.
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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 PDBsum; 1UN0; -.
DR PDBsum; 2C1T; -.
DR AlphaFoldDB; P32499; -.
DR SMR; P32499; -.
DR BioGRID; 31599; 215.
DR ComplexPortal; CPX-824; Nuclear pore complex.
DR DIP; DIP-859N; -.
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; 15 sites, 1 O-linked glycan (15 sites).
DR iPTMnet; P32499; -.
DR MaxQB; 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; 2730050at2759; -.
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 Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR IDEAL; IID50007; -.
DR InterPro; IPR015007; NUP2/50/61.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000156; Ran_bind_dom.
DR InterPro; IPR045255; RanBP1-like.
DR PANTHER; PTHR23138:SF101; NUCLEOPORIN NUP2; 1.
DR PANTHER; PTHR23138; RAN BINDING PROTEIN; 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.
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 1..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..213
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..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..585
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
//
