ID   ASH1_YEAST              Reviewed;         588 AA.
AC   P34233; D6VX15;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   27-MAR-2024, entry version 183.
DE   RecName: Full=Transcriptional regulatory protein ASH1;
DE   AltName: Full=Daughter cells HO repressor protein;
GN   Name=ASH1; OrderedLocusNames=YKL185W;
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].
RX   PubMed=8154185; DOI=10.1002/yea.320091208;
RA   Wiemann S., Voss H., Schwager C., Rupp T., Stegemann J., Zimmermann J.,
RA   Grothues D., Sensen C., Erfle H., Hewitt N., Banrevi A., Ansorge W.;
RT   "Sequencing and analysis of 51.6 kilobases on the left arm of chromosome XI
RT   from Saccharomyces cerevisiae reveals 23 open reading frames including the
RT   FAS1 gene.";
RL   Yeast 9:1343-1348(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8196765; DOI=10.1038/369371a0;
RA   Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA   Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA   Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA   Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA   Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA   Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA   Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA   Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA   Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA   Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA   Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA   Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA   Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA   Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA   Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA   Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA   Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA   Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA   Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA   van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA   von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA   Becker I., Mewes H.-W.;
RT   "Complete DNA sequence of yeast chromosome XI.";
RL   Nature 369:371-378(1994).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 110-563.
RA   Cusick M.E.;
RL   Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=8625408; DOI=10.1016/s0092-8674(00)81048-x;
RA   Bobola N., Jansen R.-P., Shin T.H., Nasmyth K.;
RT   "Asymmetric accumulation of Ash1p in postanaphase nuclei depends on a
RT   myosin and restricts yeast mating-type switching to mother cells.";
RL   Cell 84:699-709(1996).
RN   [6]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=8625409; DOI=10.1016/s0092-8674(00)81049-1;
RA   Sil A., Herskowitz I.;
RT   "Identification of asymmetrically localized determinant, Ash1p, required
RT   for lineage-specific transcription of the yeast HO gene.";
RL   Cell 84:711-722(1996).
RN   [7]
RP   TRANSPORT AND ASYMMETRIC LOCATION OF MRNA.
RX   PubMed=9288973; DOI=10.1038/38015;
RA   Takizawa P.A., Sil A., Swedlow J.R., Herskowitz I., Vale R.D.;
RT   "Actin-dependent localization of an RNA encoding a cell-fate determinant in
RT   yeast.";
RL   Nature 389:90-93(1997).
RN   [8]
RP   TRANSPORT AND ASYMMETRIC LOCATION OF MRNA.
RX   PubMed=9219698; DOI=10.1126/science.277.5324.383;
RA   Long R.M., Singer R.H., Meng X., Gonzalez I., Nasmyth K., Jansen R.-P.;
RT   "Mating type switching in yeast controlled by asymmetric localization of
RT   ASH1 mRNA.";
RL   Science 277:383-387(1997).
RN   [9]
RP   SUBCELLULAR LOCATION, AND MRNA TRANSPORT.
RX   PubMed=9809065; DOI=10.1016/s1097-2765(00)80143-4;
RA   Bertrand E., Chartrand P., Schaefer M., Shenoy S.M., Singer R.H.,
RA   Long R.M.;
RT   "Localization of ASH1 mRNA particles in living yeast.";
RL   Mol. Cell 2:437-445(1998).
RN   [10]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=9566907; DOI=10.1128/mcb.18.5.2884;
RA   Chandarlapaty S., Errede B.;
RT   "Ash1, a daughter cell-specific protein, is required for pseudohyphal
RT   growth of Saccharomyces cerevisiae.";
RL   Mol. Cell. Biol. 18:2884-2891(1998).
RN   [11]
RP   FUNCTION, DOMAIN, AND DNA-BINDING.
RX   PubMed=11171979; DOI=10.1073/pnas.98.4.1495;
RA   Maxon M.E., Herskowitz I.;
RT   "Ash1p is a site-specific DNA-binding protein that actively represses
RT   transcription.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:1495-1500(2001).
RN   [12]
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   [13]
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   [14]
RP   IDENTIFICATION IN THE RPD3C(L) COMPLEX, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=16314178; DOI=10.1016/j.bbaexp.2005.09.005;
RA   Carrozza M.J., Florens L., Swanson S.K., Shia W.-J., Anderson S., Yates J.,
RA   Washburn M.P., Workman J.L.;
RT   "Stable incorporation of sequence specific repressors Ash1 and Ume6 into
RT   the Rpd3L complex.";
RL   Biochim. Biophys. Acta 1731:77-87(2005).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-465, 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   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56 AND SER-465, 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).
CC   -!- FUNCTION: Component of the RPD3C(L) histone deacetylase complex (HDAC).
CC       Responsible for the deacetylation of lysine residues on the N-terminal
CC       part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation
CC       gives a tag for epigenetic repression and plays an important role in
CC       transcriptional regulation, cell cycle progression and developmental
CC       events. ASH1 is necessary to repress HO in daughter cells to block
CC       mating-type switching through its binding to HO promoter 5'-YTGAT-3'
CC       sites. Also involved in pseudohyphal growth.
CC       {ECO:0000269|PubMed:11171979, ECO:0000269|PubMed:8625408,
CC       ECO:0000269|PubMed:8625409, ECO:0000269|PubMed:9566907}.
CC   -!- SUBUNIT: Component of the RPD3C(L) complex composed of at least ASH1,
CC       CTI6, DEP1, PHO23, RPD3, RXT2, RXT3, SAP30, SDS3, SIN3, UME1 and UME6.
CC       {ECO:0000269|PubMed:16314178}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095,
CC       ECO:0000269|PubMed:8625408, ECO:0000269|PubMed:8625409,
CC       ECO:0000269|PubMed:9566907, ECO:0000269|PubMed:9809065}.
CC       Note=Preferentially accumulates in daughter cell nuclei at the end of
CC       anaphase.
CC   -!- MISCELLANEOUS: The ASH1 mRNA is transported to the daughter cell before
CC       cytokinesis where translation produces the protein to block mating-type
CC       switching. The ASH1 mRNA 3'-UTR and the mRNA localization machinery
CC       that are essential to restrict accumulation to the bud.
CC   -!- MISCELLANEOUS: Present with 1800 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; X74151; CAA52253.1; -; Genomic_DNA.
DR   EMBL; Z28185; CAA82028.1; -; Genomic_DNA.
DR   EMBL; M88605; AAA34830.1; -; Genomic_DNA.
DR   EMBL; BK006944; DAA08981.1; -; Genomic_DNA.
DR   PIR; S34685; S34685.
DR   RefSeq; NP_012736.1; NM_001179751.1.
DR   AlphaFoldDB; P34233; -.
DR   BioGRID; 33937; 168.
DR   DIP; DIP-8053N; -.
DR   IntAct; P34233; 9.
DR   MINT; P34233; -.
DR   STRING; 4932.YKL185W; -.
DR   iPTMnet; P34233; -.
DR   MaxQB; P34233; -.
DR   PaxDb; 4932-YKL185W; -.
DR   PeptideAtlas; P34233; -.
DR   EnsemblFungi; YKL185W_mRNA; YKL185W; YKL185W.
DR   GeneID; 853650; -.
DR   KEGG; sce:YKL185W; -.
DR   AGR; SGD:S000001668; -.
DR   SGD; S000001668; ASH1.
DR   VEuPathDB; FungiDB:YKL185W; -.
DR   eggNOG; ENOG502QX5C; Eukaryota.
DR   HOGENOM; CLU_041192_0_0_1; -.
DR   InParanoid; P34233; -.
DR   OMA; SDSPCWR; -.
DR   OrthoDB; 3616433at2759; -.
DR   BioCyc; YEAST:G3O-31948-MONOMER; -.
DR   BioGRID-ORCS; 853650; 0 hits in 13 CRISPR screens.
DR   PRO; PR:P34233; -.
DR   Proteomes; UP000002311; Chromosome XI.
DR   RNAct; P34233; Protein.
DR   GO; GO:0005933; C:cellular bud; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0033698; C:Rpd3L complex; IDA:SGD.
DR   GO; GO:0070210; C:Rpd3L-Expanded complex; HDA:SGD.
DR   GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:SGD.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:SGD.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR   GO; GO:1900461; P:positive regulation of pseudohyphal growth by positive regulation of transcription from RNA polymerase II promoter; IMP:SGD.
DR   CDD; cd00202; ZnF_GATA; 1.
DR   DisProt; DP01579; -.
DR   Gene3D; 3.30.50.10; Erythroid Transcription Factor GATA-1, subunit A; 1.
DR   InterPro; IPR000679; Znf_GATA.
DR   InterPro; IPR013088; Znf_NHR/GATA.
DR   Pfam; PF00320; GATA; 1.
DR   SMART; SM00401; ZnF_GATA; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR   PROSITE; PS00344; GATA_ZN_FINGER_1; 1.
DR   PROSITE; PS50114; GATA_ZN_FINGER_2; 1.
PE   1: Evidence at protein level;
KW   Chromatin regulator; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repressor; Transcription; Transcription regulation;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..588
FT                   /note="Transcriptional regulatory protein ASH1"
FT                   /id="PRO_0000083492"
FT   ZN_FING         499..526
FT                   /note="GATA-type; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00094"
FT   REGION          85..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          377..398
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          417..495
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        417..448
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        467..495
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         56
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         465
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956,
FT                   ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   588 AA;  65685 MW;  7DFFD1B9392DAC08 CRC64;
     MSSLYIKTPL HALSAGPDSH ANSSYYDNLL LPSFSNLSSN ISRNNITTDN NINSASPRKY
     SFHSLNVSPI LSPISLANEI LGKKSNTAPA SPHHMDYNPI SSLTPGNSPE FNKASLSQIS
     FTNPLNYGSG LGFSSNSQPR LPLLDRLSSV SLSKRPERPQ QSLPSLRHLQ LLPSPLLQEN
     AARFPDTSKR TSNWKTDLTH WCKDTNYQDY VKIREEVAHF KPLSIPNLTN NQNNDSFNYG
     KELESTRSSK FHSPSKESFD RTKLIPSILE AKDQFKDLSN NAWSITPPVT PPMSPPTNRT
     MERTTLRGVE ASFFEGKSSN NDSIFNPIIS EKLVQEVKHQ RQLRGNSFPM PNASHKKTNS
     FKALQIKKLL ANRDILSNNS KSNVRKPSKN KISKQASNVF GNTARQLVMK LDNASYSSVS
     ASSSPSPSTP TKSGKMRSRS SSPVRPKAYT PSPRSPNYHR FALDSPPQSP RRSSNSSITK
     KGSRRSSGSS PTRHTTRVCV SCHSSDSPCW RPSWSPRKQD QLCNSCGLRY KKTHTRCLND
     LCRKIPTKGE INIMKSNGID KEFVPERNCE IEGYRCLFCN YITETVEN
//