IES1_YEAST
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 03-AUG-2022, entry version 155.
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=4; 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}.
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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; 502.
DR ComplexPortal; CPX-863; INO80 chromatin remodeling complex.
DR DIP; DIP-3869N; -.
DR IntAct; P43579; 19.
DR MINT; P43579; -.
DR STRING; 4932.YFL013C; -.
DR iPTMnet; P43579; -.
DR MaxQB; P43579; -.
DR PaxDb; P43579; -.
DR PRIDE; P43579; -.
DR EnsemblFungi; YFL013C_mRNA; YFL013C; YFL013C.
DR GeneID; 850534; -.
DR KEGG; sce:YFL013C; -.
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 BioCyc; YEAST:G3O-30443-MON; -.
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; IC:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR InterPro; IPR038014; Ies1.
DR PANTHER; PTHR37287; PTHR37287; 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..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 25..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..493
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..532
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
