ID YB75_YEAST Reviewed; 900 AA. AC P38321; D6VQM1; DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1994, sequence version 1. DT 02-OCT-2024, entry version 146. DE RecName: Full=Uncharacterized protein YBR225W; GN OrderedLocusNames=YBR225W; ORFNames=YBR1522; 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 [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x; RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H., RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., RA Mewes H.-W., Kleine K.; RT "Complete DNA sequence of yeast chromosome II."; RL EMBO J. 13:5795-5809(1994). RN [2] 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 [3] 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 [4] RP 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 [5] 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 [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-105, 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). CC -!- MISCELLANEOUS: Present with 623 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; Z36092; CAA85188.1; -; Genomic_DNA. DR EMBL; BK006936; DAA07341.1; -; Genomic_DNA. DR PIR; S46101; S46101. DR RefSeq; NP_009784.1; NM_001178573.1. DR AlphaFoldDB; P38321; -. DR BioGRID; 32921; 102. DR DIP; DIP-6382N; -. DR IntAct; P38321; 17. DR MINT; P38321; -. DR STRING; 4932.YBR225W; -. DR GlyGen; P38321; 19 sites, 1 O-linked glycan (19 sites). DR iPTMnet; P38321; -. DR PaxDb; 4932-YBR225W; -. DR PeptideAtlas; P38321; -. DR EnsemblFungi; YBR225W_mRNA; YBR225W; YBR225W. DR GeneID; 852526; -. DR KEGG; sce:YBR225W; -. DR AGR; SGD:S000000429; -. DR SGD; S000000429; YBR225W. DR VEuPathDB; FungiDB:YBR225W; -. DR eggNOG; ENOG502QRP4; Eukaryota. DR HOGENOM; CLU_011913_0_0_1; -. DR InParanoid; P38321; -. DR OMA; HIHPTKH; -. DR OrthoDB; 2019419at2759; -. DR BioCyc; YEAST:G3O-29159-MONOMER; -. DR BioGRID-ORCS; 852526; 1 hit in 10 CRISPR screens. DR PRO; PR:P38321; -. DR Proteomes; UP000002311; Chromosome II. DR RNAct; P38321; protein. DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1. PE 1: Evidence at protein level; KW Phosphoprotein; Reference proteome. FT CHAIN 1..900 FT /note="Uncharacterized protein YBR225W" FT /id="PRO_0000202515" FT REGION 1..84 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 103..160 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 512..556 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 568..613 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 648..676 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 14..35 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 36..57 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 58..82 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 103..123 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 126..140 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 141..155 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 514..536 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 568..601 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 105 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19779198" SQ SEQUENCE 900 AA; 101236 MW; DDCD01F45CCA326A CRC64; MGSNKEAKNI DSKNDRGLTS ITSNKISNLK AHDNHTSSMI TEHKNADKEK GKQEKESRNG TTQSSSSVES HSPQVSHHSD KLSSFDSPLH LPNFRLADDL FSNSSRRSSD SAASSSVSKL KSAQLSKIGL HHHHTSNNKH SHRSGTPTSE VKANYSPDPS APRFIVSNMV GNGRGGGGLH GATSNVVKKL HSRKKWDWNT LPASDSSLLI KTVSGNHNLI NICIDGEFKQ IMYDPNHNEL FNRMDLFLSF NMDSSPEDSL IFAKKRLRSY IDFLTKYLES RKYAFECYPF NIENIINIET EVKCFPSFDP LKDYSEIESL IQLWLAQSQK FLLQSNSFFF SSEVVEELIK RKPTTRQHSN PTISTTSNKI SDPTLYIQQL DIEANSPRPV ISDPLDEIDI LLIRPLHKTL GGWQLAYDEP SLNIADFALD LSPWMIDSSD NDAQNKNASE IAPEYLTNLQ NYLPRKGSRA KIVSDEQEVI ELNSSNASEY MYDCMNRKFF TDDAKERISR NNFNQGVEED PLNDQFASSR SLSLPSSGAD AVKRKKSPTK ATKKSGFVNF FKRKHSQLAS TSHTTSPSVS PSISSSSSPK IQPQSHISSP PRTEKAPHVK SANQAHQNEW LENFFCRTLN NYKEIDLPTQ FILPKEVKRS SNAQLQPEDE PPLSSPISSN SDNSFPNEGL DRAKSAAIYG KEYLKLRLPF ASDTIPAVIC PWVWTSLSYY KWKALLREIY RSIIPGGYAL AIVPDLRISN TYYTGILGNA DAEKANNSSE EFLTTKERDK TFDAMAIDAI NKGLHIHPTK HLTRTFKDVG FTGIKSSVLS LKTGDFKTDM GFLNEFNSLD MWDYMLRRQL PDSSCPPKDT DPTTLFKRYV EEHIGKIDDN AGCFRTLYVV AQKPKLPYTK //