ID NOP3_YEAST Reviewed; 414 AA. AC Q01560; D6VT60; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 27-MAR-2024, entry version 227. DE RecName: Full=Serine/arginine (SR)-type shuttling mRNA binding protein NPL3 {ECO:0000305}; DE AltName: Full=Mitochondrial targeting suppressor 1 protein {ECO:0000303|PubMed:8224861}; DE AltName: Full=Nuclear polyadenylated RNA-binding protein 1 {ECO:0000303|PubMed:7962083}; DE AltName: Full=Nuclear protein localization protein 3 {ECO:0000303|PubMed:1392078}; DE AltName: Full=Polyadenylate-binding protein NPL3 {ECO:0000305}; GN Name=NPL3 {ECO:0000303|PubMed:1392078}; GN Synonyms=MTR13, MTS1 {ECO:0000303|PubMed:8224861}, NAB1 GN {ECO:0000303|PubMed:7962083}, NOP3 {ECO:0000303|PubMed:1429834}; GN OrderedLocusNames=YDR432W; ORFNames=D9461.19; 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], AND FUNCTION. RX PubMed=1429834; DOI=10.1083/jcb.119.4.737; RA Russell I.D., Tollervey D.; RT "NOP3 is an essential yeast protein which is required for pre-rRNA RT processing."; RL J. Cell Biol. 119:737-747(1992). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=1392078; DOI=10.1091/mbc.3.8.875; RA Bossie M.A., Dehoratious C., Barcelo G., Silver P.; RT "A mutant nuclear protein with similarity to RNA binding proteins RT interferes with nuclear import in yeast."; RL Mol. Biol. Cell 3:875-893(1992). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8224861; DOI=10.1016/0378-1119(93)90193-7; RA Ellis E.M., Reid G.A.; RT "The Saccharomyces cerevisiae MTS1 gene encodes a putative RNA-binding RT protein involved in mitochondrial protein targeting."; RL Gene 132:175-183(1993). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169867; RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., RA Mewes H.-W., Zollner A., Zaccaria P.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."; RL Nature 387:75-78(1997). RN [5] 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 [6] RP SUBCELLULAR LOCATION, AND BINDING TO POLYADENYLATED RNA. RX PubMed=7962083; DOI=10.1083/jcb.127.5.1173; RA Wilson S.M., Datar K.V., Paddy M.R., Swedlow J.R., Swanson M.S.; RT "Characterization of nuclear polyadenylated RNA-binding proteins in RT Saccharomyces cerevisiae."; RL J. Cell Biol. 127:1173-1184(1994). RN [7] RP FUNCTION. RX PubMed=8675010; DOI=10.1101/gad.10.10.1233; RA Lee M.S., Henry M., Silver P.A.; RT "A protein that shuttles between the nucleus and the cytoplasm is an RT important mediator of RNA export."; RL Genes Dev. 10:1233-1246(1996). RN [8] RP SUBCELLULAR LOCATION, AND METHYLATION BY HMT1. RX PubMed=9499403; DOI=10.1101/gad.12.5.679; RA Shen E.C., Henry M.F., Weiss V.H., Valentini S.R., Silver P.A., Lee M.S.; RT "Arginine methylation facilitates the nuclear export of hnRNP proteins."; RL Genes Dev. 12:679-691(1998). RN [9] RP INTERACTION WITH RRP6. RX PubMed=10611239; DOI=10.1128/mcb.20.2.604-616.2000; RA Burkard K.T.D., Butler J.S.; RT "A nuclear 3'-5' exonuclease involved in mRNA degradation interacts with RT Poly(A) polymerase and the hnRNA protein Npl3p."; RL Mol. Cell. Biol. 20:604-616(2000). RN [10] RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. RX PubMed=14562095; DOI=10.1038/nature02026; RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., RA Weissman J.S., O'Shea E.K.; RT "Global analysis of protein localization in budding yeast."; RL Nature 425:686-691(2003). RN [11] 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 [12] RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-411. RX PubMed=14676199; DOI=10.1074/jbc.c300522200; RA Haecker S., Krebber H.; RT "Differential export requirements for shuttling serine/arginine-type mRNA- RT binding proteins."; RL J. Biol. Chem. 279:5049-5052(2004). RN [13] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=15542855; DOI=10.1128/mcb.24.23.10479-10491.2004; RA Windgassen M., Sturm D., Cajigas I.J., Gonzalez C.I., Seedorf M., RA Bastians H., Krebber H.; RT "Yeast shuttling SR proteins Npl3p, Gbp2p, and Hrb1p are part of the RT translating mRNPs, and Npl3p can function as a translational repressor."; RL Mol. Cell. Biol. 24:10479-10491(2004). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, AND IDENTIFICATION BY RP 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 [15] RP FUNCTION. RX PubMed=19061647; DOI=10.1016/j.molcel.2008.11.013; RA Kress T.L., Krogan N.J., Guthrie C.; RT "A single SR-like protein, Npl3, promotes pre-mRNA splicing in budding RT yeast."; RL Mol. Cell 32:727-734(2008). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182 AND SER-224, 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 [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, 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 [18] RP FUNCTION. RX PubMed=23209445; DOI=10.1371/journal.pgen.1003101; RA Moehle E.A., Ryan C.J., Krogan N.J., Kress T.L., Guthrie C.; RT "The yeast SR-like protein Npl3 links chromatin modification to mRNA RT processing."; RL PLoS Genet. 8:e1003101-e1003101(2012). RN [19] RP METHYLATION AT ARG-307; ARG-314 AND ARG-321. RX PubMed=26081071; DOI=10.1002/pmic.201500075; RA Yagoub D., Hart-Smith G., Moecking J., Erce M.A., Wilkins M.R.; RT "Yeast proteins Gar1p, Nop1p, Npl3p, Nsr1p, and Rps2p are natively RT methylated and are substrates of the arginine methyltransferase Hmt1p."; RL Proteomics 15:3209-3218(2015). RN [20] RP METHYLATION AT ARG-307; ARG-314; ARG-321; ARG-329; ARG-337; ARG-344; RP ARG-351; ARG-358; ARG-363; ARG-377; ARG-384 AND ARG-391. RX PubMed=26046779; DOI=10.1002/pmic.201500032; RA Plank M., Fischer R., Geoghegan V., Charles P.D., Konietzny R., Acuto O., RA Pears C., Schofield C.J., Kessler B.M.; RT "Expanding the yeast protein arginine methylome."; RL Proteomics 15:3232-3243(2015). RN [21] RP SUBCELLULAR LOCATION. RX PubMed=26777405; DOI=10.1016/j.cell.2015.12.038; RA Jain S., Wheeler J.R., Walters R.W., Agrawal A., Barsic A., Parker R.; RT "ATPase-modulated stress granules contain a diverse proteome and RT substructure."; RL Cell 164:487-498(2016). RN [22] RP METHYLATION AT ARG-288; ARG-290; ARG-294; ARG-298; ARG-302; ARG-307; RP ARG-314; ARG-344; ARG-351; ARG-358; ARG-363; ARG-377; ARG-384 AND ARG-391, RP AND PHOSPHORYLATION AT SER-15; SER-79; SER-212; SER-224 AND SER-356. RX PubMed=33856219; DOI=10.1021/acs.jproteome.0c00927; RA Hamey J.J., Nguyen A., Wilkins M.R.; RT "Discovery of arginine methylation, phosphorylation, and their co- RT occurrence in condensate-associated proteins in Saccharomyces cerevisiae."; RL J. Proteome Res. 20:2420-2434(2021). RN [23] {ECO:0007744|PDB:2JD5} RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 408-414. RX PubMed=17239901; DOI=10.1016/j.jmb.2006.12.031; RA Lukasiewicz R., Nolen B., Adams J.A., Ghosh G.; RT "The RGG domain of Npl3p recruits Sky1p through docking interactions."; RL J. Mol. Biol. 367:249-261(2007). RN [24] {ECO:0007744|PDB:2OSQ, ECO:0007744|PDB:2OSR} RP STRUCTURE BY NMR OF 194-280. RX PubMed=18022637; DOI=10.1016/j.jmb.2007.09.029; RA Deka P., Bucheli M.E., Moore C., Buratowski S., Varani G.; RT "Structure of the yeast SR protein Npl3 and Interaction with mRNA 3'-end RT processing signals."; RL J. Mol. Biol. 375:136-150(2008). RN [25] {ECO:0007744|PDB:2JVO, ECO:0007744|PDB:2JVR} RP STRUCTURE BY NMR OF 193-282. RX PubMed=17936301; DOI=10.1016/j.jmb.2007.09.030; RA Skrisovska L., Allain F.H.; RT "Improved segmental isotope labeling methods for the NMR study of RT multidomain or large proteins: application to the RRMs of Npl3p and hnRNP RT L."; RL J. Mol. Biol. 375:151-164(2008). CC -!- FUNCTION: Involved in mRNA processing and export (PubMed:1429834, CC PubMed:8675010, PubMed:15542855, PubMed:19061647). Required for CC efficient splicing of a large set of pre-mRNAs by efficient co- CC transcriptional recruitment of the splicing machinery (PubMed:19061647, CC PubMed:23209445). Remains associated with the mRNP during early steps CC of translation elongation (PubMed:15542855). CC {ECO:0000269|PubMed:1429834, ECO:0000269|PubMed:15542855, CC ECO:0000269|PubMed:19061647, ECO:0000269|PubMed:23209445, CC ECO:0000269|PubMed:8675010}. CC -!- SUBUNIT: Interacts with RRP6. {ECO:0000269|PubMed:10611239}. CC -!- INTERACTION: CC Q01560; P40507: AIR1; NbExp=3; IntAct=EBI-12114, EBI-25083; CC Q01560; P25555: GBP2; NbExp=3; IntAct=EBI-12114, EBI-7410; CC Q01560; P38074: HMT1; NbExp=9; IntAct=EBI-12114, EBI-8394; CC Q01560; Q01560: NPL3; NbExp=3; IntAct=EBI-12114, EBI-12114; CC Q01560; P04456: RPL25; NbExp=2; IntAct=EBI-12114, EBI-15308; CC Q01560; P39940: RSP5; NbExp=2; IntAct=EBI-12114, EBI-16219; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14676199, CC ECO:0000269|PubMed:9499403}. Nucleus {ECO:0000269|PubMed:14562095, CC ECO:0000269|PubMed:14676199, ECO:0000269|PubMed:7962083, CC ECO:0000269|PubMed:9499403}. Cytoplasm, Stress granule CC {ECO:0000269|PubMed:26777405}. Note=Nuclear at steady state and its CC import is mediated by the karyopherin MTR10 (PubMed:14676199, CC PubMed:15542855). Export is dependent on active transcription and the CC export of mRNAs in general (PubMed:8675010, PubMed:14676199). CC {ECO:0000269|PubMed:14676199, ECO:0000269|PubMed:15542855, CC ECO:0000269|PubMed:8675010}. CC -!- PTM: Methylated by HMT1. The methylation is required for nuclear CC export. {ECO:0000269|PubMed:9499403}. CC -!- MISCELLANEOUS: Present with 78700 molecules/cell in log phase SD CC medium. {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the RRM GAR family. {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; X66019; CAA46817.1; -; Genomic_DNA. DR EMBL; M86731; AAA34818.1; -; Genomic_DNA. DR EMBL; X70951; CAA50291.1; -; Genomic_DNA. DR EMBL; U33007; AAB64865.1; -; Genomic_DNA. DR EMBL; BK006938; DAA12270.1; -; Genomic_DNA. DR PIR; JN0866; JN0866. DR RefSeq; NP_010720.3; NM_001180740.3. DR PDB; 2JD5; X-ray; 2.50 A; C=408-414. DR PDB; 2JVO; NMR; -; A=116-201. DR PDB; 2JVR; NMR; -; A=193-282. DR PDB; 2OSQ; NMR; -; A=121-194. DR PDB; 2OSR; NMR; -; A=194-280. DR PDB; 7QDD; NMR; -; B=114-201. DR PDB; 7QDE; NMR; -; B=114-282. DR PDB; 8B8S; Other; -; A=120-280. DR PDBsum; 2JD5; -. DR PDBsum; 2JVO; -. DR PDBsum; 2JVR; -. DR PDBsum; 2OSQ; -. DR PDBsum; 2OSR; -. DR PDBsum; 7QDD; -. DR PDBsum; 7QDE; -. DR PDBsum; 8B8S; -. DR AlphaFoldDB; Q01560; -. DR BMRB; Q01560; -. DR SASBDB; Q01560; -. DR SMR; Q01560; -. DR BioGRID; 32489; 1212. DR DIP; DIP-6464N; -. DR IntAct; Q01560; 40. DR MINT; Q01560; -. DR STRING; 4932.YDR432W; -. DR iPTMnet; Q01560; -. DR MaxQB; Q01560; -. DR PaxDb; 4932-YDR432W; -. DR PeptideAtlas; Q01560; -. DR EnsemblFungi; YDR432W_mRNA; YDR432W; YDR432W. DR GeneID; 852042; -. DR KEGG; sce:YDR432W; -. DR AGR; SGD:S000002840; -. DR SGD; S000002840; NPL3. DR VEuPathDB; FungiDB:YDR432W; -. DR eggNOG; KOG0106; Eukaryota. DR HOGENOM; CLU_054994_1_0_1; -. DR InParanoid; Q01560; -. DR OMA; PREPAYP; -. DR OrthoDB; 132255at2759; -. DR BioCyc; YEAST:G3O-29970-MONOMER; -. DR BioGRID-ORCS; 852042; 4 hits in 10 CRISPR screens. DR EvolutionaryTrace; Q01560; -. DR PRO; PR:Q01560; -. DR Proteomes; UP000002311; Chromosome IV. DR RNAct; Q01560; Protein. DR GO; GO:0005737; C:cytoplasm; IMP:SGD. DR GO; GO:0010494; C:cytoplasmic stress granule; HDA:SGD. DR GO; GO:0005634; C:nucleus; IDA:SGD. DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central. DR GO; GO:0031370; F:eukaryotic initiation factor 4G binding; IDA:SGD. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0003729; F:mRNA binding; IDA:SGD. DR GO; GO:0008143; F:poly(A) binding; IDA:SGD. DR GO; GO:0000993; F:RNA polymerase II complex binding; IPI:SGD. DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:SGD. DR GO; GO:2000805; P:negative regulation of termination of RNA polymerase II transcription, poly(A)-coupled; IDA:SGD. DR GO; GO:0017148; P:negative regulation of translation; IDA:SGD. DR GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; IDA:SGD. DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW. DR GO; GO:0006415; P:translational termination; IMP:SGD. DR CDD; cd12340; RBD_RRM1_NPL3; 1. DR CDD; cd12339; RRM2_SRSF1_4_like; 1. DR Gene3D; 3.30.70.330; -; 2. DR InterPro; IPR034166; Npl3_RRM1. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf. DR InterPro; IPR035979; RBD_domain_sf. DR InterPro; IPR000504; RRM_dom. DR PANTHER; PTHR23003:SF56; NUCLEOLAR PROTEIN 3-RELATED; 1. DR PANTHER; PTHR23003; RNA RECOGNITION MOTIF RRM DOMAIN CONTAINING PROTEIN; 1. DR Pfam; PF00076; RRM_1; 2. DR SMART; SM00360; RRM; 2. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2. DR PROSITE; PS50102; RRM; 2. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Methylation; mRNA processing; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein; KW Ribosome biogenesis; RNA-binding. FT CHAIN 1..414 FT /note="Serine/arginine (SR)-type shuttling mRNA binding FT protein NPL3" FT /id="PRO_0000081676" FT DOMAIN 125..195 FT /note="RRM 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT DOMAIN 200..275 FT /note="RRM 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176" FT REGION 1..119 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 269..299 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 343..414 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 48..64 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 93..108 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 395..414 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 15 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:33856219" FT MOD_RES 79 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:33856219" FT MOD_RES 182 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18407956" FT MOD_RES 212 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:33856219" FT MOD_RES 224 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:33856219, FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, FT ECO:0007744|PubMed:19779198" FT MOD_RES 288 FT /note="Dimethylated arginine" FT /evidence="ECO:0000269|PubMed:33856219" FT MOD_RES 290 FT /note="Dimethylated arginine" FT /evidence="ECO:0000269|PubMed:33856219" FT MOD_RES 294 FT /note="Dimethylated arginine" FT /evidence="ECO:0000269|PubMed:33856219" FT MOD_RES 298 FT /note="Dimethylated arginine" FT /evidence="ECO:0000269|PubMed:33856219" FT MOD_RES 302 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000269|PubMed:33856219" FT MOD_RES 307 FT /note="Dimethylated arginine; alternate" FT /evidence="ECO:0000269|PubMed:26081071, FT ECO:0000269|PubMed:33856219" FT MOD_RES 307 FT /note="Omega-N-methylarginine; alternate" FT /evidence="ECO:0000269|PubMed:26046779, FT ECO:0000269|PubMed:26081071, ECO:0000269|PubMed:33856219" FT MOD_RES 314 FT /note="Dimethylated arginine; alternate" FT /evidence="ECO:0000269|PubMed:33856219" FT MOD_RES 314 FT /note="Omega-N-methylarginine; alternate" FT /evidence="ECO:0000269|PubMed:26046779, FT ECO:0000269|PubMed:26081071, ECO:0000269|PubMed:33856219" FT MOD_RES 321 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000269|PubMed:26046779, FT ECO:0000269|PubMed:26081071" FT MOD_RES 329 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000269|PubMed:26046779" FT MOD_RES 337 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000269|PubMed:26046779" FT MOD_RES 344 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000269|PubMed:26046779, FT ECO:0000269|PubMed:33856219" FT MOD_RES 351 FT /note="Dimethylated arginine; alternate" FT /evidence="ECO:0000269|PubMed:33856219" FT MOD_RES 351 FT /note="Omega-N-methylarginine; alternate" FT /evidence="ECO:0000269|PubMed:26046779, FT ECO:0000269|PubMed:33856219" FT MOD_RES 356 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:33856219" FT MOD_RES 358 FT /note="Dimethylated arginine; alternate" FT /evidence="ECO:0000269|PubMed:33856219" FT MOD_RES 358 FT /note="Omega-N-methylarginine; alternate" FT /evidence="ECO:0000269|PubMed:26046779, FT ECO:0000269|PubMed:33856219" FT MOD_RES 363 FT /note="Dimethylated arginine; alternate" FT /evidence="ECO:0000269|PubMed:33856219" FT MOD_RES 363 FT /note="Omega-N-methylarginine; alternate" FT /evidence="ECO:0000269|PubMed:26046779, FT ECO:0000269|PubMed:33856219" FT MOD_RES 377 FT /note="Dimethylated arginine; alternate" FT /evidence="ECO:0000269|PubMed:33856219" FT MOD_RES 377 FT /note="Omega-N-methylarginine; alternate" FT /evidence="ECO:0000269|PubMed:26046779, FT ECO:0000269|PubMed:33856219" FT MOD_RES 384 FT /note="Dimethylated arginine; alternate" FT /evidence="ECO:0000269|PubMed:33856219" FT MOD_RES 384 FT /note="Omega-N-methylarginine; alternate" FT /evidence="ECO:0000269|PubMed:26046779, FT ECO:0000269|PubMed:33856219" FT MOD_RES 391 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000269|PubMed:26046779, FT ECO:0000269|PubMed:33856219" FT MUTAGEN 411 FT /note="S->A: Shifts localization of the protein to the FT cytoplasm at steady state." FT /evidence="ECO:0000269|PubMed:15542855" FT STRAND 125..129 FT /evidence="ECO:0007829|PDB:2JVO" FT HELIX 138..145 FT /evidence="ECO:0007829|PDB:2JVO" FT TURN 146..148 FT /evidence="ECO:0007829|PDB:2JVO" FT STRAND 153..157 FT /evidence="ECO:0007829|PDB:2JVO" FT STRAND 160..164 FT /evidence="ECO:0007829|PDB:2JVO" FT HELIX 168..178 FT /evidence="ECO:0007829|PDB:2JVO" FT STRAND 189..192 FT /evidence="ECO:0007829|PDB:2JVO" FT STRAND 200..205 FT /evidence="ECO:0007829|PDB:2JVR" FT HELIX 213..223 FT /evidence="ECO:0007829|PDB:2JVR" FT STRAND 228..231 FT /evidence="ECO:0007829|PDB:2JVR" FT STRAND 236..238 FT /evidence="ECO:0007829|PDB:2JVR" FT STRAND 241..247 FT /evidence="ECO:0007829|PDB:2JVR" FT HELIX 248..257 FT /evidence="ECO:0007829|PDB:2JVR" FT STRAND 261..263 FT /evidence="ECO:0007829|PDB:2JVR" FT STRAND 266..273 FT /evidence="ECO:0007829|PDB:2JVR" SQ SEQUENCE 414 AA; 45407 MW; 024439E4B6578787 CRC64; MSEAQETHVE QLPESVVDAP VEEQHQEPPQ APDAPQEPQV PQESAPQESA PQEPPAPQEQ NDVPPPSNAP IYEGEESHSV QDYQEAHQHH QPPEPQPYYP PPPPGEHMHG RPPMHHRQEG ELSNTRLFVR PFPLDVQESE LNEIFGPFGP MKEVKILNGF AFVEFEEAES AAKAIEEVHG KSFANQPLEV VYSKLPAKRY RITMKNLPEG CSWQDLKDLA RENSLETTFS SVNTRDFDGT GALEFPSEEI LVEALERLNN IEFRGSVITV ERDDNPPPIR RSNRGGFRGR GGFRGGFRGG FRGGFSRGGF GGPRGGFGGP RGGYGGYSRG GYGGYSRGGY GGSRGGYDSP RGGYDSPRGG YSRGGYGGPR NDYGPPRGSY GGSRGGYDGP RGDYGPPRDA YRTRDAPRER SPTR //