ID   PP4R2_YEAST             Reviewed;         441 AA.
AC   P38193; D6VPV2; Q6B302;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   02-SEP-2026, entry version 173.
DE   RecName: Full=Serine/threonine-protein phosphatase 4 regulatory subunit 2;
DE            Short=PP4R2;
GN   Name=PSY4; Synonyms=HTP3; OrderedLocusNames=YBL046W; ORFNames=YBL0402;
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=ATCC 204508 / S288c;
RX   PubMed=7871888; DOI=10.1002/yea.320101113;
RA   de Wergifosse P., Jacques B., Jonniaux J.-L., Purnelle B., Skala J.,
RA   Goffeau A.;
RT   "The sequence of a 22.4 kb DNA fragment from the left arm of yeast
RT   chromosome II reveals homologues to bacterial proline synthetase and murine
RT   alpha-adaptin, as well as a new permease and a DNA-binding protein.";
RL   Yeast 10:1489-1496(1994).
RN   [2]
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   [3]
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   [4]
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   [5]
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   [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   IDENTIFICATION IN HTP-C COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   INTERACTION WITH SPT4 AND SPT5.
RX   PubMed=16085932; DOI=10.1074/mcp.m500231-mcp200;
RA   Gingras A.-C., Caballero M., Zarske M., Sanchez A., Hazbun T.R., Fields S.,
RA   Sonenberg N., Hafen E., Raught B., Aebersold R.;
RT   "A novel, evolutionarily conserved protein phosphatase complex involved in
RT   cisplatin sensitivity.";
RL   Mol. Cell. Proteomics 4:1725-1740(2005).
RN   [8]
RP   FUNCTION, IDENTIFICATION IN HTP-C COMPLEX, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=16299494; DOI=10.1038/nature04384;
RA   Keogh M.-C., Kim J.-A., Downey M., Fillingham J., Chowdhury D.,
RA   Harrison J.C., Onishi M., Datta N., Galicia S., Emili A., Lieberman J.,
RA   Shen X., Buratowski S., Haber J.E., Durocher D., Greenblatt J.F.,
RA   Krogan N.J.;
RT   "A phosphatase complex that dephosphorylates gamma-H2AX regulates DNA
RT   damage checkpoint recovery.";
RL   Nature 439:497-501(2006).
RN   [9]
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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-347, 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   -!- FUNCTION: Regulatory subunit of the histone H2A phosphatase complex,
CC       which dephosphorylates H2AS128ph (gamma-H2A) that has been displaced
CC       from sites of DNA lesions in the double-stranded DNA break repair
CC       process. Dephosphorylation is necessary for efficient recovery from the
CC       DNA damage checkpoint. {ECO:0000269|PubMed:16299494}.
CC   -!- SUBUNIT: Regulatory subunit (R2) of the histone H2A phosphatase complex
CC       (HTP-C) consisting of PPH3, PSY2 and PSY4. Interacts with SPT4 and
CC       SPT5. {ECO:0000269|PubMed:16085932, ECO:0000269|PubMed:16299494}.
CC   -!- INTERACTION:
CC       P38193; P32345: PPH3; NbExp=11; IntAct=EBI-21239, EBI-12759;
CC       P38193; P40164: PSY2; NbExp=10; IntAct=EBI-21239, EBI-29107;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 1010 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the PPP4R2 family. {ECO:0000305}.
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DR   EMBL; X78214; CAA55049.1; -; Genomic_DNA.
DR   EMBL; Z35807; CAA84866.1; -; Genomic_DNA.
DR   EMBL; AY692578; AAT92597.1; -; Genomic_DNA.
DR   EMBL; BK006936; DAA07072.1; -; Genomic_DNA.
DR   PIR; S42499; S42499.
DR   RefSeq; NP_009507.1; NM_001178286.1.
DR   AlphaFoldDB; P38193; -.
DR   BioGRID; 32651; 78.
DR   ComplexPortal; CPX-1846; Histone H2A phosphatase complex.
DR   DIP; DIP-4295N; -.
DR   FunCoup; P38193; 81.
DR   IntAct; P38193; 10.
DR   MINT; P38193; -.
DR   STRING; 4932.YBL046W; -.
DR   iPTMnet; P38193; -.
DR   PaxDb; 4932-YBL046W; -.
DR   PeptideAtlas; P38193; -.
DR   EnsemblFungi; YBL046W_mRNA; YBL046W; YBL046W.
DR   GeneID; 852234; -.
DR   KEGG; sce:YBL046W; -.
DR   AGR; SGD:S000000142; -.
DR   SGD; S000000142; PSY4.
DR   VEuPathDB; FungiDB:YBL046W; -.
DR   eggNOG; ENOG502S2WZ; Eukaryota.
DR   HOGENOM; CLU_036743_1_0_1; -.
DR   InParanoid; P38193; -.
DR   OMA; CYDPFKY; -.
DR   OrthoDB; 341898at2759; -.
DR   BioCyc; YEAST:G3O-28946-MONOMER; -.
DR   BioGRID-ORCS; 852234; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P38193; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P38193; protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0030289; C:protein phosphatase 4 complex; IDA:SGD.
DR   GO; GO:0019888; F:protein phosphatase regulator activity; IMP:SGD.
DR   GO; GO:0051598; P:meiotic recombination checkpoint signaling; NAS:ComplexPortal.
DR   GO; GO:1904290; P:negative regulation of mitotic DNA damage checkpoint; IMP:SGD.
DR   InterPro; IPR015267; PPP4R2.
DR   PANTHER; PTHR16487; PPP4R2-RELATED PROTEIN; 1.
DR   PANTHER; PTHR16487:SF0; PROTEIN PHOSPHATASE 4 REGULATORY SUBUNIT 2-RELATED; 1.
DR   Pfam; PF09184; PPP4R2; 1.
PE   1: Evidence at protein level;
KW   Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..441
FT                   /note="Serine/threonine-protein phosphatase 4 regulatory
FT                   subunit 2"
FT                   /id="PRO_0000202458"
FT   REGION          201..220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          242..348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          364..418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        201..213
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        249..261
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        264..302
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        388..398
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         347
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   CONFLICT        374
FT                   /note="D -> V (in Ref. 4; AAT92597)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   441 AA;  50655 MW;  74BCA72FCF2BD9A2 CRC64;
     MSSTMLDDVD NNMMGIKSIS LYELLSDVVK QGDKTRLVTA GPEQVLPDLI RHITETIPFD
     LFINLKNEMN DARNLVTRLN WLGKFLNDNF LQNHTFPFTI LRICELCYDP FKYYKINELE
     KFVNALEKCC MVTSSWQVFD KTHGEKQEDD KEKDINFIKN QEDVSLMKIP WMTENNTREL
     APFIREIDSI MSVNLGYDDE DEEEGFFDGD EDREMGNKSK RNVLLKDENF MVEEYYEDDC
     GINDDNSDNK GQNCQSDVTK NNSDDEDDDD NDDDYREDGA DEDDEDDDHM GSTDDDEDDD
     EDRQAGESTK VQNFDKKNET PRKRKPTDLD NFEYDESPSF TNMDLTTPKK YKHTATGRFS
     IIESPSSSLL NAMDGSNEIS SSQEEEKEDA HENHEGRSEG LLPGDELVSP SMSSSQEDKM
     VAIAGITYRE NISSPLGKKS R
//