HOT1_YEAST
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 03-AUG-2022, entry version 154.
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; 86.
DR DIP; DIP-2367N; -.
DR IntAct; Q03213; 8.
DR MINT; Q03213; -.
DR STRING; 4932.YMR172W; -.
DR iPTMnet; Q03213; -.
DR MaxQB; Q03213; -.
DR PaxDb; Q03213; -.
DR PRIDE; Q03213; -.
DR TopDownProteomics; Q03213; -.
DR EnsemblFungi; YMR172W_mRNA; YMR172W; YMR172W.
DR GeneID; 855208; -.
DR KEGG; sce:YMR172W; -.
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 BioCyc; YEAST:G3O-32860-MON; -.
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 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
