PSP2_YEAST
ID PSP2_YEAST Reviewed; 593 AA.
AC P50109; D6VZF7; Q07170; Q870H3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Protein PSP2 {ECO:0000305};
DE AltName: Full=Mitochondrial regulator of splicing 15 {ECO:0000303|PubMed:8252639};
DE AltName: Full=Polymerase suppressor protein 2 {ECO:0000303|PubMed:9529527};
GN Name=PSP2 {ECO:0000303|PubMed:9529527};
GN Synonyms=MRS15 {ECO:0000303|PubMed:8252639}; OrderedLocusNames=YML017W;
GN ORFNames=YM9571.01;
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 44774 / DBY747;
RA Teply R.;
RT "Suppressors of pet- phenotype due to MRS2 disruption.";
RL Thesis (1995), Vienna Biocentre, Austria.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-167.
RC STRAIN=ATCC 204511 / S288c / AB972;
RX PubMed=12844361; DOI=10.1186/gb-2003-4-7-r45;
RA Brachat S., Dietrich F.S., Voegeli S., Zhang Z., Stuart L., Lerch A.,
RA Gates K., Gaffney T.D., Philippsen P.;
RT "Reinvestigation of the Saccharomyces cerevisiae genome annotation by
RT comparison to the genome of a related fungus: Ashbya gossypii.";
RL Genome Biol. 4:R45.1-R45.13(2003).
RN [6]
RP FUNCTION.
RX PubMed=8252639; DOI=10.1007/bf00336780;
RA Waldherr M., Ragnini A., Jank B., Teply R., Wiesenberger G., Schweyen R.J.;
RT "A multitude of suppressors of group II intron-splicing defects in yeast.";
RL Curr. Genet. 24:301-306(1993).
RN [7]
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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238 AND SER-340, AND
RP IDENTIFICATION BY 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340, AND IDENTIFICATION BY
RP 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-238 AND SER-340, AND
RP IDENTIFICATION BY 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).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=23222640; DOI=10.1038/nsmb.2468;
RA Mitchell S.F., Jain S., She M., Parker R.;
RT "Global analysis of yeast mRNPs.";
RL Nat. Struct. Mol. Biol. 20:127-133(2013).
RN [14]
RP METHYLATION AT ARG-419; ARG-425; ARG-538; ARG-551 AND ARG-575.
RX PubMed=26046779; DOI=10.1002/pmic.201500032;
RA Plank M., Fischer R., Geoghegan V., Charles P.D., Konietzny R., Acuto O.,
RA Pears C., Schofield C.J., Kessler B.M.;
RT "Expanding the yeast protein arginine methylome.";
RL Proteomics 15:3232-3243(2015).
RN [15]
RP METHYLATION AT ARG-425; ARG-440; ARG-443 AND ARG-447, AND PHOSPHORYLATION
RP AT SER-150; SER-238; SER-340 AND SER-522.
RX PubMed=33856219; DOI=10.1021/acs.jproteome.0c00927;
RA Hamey J.J., Nguyen A., Wilkins M.R.;
RT "Discovery of arginine methylation, phosphorylation, and their co-
RT occurrence in condensate-associated proteins in Saccharomyces cerevisiae.";
RL J. Proteome Res. 20:2420-2434(2021).
CC -!- FUNCTION: DNA polymerase alpha mutation suppressor. Suppressor of group
CC II intron splicing defects of a mutation in MRS2. May play a role in
CC mitochondrial mRNA splicing. {ECO:0000269|PubMed:8252639,
CC ECO:0000269|PubMed:9529527}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:23222640}. Cytoplasm, P-body
CC {ECO:0000269|PubMed:23222640}. Cytoplasm, Stress granule
CC {ECO:0000269|PubMed:23222640}.
CC -!- MISCELLANEOUS: Present with 2190 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB50177.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAC49960.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAA89935.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U33116; AAC49960.1; ALT_SEQ; Genomic_DNA.
DR EMBL; U29398; AAB50177.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Z49810; CAA89935.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY245793; AAP04343.1; -; mRNA.
DR EMBL; BK006946; DAA09881.1; -; Genomic_DNA.
DR PIR; S55102; S55102.
DR RefSeq; NP_013695.2; NM_001182375.1.
DR AlphaFoldDB; P50109; -.
DR BioGRID; 35152; 322.
DR IntAct; P50109; 6.
DR MINT; P50109; -.
DR STRING; 4932.YML017W; -.
DR iPTMnet; P50109; -.
DR MaxQB; P50109; -.
DR PaxDb; P50109; -.
DR PRIDE; P50109; -.
DR EnsemblFungi; YML017W_mRNA; YML017W; YML017W.
DR GeneID; 854991; -.
DR KEGG; sce:YML017W; -.
DR SGD; S000004479; PSP2.
DR VEuPathDB; FungiDB:YML017W; -.
DR eggNOG; ENOG502QWA7; Eukaryota.
DR HOGENOM; CLU_032585_0_0_1; -.
DR InParanoid; P50109; -.
DR OMA; FKLFWEL; -.
DR BioCyc; YEAST:G3O-32621-MON; -.
DR Reactome; R-SCE-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:P50109; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P50109; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0000932; C:P-body; IDA:SGD.
DR GO; GO:0000172; C:ribonuclease MRP complex; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0001682; P:tRNA 5'-leader removal; IBA:GO_Central.
PE 1: Evidence at protein level;
KW Cytoplasm; Methylation; Phosphoprotein; Reference proteome.
FT CHAIN 1..593
FT /note="Protein PSP2"
FT /id="PRO_0000097069"
FT REGION 56..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..405
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:33856219,
FT ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 419
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|PubMed:26046779"
FT MOD_RES 425
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|PubMed:26046779,
FT ECO:0000269|PubMed:33856219"
FT MOD_RES 440
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 443
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 447
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 538
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|PubMed:26046779"
FT MOD_RES 551
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|PubMed:26046779"
FT MOD_RES 575
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|PubMed:26046779"
SQ SEQUENCE 593 AA; 65584 MW; 69790FE7ECCEC6AA CRC64;
MGTNNTSNNN GTTKKMSLEE FLGNDTLGES VWDEEDINLD AISNTTNIDI LKQTKAGEHQ
RDGHQQHPHG GHGPMNRSRF SNAGPFGGGS MGDFANHHHP LQHQQGPPYI VKFSDLPPRF
SNFDIEDLFQ AKFTKFIKFK LFWEINKNPS ISTLKSGSIF DQNFKRDSKV AFVELYTSRD
MDKILNYWTT PLKEIYHITT APAEFEDFKD YSTKVKLLTD PKDDAGKPFI TKTQRSKSNP
FGSAKPVDTQ SKILDIEEKM ENLHVEDTTT LRASLIPSSD SMATTATGSK ITILKKQTPT
EEESHSATPT PKPLSYSEVV ERSVVNETSK KGTPLSKLDS PALELQSKPD KSDEFKGGDE
QGFEKGGDDK AQLDVSNDKD KGSETDVDKQ FTFKNVEREH SMSRTKYNGN HNNNNGNFRG
SNRYRGGPNG SSYKGGHNNR GNRGGYRGGS SYNNNNNNTN DNNNNNNNSS SNNNNGSRYH
DRQNNEEGLT SDSSLDASGN KKNDFTNSTS NTQQYSIFKP ASGFLGQGNN DSIRNNGRGN
YNSSGMNGGS RGRGFGRGRG FGRGAYNNRG SRGGRGSSGN YSNYNNRTTD MPL
