PSP1_YEAST
ID PSP1_YEAST Reviewed; 841 AA.
AC P50896; D6VTC7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Protein PSP1;
DE AltName: Full=Growth inhibitory protein 5;
DE AltName: Full=Polymerase suppressor protein 1;
GN Name=PSP1; Synonyms=GIN5; OrderedLocusNames=YDR505C; ORFNames=D9719.11;
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].
RX PubMed=9529527; DOI=10.1007/s004380050670;
RA Formosa T., Nittis T.;
RT "Suppressors of the temperature sensitivity of DNA polymerase alpha
RT mutations in Saccharomyces cerevisiae.";
RL Mol. Gen. Genet. 257:461-468(1998).
RN [2]
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 [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 732.
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-520, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-34 AND SER-520, AND
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-34; SER-36; SER-237;
RP THR-334 AND SER-520, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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: DNA polymerase alpha mutation suppressor.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion.
CC -!- MISCELLANEOUS: Present with 259 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the PSP1 family. {ECO:0000305}.
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DR EMBL; U33115; AAA93076.1; -; Genomic_DNA.
DR EMBL; U33057; AAB64947.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12337.2; -; Genomic_DNA.
DR PIR; S69563; S69563.
DR RefSeq; NP_010793.2; NM_001180813.2.
DR AlphaFoldDB; P50896; -.
DR BioGRID; 32556; 140.
DR DIP; DIP-5018N; -.
DR IntAct; P50896; 7.
DR MINT; P50896; -.
DR STRING; 4932.YDR505C; -.
DR iPTMnet; P50896; -.
DR MaxQB; P50896; -.
DR PaxDb; P50896; -.
DR PRIDE; P50896; -.
DR EnsemblFungi; YDR505C_mRNA; YDR505C; YDR505C.
DR GeneID; 852116; -.
DR KEGG; sce:YDR505C; -.
DR SGD; S000002913; PSP1.
DR VEuPathDB; FungiDB:YDR505C; -.
DR eggNOG; KOG4679; Eukaryota.
DR GeneTree; ENSGT00940000176361; -.
DR HOGENOM; CLU_012771_0_0_1; -.
DR InParanoid; P50896; -.
DR OMA; YYVCQER; -.
DR BioCyc; YEAST:G3O-30026-MON; -.
DR PRO; PR:P50896; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P50896; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0000932; C:P-body; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR InterPro; IPR007557; PSP1_C.
DR Pfam; PF04468; PSP1; 1.
DR PROSITE; PS51411; PSP1_C; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Mitochondrion; Phosphoprotein; Reference proteome.
FT CHAIN 1..841
FT /note="Protein PSP1"
FT /id="PRO_0000097068"
FT DOMAIN 653..765
FT /note="PSP1 C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00744"
FT REGION 33..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 334
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT CONFLICT 116
FT /note="S -> C (in Ref. 1; AAA93076)"
FT /evidence="ECO:0000305"
FT CONFLICT 122..133
FT /note="QMSSSNSEPMSA -> KCLRLIQSCVP (in Ref. 1; AAA93076)"
FT /evidence="ECO:0000305"
FT CONFLICT 198..210
FT /note="GSNFAAPSHSAGN -> RAILLPHHTVLAT (in Ref. 1;
FT AAA93076)"
FT /evidence="ECO:0000305"
FT CONFLICT 732
FT /note="K -> E (in Ref. 2; AAB64947)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 841 AA; 95348 MW; 03B5C27F96F71F2C CRC64;
MDLPTVNSTT SISDNVDLKN YYEDLLFKNN SGKSLSDLPR KLNDNSNNSG SDTVDPLAGL
NNLRNSIKSA GNGMENRRTF DDIDFMGRFP YLPPVPNQQQ QPFSHQNGFI QEHPSSNLTS
FQMSSSNSEP MSAPPISSNN NNLNSTQMGN YQAQQRSFPQ FNGNSFHSNG NDLMGNRMDS
DYMRLMNKTN IGFTSNSGSN FAAPSHSAGN PSSMNNQQVP SFNWQQPSHP ESTIRRSSYI
SDTLINHQMP DARQKQTSQV QQQHAQGFNL FNSRFNYDNL NSTHLTAKGV PEFGNGVQPP
YPYDNEPNNA SISNSNNNNN SHNMVPMQQF RRNTQPVASF NPSLPTFQQQ QQQPQQPQQP
RNVNVPTSFN GERVDDVQLV QLQRSSSVPS STNSHNLQNE NSNEGNVSLD NGLVLIQGKH
LTSSKTLHDL YSDCGSGYFA SSAVFEFTDN IKKMLKLHDS NESYDAKNMG LIDEEGNTYQ
SLLNFLDILR SCNMNYVNDP ESNNGIVSNN GGNKNRRKGS FTTELSCRNA NNSFLPYTPL
VLVALKNGKL ELLSTPQATN LLLKRGDLVI IDGDRGRDLV LVVEPSVDLN LALFINFLKK
KIHFDSLITS ESQHYRNDEF IQMLIDSKNG QKKKLNPKLY DVVELTELII PSKQVLRFAT
PWEVTTNLHN KFEDELKALH IAQSKLQALN DNSKSQNTND SSSNNFTNAA TYSKPKLNIK
ILNAEFQFDR KKLTFYYVCE ERNDFRDLIK ELFKYYKTRI WLCAIPNNLS IDSKYYDKQQ
KELKLYQNIV KNYNAEDLMN VNEFSQNRGN NRVNFAPPLN EIELDNFQIA VYEELVHELF
H
