THO1_YEAST
ID THO1_YEAST Reviewed; 218 AA.
AC P40040; D3DLW8;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Protein THO1;
GN Name=THO1; OrderedLocusNames=YER063W;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(1997).
RN [2]
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 [3]
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 [4]
RP CHARACTERIZATION.
RX PubMed=9707445; DOI=10.1093/emboj/17.16.4859;
RA Piruat J.I., Aguilera A.;
RT "A novel yeast gene, THO2, is involved in RNA pol II transcription and
RT provides new evidence for transcriptional elongation-associated
RT recombination.";
RL EMBO J. 17:4859-4872(1998).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-58 AND SER-68, 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 [8]
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: Unknown; suppressor of the transcriptional defect of HPR1 by
CC overexpression.
CC -!- MISCELLANEOUS: Present with 6580 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U18813; AAB64599.1; -; Genomic_DNA.
DR EMBL; AY557779; AAS56105.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07722.1; -; Genomic_DNA.
DR PIR; S50566; S50566.
DR RefSeq; NP_010985.1; NM_001178954.1.
DR PDB; 1H1J; NMR; -; S=2-50.
DR PDB; 2WQG; NMR; -; A=2-50.
DR PDB; 4UZW; NMR; -; A=2-50.
DR PDB; 4UZX; NMR; -; A=119-183.
DR PDBsum; 1H1J; -.
DR PDBsum; 2WQG; -.
DR PDBsum; 4UZW; -.
DR PDBsum; 4UZX; -.
DR AlphaFoldDB; P40040; -.
DR BMRB; P40040; -.
DR SMR; P40040; -.
DR BioGRID; 36805; 60.
DR DIP; DIP-3983N; -.
DR IntAct; P40040; 2.
DR MINT; P40040; -.
DR STRING; 4932.YER063W; -.
DR iPTMnet; P40040; -.
DR MaxQB; P40040; -.
DR PaxDb; P40040; -.
DR PRIDE; P40040; -.
DR EnsemblFungi; YER063W_mRNA; YER063W; YER063W.
DR GeneID; 856792; -.
DR KEGG; sce:YER063W; -.
DR SGD; S000000865; THO1.
DR VEuPathDB; FungiDB:YER063W; -.
DR eggNOG; ENOG502SARN; Eukaryota.
DR HOGENOM; CLU_088651_1_0_1; -.
DR InParanoid; P40040; -.
DR OMA; RNLPHTG; -.
DR BioCyc; YEAST:G3O-30238-MON; -.
DR EvolutionaryTrace; P40040; -.
DR PRO; PR:P40040; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P40040; protein.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0003682; F:chromatin binding; IDA:SGD.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IDA:SGD.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IGI:SGD.
DR GO; GO:0022618; P:ribonucleoprotein complex assembly; IMP:SGD.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IGI:SGD.
DR Gene3D; 1.10.720.30; -; 1.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR InterPro; IPR040746; THO1_MOS11_C.
DR Pfam; PF02037; SAP; 1.
DR Pfam; PF18592; Tho1_MOS11_C; 1.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF68906; SSF68906; 1.
DR PROSITE; PS50800; SAP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Phosphoprotein; Reference proteome.
FT CHAIN 1..218
FT /note="Protein THO1"
FT /id="PRO_0000072519"
FT DOMAIN 4..38
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT REGION 37..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..218
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 68
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:1H1J"
FT HELIX 9..18
FT /evidence="ECO:0007829|PDB:1H1J"
FT HELIX 27..40
FT /evidence="ECO:0007829|PDB:1H1J"
FT HELIX 122..143
FT /evidence="ECO:0007829|PDB:4UZX"
FT HELIX 147..162
FT /evidence="ECO:0007829|PDB:4UZX"
FT HELIX 170..175
FT /evidence="ECO:0007829|PDB:4UZX"
SQ SEQUENCE 218 AA; 24138 MW; 39CB897BA9FBA94A CRC64;
MADYSSLTVV QLKDLLTKRN LSVGGLKNEL VQRLIKDDEE SKGESEVSPQ EQNQEQGSEP
AAIEEPASQN ITEKKEVSSE PKETNEPKEE NKDVQKPSDG PSATASENEQ AAASTAAPAL
SPEEIKAKAL DLLNKKLHRA NKFGQDQADI DSLQRQINRV EKFGVDLNSK LAEELGLVSR
KNEPESGNNG KFKNRNKNAN NRSRVSKNRR GNRSGYRR
