PSY3_YEAST
ID PSY3_YEAST Reviewed; 242 AA.
AC Q12318; D6VZ12;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Platinum sensitivity protein 3;
GN Name=PSY3; OrderedLocusNames=YLR376C; ORFNames=L8039.17;
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 28383 / FL100 / VTT C-80102;
RA Mercado J., Gancedo J.M.;
RT "A new open reading frame.";
RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 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 FUNCTION.
RX PubMed=12149442; DOI=10.1073/pnas.152264899;
RA Hanway D., Chin J.K., Xia G., Oshiro G., Winzeler E.A., Romesberg F.E.;
RT "Previously uncharacterized genes in the UV- and MMS-induced DNA damage
RT response in yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:10605-10610(2002).
RN [6]
RP FUNCTION IN MMS RESISTANCE.
RX PubMed=12482937; DOI=10.1073/pnas.262669299;
RA Chang M., Bellaoui M., Boone C., Brown G.W.;
RT "A genome-wide screen for methyl methanesulfonate-sensitive mutants reveals
RT genes required for S phase progression in the presence of DNA damage.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16934-16939(2002).
RN [7]
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 [8]
RP FUNCTION IN MUTATION SUPPRESSION.
RX PubMed=12972632; DOI=10.1073/pnas.2035018100;
RA Huang M.-E., Rio A.-G., Nicolas A., Kolodner R.D.;
RT "A genomewide screen in Saccharomyces cerevisiae for genes that suppress
RT the accumulation of mutations.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11529-11534(2003).
RN [9]
RP FUNCTION.
RX PubMed=15173006; DOI=10.1158/0008-5472.can-03-3113;
RA Wu H.I., Brown J.A., Dorie M.J., Lazzeroni L., Brown J.M.;
RT "Genome-wide identification of genes conferring resistance to the
RT anticancer agents cisplatin, oxaliplatin, and mitomycin C.";
RL Cancer Res. 64:3940-3948(2004).
RN [10]
RP IDENTIFICATION IN THE SHU COMPLEX, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=15654096; DOI=10.1534/genetics.104.036764;
RA Shor E., Weinstein J., Rothstein R.;
RT "A genetic screen for top3 suppressors in Saccharomyces cerevisiae
RT identifies SHU1, SHU2, PSY3 and CSM2: four genes involved in error-free DNA
RT repair.";
RL Genetics 169:1275-1289(2005).
RN [11]
RP IDENTIFICATION IN THE SHU COMPLEX, AND FUNCTION.
RX PubMed=19496932; DOI=10.1111/j.1365-2958.2009.06748.x;
RA Ball L.G., Zhang K., Cobb J.A., Boone C., Xiao W.;
RT "The yeast Shu complex couples error-free post-replication repair to
RT homologous recombination.";
RL Mol. Microbiol. 73:89-102(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [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: Required for resistance to the DNA-damaging agents methyl
CC methanesulfonate (MMS), cisplatin and oxaliplatin, but not to mitomycin
CC C. Plays a role in protection against mutation accumulation. May be a
CC component of the recombination-repair pathway.
CC {ECO:0000269|PubMed:12149442, ECO:0000269|PubMed:12482937,
CC ECO:0000269|PubMed:12972632, ECO:0000269|PubMed:15173006,
CC ECO:0000269|PubMed:15654096, ECO:0000269|PubMed:19496932}.
CC -!- SUBUNIT: Component of the SHU complex composed of at least CSM2, PSY3,
CC SHU1 and SHU2. {ECO:0000269|PubMed:15654096,
CC ECO:0000269|PubMed:19496932}.
CC -!- INTERACTION:
CC Q12318; P40465: CSM2; NbExp=4; IntAct=EBI-37340, EBI-25229;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15654096}.
CC -!- MISCELLANEOUS: Present with 876 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; Z27407; CAA81795.1; -; Genomic_DNA.
DR EMBL; U19103; AAB67578.1; -; Genomic_DNA.
DR EMBL; AY692738; AAT92757.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09678.1; -; Genomic_DNA.
DR PIR; S47544; S47544.
DR RefSeq; NP_013480.1; NM_001182265.1.
DR PDB; 3VU9; X-ray; 1.75 A; A=1-242.
DR PDB; 4DT1; X-ray; 1.90 A; B=1-242.
DR PDB; 4EQ6; X-ray; 1.80 A; B=1-242.
DR PDB; 5XYN; X-ray; 3.30 A; A=1-242.
DR PDBsum; 3VU9; -.
DR PDBsum; 4DT1; -.
DR PDBsum; 4EQ6; -.
DR PDBsum; 5XYN; -.
DR AlphaFoldDB; Q12318; -.
DR SMR; Q12318; -.
DR BioGRID; 31635; 78.
DR ComplexPortal; CPX-3087; Shu complex.
DR DIP; DIP-1903N; -.
DR IntAct; Q12318; 4.
DR MINT; Q12318; -.
DR STRING; 4932.YLR376C; -.
DR iPTMnet; Q12318; -.
DR PaxDb; Q12318; -.
DR PRIDE; Q12318; -.
DR EnsemblFungi; YLR376C_mRNA; YLR376C; YLR376C.
DR GeneID; 851091; -.
DR KEGG; sce:YLR376C; -.
DR SGD; S000004368; PSY3.
DR VEuPathDB; FungiDB:YLR376C; -.
DR eggNOG; ENOG502S12B; Eukaryota.
DR HOGENOM; CLU_103058_0_0_1; -.
DR InParanoid; Q12318; -.
DR OMA; AHCRVYP; -.
DR BioCyc; YEAST:G3O-32444-MON; -.
DR PRO; PR:Q12318; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12318; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0097196; C:Shu complex; IDA:SGD.
DR GO; GO:0035861; C:site of double-strand break; IMP:SGD.
DR GO; GO:0000730; P:DNA recombinase assembly; IMP:SGD.
DR GO; GO:0042275; P:error-free postreplication DNA repair; IC:ComplexPortal.
DR GO; GO:0070987; P:error-free translesion synthesis; IGI:SGD.
DR GO; GO:1903112; P:positive regulation of single-strand break repair via homologous recombination; IC:ComplexPortal.
DR GO; GO:0000725; P:recombinational repair; IMP:SGD.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR031779; Psy3.
DR Pfam; PF16836; PSY3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA repair; Nucleus; Reference proteome.
FT CHAIN 1..242
FT /note="Platinum sensitivity protein 3"
FT /id="PRO_0000262753"
FT HELIX 2..6
FT /evidence="ECO:0007829|PDB:4EQ6"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:5XYN"
FT HELIX 12..16
FT /evidence="ECO:0007829|PDB:3VU9"
FT HELIX 27..29
FT /evidence="ECO:0007829|PDB:3VU9"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:3VU9"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:3VU9"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:3VU9"
FT HELIX 55..61
FT /evidence="ECO:0007829|PDB:3VU9"
FT STRAND 66..74
FT /evidence="ECO:0007829|PDB:3VU9"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:3VU9"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:3VU9"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:3VU9"
FT HELIX 100..112
FT /evidence="ECO:0007829|PDB:3VU9"
FT HELIX 114..120
FT /evidence="ECO:0007829|PDB:3VU9"
FT STRAND 128..136
FT /evidence="ECO:0007829|PDB:3VU9"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:3VU9"
FT HELIX 152..171
FT /evidence="ECO:0007829|PDB:3VU9"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:3VU9"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:3VU9"
FT TURN 189..192
FT /evidence="ECO:0007829|PDB:3VU9"
FT HELIX 213..216
FT /evidence="ECO:0007829|PDB:3VU9"
FT STRAND 220..236
FT /evidence="ECO:0007829|PDB:3VU9"
SQ SEQUENCE 242 AA; 28251 MW; B652FD8113EB4C12 CRC64;
MEVLKNIRIY PLSNFITSTK NYINLPNELR NLISEEQESK LGFLHIIESD FKPSVALQKL
VNCTTGDEKI LIIDIVSIWS QQKQRQHGAI YMNSLSCINI TGLIVFLELL YDSPMDALRR
CQVDNFNFQL RGIVIDNLSF LNFESDKNYD VINLSKFEKL FKILRKLREF LGCWIITKSF
PTDFYNGIEN TLVDKWSIKR KSGVTLYPTK LPDSYMKGMD LIIYREVVDG RPQYRRIAAL
EE
