HFI1_YEAST
ID HFI1_YEAST Reviewed; 488 AA.
AC Q12060; D6W3B7; O00039; Q02813;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Transcriptional coactivator HFI1/ADA1;
GN Name=HFI1; Synonyms=ADA1, SUP110; OrderedLocusNames=YPL254W;
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], AND IDENTIFICATION IN THE ADA/GCN5
RP COMPLEX.
RC STRAIN=ATCC MYA-3516 / BWG1-7A;
RX PubMed=9154821; DOI=10.1128/mcb.17.6.3220;
RA Horiuchi J., Silverman N., Pina B., Marcus G.A., Guarente L.;
RT "ADA1, a novel component of the ADA/GCN5 complex, has broader effects than
RT GCN5, ADA2, or ADA3.";
RL Mol. Cell. Biol. 17:3220-3228(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Brown N.G.;
RL Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [4]
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 [5]
RP IDENTIFICATION IN THE SAGA COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=9674426; DOI=10.1016/s0092-8674(00)81220-9;
RA Grant P.A., Schieltz D., Pray-Grant M.G., Steger D.J., Reese J.C.,
RA Yates J.R. III, Workman J.L.;
RT "A subset of TAF(II)s are integral components of the SAGA complex required
RT for nucleosome acetylation and transcriptional stimulation.";
RL Cell 94:45-53(1998).
RN [6]
RP IDENTIFICATION IN A SAGA COMPLEX WITH SPT2; SPT7; SPT8; GCN5; SPT20; ADA2;
RP ADA3 AND TRA1.
RX PubMed=9885573; DOI=10.1016/s1097-2765(00)80300-7;
RA Grant P.A., Schieltz D., Pray-Grant M.G., Yates J.R. III, Workman J.L.;
RT "The ATM-related cofactor Tra1 is a component of the purified SAGA
RT complex.";
RL Mol. Cell 2:863-867(1998).
RN [7]
RP FUNCTION IN HISTONE ACETYLATION AT THE SAGA COMPLEX.
RX PubMed=10026213; DOI=10.1074/jbc.274.9.5895;
RA Grant P.A., Eberharter A., John S., Cook R.G., Turner B.M., Workman J.L.;
RT "Expanded lysine acetylation specificity of Gcn5 in native complexes.";
RL J. Biol. Chem. 274:5895-5900(1999).
RN [8]
RP IDENTIFICATION IN THE SLIK COMPLEX.
RX PubMed=12446794; DOI=10.1128/mcb.22.24.8774-8786.2002;
RA Pray-Grant M.G., Schieltz D., McMahon S.J., Wood J.M., Kennedy E.L.,
RA Cook R.G., Workman J.L., Yates J.R. III, Grant P.A.;
RT "The novel SLIK histone acetyltransferase complex functions in the yeast
RT retrograde response pathway.";
RL Mol. Cell. Biol. 22:8774-8786(2002).
RN [9]
RP IDENTIFICATION IN THE SALSA COMPLEX.
RX PubMed=12186975; DOI=10.1073/pnas.182021199;
RA Sterner D.E., Belotserkovskaya R., Berger S.L.;
RT "SALSA, a variant of yeast SAGA, contains truncated Spt7, which correlates
RT with activated transcription.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:11622-11627(2002).
RN [10]
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 [11]
RP IDENTIFICATION IN THE SLIK COMPLEX.
RX PubMed=15647753; DOI=10.1038/nature03242;
RA Pray-Grant M.G., Daniel J.A., Schieltz D., Yates J.R. III, Grant P.A.;
RT "Chd1 chromodomain links histone H3 methylation with SAGA- and SLIK-
RT dependent acetylation.";
RL Nature 433:434-438(2005).
RN [12]
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 [13]
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 [14]
RP 3D-STRUCTURE MODELING OF THE SAGA COMPLEX.
RX PubMed=15260971; DOI=10.1016/j.molcel.2004.06.005;
RA Wu P.Y., Ruhlmann C., Winston F., Schultz P.;
RT "Molecular architecture of the S. cerevisiae SAGA complex.";
RL Mol. Cell 15:199-208(2004).
CC -!- FUNCTION: Functions as component of the transcription regulatory
CC histone acetylation (HAT) complexes SAGA, SALSA and SLIK. SAGA is
CC involved in RNA polymerase II-dependent transcriptional regulation of
CC approximately 10% of yeast genes. At the promoters, SAGA is required
CC for recruitment of the basal transcription machinery. It influences RNA
CC polymerase II transcriptional activity through different activities
CC such as TBP interaction (SPT3, SPT8 and SPT20) and promoter
CC selectivity, interaction with transcription activators (GCN5, ADA2,
CC ADA3 and TRA1), and chromatin modification through histone acetylation
CC (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone
CC H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA
CC interacts with DNA via upstream activating sequences (UASs). SALSA, an
CC altered form of SAGA, may be involved in positive transcriptional
CC regulation. SLIK is proposed to have partly overlapping functions with
CC SAGA. It preferentially acetylates methylated histone H3, at least
CC after activation at the GAL1-10 locus. HFI1/ADA1 and SPT20/ADA5 may
CC recruit TATA binding protein (TBP) and possibly other basal factors to
CC bind to the TATA box. {ECO:0000269|PubMed:10026213}.
CC -!- SUBUNIT: Component of the 1.8 MDa SAGA complex, which consists of at
CC least TRA1, CHD1, SPT7, TAF5, ADA3, SGF73, SPT20/ADA5, SPT8, TAF12,
CC TAF6, HFI1/ADA1, UBP8, GCN5, ADA2, SPT3, SGF29, TAF10, TAF9, SGF11 and
CC SUS1. TAF5, TAF6, TAF9, TAF19, TAF12 and ADA1 seem to be present in 2
CC copies. SAGA is built of 5 distinct domains with specialized functions.
CC Domain I (containing TRA1) probably represents the activator
CC interaction surface. Domain II (containing TAF5 and TAF6, and probably
CC TAF9 and TAF10), domain III (containing GCN5, TAF10, SPT7, TAF5 and
CC ADA1, and probably ADA2, ADA3 and TAF12), and domain IV (containing
CC HFI1/ADA1 and TAF6, and probably TAF9) are believed to play primarily
CC an architectural role. Domain III also harbors the HAT activity. Domain
CC V (containing SPT3 and SPT20, and probably SPT8) represents the TBP-
CC interacting module, which may be associated transiently with SAGA.
CC Component of the SALSA complex, which consists of at least TRA1, SPT7
CC (C-terminal truncated form), TAF5, ADA3, SPT20, TAF12, TAF6, HFI1,
CC GCN5, ADA2 and SPT3. Component of the SLIK complex, which consists of
CC at least TRA1, CHD1, SPT7, TAF5, ADA3, SPT20, RTG2, TAF12, TAF6, HFI1,
CC UBP8, GCN5, ADA2, SPT3, SGF29, TAF10 and TAF9. Component of the
CC ADA/GCN5 complex, that consists of HFI1/ADA1, ADA2, ADA3, SPT20/ADA5
CC and GCN5 and is probably a subcomplex of SAGA.
CC {ECO:0000269|PubMed:12186975, ECO:0000269|PubMed:12446794,
CC ECO:0000269|PubMed:15647753, ECO:0000269|PubMed:9154821,
CC ECO:0000269|PubMed:9674426, ECO:0000269|PubMed:9885573}.
CC -!- INTERACTION:
CC Q12060; Q02336: ADA2; NbExp=25; IntAct=EBI-8287, EBI-2186;
CC Q12060; Q03330: GCN5; NbExp=21; IntAct=EBI-8287, EBI-7458;
CC Q12060; P32494: NGG1; NbExp=5; IntAct=EBI-8287, EBI-2192;
CC Q12060; P25554: SGF29; NbExp=9; IntAct=EBI-8287, EBI-21678;
CC Q12060; P50875: SPT20; NbExp=13; IntAct=EBI-8287, EBI-17751;
CC Q12060; P06844: SPT3; NbExp=9; IntAct=EBI-8287, EBI-17921;
CC Q12060; P35177: SPT7; NbExp=15; IntAct=EBI-8287, EBI-17958;
CC Q12060; P38915: SPT8; NbExp=14; IntAct=EBI-8287, EBI-17964;
CC Q12060; Q12030: TAF10; NbExp=7; IntAct=EBI-8287, EBI-18889;
CC Q12060; Q03761: TAF12; NbExp=10; IntAct=EBI-8287, EBI-35097;
CC Q12060; P38129: TAF5; NbExp=15; IntAct=EBI-8287, EBI-18868;
CC Q12060; P53040: TAF6; NbExp=9; IntAct=EBI-8287, EBI-18876;
CC Q12060; P38811: TRA1; NbExp=8; IntAct=EBI-8287, EBI-24638;
CC Q12060; P50102: UBP8; NbExp=9; IntAct=EBI-8287, EBI-19863;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 7950 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U76735; AAB58359.1; -; Genomic_DNA.
DR EMBL; U41324; AAA84983.1; -; Genomic_DNA.
DR EMBL; Z67751; CAA91590.1; -; Genomic_DNA.
DR EMBL; Z73610; CAA97979.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11183.1; -; Genomic_DNA.
DR PIR; S61010; S61010.
DR RefSeq; NP_015069.1; NM_001184068.1.
DR PDB; 6T9I; EM; 3.90 A; H=1-488.
DR PDB; 6T9K; EM; 3.30 A; H=1-488.
DR PDBsum; 6T9I; -.
DR PDBsum; 6T9K; -.
DR AlphaFoldDB; Q12060; -.
DR SMR; Q12060; -.
DR BioGRID; 35909; 220.
DR ComplexPortal; CPX-656; SAGA complex.
DR ComplexPortal; CPX-675; SLIK (SAGA-like) complex.
DR DIP; DIP-955N; -.
DR IntAct; Q12060; 100.
DR MINT; Q12060; -.
DR STRING; 4932.YPL254W; -.
DR iPTMnet; Q12060; -.
DR MaxQB; Q12060; -.
DR PaxDb; Q12060; -.
DR PRIDE; Q12060; -.
DR EnsemblFungi; YPL254W_mRNA; YPL254W; YPL254W.
DR GeneID; 855821; -.
DR KEGG; sce:YPL254W; -.
DR SGD; S000006175; HFI1.
DR VEuPathDB; FungiDB:YPL254W; -.
DR eggNOG; ENOG502RX84; Eukaryota.
DR GeneTree; ENSGT00390000011644; -.
DR HOGENOM; CLU_033254_1_0_1; -.
DR InParanoid; Q12060; -.
DR OMA; YKKIVMS; -.
DR BioCyc; YEAST:G3O-34139-MON; -.
DR PRO; PR:Q12060; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12060; protein.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0000124; C:SAGA complex; IDA:SGD.
DR GO; GO:0046695; C:SLIK (SAGA-like) complex; IDA:SGD.
DR GO; GO:0003713; F:transcription coactivator activity; IMP:SGD.
DR GO; GO:0003712; F:transcription coregulator activity; IMP:SGD.
DR GO; GO:0006325; P:chromatin organization; IDA:SGD.
DR GO; GO:0016573; P:histone acetylation; IDA:SGD.
DR GO; GO:0016578; P:histone deubiquitination; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:SGD.
DR InterPro; IPR024738; Hfi1/Tada1.
DR PANTHER; PTHR21277; PTHR21277; 1.
DR Pfam; PF12767; SAGA-Tad1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..488
FT /note="Transcriptional coactivator HFI1/ADA1"
FT /id="PRO_0000083959"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 19
FT /note="A -> V (in Ref. 2; AAA84983)"
FT /evidence="ECO:0000305"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:6T9K"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 192..198
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 212..220
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 230..238
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 244..255
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 260..263
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 269..283
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 293..316
FT /evidence="ECO:0007829|PDB:6T9K"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:6T9K"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 341..348
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 357..364
FT /evidence="ECO:0007829|PDB:6T9K"
FT TURN 384..386
FT /evidence="ECO:0007829|PDB:6T9K"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:6T9K"
FT HELIX 408..417
FT /evidence="ECO:0007829|PDB:6T9K"
SQ SEQUENCE 488 AA; 54466 MW; B3ACF3C6101AB541 CRC64;
MSAIQSPAPK PLQPTYPAAS PASTNAYMKP GLIGSPAVSN HTEPNNGNNE TAEPQGPNQR
IDLGAMIEEL TSLLGKESWT KYAQIISLFI LGKLSRKELS NELELVFSPS AASLEKSNTN
HHHSLVRLHN QLLLGIFANS LRENPLGRNG NESSWGFGNG SNNPNNKLKR INKHNSQIEV
YKKIVMSLPL NDRNRLKMIT KEAGKRGFIF CSVFQARLNN IPKIPIVTNP ESLKRVKSNN
LKTPLEWSQD IMNGFNVPLA SESHSLPDTD SFYLRMVGIA REHGLVGTVD ARCVELISLA
LDQYLKNIIE FTIDTVRYRR KKYSDYYDLN ESGLYKSVSE MAADKRDAKI KQLDDDKNED
ECADEAKSIN NGNNSSKDDI GDISMSSITK AGEAVNEELH ENRTISLTNE DIYDSLSIFP
NLVEPSGSYY ALTNLGLVND DELVDMKSNI DDLPDFLNEK PTFTPLDERN VGTRHELNWL
IKGILTED
