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   27-MAR-2024, entry version 177.
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   PDB; 8ENK; X-ray; 2.50 A; E=123-178.
DR   PDBsum; 1H1J; -.
DR   PDBsum; 2WQG; -.
DR   PDBsum; 4UZW; -.
DR   PDBsum; 4UZX; -.
DR   PDBsum; 8ENK; -.
DR   AlphaFoldDB; P40040; -.
DR   BMRB; P40040; -.
DR   SMR; P40040; -.
DR   BioGRID; 36805; 78.
DR   DIP; DIP-3983N; -.
DR   IntAct; P40040; 2.
DR   MINT; P40040; -.
DR   STRING; 4932.YER063W; -.
DR   iPTMnet; P40040; -.
DR   MaxQB; P40040; -.
DR   PaxDb; 4932-YER063W; -.
DR   PeptideAtlas; P40040; -.
DR   EnsemblFungi; YER063W_mRNA; YER063W; YER063W.
DR   GeneID; 856792; -.
DR   KEGG; sce:YER063W; -.
DR   AGR; SGD:S000000865; -.
DR   SGD; S000000865; THO1.
DR   VEuPathDB; FungiDB:YER063W; -.
DR   eggNOG; ENOG502SARN; Eukaryota.
DR   HOGENOM; CLU_088651_1_0_1; -.
DR   InParanoid; P40040; -.
DR   OMA; WSEKDNA; -.
DR   OrthoDB; 2039426at2759; -.
DR   BioCyc; YEAST:G3O-30238-MONOMER; -.
DR   BioGRID-ORCS; 856792; 0 hits in 10 CRISPR screens.
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:protein-RNA complex assembly; IMP:SGD.
DR   GO; GO:0006368; P:transcription elongation by RNA polymerase II; IGI:SGD.
DR   Gene3D; 1.10.720.30; SAP domain; 1.
DR   InterPro; IPR003034; SAP_dom.
DR   InterPro; IPR036361; SAP_dom_sf.
DR   InterPro; IPR040746; THO1_MOS11_C.
DR   PANTHER; PTHR46551; SAP DOMAIN-CONTAINING RIBONUCLEOPROTEIN; 1.
DR   PANTHER; PTHR46551:SF1; SAP DOMAIN-CONTAINING RIBONUCLEOPROTEIN; 1.
DR   Pfam; PF02037; SAP; 1.
DR   Pfam; PF18592; Tho1_MOS11_C; 1.
DR   SMART; SM00513; SAP; 1.
DR   SUPFAM; SSF68906; SAP domain; 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           124..142
FT                   /evidence="ECO:0007829|PDB:8ENK"
FT   HELIX           147..162
FT                   /evidence="ECO:0007829|PDB:8ENK"
FT   HELIX           170..174
FT                   /evidence="ECO:0007829|PDB:8ENK"
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
//