ID   IES1_YEAST              Reviewed;         692 AA.
AC   P43579; D6VTL6; E9P952;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   02-SEP-2026, entry version 170.
DE   RecName: Full=Ino eighty subunit 1;
GN   Name=IES1; OrderedLocusNames=YFL013C;
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=7670463; DOI=10.1038/ng0795-261;
RA   Murakami Y., Naitou M., Hagiwara H., Shibata T., Ozawa M., Sasanuma S.,
RA   Sasanuma M., Tsuchiya Y., Soeda E., Yokoyama K., Yamazaki M., Tashiro H.,
RA   Eki T.;
RT   "Analysis of the nucleotide sequence of chromosome VI from Saccharomyces
RT   cerevisiae.";
RL   Nat. Genet. 10:261-268(1995).
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   PARTIAL PROTEIN SEQUENCE, AND IDENTIFICATION IN THE INO80 COMPLEX.
RX   PubMed=12887900; DOI=10.1016/s1097-2765(03)00264-8;
RA   Shen X., Ranallo R., Choi E., Wu C.;
RT   "Involvement of actin-related proteins in ATP-dependent chromatin
RT   remodeling.";
RL   Mol. Cell 12:147-155(2003).
RN   [5]
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   [6]
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   [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   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-27; SER-487; SER-493; SER-504
RP   AND THR-507, 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).
CC   -!- FUNCTION: Probably involved in transcription regulation via its
CC       interaction with the INO80 complex, a chromatin-remodeling complex.
CC   -!- SUBUNIT: Component of the chromatin-remodeling INO80 complex, at least
CC       composed of ARP4, ARP5, ARP8, RVB1, RVB2, TAF14, NHP10, IES1, IES3,
CC       IES4, IES6, ACT1, IES2, IES5 and INO80. {ECO:0000269|PubMed:12887900}.
CC   -!- INTERACTION:
CC       P43579; Q03435: NHP10; NbExp=5; IntAct=EBI-22775, EBI-12010;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 1400 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; D50617; BAA09225.1; -; Genomic_DNA.
DR   EMBL; Z46255; CAA86347.1; -; Genomic_DNA.
DR   EMBL; AY723802; AAU09719.1; -; Genomic_DNA.
DR   EMBL; BK006940; DAA12426.1; -; Genomic_DNA.
DR   PIR; S48316; S48316.
DR   RefSeq; NP_116641.1; NM_001179953.1.
DR   AlphaFoldDB; P43579; -.
DR   BioGRID; 31133; 511.
DR   ComplexPortal; CPX-863; INO80 chromatin remodeling complex.
DR   DIP; DIP-3869N; -.
DR   FunCoup; P43579; 272.
DR   IntAct; P43579; 28.
DR   MINT; P43579; -.
DR   STRING; 4932.YFL013C; -.
DR   iPTMnet; P43579; -.
DR   PaxDb; 4932-YFL013C; -.
DR   PeptideAtlas; P43579; -.
DR   EnsemblFungi; YFL013C_mRNA; YFL013C; YFL013C.
DR   GeneID; 850534; -.
DR   KEGG; sce:YFL013C; -.
DR   AGR; SGD:S000001881; -.
DR   SGD; S000001881; IES1.
DR   VEuPathDB; FungiDB:YFL013C; -.
DR   eggNOG; ENOG502QVDM; Eukaryota.
DR   HOGENOM; CLU_409922_0_0_1; -.
DR   InParanoid; P43579; -.
DR   OMA; VYDPIHD; -.
DR   OrthoDB; 5413003at2759; -.
DR   BioCyc; YEAST:G3O-30443-MONOMER; -.
DR   BioGRID-ORCS; 850534; 0 hits in 10 CRISPR screens.
DR   PRO; PR:P43579; -.
DR   Proteomes; UP000002311; Chromosome VI.
DR   RNAct; P43579; protein.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0031011; C:Ino80 complex; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0006338; P:chromatin remodeling; IDA:SGD.
DR   GO; GO:0006281; P:DNA repair; NAS:ComplexPortal.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; NAS:ComplexPortal.
DR   InterPro; IPR038014; Ies1.
DR   InterPro; IPR060627; Ies1_C.
DR   InterPro; IPR060628; Ies1_helical.
DR   InterPro; IPR060625; IES1_N.
DR   PANTHER; PTHR37287; INO EIGHTY SUBUNIT 1; 1.
DR   PANTHER; PTHR37287:SF1; INO EIGHTY SUBUNIT 1; 1.
DR   Pfam; PF27816; Ies1_C; 1.
DR   Pfam; PF27817; Ies1_helical; 1.
DR   Pfam; PF27809; IES1_N; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Direct protein sequencing; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..692
FT                   /note="Ino eighty subunit 1"
FT                   /id="PRO_0000084153"
FT   REGION          1..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          465..550
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          340..385
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..25
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..80
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..109
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        465..485
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        493..504
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        513..528
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         27
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         487
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         493
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         504
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         507
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   CONFLICT        219
FT                   /note="D -> G (in Ref. 3; AAU09719)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   692 AA;  78753 MW;  9C0084A36431B241 CRC64;
     MGKRVYDPIH DTFQLREDNS DETKADSPMQ SVKSGSQEEA SPSSIQSETE TVTTKSIPVI
     HEIEIDDKND DDSTQSEEEN TNILLNFEPS TVPEATGAST ATGPVTTNTV RRKPKESNAS
     KYNRHLKKPD GEPFNRKDIQ FSFMQELLMD KRQIFTNVLK PLYKNSIVPI NIDGDKLSIN
     VTDKEYDART FVFNDKLTFA QLYVLTIATS IKCSKILRDK LLLDQQVAFS TCVLALLVNI
     GRLNTTINFY LEMTSQLRTF HSVPVLQLHA NDPKLLQDTP RLKSILKNLP WGNEQLSLME
     TYKKVDQNDG EVDTVNKFNI INMLFSICDN SGLIDKRFLS KYVEVESKAQ EQDMVDEQNE
     VKETEAENEK QESKAAYATT LFDILDYSKY EPKDRSNILI WLLYIHLETN LSQEEVEESV
     RFFNGLEDGA PAGKFILRCT ERSYDTDPED ELEFGANQRI KRREFMSKME EGRKRERTNV
     TEVKKPSIGG DKSEEDGEGE DDKSEETVEE TRSLLTPTPI LESSSPMTLN RKKVTPQLPK
     VTPAAPTETE EEITSAAIID KNDLNLTPLK KYNSSATVNK VDKLISLDLN KHVSENGKTQ
     EEFLADLKKS QVPNRLKRRD IGLIKIFNEF EDIPVASVLG IRGKKRKKFK DNLLGFETDF
     MKNLGASKKV LLNKIERAEI DDEEATAMFK LE
//