ID   HOT1_YEAST              Reviewed;         719 AA.
AC   Q03213; D6VZZ4;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   27-MAR-2024, entry version 159.
DE   RecName: Full=High-osmolarity-induced transcription protein 1;
GN   Name=HOT1; OrderedLocusNames=YMR172W; ORFNames=YM8010.02;
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=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   [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   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HOG1.
RX   PubMed=10409737; DOI=10.1128/mcb.19.8.5474;
RA   Rep M., Reiser V., Gartner U., Thevelein J.M., Hohmann S., Ammerer G.,
RA   Ruis H.;
RT   "Osmotic stress-induced gene expression in Saccharomyces cerevisiae
RT   requires Msn1p and the novel nuclear factor Hot1p.";
RL   Mol. Cell. Biol. 19:5474-5485(1999).
RN   [4]
RP   FUNCTION.
RX   PubMed=10722658; DOI=10.1074/jbc.275.12.8290;
RA   Rep M., Krantz M., Thevelein J.M., Hohmann S.;
RT   "The transcriptional response of Saccharomyces cerevisiae to osmotic shock.
RT   Hot1p and Msn2p/Msn4p are required for the induction of subsets of high
RT   osmolarity glycerol pathway-dependent genes.";
RL   J. Biol. Chem. 275:8290-8300(2000).
RN   [5]
RP   FUNCTION, PHOSPHORYLATION, AND PROMOTER BINDING.
RX   PubMed=11336700; DOI=10.1016/s1097-2765(01)00221-0;
RA   Alepuz P.M., Jovanovic A., Reiser V., Ammerer G.;
RT   "Stress-induced map kinase Hog1 is part of transcription activation
RT   complexes.";
RL   Mol. Cell 7:767-777(2001).
RN   [6]
RP   FUNCTION, INTERACTION WITH HOG1, PHOSPHORYLATION, AND MUTAGENESIS OF
RP   SER-30; SER-70; SER-153; SER-360 AND SER-410.
RX   PubMed=12743037; DOI=10.1093/emboj/cdg243;
RA   Alepuz P.M., de Nadal E., Zapater M., Ammerer G., Posas F.;
RT   "Osmostress-induced transcription by Hot1 depends on a Hog1-mediated
RT   recruitment of the RNA Pol II.";
RL   EMBO J. 22:2433-2442(2003).
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-146, 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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153, 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).
CC   -!- FUNCTION: Required for a complete transcriptional response to osmotic
CC       stress, through recruitment of HOG1 followed by pol II recruitment to
CC       the promoters of GPD1 and other HOG-dependent genes.
CC       {ECO:0000269|PubMed:10409737, ECO:0000269|PubMed:10722658,
CC       ECO:0000269|PubMed:11336700, ECO:0000269|PubMed:12743037}.
CC   -!- SUBUNIT: Interacts with HOG1. {ECO:0000269|PubMed:10409737,
CC       ECO:0000269|PubMed:12743037}.
CC   -!- INTERACTION:
CC       Q03213; P32485: HOG1; NbExp=4; IntAct=EBI-27376, EBI-8437;
CC       Q03213; P32561: RPD3; NbExp=3; IntAct=EBI-27376, EBI-15864;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10409737,
CC       ECO:0000269|PubMed:14562095}.
CC   -!- PTM: Hyperphosphorylated during acute stress.
CC   -!- MISCELLANEOUS: Present with 149 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the HOT1 family. {ECO:0000305}.
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DR   EMBL; Z49808; CAA89905.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA10068.1; -; Genomic_DNA.
DR   PIR; S55119; S55119.
DR   RefSeq; NP_013895.1; NM_001182677.1.
DR   AlphaFoldDB; Q03213; -.
DR   SMR; Q03213; -.
DR   BioGRID; 35350; 90.
DR   DIP; DIP-2367N; -.
DR   IntAct; Q03213; 8.
DR   MINT; Q03213; -.
DR   STRING; 4932.YMR172W; -.
DR   GlyGen; Q03213; 4 sites, 1 O-linked glycan (4 sites).
DR   iPTMnet; Q03213; -.
DR   MaxQB; Q03213; -.
DR   PaxDb; 4932-YMR172W; -.
DR   PeptideAtlas; Q03213; -.
DR   TopDownProteomics; Q03213; -.
DR   EnsemblFungi; YMR172W_mRNA; YMR172W; YMR172W.
DR   GeneID; 855208; -.
DR   KEGG; sce:YMR172W; -.
DR   AGR; SGD:S000004783; -.
DR   SGD; S000004783; HOT1.
DR   VEuPathDB; FungiDB:YMR172W; -.
DR   eggNOG; ENOG502QQ7G; Eukaryota.
DR   HOGENOM; CLU_023418_0_0_1; -.
DR   InParanoid; Q03213; -.
DR   OMA; KTIWEEY; -.
DR   OrthoDB; 2031320at2759; -.
DR   BioCyc; YEAST:G3O-32860-MONOMER; -.
DR   BioGRID-ORCS; 855208; 3 hits in 10 CRISPR screens.
DR   PRO; PR:Q03213; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; Q03213; Protein.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:SGD.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IDA:SGD.
DR   GO; GO:0060963; P:positive regulation of ribosomal protein gene transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IDA:SGD.
DR   InterPro; IPR022210; TF_GCR1-like.
DR   PANTHER; PTHR37784:SF7; HIGH-OSMOLARITY-INDUCED TRANSCRIPTION PROTEIN 1; 1.
DR   PANTHER; PTHR37784; PROTEIN MSN1; 1.
DR   Pfam; PF12550; GCR1_C; 1.
PE   1: Evidence at protein level;
KW   Activator; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..719
FT                   /note="High-osmolarity-induced transcription protein 1"
FT                   /id="PRO_0000203317"
FT   REGION          68..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          102..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          353..402
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          496..610
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..89
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..159
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..373
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        382..402
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        496..527
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        537..572
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        582..596
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         146
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         153
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MUTAGEN         30
FT                   /note="S->A: Impairs HOT1 phosphorylation; when associated
FT                   with A-70; A-153; A-360 and A-410."
FT                   /evidence="ECO:0000269|PubMed:12743037"
FT   MUTAGEN         70
FT                   /note="S->A: Impairs HOT1 phosphorylation; when associated
FT                   with A-30; A-153; A-360 and A-410."
FT                   /evidence="ECO:0000269|PubMed:12743037"
FT   MUTAGEN         153
FT                   /note="S->A: Impairs HOT1 phosphorylation; when associated
FT                   with A-30; A-70; A-360 and A-410."
FT                   /evidence="ECO:0000269|PubMed:12743037"
FT   MUTAGEN         360
FT                   /note="S->A: Impairs HOT1 phosphorylation; when associated
FT                   with A-30; A-70; A-153 and A-410."
FT                   /evidence="ECO:0000269|PubMed:12743037"
FT   MUTAGEN         410
FT                   /note="S->A: Impairs HOT1 phosphorylation; when associated
FT                   with A-30; A-70; A-153 and A-360."
FT                   /evidence="ECO:0000269|PubMed:12743037"
SQ   SEQUENCE   719 AA;  79416 MW;  4652BE93743D5A54 CRC64;
     MSGMGIAILC IVRTKIYRIT ISFDYSTLMS PFFLFLMMPT TLKDGYRMNS QVNEDAIGIN
     LDLSLPTHIS PTTGSESASG SNASTLRNDG NALDGGLLRT SAAISAPTGT SQPTETIGEK
     LSNEERVNSN VSASNSTTAG TGRMLSQSLT NDSPSNEIST DQLKIFQRMD EMSARMIEME
     ESFNKLSNKI AEQNTMVLNL KQDNYKVMNK LNILLKLVAQ PSARPSTNNA QNKLAIELLN
     SISAVSSAYL QKMQNNGSGR QHTADLCTGD SNTHSGINQH RTTNGTIDVN TNTAQLNNQF
     SNALNTILPD QQHNRNNVSQ NINQSLPNRQ LGPVINTQAN QNQSQVLIHN TNTHQQVNRS
     PISFPNASTD KPFKLNPNGI KRRRRNTQSN NNASTNDHAS AAQKPISALS PLTNSHNSTT
     SMNYTNSSIH SGVTSASNSF HDLNSLNNFG TTTALSLPSL ALDNASFPPN QNVIPPIINN
     TQQPLSFSQL INQDSTTSEL LPSGKSGVNT NIVNRNRAST LPSYPKPMTV KSNVDDDGYQ
     EDDDDDGDDE GDGRDNEEDS TAEEDEVDDE IETDMKNASI NKRRRSLHHK KSNSLNGRRK
     LHGESATKPN INSDLHYRIL KAPTDVKTIW EEYDTGIRGK PSIKHLEAKY GNKWRLNKNK
     KTFSRRKRLY KFILNGMERG KTAQEMIETL ENKRLYKDDE DGEVKKRTIG WLQESLAGI
//