ID   IES2_YEAST              Reviewed;         320 AA.
AC   P40154; D6W0X5;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 159.
DE   RecName: Full=Ino eighty subunit 2;
GN   Name=IES2; OrderedLocusNames=YNL215W; ORFNames=N1315;
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].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=7762305; DOI=10.1002/yea.320110111;
RA   Coster F., van Dyck L., Jonniaux J.-L., Purnelle B., Goffeau A.;
RT   "The sequence of a 13.5 kb DNA segment from the left arm of yeast
RT   chromosome XIV reveals MER1; RAP1; a new putative member of the DNA
RT   replication complex and a new putative serine/threonine phosphatase gene.";
RL   Yeast 11:85-91(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(1997).
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   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   [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   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   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67, 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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, AND IDENTIFICATION BY
RP   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 INO80 complex which remodels chromatin by
CC       shifting nucleosomes and is involved in DNA repair.
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 1470 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the IES2 family. {ECO:0000305}.
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; X78898; CAA55493.1; -; Genomic_DNA.
DR   EMBL; Z71491; CAA96117.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10341.1; -; Genomic_DNA.
DR   PIR; S50716; S50716.
DR   RefSeq; NP_014184.1; NM_001183053.1.
DR   PDB; 8ETS; EM; 3.04 A; Z=293-320.
DR   PDB; 8ETU; EM; 2.80 A; Z=293-320.
DR   PDB; 8ETW; EM; 2.64 A; Z=293-320.
DR   PDB; 8EU9; EM; 3.48 A; Z=293-320.
DR   PDB; 8EUF; EM; 3.41 A; Z=1-320.
DR   PDBsum; 8ETS; -.
DR   PDBsum; 8ETU; -.
DR   PDBsum; 8ETW; -.
DR   PDBsum; 8EU9; -.
DR   PDBsum; 8EUF; -.
DR   AlphaFoldDB; P40154; -.
DR   EMDB; EMD-28597; -.
DR   EMDB; EMD-28599; -.
DR   EMDB; EMD-28601; -.
DR   EMDB; EMD-28609; -.
DR   EMDB; EMD-28613; -.
DR   SMR; P40154; -.
DR   BioGRID; 35621; 364.
DR   ComplexPortal; CPX-863; INO80 chromatin remodeling complex.
DR   DIP; DIP-5062N; -.
DR   IntAct; P40154; 7.
DR   MINT; P40154; -.
DR   STRING; 4932.YNL215W; -.
DR   iPTMnet; P40154; -.
DR   MaxQB; P40154; -.
DR   PaxDb; 4932-YNL215W; -.
DR   PeptideAtlas; P40154; -.
DR   EnsemblFungi; YNL215W_mRNA; YNL215W; YNL215W.
DR   GeneID; 855506; -.
DR   KEGG; sce:YNL215W; -.
DR   AGR; SGD:S000005159; -.
DR   SGD; S000005159; IES2.
DR   VEuPathDB; FungiDB:YNL215W; -.
DR   eggNOG; ENOG502S7M7; Eukaryota.
DR   HOGENOM; CLU_066892_0_0_1; -.
DR   InParanoid; P40154; -.
DR   OMA; YEEDLFC; -.
DR   OrthoDB; 1978390at2759; -.
DR   BioCyc; YEAST:G3O-33221-MONOMER; -.
DR   BioGRID-ORCS; 855506; 1 hit in 10 CRISPR screens.
DR   PRO; PR:P40154; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P40154; Protein.
DR   GO; GO:0031011; C:Ino80 complex; IPI:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal.
DR   GO; GO:0006281; P:DNA repair; NAS:ComplexPortal.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; NAS:ComplexPortal.
DR   InterPro; IPR029523; INO80B/Ies2.
DR   InterPro; IPR006880; INO80B_C.
DR   PANTHER; PTHR21561; INO80 COMPLEX SUBUNIT B; 1.
DR   PANTHER; PTHR21561:SF12; INO80 COMPLEX SUBUNIT B; 1.
DR   Pfam; PF04795; PAPA-1; 1.
DR   SMART; SM01406; PAPA-1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chromatin regulator; DNA damage; DNA repair; DNA-binding;
KW   Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..320
FT                   /note="Ino eighty subunit 2"
FT                   /id="PRO_0000084154"
FT   REGION          1..232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          244..306
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        129..148
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        244..292
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         67
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18407956"
FT   MOD_RES         129
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
SQ   SEQUENCE   320 AA;  36154 MW;  6F0AA04387A3B3E8 CRC64;
     MDSEASDIEA ELSDSVSAGG EEYIDDDDYT EDIDDQIVTA KSSRRTARRS VPKGVRTSKR
     IRDKELSVEV DEDYDEEEDV LSPSKKRHLH TRSMDKRQVA ATASEKSDIG DSKGNDGEIE
     DGILEEEESL EKELNRGGGK EVEKSEESYY AQNDVGQKGE EEQDGESGGY EDNEPSISKE
     SDELVSVVNG NGNEEDDEVE ATKENTTDST RSTTTRSKML LDLLEDGGSK KKLTDEEIQL
     RRAENARKRK NLSEKRLEEE KQDTINKLLK KRAGKSRSHL PNDDEKNDGS SSFVKPRRPY
     NSEGMTRILR RYEEDLFCTF
//