YPI1_YEAST
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 03-AUG-2022, entry version 165.
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 BioGRID; 31151; 161.
DR ComplexPortal; CPX-1260; SDS22-GLC7-YPI1 phosphatase complex.
DR DIP; DIP-5442N; -.
DR IntAct; P43587; 15.
DR MINT; P43587; -.
DR STRING; 4932.YFR003C; -.
DR iPTMnet; P43587; -.
DR PaxDb; P43587; -.
DR PRIDE; P43587; -.
DR EnsemblFungi; YFR003C_mRNA; YFR003C; YFR003C.
DR GeneID; 850553; -.
DR KEGG; sce:YFR003C; -.
DR SGD; S000001899; YPI1.
DR VEuPathDB; FungiDB:YFR003C; -.
DR eggNOG; KOG4102; Eukaryota.
DR GeneTree; ENSGT00390000001153; -.
DR HOGENOM; CLU_098333_3_0_1; -.
DR InParanoid; P43587; -.
DR OMA; HPQQNFD; -.
DR BioCyc; YEAST:G3O-30456-MON; -.
DR PRO; PR:P43587; -.
DR Proteomes; UP000002311; Chromosome VI.
DR RNAct; P43587; protein.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
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:0004865; F:protein serine/threonine phosphatase inhibitor activity; IDA:SGD.
DR GO; GO:0006873; P:cellular ion homeostasis; IMP:SGD.
DR GO; GO:0051276; P:chromosome organization; IC:ComplexPortal.
DR GO; GO:0005977; P:glycogen metabolic process; IMP:SGD.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IGI:SGD.
DR GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; IDA:SGD.
DR GO; GO:0035308; P:negative regulation of protein dephosphorylation; IDA:SGD.
DR GO; GO:1905183; P:negative regulation of protein serine/threonine phosphatase activity; IDA:ComplexPortal.
DR GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; IGI:SGD.
DR GO; GO:1900180; P:regulation of protein localization to nucleus; IDA:SGD.
DR InterPro; IPR011107; PPI_Ypi1.
DR PANTHER; PTHR20835; PTHR20835; 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 103..117
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
