PP4R2_YEAST
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 03-AUG-2022, entry version 159.
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=10; IntAct=EBI-21239, EBI-12759;
CC P38193; P40164: PSY2; NbExp=9; 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}.
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; 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; 66.
DR ComplexPortal; CPX-1846; Histone H2A phosphatase complex.
DR DIP; DIP-4295N; -.
DR IntAct; P38193; 10.
DR MINT; P38193; -.
DR STRING; 4932.YBL046W; -.
DR iPTMnet; P38193; -.
DR MaxQB; P38193; -.
DR PaxDb; P38193; -.
DR PRIDE; P38193; -.
DR EnsemblFungi; YBL046W_mRNA; YBL046W; YBL046W.
DR GeneID; 852234; -.
DR KEGG; sce:YBL046W; -.
DR SGD; S000000142; PSY4.
DR VEuPathDB; FungiDB:YBL046W; -.
DR eggNOG; ENOG502S2WZ; Eukaryota.
DR HOGENOM; CLU_036743_1_0_1; -.
DR InParanoid; P38193; -.
DR OMA; NMMGIKS; -.
DR BioCyc; YEAST:G3O-28946-MON; -.
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; IC:ComplexPortal.
DR GO; GO:2000002; P:negative regulation of DNA damage checkpoint; IMP:SGD.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR InterPro; IPR015267; PPP4R2.
DR PANTHER; PTHR16487; PTHR16487; 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 262..303
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..401
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