IOC2_YEAST
ID IOC2_YEAST Reviewed; 812 AA.
AC Q12072; D6VY95;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=ISWI one complex protein 2;
GN Name=IOC2; OrderedLocusNames=YLR095C;
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=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(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 FUNCTION OF THE ISW1B COMPLEX.
RX PubMed=14622597; DOI=10.1016/s0092-8674(03)00880-8;
RA Morillon A., Karabetsou N., O'Sullivan J., Kent N., Proudfoot N.,
RA Mellor J.;
RT "Isw1 chromatin remodeling ATPase coordinates transcription elongation and
RT termination by RNA polymerase II.";
RL Cell 115:425-435(2003).
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 ISW1B COMPLEX, AND FUNCTION OF THE ISW1B COMPLEX.
RX PubMed=12482963; DOI=10.1128/mcb.23.1.80-91.2003;
RA Vary J.C. Jr., Gangaraju V.K., Qin J., Landel C.C., Kooperberg C.,
RA Bartholomew B., Tsukiyama T.;
RT "Yeast Isw1p forms two separable complexes in vivo.";
RL Mol. Cell. Biol. 23:80-91(2003).
RN [7]
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 [8]
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: Functions as component of the ISW1B complex, which acts in
CC remodeling the chromatin by catalyzing an ATP-dependent alteration in
CC the structure of nucleosomal DNA. The ISW1B complex acts within coding
CC regions to control the amount of RNA polymerase II released into
CC productive elongation and to coordinate elongation with termination and
CC pre-mRNA processing. {ECO:0000269|PubMed:12482963,
CC ECO:0000269|PubMed:14622597}.
CC -!- SUBUNIT: Component of the ISW1B complex, which at least consists of
CC ISW1, IOC2 and IOC4. {ECO:0000269|PubMed:12482963}.
CC -!- INTERACTION:
CC Q12072; P38144: ISW1; NbExp=6; IntAct=EBI-30191, EBI-21087;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 7520 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z73267; CAA97657.1; -; Genomic_DNA.
DR EMBL; U53876; AAB67539.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09411.1; -; Genomic_DNA.
DR PIR; S64929; S64929.
DR RefSeq; NP_013196.1; NM_001181982.1.
DR AlphaFoldDB; Q12072; -.
DR SMR; Q12072; -.
DR BioGRID; 31368; 112.
DR ComplexPortal; CPX-636; ISW1b chromatin remodeling complex.
DR DIP; DIP-5201N; -.
DR IntAct; Q12072; 18.
DR MINT; Q12072; -.
DR STRING; 4932.YLR095C; -.
DR iPTMnet; Q12072; -.
DR MaxQB; Q12072; -.
DR PaxDb; Q12072; -.
DR PRIDE; Q12072; -.
DR EnsemblFungi; YLR095C_mRNA; YLR095C; YLR095C.
DR GeneID; 850784; -.
DR KEGG; sce:YLR095C; -.
DR SGD; S000004085; IOC2.
DR VEuPathDB; FungiDB:YLR095C; -.
DR eggNOG; ENOG502QPXN; Eukaryota.
DR HOGENOM; CLU_016629_0_0_1; -.
DR InParanoid; Q12072; -.
DR OMA; WQHWECQ; -.
DR BioCyc; YEAST:G3O-32245-MON; -.
DR PRO; PR:Q12072; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q12072; protein.
DR GO; GO:0016587; C:Isw1 complex; IPI:ComplexPortal.
DR GO; GO:0036437; C:Isw1b complex; IDA:SGD.
DR GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0009408; P:response to heat; IC:ComplexPortal.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR SUPFAM; SSF57903; SSF57903; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..812
FT /note="ISWI one complex protein 2"
FT /id="PRO_0000240452"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 762..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 673..714
FT /evidence="ECO:0000255"
FT COMPBIAS 617..636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 812 AA; 93446 MW; 632AD02AA8229D87 CRC64;
MRTKRTRGTR NVGASMPAGA ANADSEDWKE YVSEDIIAQL NKHQLPYSEI LDEKIADLAN
HWHFQYVMAW LSNVCESYTT TTFNTDQYGG SSTKCLWKNI KFDEGVFVTD VFSKIDGKDS
NYYNDEVDVD EGSQNLYDRI RLQLLHQLAG NKSGQLKDWN VIVNHHLQNS SAYSDLVTDL
PFLELEIARQ FDIIYSIIKL IEMKNMIFKN YLANNLHLFT FSEVILDDDN SGGEEMKSLF
ALPNVGVLVK KTIHRVKEGS SSQVSQTLNI PIKLQNCTIK ESDPDIPDSV ELIHLEYSHD
IDAYLQSITI DYDVITTNWG SMLEYWSENK SSKAIDEFIT NLIPVYAEHR LYSAKLLANR
EKERAIAELM TRRKRSSRLV AKEEENKKKD LESEWFEKLD EREQFIRHRN KLVSKEIKKI
KDLLWNQLWQ LYDQDYRDEK LTRRNELKDR SGSGTPFFET SLGREEDNPL NEIDIGVLDH
GPNFQSSIIP VEPPIPGTVG PLQTGDVPEL PSDFCITKEE LDELANYGIF TPQQEPDNQD
SVFQCPGEPE LAPMIITEDT ETDLFNNRPL ICCDHCYRWQ HWECQPPKII ELISSTTKSP
QHTLSQRDFG VIIMGNSHGN RRSSRRPQST LEPSTKSSRP TDKRKPLSEC STFICAWCIR
DLELELRNIF VPELKIIRAK QRKQQEDRER RKKMKEEKKR LEELAKKREL TESVSPPVFN
NAFANMSSST TPSIAAYEKT NPAINPAPNV NAAHPIITYS QQTGSKTVPQ APQAPQTSQA
SIQPQQQQQQ QQQQQPLHPK EQNFHFQFPP TN
