ID   SSBP1_YEAST             Reviewed;         294 AA.
AC   P10080; D3DKT4;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 2.
DT   02-SEP-2026, entry version 208.
DE   RecName: Full=Single-stranded nucleic acid-binding protein;
GN   Name=SBP1; Synonyms=SSB1 {ECO:0000303|PubMed:2823109}, SSBR1;
GN   OrderedLocusNames=YHL034C;
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=2823109; DOI=10.1128/mcb.7.8.2947-2955.1987;
RA   Jong A.Y.-S., Clark M.W., Gilbert M., Oehm A., Campbell J.L.;
RT   "Saccharomyces cerevisiae SSB1 protein and its relationship to nucleolar
RT   RNA-binding proteins.";
RL   Mol. Cell. Biol. 7:2947-2955(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA   Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA   Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA   Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA   St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA   Waterston R., Wilson R., Vaudin M.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   VIII.";
RL   Science 265:2077-2082(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] OF 162-294.
RX   PubMed=1429834; DOI=10.1083/jcb.119.4.737;
RA   Russell I.D., Tollervey D.;
RT   "NOP3 is an essential yeast protein which is required for pre-rRNA
RT   processing.";
RL   J. Cell Biol. 119:737-747(1992).
RN   [5]
RP   SUBCELLULAR LOCATION.
RX   PubMed=2121740; DOI=10.1083/jcb.111.5.1741;
RA   Clark M.W., Yip M.L.R., Campbell J., Abelson J.;
RT   "SSB-1 of the yeast Saccharomyces cerevisiae is a nucleolar-specific,
RT   silver-binding protein that is associated with the snR10 and snR11 small
RT   nuclear RNAs.";
RL   J. Cell Biol. 111:1741-1751(1990).
RN   [6]
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   [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, AND SUBCELLULAR LOCATION.
RX   PubMed=16782896; DOI=10.1128/mcb.01913-05;
RA   Segal S.P., Dunckley T., Parker R.;
RT   "Sbp1p affects translational repression and decapping in Saccharomyces
RT   cerevisiae.";
RL   Mol. Cell. Biol. 26:5120-5130(2006).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-91, 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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-242 AND SER-244, AND
RP   IDENTIFICATION BY 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 THR-91 AND THR-119, 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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-91, 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).
RN   [13]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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).
RN   [14]
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   [15]
RP   METHYLATION AT ARG-125; ARG-145 AND ARG-165.
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   [16]
RP   METHYLATION AT ARG-135; ARG-137; ARG-141; ARG-145; ARG-149; ARG-153;
RP   ARG-155; ARG-159; ARG-161 AND ARG-165, AND PHOSPHORYLATION AT SER-2;
RP   SER-16; THR-49; SER-66; THR-91; THR-287 AND SER-289.
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: Functions in the transition of mRNAs from translation to an
CC       mRNP complex destined for decapping. High-copy-number suppressor of
CC       decapping defects. Overexpression suppresses decapping defects in both
CC       DCP1-2 and DCP2-7 mutations. Acts to promote translational repression
CC       of mRNA in conjunction with DHH1 and subsequent mRNA localization to P
CC       bodies. Promotes translational repression of mRNA during glucose
CC       deprivation. {ECO:0000269|PubMed:16782896}.
CC   -!- SUBUNIT: Associated with snR10 and snR11 small nuclear RNAs.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16782896,
CC       ECO:0000269|PubMed:23222640}. Nucleus, nucleolus
CC       {ECO:0000269|PubMed:16782896, ECO:0000269|PubMed:2121740}. Cytoplasm,
CC       P-body {ECO:0000269|PubMed:16782896, ECO:0000269|PubMed:23222640}.
CC       Cytoplasm, Stress granule {ECO:0000269|PubMed:23222640}.
CC   -!- MISCELLANEOUS: Present with 12800 molecules/cell in log phase SD
CC       medium. {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the RRM GAR family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA35098.1; Type=Frameshift; Evidence={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; M17244; AAA35098.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; U11583; AAB65046.1; -; Genomic_DNA.
DR   EMBL; X66278; CAA46989.1; -; Genomic_DNA.
DR   EMBL; BK006934; DAA06651.1; -; Genomic_DNA.
DR   PIR; S48934; S48934.
DR   RefSeq; NP_011829.1; NM_001179114.1.
DR   AlphaFoldDB; P10080; -.
DR   BioGRID; 36388; 1341.
DR   DIP; DIP-6824N; -.
DR   FunCoup; P10080; 802.
DR   IntAct; P10080; 168.
DR   MINT; P10080; -.
DR   STRING; 4932.YHL034C; -.
DR   iPTMnet; P10080; -.
DR   PaxDb; 4932-YHL034C; -.
DR   PeptideAtlas; P10080; -.
DR   EnsemblFungi; YHL034C_mRNA; YHL034C; YHL034C.
DR   GeneID; 856351; -.
DR   KEGG; sce:YHL034C; -.
DR   AGR; SGD:S000001026; -.
DR   SGD; S000001026; SBP1.
DR   VEuPathDB; FungiDB:YHL034C; -.
DR   eggNOG; ENOG502QTE4; Eukaryota.
DR   HOGENOM; CLU_068713_0_0_1; -.
DR   InParanoid; P10080; -.
DR   OMA; FFSKRMN; -.
DR   OrthoDB; 439808at2759; -.
DR   BioCyc; YEAST:G3O-31053-MONOMER; -.
DR   BioGRID-ORCS; 856351; 2 hits in 10 CRISPR screens.
DR   CD-CODE; A777E0F8; P-body.
DR   CD-CODE; E03F929F; Stress granule.
DR   PRO; PR:P10080; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   RNAct; P10080; protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
DR   GO; GO:0005730; C:nucleolus; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000932; C:P-body; IDA:SGD.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR   GO; GO:0031370; F:eukaryotic initiation factor 4G binding; IDA:SGD.
DR   GO; GO:0048027; F:mRNA 5'-UTR binding; IDA:SGD.
DR   GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR   GO; GO:0017148; P:negative regulation of translation; IDA:SGD.
DR   GO; GO:0032055; P:negative regulation of translation in response to stress; IMP:SGD.
DR   GO; GO:0045947; P:negative regulation of translational initiation; IDA:SGD.
DR   GO; GO:0035617; P:stress granule disassembly; IDA:SGD.
DR   CDD; cd00590; RRM_SF; 1.
DR   FunFam; 3.30.70.330:FF:000930; Sbp1p; 1.
DR   FunFam; 3.30.70.330:FF:000975; Sbp1p; 1.
DR   Gene3D; 3.30.70.330; -; 2.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR050374; RRT5_SRSF_SR.
DR   PANTHER; PTHR23003:SF56; RIBONUCLEOPROTEIN 1-RELATED; 1.
DR   PANTHER; PTHR23003; RNA RECOGNITION MOTIF RRM DOMAIN CONTAINING PROTEIN; 1.
DR   Pfam; PF00076; RRM_1; 1.
DR   SMART; SM00360; RRM; 2.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
DR   PROSITE; PS50102; RRM; 2.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Methylation; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; RNA-binding; Stress response.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..294
FT                   /note="Single-stranded nucleic acid-binding protein"
FT                   /id="PRO_0000081964"
FT   DOMAIN          37..119
FT                   /note="RRM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   DOMAIN          186..274
FT                   /note="RRM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          131..151
FT                   /note="RNA-binding RGG-box"
FT                   /evidence="ECO:0000250"
FT   REGION          151..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          275..294
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        151..169
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        278..288
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         2
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:33856219"
FT   MOD_RES         16
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:33856219"
FT   MOD_RES         49
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:33856219"
FT   MOD_RES         66
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:33856219"
FT   MOD_RES         91
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:33856219,
FT                   ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         119
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         125
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000269|PubMed:26046779"
FT   MOD_RES         135
FT                   /note="Dimethylated arginine"
FT                   /evidence="ECO:0000269|PubMed:33856219"
FT   MOD_RES         137
FT                   /note="Dimethylated arginine"
FT                   /evidence="ECO:0000269|PubMed:33856219"
FT   MOD_RES         141
FT                   /note="Dimethylated arginine"
FT                   /evidence="ECO:0000269|PubMed:33856219"
FT   MOD_RES         145
FT                   /note="Dimethylated arginine; alternate"
FT                   /evidence="ECO:0000269|PubMed:33856219"
FT   MOD_RES         145
FT                   /note="Omega-N-methylarginine; alternate"
FT                   /evidence="ECO:0000269|PubMed:26046779,
FT                   ECO:0000269|PubMed:33856219"
FT   MOD_RES         149
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000269|PubMed:33856219"
FT   MOD_RES         153
FT                   /note="Dimethylated arginine"
FT                   /evidence="ECO:0000269|PubMed:33856219"
FT   MOD_RES         155
FT                   /note="Dimethylated arginine"
FT                   /evidence="ECO:0000269|PubMed:33856219"
FT   MOD_RES         159
FT                   /note="Dimethylated arginine"
FT                   /evidence="ECO:0000269|PubMed:33856219"
FT   MOD_RES         161
FT                   /note="Dimethylated arginine; alternate"
FT                   /evidence="ECO:0000269|PubMed:33856219"
FT   MOD_RES         161
FT                   /note="Omega-N-methylarginine; alternate"
FT                   /evidence="ECO:0000269|PubMed:33856219"
FT   MOD_RES         165
FT                   /note="Dimethylated arginine; alternate"
FT                   /evidence="ECO:0000269|PubMed:33856219"
FT   MOD_RES         165
FT                   /note="Omega-N-methylarginine; alternate"
FT                   /evidence="ECO:0000269|PubMed:26046779"
FT   MOD_RES         242
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   MOD_RES         244
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   MOD_RES         287
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:33856219"
FT   MOD_RES         289
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:33856219"
FT   CONFLICT        162
FT                   /note="G -> S (in Ref. 1; AAA35098)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   294 AA;  32990 MW;  FF740B206DDE5EC8 CRC64;
     MSAEIEEATN AVNNLSINDS EQQPRAPTHK TVIDPEDTIF IGNVAHECTE DDLKQLFVEE
     FGDEVSVEIP IKEHTDGHIP ASKHALVKFP TKIDFDNIKE NYDTKVVKDR EIHIKRARTP
     GQMQRGGFRG RGGFRGRGGF RGGFRGGYRG GFRGRGNFRG RGGARGGFNG QKREKIPLDQ
     MERSKDTLYI NNVPFKATKE EVAEFFGTDA DSISLPMRKM RDQHTGRIFT SDSANRGMAF
     VTFSGENVDI EAKAEEFKGK VFGDRELTVD VAVIRPENDE EEIEQETGSE EKQE
//