IOC4_YEAST
ID IOC4_YEAST Reviewed; 475 AA.
AC Q04213; D6VZL9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=ISWI one complex protein 4;
GN Name=IOC4; OrderedLocusNames=YMR044W; ORFNames=YM9532.09;
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=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73 AND SER-242, AND
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; THR-9; SER-65; SER-73 AND
RP SER-242, AND 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-73 AND SER-242, 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: 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 5820 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z48502; CAA88410.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09943.1; -; Genomic_DNA.
DR PIR; S52893; S52893.
DR RefSeq; NP_013758.1; NM_001182541.1.
DR PDB; 7E29; X-ray; 2.30 A; A=1-178.
DR PDBsum; 7E29; -.
DR AlphaFoldDB; Q04213; -.
DR SMR; Q04213; -.
DR BioGRID; 35217; 184.
DR ComplexPortal; CPX-636; ISW1b chromatin remodeling complex.
DR DIP; DIP-876N; -.
DR IntAct; Q04213; 9.
DR MINT; Q04213; -.
DR STRING; 4932.YMR044W; -.
DR iPTMnet; Q04213; -.
DR MaxQB; Q04213; -.
DR PaxDb; Q04213; -.
DR PRIDE; Q04213; -.
DR EnsemblFungi; YMR044W_mRNA; YMR044W; YMR044W.
DR GeneID; 855061; -.
DR KEGG; sce:YMR044W; -.
DR SGD; S000004647; IOC4.
DR VEuPathDB; FungiDB:YMR044W; -.
DR eggNOG; ENOG502QTTV; Eukaryota.
DR HOGENOM; CLU_031574_0_0_1; -.
DR InParanoid; Q04213; -.
DR OMA; WPAMIIP; -.
DR BioCyc; YEAST:G3O-32749-MON; -.
DR PRO; PR:Q04213; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q04213; protein.
DR GO; GO:0016587; C:Isw1 complex; IPI:ComplexPortal.
DR GO; GO:0036437; C:Isw1b complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0009408; P:response to heat; IC:ComplexPortal.
DR GO; GO:0007062; P:sister chromatid cohesion; IMP:SGD.
DR CDD; cd05840; SPBC215_ISWI_like; 1.
DR InterPro; IPR035503; IOC4-like_PWWP.
DR InterPro; IPR000313; PWWP_dom.
DR Pfam; PF00855; PWWP; 1.
DR SMART; SM00293; PWWP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..475
FT /note="ISWI one complex protein 4"
FT /id="PRO_0000203276"
FT REGION 42..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..68
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..84
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..290
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 9
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 242
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
SQ SEQUENCE 475 AA; 55427 MW; DFD6189E81178060 CRC64;
MSEAIFQPTD IVLAKVKGFS AWPAMIIPNE LIPDNILKTK PVSVHKGKSG SDKKANEDID
ADMESEARDR EQSEEEEDIE DFGESEANPE KFIIYTPVLK FRKNDTLKST YCVKFFCDDS
YIWVKPMDMK ILTSEDCRKW LSGKQRKNKK LIPAYEMAMR GKNGIDIWEF VEYGSYGKPD
EEEYVEEEEE ENEPEKKAIR PTRSSSRQRQ KRASETEKSE GGNSNKRKRV TRSTRQQAID
ASEEEEEEEE EKVQEAVRKR PQRTKTKKVV VSKTKPNPKT KAKKEKPKPP KPIKYHFEDD
EDWSIVGLGP QDLSIEKTMD PIAKKLSQKK NLEKHVEIKL DLEDKLAGIN KLLCDVLCSA
INQAVSIKDD FEIILDELQI ALDTRGSRNE FITIFQSNNS LLLNFRILFN LRKRELNKWD
LWDRFQDIFK HIYSYQFIPD TEDWQLEQNM EIEEMDREKP SFSEDVKEEE SKVGA
