ID YPI1_YEAST Reviewed; 155 AA. AC P43587; D6VTN3; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 04-NOV-2026, entry version 182. DE RecName: Full=Type 1 phosphatases regulator YPI1; GN Name=YPI1; OrderedLocusNames=YFR003C; 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=7670463; DOI=10.1038/ng0795-261; RA Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S., RA Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H., RA Eki T.; RT "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces RT cerevisiae."; RL Nat. Genet. 10:261-268(1995). 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=17322287; DOI=10.1101/gr.6037607; RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., RA LaBaer J.; RT "Approaching a complete repository of sequence-verified protein-encoding RT clones for Saccharomyces cerevisiae."; RL Genome Res. 17:536-543(2007). RN [4] RP FUNCTION, MUTAGENESIS OF TRP-53, AND INTERACTION WITH GLC7 AND PPZ1. RX PubMed=14506263; DOI=10.1074/jbc.m306157200; RA Garcia-Gimeno M.A., Munoz I., Arino J., Sanz P.; RT "Molecular characterization of Ypi1, a novel Saccharomyces cerevisiae type RT 1 protein phosphatase inhibitor."; RL J. Biol. Chem. 278:47744-47752(2003). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH GLC7 AND SDS22. RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3; RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M., RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E., RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.; RT "Assigning function to yeast proteins by integration of technologies."; RL Mol. Cell 12:1353-1365(2003). RN [6] 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 [7] RP FUNCTION. RX PubMed=16137619; DOI=10.1016/j.molcel.2005.07.016; RA He X., Moore C.; RT "Regulation of yeast mRNA 3' end processing by phosphorylation."; RL Mol. Cell 19:619-629(2005). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=YAL6B; RX PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200; RA Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., RA Jensen O.N.; RT "Quantitative phosphoproteomics applied to the yeast pheromone signaling RT pathway."; RL Mol. Cell. Proteomics 4:310-327(2005). RN [9] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH GLC7 AND SDS22. RX PubMed=17142459; DOI=10.1074/jbc.m607171200; RA Pedelini L., Marquina M., Arino J., Casamayor A., Sanz L., Bollen M., RA Sanz P., Garcia-Gimeno M.A.; RT "YPI1 and SDS22 proteins regulate the nuclear localization and function of RT yeast type 1 phosphatase Glc7."; RL J. Biol. Chem. 282:3282-3292(2007). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, 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 [11] 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 [12] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH GLC7, AND MUTAGENESIS OF RP VAL-51 AND TRP-53. RX PubMed=18172024; DOI=10.1091/mbc.e07-05-0499; RA Bharucha J.P., Larson J.R., Gao L., Daves L.K., Tatchell K.; RT "Ypi1, a positive regulator of nuclear protein phosphatase type 1 activity RT in Saccharomyces cerevisiae."; RL Mol. Biol. Cell 19:1032-1045(2008). RN [13] 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, 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 [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). CC -!- FUNCTION: Regulator of type 1 phosphatases which maintains protein CC phosphatase activity under strict control. Regulates the nuclear CC localization of type 1 phosphatase GLC7 and SDS22, and is involved in CC the regulation of mRNA 3'-end processing. May also regulate the CC activity of type 1 phosphatase PPZ1. {ECO:0000269|PubMed:14506263, CC ECO:0000269|PubMed:16137619, ECO:0000269|PubMed:17142459, CC ECO:0000269|PubMed:18172024}. CC -!- SUBUNIT: Interacts with GLC7, PPZ1 and SDS22. CC {ECO:0000269|PubMed:14506263, ECO:0000269|PubMed:14690591, CC ECO:0000269|PubMed:17142459, ECO:0000269|PubMed:18172024}. CC -!- INTERACTION: CC P43587; P32598: GLC7; NbExp=11; IntAct=EBI-22913, EBI-13715; CC P43587; P36047: SDS22; NbExp=10; IntAct=EBI-22913, EBI-16783; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17142459, CC ECO:0000269|PubMed:18172024}. CC -!- MISCELLANEOUS: Present with 1080 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the YPI1 family. {ECO:0000305}. CC -!- CAUTION: Was originally (PubMed:14506263) thought to be an inhibitor of CC type 1 phosphatases using in vitro experiments, but further in vivo CC experiments (PubMed:18172024) showed that it was rather an activator of CC these phosphatases. {ECO:0000305|PubMed:14506263, CC ECO:0000305|PubMed:18172024}. 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; D50617; BAA09242.1; -; Genomic_DNA. DR EMBL; AY557803; AAS56129.1; -; Genomic_DNA. DR EMBL; BK006940; DAA12443.1; -; Genomic_DNA. DR PIR; S56258; S56258. DR RefSeq; NP_116658.1; NM_001179968.1. DR AlphaFoldDB; P43587; -. DR SMR; P43587; -. DR BioGRID; 31151; 167. DR ComplexPortal; CPX-1260; SDS22-GLC7-YPI1 phosphatase complex. DR DIP; DIP-5442N; -. DR FunCoup; P43587; 220. DR IntAct; P43587; 15. DR STRING; 4932.YFR003C; -. DR iPTMnet; P43587; -. DR PaxDb; 4932-YFR003C; -. DR PeptideAtlas; P43587; -. DR EnsemblFungi; YFR003C_mRNA; YFR003C; YFR003C. DR GeneID; 850553; -. DR KEGG; sce:YFR003C; -. DR AGR; SGD:S000001899; -. DR SGD; S000001899; YPI1. DR VEuPathDB; FungiDB:YFR003C; -. DR eggNOG; KOG4102; Eukaryota. DR HOGENOM; CLU_098333_3_0_1; -. DR InParanoid; P43587; -. DR OMA; AEDCSCD; -. DR OrthoDB; 307488at2759; -. DR BioCyc; YEAST:G3O-30456-MONOMER; -. DR BioGRID-ORCS; 850553; 1 hit in 10 CRISPR screens. DR PRO; PR:P43587; -. DR Proteomes; UP000002311; Chromosome VI. DR RNAct; P43587; protein. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal. DR GO; GO:0000164; C:protein phosphatase type 1 complex; IPI:ComplexPortal. DR GO; GO:0008157; F:protein phosphatase 1 binding; IBA:GO_Central. DR GO; GO:0072542; F:protein phosphatase activator activity; IGI:SGD. DR GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central. DR GO; GO:0004865; F:protein serine/threonine phosphatase inhibitor activity; IDA:SGD. DR GO; GO:0051276; P:chromosome organization; NAS:ComplexPortal. DR GO; GO:0005977; P:glycogen metabolic process; IMP:SGD. DR GO; GO:0006873; P:intracellular monoatomic ion homeostasis; IMP:SGD. DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IGI:SGD. DR GO; GO:1900180; P:regulation of protein localization to nucleus; IDA:SGD. DR InterPro; IPR011107; PPI_Ypi1. DR PANTHER; PTHR20835:SF0; E3 UBIQUITIN-PROTEIN LIGASE PPP1R11; 1. DR PANTHER; PTHR20835; E3 UBIQUITIN-PROTEIN LIGASE PPP1R11-RELATED; 1. DR Pfam; PF07491; PPI_Ypi1; 1. PE 1: Evidence at protein level; KW Acetylation; Nucleus; Phosphoprotein; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22814378" FT CHAIN 2..155 FT /note="Type 1 phosphatases regulator YPI1" FT /id="PRO_0000202681" FT REGION 1..56 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 79..155 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 51..53 FT /note="GLC7-binding" FT COMPBIAS 1..21 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 93..102 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 104..114 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 115..128 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 144..155 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 22 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:15665377" FT MOD_RES 133 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:19779198" FT MUTAGEN 51 FT /note="V->A: Prevents interaction with GLC7." FT /evidence="ECO:0000269|PubMed:18172024" FT MUTAGEN 53 FT /note="W->A: Prevents interaction with GLC7 and reduces FT nuclear levels of GLC7 and SDS22." FT /evidence="ECO:0000269|PubMed:14506263, FT ECO:0000269|PubMed:18172024" SQ SEQUENCE 155 AA; 18187 MW; E191184DCD5EF8A1 CRC64; MSGNQMAMGS EQQQTVGSRT VSVEEVPAVL QLRATQDPPR SQEAMPTRHN VRWEENVIDN ENMNKKKTKI CCIFHPQNED EEECNHHSDD DGSSSSGSSS SESENEKDLD FNERRQRRLE RRHRKLEKKR SYSPNAYEIQ PDYSEYRRKQ QEKKD //