PP2A2_YEAST
ID PP2A2_YEAST Reviewed; 377 AA.
AC P23595; D6VRG5;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Serine/threonine-protein phosphatase PP2A-2 catalytic subunit;
DE EC=3.1.3.16;
GN Name=PPH22; Synonyms=SIS4; OrderedLocusNames=YDL188C; ORFNames=D1271;
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=LL20;
RX PubMed=2176150; DOI=10.1002/j.1460-2075.1990.tb07883.x;
RA Sneddon A.A., Cohen P.T.W., Stark M.J.R.;
RT "Saccharomyces cerevisiae protein phosphatase 2A performs an essential
RT cellular function and is encoded by two genes.";
RL EMBO J. 9:4339-4346(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1848673; DOI=10.1128/mcb.11.4.2133-2148.1991;
RA Sutton A., Immanuel D., Arndt K.T.;
RT "The SIT4 protein phosphatase functions in late G1 for progression into S
RT phase.";
RL Mol. Cell. Biol. 11:2133-2148(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 208353 / W303-1A;
RX PubMed=1656215; DOI=10.1128/mcb.11.10.4876-4884.1991;
RA Ronne H., Carlberg M., Hu G.-Z., Nehlin J.O.;
RT "Protein phosphatase 2A in Saccharomyces cerevisiae: effects on cell growth
RT and bud morphogenesis.";
RL Mol. Cell. Biol. 11:4876-4884(1991).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8533471; DOI=10.1002/yea.320111007;
RA Verhasselt P., Voet M., Volckaert G.;
RT "New open reading frames, one of which is similar to the nifV gene of
RT Azotobacter vinelandii, found on a 12.5 kbp fragment of chromosome IV of
RT Saccharomyces cerevisiae.";
RL Yeast 11:961-966(1995).
RN [5]
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 [6]
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 [7]
RP METHYLATION AT LEU-377 BY PPM1, AND DEMETHYLATION BY PPE1.
RX PubMed=11060018; DOI=10.1093/emboj/19.21.5672;
RA Wu J., Tolstykh T., Lee J., Boyd K., Stock J.B., Broach J.R.;
RT "Carboxyl methylation of the phosphoprotein phosphatase 2A catalytic
RT subunit promotes its functional association with regulatory subunits in
RT vivo.";
RL EMBO J. 19:5672-5681(2000).
RN [8]
RP METHYLATION AT LEU-377 BY PPM1.
RX PubMed=11697862; DOI=10.1006/abbi.2001.2558;
RA Kalhor H.R., Luk K., Ramos A., Zobel-Thropp P., Clarke S.;
RT "Protein phosphatase methyltransferase 1 (Ppm1p) is the sole activity
RT responsible for modification of the major forms of protein phosphatase 2A
RT in yeast.";
RL Arch. Biochem. Biophys. 395:239-245(2001).
RN [9]
RP INTERACTION WITH TAP42.
RX PubMed=14551259; DOI=10.1091/mbc.e03-02-0072;
RA Wang H., Wang X., Jiang Y.;
RT "Interaction with Tap42 is required for the essential function of Sit4 and
RT type 2A phosphatases.";
RL Mol. Biol. Cell 14:4342-4351(2003).
RN [10]
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 [11]
RP INTERACTION WITH PPE1 AND RRD2.
RX PubMed=15447631; DOI=10.1042/bj20040887;
RA Van Hoof C., Martens E., Longin S., Jordens J., Stevens I., Janssens V.,
RA Goris J.;
RT "Specific interactions of PP2A and PP2A-like phosphatases with the yeast
RT PTPA homologues, Ypa1 and Ypa2.";
RL Biochem. J. 386:93-102(2005).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-43, 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-43, AND IDENTIFICATION BY
RP 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-38 AND THR-43, AND
RP IDENTIFICATION BY 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 -!- FUNCTION: Exact function not known, phosphatase 2A performs an
CC essential cellular function.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Inactivated in a complex with phosphatase methylesterase PPE1
CC (PP2Ai). Interacts with phosphatase 2A activator RRD2, which can
CC reactivate PP2Ai by dissociating the catalytic subunit from the
CC complex. Interacts with TAP42. {ECO:0000269|PubMed:14551259,
CC ECO:0000269|PubMed:15447631}.
CC -!- INTERACTION:
CC P23595; P38074: HMT1; NbExp=3; IntAct=EBI-12752, EBI-8394;
CC P23595; Q04372: TAP42; NbExp=5; IntAct=EBI-12752, EBI-18926;
CC -!- PTM: Reversibly methyl esterified on Leu-377 by leucine carboxyl
CC methyltransferase 1 (PPM1) and protein phosphatase methylesterase 1
CC (PPE1). Carboxyl methylation influences the affinity of the catalytic
CC subunit for the different regulatory subunits, thereby modulating the
CC PP2A holoenzyme's substrate specificity, enzyme activity and cellular
CC localization. {ECO:0000269|PubMed:11060018,
CC ECO:0000269|PubMed:11697862}.
CC -!- MISCELLANEOUS: Present with 4110 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-2A subfamily.
CC {ECO:0000305}.
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DR EMBL; X56262; CAA39703.1; -; Genomic_DNA.
DR EMBL; M60317; AAB04032.1; -; Genomic_DNA.
DR EMBL; X58857; CAA41659.1; -; Genomic_DNA.
DR EMBL; X83276; CAA58259.1; -; Genomic_DNA.
DR EMBL; Z74236; CAA98765.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11675.1; -; Genomic_DNA.
DR PIR; B41525; PABY22.
DR RefSeq; NP_010093.1; NM_001180248.1.
DR AlphaFoldDB; P23595; -.
DR SMR; P23595; -.
DR BioGRID; 31857; 162.
DR ComplexPortal; CPX-1382; TAP42-RRD2-PPH22 phosphatase complex.
DR ComplexPortal; CPX-1858; Serine/threonine-protein phosphatase PP2A variant 4.
DR ComplexPortal; CPX-1859; Serine/threonine-protein phosphatase PP2A variant 3.
DR DIP; DIP-2283N; -.
DR IntAct; P23595; 35.
DR MINT; P23595; -.
DR STRING; 4932.YDL188C; -.
DR iPTMnet; P23595; -.
DR MaxQB; P23595; -.
DR PaxDb; P23595; -.
DR PRIDE; P23595; -.
DR EnsemblFungi; YDL188C_mRNA; YDL188C; YDL188C.
DR GeneID; 851339; -.
DR KEGG; sce:YDL188C; -.
DR SGD; S000002347; PPH22.
DR VEuPathDB; FungiDB:YDL188C; -.
DR eggNOG; KOG0371; Eukaryota.
DR GeneTree; ENSGT00940000176641; -.
DR HOGENOM; CLU_004962_8_1_1; -.
DR InParanoid; P23595; -.
DR OMA; SWSHQES; -.
DR BioCyc; YEAST:G3O-29573-MON; -.
DR PRO; PR:P23595; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P23595; protein.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0034399; C:nuclear periphery; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000159; C:protein phosphatase type 2A complex; IPI:ComplexPortal.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:SGD.
DR GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IGI:SGD.
DR GO; GO:2000198; P:negative regulation of ribonucleoprotein complex localization; IMP:SGD.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; IGI:SGD.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:ComplexPortal.
DR GO; GO:0006417; P:regulation of translation; IPI:SGD.
DR GO; GO:0031929; P:TOR signaling; IC:ComplexPortal.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Manganese; Metal-binding; Methylation; Phosphoprotein;
KW Protein phosphatase; Reference proteome.
FT CHAIN 1..377
FT /note="Serine/threonine-protein phosphatase PP2A-2
FT catalytic subunit"
FT /id="PRO_0000058874"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..41
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 186
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 235
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 309
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 38
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 43
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 377
FT /note="Leucine methyl ester"
FT /evidence="ECO:0000269|PubMed:11060018,
FT ECO:0000269|PubMed:11697862"
SQ SEQUENCE 377 AA; 43047 MW; 549D3C6F1E2EB335 CRC64;
MDMEIDDPMH GSDEDQLSPT LDEDMNSDDG KNNTKARSND EDTDEELEDF NFKPGSSGIA
DHKSSKPLKL TNTNINQLDQ WIEHLSKCEP LSEDDVARLC KMAVDVLQFE ENVKPINVPV
TICGDVHGQF HDLLELFKIG GPCPDTNYLF MGDYVDRGYY SVETVSYLVA MKVRYPHRIT
ILRGNHESRQ ITQVYGFYDE CLRKYGSANV WKMFTDLFDY FPVTALVDNK IFCLHGGLSP
MIETIDQVRD LNRIQEVPHE GPMCDLLWSD PDDRGGWGIS PRGAGFTFGQ DISEQFNHTN
DLSLIARAHQ LVMEGYSWSH QQNVVTIFSA PNYCYRCGNQ AAIMEVDENH NRQFLQYDPS
VRPGEPTVTR KTPDYFL
