HSF_YEAST
ID HSF_YEAST Reviewed; 833 AA.
AC P10961; D6VU70; P11529;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Heat shock transcription factor {ECO:0000303|PubMed:3044612};
DE Short=HSTF {ECO:0000305};
DE AltName: Full=Heat shock factor protein {ECO:0000305};
DE Short=HSF {ECO:0000303|PubMed:3044612};
GN Name=HSF1 {ECO:0000303|PubMed:3044612}; OrderedLocusNames=YGL073W;
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], PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP SUBCELLULAR LOCATION, PHOSPHORYLATION, AND DISRUPTION PHENOTYPE.
RX PubMed=3044613; DOI=10.1016/s0092-8674(88)91219-6;
RA Sorger P.K., Pelham H.R.B.;
RT "Yeast heat shock factor is an essential DNA-binding protein that exhibits
RT temperature-dependent phosphorylation.";
RL Cell 54:855-864(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=3044612; DOI=10.1016/s0092-8674(88)91197-x;
RA Wiederrecht G., Seto D., Parker C.S.;
RT "Isolation of the gene encoding the S. cerevisiae heat shock transcription
RT factor.";
RL Cell 54:841-853(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [5]
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 [6]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF 260-ASN--ASN-280.
RX PubMed=8175654; DOI=10.1016/s0021-9258(18)99899-6;
RA Flick K.E., Gonzalez L. Jr., Harrison C.J., Nelson H.C.;
RT "Yeast heat shock transcription factor contains a flexible linker between
RT the DNA-binding and trimerization domains. Implications for DNA binding by
RT trimeric proteins.";
RL J. Biol. Chem. 269:12475-12481(1994).
RN [7]
RP IDENTIFICATION BY 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450 AND SER-458, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-97; SER-458; SER-471; SER-478
RP AND SER-528, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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: DNA-binding transcription factor that specifically binds heat
CC shock promoter elements (HSE) and activates transcription.
CC {ECO:0000269|PubMed:3044612, ECO:0000269|PubMed:3044613,
CC ECO:0000269|PubMed:8175654}.
CC -!- SUBUNIT: Homotrimer (PubMed:8175654). Homotrimerization increases the
CC affinity of HSF1 to DNA (PubMed:8175654). {ECO:0000269|PubMed:8175654}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:3044613}.
CC -!- PTM: Exhibits temperature-dependent phosphorylation that activates the
CC transcriptional capacity. {ECO:0000269|PubMed:3044613}.
CC -!- DISRUPTION PHENOTYPE: Inviable vegetative cell population.
CC {ECO:0000269|PubMed:3044612, ECO:0000269|PubMed:3044613}.
CC -!- SIMILARITY: Belongs to the HSF family. {ECO:0000305}.
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DR EMBL; J03139; AAA34688.1; -; Genomic_DNA.
DR EMBL; M22040; AAA34689.1; -; Genomic_DNA.
DR EMBL; Z72596; CAA96777.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08031.1; -; Genomic_DNA.
DR PIR; A31593; A31593.
DR RefSeq; NP_011442.3; NM_001180938.3.
DR AlphaFoldDB; P10961; -.
DR SMR; P10961; -.
DR BioGRID; 33176; 417.
DR DIP; DIP-2374N; -.
DR IntAct; P10961; 14.
DR MINT; P10961; -.
DR STRING; 4932.YGL073W; -.
DR iPTMnet; P10961; -.
DR MaxQB; P10961; -.
DR PaxDb; P10961; -.
DR PRIDE; P10961; -.
DR EnsemblFungi; YGL073W_mRNA; YGL073W; YGL073W.
DR GeneID; 852806; -.
DR KEGG; sce:YGL073W; -.
DR SGD; S000003041; HSF1.
DR VEuPathDB; FungiDB:YGL073W; -.
DR eggNOG; KOG0627; Eukaryota.
DR GeneTree; ENSGT00940000169930; -.
DR HOGENOM; CLU_017670_1_0_1; -.
DR InParanoid; P10961; -.
DR OMA; NKLWSML; -.
DR BioCyc; YEAST:G3O-30575-MON; -.
DR Reactome; R-SCE-3371453; Regulation of HSF1-mediated heat shock response.
DR Reactome; R-SCE-3371511; HSF1 activation.
DR Reactome; R-SCE-3371568; Attenuation phase.
DR Reactome; R-SCE-3371571; HSF1-dependent transactivation.
DR PRO; PR:P10961; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P10961; protein.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0032993; C:protein-DNA complex; IMP:CAFA.
DR GO; GO:0003677; F:DNA binding; IMP:CAFA.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:SGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0070202; P:regulation of establishment of protein localization to chromosome; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0043555; P:regulation of translation in response to stress; IDA:SGD.
DR GO; GO:0009408; P:response to heat; IMP:SGD.
DR DisProt; DP00135; -.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR000232; HSF_DNA-bd.
DR InterPro; IPR027725; HSF_fam.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR10015; PTHR10015; 1.
DR Pfam; PF00447; HSF_DNA-bind; 1.
DR PRINTS; PR00056; HSFDOMAIN.
DR SMART; SM00415; HSF; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS00434; HSF_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Direct protein sequencing; DNA-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Stress response; Transcription;
KW Transcription regulation.
FT CHAIN 1..833
FT /note="Heat shock transcription factor"
FT /id="PRO_0000124581"
FT DNA_BIND 170..259
FT /evidence="ECO:0000269|PubMed:3044612,
FT ECO:0000269|PubMed:8175654"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..280
FT /note="Flexible linker"
FT /evidence="ECO:0000269|PubMed:8175654"
FT REGION 277..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..403
FT /note="Involved in trimerization"
FT /evidence="ECO:0000250|UniProtKB:P22121"
FT REGION 447..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..765
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 542..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 606..626
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..765
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..797
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 97
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 458
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 471
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 478
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 528
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 260..332
FT /note="Missing: Inviable vegetative cell population."
FT /evidence="ECO:0000269|PubMed:8175654"
FT MUTAGEN 260..312
FT /note="Missing: Inviable vegetative cell population."
FT /evidence="ECO:0000269|PubMed:8175654"
FT MUTAGEN 270..332
FT /note="Missing: Inviable vegetative cell population."
FT /evidence="ECO:0000269|PubMed:8175654"
FT CONFLICT 522
FT /note="S -> F (in Ref. 2; AAA34689)"
FT /evidence="ECO:0000305"
FT CONFLICT 557..580
FT /note="FDIESNNDRKISEIPFDDEEEEET -> LISNLIMTAKFQKFLLMTKKKKKP
FT (in Ref. 2; AAA34689)"
FT /evidence="ECO:0000305"
FT CONFLICT 831
FT /note="A -> V (in Ref. 2; AAA34689)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 833 AA; 93282 MW; DE66A4DFC9BEEA1A CRC64;
MNNAANTGTT NESNVSDAPR IEPLPSLNDD DIEKILQPND IFTTDRTDAS TTSSTAIEDI
INPSLDPQSA ASPVPSSSFF HDSRKPSTST HLVRRGTPLG IYQTNLYGHN SRENTNPNST
LLSSKLLAHP PVPYGQNPDL LQHAVYRAQP SSGTTNAQPR QTTRRYQSHK SRPAFVNKLW
SMLNDDSNTK LIQWAEDGKS FIVTNREEFV HQILPKYFKH SNFASFVRQL NMYGWHKVQD
VKSGSIQSSS DDKWQFENEN FIRGREDLLE KIIRQKGSSN NHNSPSGNGN PANGSNIPLD
NAAGSNNSNN NISSSNSFFN NGHLLQGKTL RLMNEANLGD KNDVTAILGE LEQIKYNQIA
ISKDLLRINK DNELLWQENM MARERHRTQQ QALEKMFRFL TSIVPHLDPK MIMDGLGDPK
VNNEKLNSAN NIGLNRDNTG TIDELKSNDS FINDDRNSFT NATTNARNNM SPNNDDNSID
TASTNTTNRK KNIDENIKNN NDIINDIIFN TNLANNLSNY NSNNNAGSPI RPYKQRYLLK
NRANSSTSSE NPSLTPFDIE SNNDRKISEI PFDDEEEEET DFRPFTSRDP NNQTSENTFD
PNRFTMLSDD DLKKDSHTND NKHNESDLFW DNVHRNIDEQ DARLQNLENM VHILSPGYPN
KSFNNKTSST NTNSNMESAV NVNSPGFNLQ DYLTGESNSP NSVHSVPSNG SGSTPLPMPN
DNDTEHASTS VNQGENGSGL TPFLTVDDHT LNDNNTSEGS TRVSPDIKFS ATENTKVSDN
LPSFNDHSYS TQADTAPENA KKRFVEEIPE PAIVEIQDPT EYNDHRLPKR AKK
