PP4R3_YEAST
ID PP4R3_YEAST Reviewed; 858 AA.
AC P40164; D6W0Y7;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Serine/threonine-protein phosphatase 4 regulatory subunit 3;
DE Short=PP4R3;
GN Name=PSY2; OrderedLocusNames=YNL201C; ORFNames=N1366;
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 96604 / S288c / FY1679;
RX PubMed=7725799; DOI=10.1002/yea.320101213;
RA Jonniaux J.-L., Coster F., Purnelle B., Goffeau A.;
RT "A 21.7 kb DNA segment on the left arm of yeast chromosome XIV carries
RT WHI3, GCR2, SPX18, SPX19, an homologue to the heat shock gene SSB1 and 8
RT new open reading frames of unknown function.";
RL Yeast 10:1639-1645(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
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 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 [5]
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 [6]
RP IDENTIFICATION IN HTP-C COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP INTERACTION WITH RAD53; SPT4; SPT5 AND TIP41.
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 [7]
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).
CC -!- FUNCTION: Core regulatory subunit of the histone H2A phosphatase
CC complex, which dephosphorylates H2AS128ph (gamma-H2A) that has been
CC displaced from sites of DNA lesions in the double-stranded DNA break
CC repair process. Dephosphorylation is necessary for efficient recovery
CC from the DNA damage checkpoint. {ECO:0000269|PubMed:16299494}.
CC -!- SUBUNIT: Regulatory subunit 3 (R3) of the histone H2A phosphatase
CC complex (HTP-C) consisting of PPH3, PSY2 and PSY4. Interacts with SPT4,
CC SPT5 and TIP41. {ECO:0000269|PubMed:16085932,
CC ECO:0000269|PubMed:16299494}.
CC -!- INTERACTION:
CC P40164; P32345: PPH3; NbExp=10; IntAct=EBI-29107, EBI-12759;
CC P40164; P38193: PSY4; NbExp=9; IntAct=EBI-29107, EBI-21239;
CC P40164; P22216: RAD53; NbExp=3; IntAct=EBI-29107, EBI-17843;
CC P40164; P40454: RRD1; NbExp=3; IntAct=EBI-29107, EBI-25278;
CC P40164; P32914: SPT4; NbExp=3; IntAct=EBI-29107, EBI-17928;
CC P40164; P27692: SPT5; NbExp=7; IntAct=EBI-29107, EBI-17937;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 7010 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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; X78898; CAA55507.1; -; Genomic_DNA.
DR EMBL; Z71477; CAA96100.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10353.1; -; Genomic_DNA.
DR PIR; S50730; S50730.
DR RefSeq; NP_014198.1; NM_001183039.1.
DR AlphaFoldDB; P40164; -.
DR SMR; P40164; -.
DR BioGRID; 35633; 152.
DR ComplexPortal; CPX-1846; Histone H2A phosphatase complex.
DR DIP; DIP-1513N; -.
DR IntAct; P40164; 23.
DR MINT; P40164; -.
DR STRING; 4932.YNL201C; -.
DR iPTMnet; P40164; -.
DR MaxQB; P40164; -.
DR PaxDb; P40164; -.
DR PRIDE; P40164; -.
DR EnsemblFungi; YNL201C_mRNA; YNL201C; YNL201C.
DR GeneID; 855520; -.
DR KEGG; sce:YNL201C; -.
DR SGD; S000005145; PSY2.
DR VEuPathDB; FungiDB:YNL201C; -.
DR eggNOG; KOG2175; Eukaryota.
DR GeneTree; ENSGT00390000018199; -.
DR HOGENOM; CLU_004909_4_0_1; -.
DR InParanoid; P40164; -.
DR OMA; YHRYMIS; -.
DR BioCyc; YEAST:G3O-33210-MON; -.
DR PRO; PR:P40164; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P40164; protein.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:CACAO.
DR GO; GO:0030289; C:protein phosphatase 4 complex; IDA:SGD.
DR GO; GO:0072542; F:protein phosphatase activator activity; IBA:GO_Central.
DR GO; GO:0019888; F:protein phosphatase regulator activity; IDA:SGD.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IGI:SGD.
DR GO; GO:0051598; P:meiotic recombination checkpoint signaling; IMP:SGD.
DR GO; GO:2000002; P:negative regulation of DNA damage checkpoint; IMP:SGD.
DR GO; GO:1902660; P:negative regulation of glucose mediated signaling pathway; IMP:SGD.
DR GO; GO:2001034; P:positive regulation of double-strand break repair via nonhomologous end joining; IMP:SGD.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR006887; DUF625.
DR InterPro; IPR011993; PH-like_dom_sf.
DR Pfam; PF04802; SMK-1; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Nucleus; Reference proteome.
FT CHAIN 1..858
FT /note="Serine/threonine-protein phosphatase 4 regulatory
FT subunit 3"
FT /id="PRO_0000203395"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..458
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 858 AA; 98053 MW; 9AB94C259FF7A55B CRC64;
MSLPGTPTTS PTPMDEDTEQ AVSVNTEPKR VKVYILENNE WKDTGTGFCI GEVDEGKFAY
LVVSDEDSPT ETLLKSKLEG NIEYQRQEET LIVWKDLGGK DIALSFEESM GCDTLCEFIV
HVQRNIESNI SLVTVKSSDN GLGSVHDIIT GPVTLPSNDQ QQNSQTLLEA LKILNENTSF
DFLKNETIEF ILQSNYIDTL ISHFHKAEEE KIPKDLFLLS NIIKTLILYN KRDILESMVE
DDRIMGIVGI LEYDTEYPTS KANHRKYLGS KGPNFKEVIP LENEDLKIIM KKCFRLQFLK
DVVLVRFLDD HNFNLISEIV MDLETCIIDF LQVGTFLDRL IELYDTKTLP ESSSEKEKFV
QKRKDGIRLL QQCVQMSINL DAVDRSKFYK TLVRKGLFKV LDYAFHMETD SNVRILATDT
IITIIEHDIL LIHNVQNEDS FKRQHKSAPD DKSSHRKYPQ DYSSSTDSKL LLILSTILLS
DRSPGLREQV VQALNTLLHP EGCVGNGEGS YDLMGRSNYE AKNTSEDFPS FSYGLNSDSI
NLNNYHYSSD EMNNLEPESE SEFQVMEYFA NFYNKIAPIL FGPLIKKDIT TEMAEIDGQI
EKVTKDDLLL IHLVKLVSFV CTEHDRVLSR RFILENGILD SVSKLIGGNH MMQLRLTAVR
CIKNLMCLDD KYYHRYMISK NLYAPVFKLF QENIDKNNLA NSCIQDFFRI IITECRAYQS
DGHNRKEKTN GSYDGNGNDV KTNVNNNRTN FTILNKYLVQ TYGDVLRKAT DIPFIQDMLE
TGEENQPDHS SFENSIEGGN DISVNMSTDG FASNHLEDID IKNVKRLHSE IEHFENDPHY
SGDQLAFKKS VDQMNAST
