SSBP1_YEAST
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 03-AUG-2022, entry version 194.
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; 1222.
DR DIP; DIP-6824N; -.
DR IntAct; P10080; 114.
DR MINT; P10080; -.
DR STRING; 4932.YHL034C; -.
DR iPTMnet; P10080; -.
DR MaxQB; P10080; -.
DR PaxDb; P10080; -.
DR PRIDE; P10080; -.
DR EnsemblFungi; YHL034C_mRNA; YHL034C; YHL034C.
DR GeneID; 856351; -.
DR KEGG; sce:YHL034C; -.
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 BioCyc; YEAST:G3O-31053-MON; -.
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: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 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 Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 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 1..27
FT /note="Polar 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
