ID   HAA1_YEAST              Reviewed;         694 AA.
AC   Q12753; D6W419;
DT   16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 177.
DE   RecName: Full=Transcriptional activator HAA1;
GN   Name=HAA1; OrderedLocusNames=YPR008W;
GN   ORFNames=LPZ8W, YP9531.01, YP9723.08;
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=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   [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   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=11504737; DOI=10.1074/jbc.m107131200;
RA   Keller G., Ray E., Brown P.O., Winge D.R.;
RT   "Haa1, a protein homologous to the copper-regulated transcription factor
RT   ace1, is a novel transcriptional activator.";
RL   J. Biol. Chem. 276:38697-38702(2001).
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-241, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=YAL6B;
RX   PubMed=15665377; DOI=10.1074/mcp.m400219-mcp200;
RA   Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M.,
RA   Jensen O.N.;
RT   "Quantitative phosphoproteomics applied to the yeast pheromone signaling
RT   pathway.";
RL   Mol. Cell. Proteomics 4:310-327(2005).
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-125 AND SER-241, 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 SER-231 AND SER-291, 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   [10]
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: Regulates the transcription of a set of genes, many of which
CC       encode membrane proteins. Among the genes regulated are YGR138C and
CC       YRO2. Does not seem to be dependent on copper.
CC       {ECO:0000269|PubMed:11504737}.
CC   -!- INTERACTION:
CC       Q12753; P11710: FUS1; NbExp=3; IntAct=EBI-8118, EBI-7179;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11504737}.
CC   -!- MISCELLANEOUS: Present with 339 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U31900; AAA97587.1; -; Genomic_DNA.
DR   EMBL; Z71255; CAA95048.1; -; Genomic_DNA.
DR   EMBL; Z48951; CAA88786.1; -; Genomic_DNA.
DR   EMBL; Z49919; CAA90152.1; -; Genomic_DNA.
DR   EMBL; AY692804; AAT92823.1; -; Genomic_DNA.
DR   EMBL; BK006949; DAA11435.1; -; Genomic_DNA.
DR   PIR; S59753; S59753.
DR   RefSeq; NP_015333.1; NM_001184105.1.
DR   AlphaFoldDB; Q12753; -.
DR   SMR; Q12753; -.
DR   BioGRID; 36186; 101.
DR   DIP; DIP-1462N; -.
DR   IntAct; Q12753; 8.
DR   MINT; Q12753; -.
DR   STRING; 4932.YPR008W; -.
DR   iPTMnet; Q12753; -.
DR   MaxQB; Q12753; -.
DR   PaxDb; 4932-YPR008W; -.
DR   PeptideAtlas; Q12753; -.
DR   EnsemblFungi; YPR008W_mRNA; YPR008W; YPR008W.
DR   GeneID; 856117; -.
DR   KEGG; sce:YPR008W; -.
DR   AGR; SGD:S000006212; -.
DR   SGD; S000006212; HAA1.
DR   VEuPathDB; FungiDB:YPR008W; -.
DR   eggNOG; ENOG502S7CA; Eukaryota.
DR   GeneTree; ENSGT00940000176728; -.
DR   HOGENOM; CLU_022338_0_0_1; -.
DR   InParanoid; Q12753; -.
DR   OMA; HHPANEY; -.
DR   OrthoDB; 2734923at2759; -.
DR   BioCyc; YEAST:G3O-34170-MONOMER; -.
DR   BioGRID-ORCS; 856117; 1 hit in 13 CRISPR screens.
DR   PRO; PR:Q12753; -.
DR   Proteomes; UP000002311; Chromosome XVI.
DR   RNAct; Q12753; Protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0005507; F:copper ion binding; IBA:GO_Central.
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:0006878; P:intracellular copper ion homeostasis; IBA:GO_Central.
DR   GO; GO:0006879; P:intracellular iron ion homeostasis; IBA:GO_Central.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:SGD.
DR   Gene3D; 3.90.430.10; Copper fist DNA-binding domain; 1.
DR   InterPro; IPR001083; Cu_fist_DNA-bd_dom.
DR   InterPro; IPR036395; Cu_fist_DNA-bd_dom_sf.
DR   PANTHER; PTHR28088; TRANSCRIPTIONAL ACTIVATOR HAA1-RELATED; 1.
DR   PANTHER; PTHR28088:SF5; TRANSCRIPTIONAL ACTIVATOR HAA1-RELATED; 1.
DR   Pfam; PF00649; Copper-fist; 1.
DR   PRINTS; PR00617; COPPERFIST.
DR   SMART; SM01090; Copper-fist; 1.
DR   SMART; SM00412; Cu_FIST; 1.
DR   SUPFAM; SSF57879; Zinc domain conserved in yeast copper-regulated transcription factors; 1.
DR   PROSITE; PS01119; COPPER_FIST_1; 1.
DR   PROSITE; PS50073; COPPER_FIST_2; 1.
PE   1: Evidence at protein level;
KW   Activator; Copper; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation; Zinc.
FT   CHAIN           1..694
FT                   /note="Transcriptional activator HAA1"
FT                   /id="PRO_0000194933"
FT   DNA_BIND        1..40
FT                   /note="Copper-fist"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00055"
FT   REGION          104..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          209..240
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          332..388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          479..514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          566..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          650..677
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        566..584
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         11
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00055"
FT   BINDING         14
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00055"
FT   BINDING         23
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00055"
FT   BINDING         25
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00055"
FT   MOD_RES         125
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         231
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         241
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:15665377,
FT                   ECO:0007744|PubMed:18407956"
FT   MOD_RES         291
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   694 AA;  76671 MW;  0A129F79B4E99CA8 CRC64;
     MVLINGIKYA CERCIRGHRV TTCNHTDQPL MMIKPKGRPS TTCDYCKQLR KNKNANPEGV
     CTCGRLEKKK LAQKAKEEAR AKAKEKQRKQ CTCGTDEVCK YHAQKRHLRK SPSSSQKKGR
     SISRSQPMFE RVLSSTSLDS NMLSGHGALS DTSSILTSTF LDSEPGVGKI SKDYHHVPSL
     ASISSLQSSQ SLDQNFSIPQ SPPLSSMSFN FLTGNINETN QNHSNHQHSK SGNNWQDSSV
     SLPAKADSRL NMMDKNNSVG LDLLGHSKRI SPISNSRVGE VSVPLEEYIP SDIDGVGRVT
     DKSSLVYDWP FDESIERNFS TTATAATGES KFDINDNCNR INSKSYSKTN SMNGNGMNNS
     NNNNINSNGN DKNNNNSSRQ EHQGNGLFDM FTDSSSISTL SRANLLLQEK IGSQENSVKQ
     ENYSKNPQLR HQLTSRSRSF IHHPANEYLK NTFGNSHSND IGKGVEVLSL TPSFMDIPEK
     ERETERSPSS NYITDRPFTR KPRSSSIDVN HRYPPMAPTT VATSPGALNN AVASNLDDQL
     SLTSLNSQPS SIANMMMDPS NLAEQSSIHS VPQSINSPRM PKTGSRQDKN IHTKKEERNP
     LNNIHDLSQL ENVPDEMNQM FSPPLKSMNR PDAIRENSSS SNFIIQGNSM ISTPSGRNDL
     PDTSPMSSIQ TASPPSQLLT DQGFADLDNF MSSL
//