CTI6_YEAST
ID CTI6_YEAST Reviewed; 506 AA.
AC Q08923; D6W3I7; Q6B1X3;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Histone deacetylase complex subunit CTI6;
DE AltName: Full=CYC8-TUP1-interacting protein 6;
DE AltName: Full=Transcriptional regulatory protein CTI6;
GN Name=CTI6; Synonyms=RXT1; OrderedLocusNames=YPL181W;
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=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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 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 FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CYC8.
RX PubMed=12086626; DOI=10.1016/s1097-2765(02)00545-2;
RA Papamichos-Chronakis M., Petrakis T., Ktistaki E., Topalidou I.,
RA Tzamarias D.;
RT "Cti6, a PHD domain protein, bridges the Cyc8-Tup1 corepressor and the SAGA
RT coactivator to overcome repression at GAL1.";
RL Mol. Cell 9:1297-1305(2002).
RN [5]
RP INTERACTION WITH RPD3 AND SIN3.
RX PubMed=11805826; DOI=10.1038/415141a;
RA Gavin A.-C., Boesche M., Krause R., Grandi P., Marzioch M., Bauer A.,
RA Schultz J., Rick J.M., Michon A.-M., Cruciat C.-M., Remor M., Hoefert C.,
RA Schelder M., Brajenovic M., Ruffner H., Merino A., Klein K., Hudak M.,
RA Dickson D., Rudi T., Gnau V., Bauch A., Bastuck S., Huhse B., Leutwein C.,
RA Heurtier M.-A., Copley R.R., Edelmann A., Querfurth E., Rybin V.,
RA Drewes G., Raida M., Bouwmeester T., Bork P., Seraphin B., Kuster B.,
RA Neubauer G., Superti-Furga G.;
RT "Functional organization of the yeast proteome by systematic analysis of
RT protein complexes.";
RL Nature 415:141-147(2002).
RN [6]
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 [7]
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 [8]
RP FUNCTION, INDUCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-95 AND
RP HIS-100.
RX PubMed=15133041; DOI=10.1074/jbc.m313463200;
RA Puig S., Lau M., Thiele D.J.;
RT "Cti6 is an Rpd3-Sin3 histone deacetylase-associated protein required for
RT growth under iron-limiting conditions in Saccharomyces cerevisiae.";
RL J. Biol. Chem. 279:30298-30306(2004).
RN [9]
RP IDENTIFICATION IN THE RPD3C(L) COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16314178; DOI=10.1016/j.bbaexp.2005.09.005;
RA Carrozza M.J., Florens L., Swanson S.K., Shia W.-J., Anderson S., Yates J.,
RA Washburn M.P., Workman J.L.;
RT "Stable incorporation of sequence specific repressors Ash1 and Ume6 into
RT the Rpd3L complex.";
RL Biochim. Biophys. Acta 1731:77-87(2005).
RN [10]
RP IDENTIFICATION IN THE RPD3C(L) COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16286008; DOI=10.1016/j.cell.2005.10.025;
RA Keogh M.-C., Kurdistani S.K., Morris S.A., Ahn S.H., Podolny V.,
RA Collins S.R., Schuldiner M., Chin K., Punna T., Thompson N.J., Boone C.,
RA Emili A., Weissman J.S., Hughes T.R., Strahl B.D., Grunstein M.,
RA Greenblatt J.F., Buratowski S., Krogan N.J.;
RT "Cotranscriptional set2 methylation of histone H3 lysine 36 recruits a
RT repressive Rpd3 complex.";
RL Cell 123:593-605(2005).
RN [11]
RP FUNCTION.
RX PubMed=16437160; DOI=10.1038/sj.emboj.7600961;
RA Crisp R.J., Adkins E.M., Kimmel E., Kaplan J.;
RT "Recruitment of Tup1p and Cti6p regulates heme-deficient expression of
RT Aft1p target genes.";
RL EMBO J. 25:512-521(2006).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-174; SER-175; THR-177;
RP SER-216 AND SER-267, 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: Component of the RPD3C(L) histone deacetylase complex (HDAC).
CC Responsible for the deacetylation of lysine residues on the N-terminal
CC part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation
CC gives a tag for epigenetic repression and plays an important role in
CC transcriptional regulation, cell cycle progression and developmental
CC events. CTI6 links the SAGA coactivator to the CYC8-TUP1 corepressor.
CC Involved in transcription regulation of heme-regulated genes and
CC required for GCN5 recruitment, histone H3 acetylation and SPT15/TBP
CC binding to promoters. {ECO:0000269|PubMed:12086626,
CC ECO:0000269|PubMed:15133041, ECO:0000269|PubMed:16437160}.
CC -!- SUBUNIT: Component of the RPD3C(L) complex composed of at least ASH1,
CC CTI6, DEP1, PHO23, RPD3, RXT2, RXT3, SAP30, SDS3, SIN3, UME1 and UME6.
CC Interacts with CYC8. {ECO:0000269|PubMed:11805826,
CC ECO:0000269|PubMed:12086626, ECO:0000269|PubMed:16286008,
CC ECO:0000269|PubMed:16314178}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12086626,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15133041}.
CC -!- INDUCTION: Under low iron conditions. {ECO:0000269|PubMed:15133041}.
CC -!- MISCELLANEOUS: Present with 1590 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z73538; CAA97891.1; -; Genomic_DNA.
DR EMBL; AY692957; AAT92976.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11253.1; -; Genomic_DNA.
DR PIR; S65193; S65193.
DR RefSeq; NP_015144.1; NM_001183995.1.
DR AlphaFoldDB; Q08923; -.
DR SMR; Q08923; -.
DR BioGRID; 36001; 383.
DR ComplexPortal; CPX-1852; RPD3L histone deacetylase complex.
DR DIP; DIP-2958N; -.
DR IntAct; Q08923; 17.
DR MINT; Q08923; -.
DR STRING; 4932.YPL181W; -.
DR iPTMnet; Q08923; -.
DR MaxQB; Q08923; -.
DR PaxDb; Q08923; -.
DR PRIDE; Q08923; -.
DR EnsemblFungi; YPL181W_mRNA; YPL181W; YPL181W.
DR GeneID; 855920; -.
DR KEGG; sce:YPL181W; -.
DR SGD; S000006102; CTI6.
DR VEuPathDB; FungiDB:YPL181W; -.
DR eggNOG; KOG1844; Eukaryota.
DR HOGENOM; CLU_020879_1_0_1; -.
DR InParanoid; Q08923; -.
DR OMA; GGLFIQC; -.
DR BioCyc; YEAST:G3O-34076-MON; -.
DR PRO; PR:Q08923; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q08923; protein.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0033698; C:Rpd3L complex; IDA:SGD.
DR GO; GO:0070210; C:Rpd3L-Expanded complex; HDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; IDA:SGD.
DR GO; GO:0061188; P:negative regulation of ribosomal DNA heterochromatin assembly; IMP:SGD.
DR GO; GO:0061186; P:negative regulation of silent mating-type cassette heterochromatin assembly; IMP:SGD.
DR GO; GO:0006334; P:nucleosome assembly; IC:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:SGD.
DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IMP:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Zinc; Zinc-finger.
FT CHAIN 1..506
FT /note="Histone deacetylase complex subunit CTI6"
FT /id="PRO_0000234079"
FT ZN_FING 72..123
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 49..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..194
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 174
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 177
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 267
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MUTAGEN 95
FT /note="C->A: Impairs growth under iron-limiting
FT conditions."
FT /evidence="ECO:0000269|PubMed:15133041"
FT MUTAGEN 100
FT /note="H->A: Impairs growth under iron-limiting
FT conditions."
FT /evidence="ECO:0000269|PubMed:15133041"
FT CONFLICT 342
FT /note="S -> P (in Ref. 3; AAT92976)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 506 AA; 57053 MW; 5123C56BB86ED991 CRC64;
MESTAIVPKG PVVGSEDMEK AEVIASGSTD IISTTSTATT TAAIGSVQEE SVKQEDVPME
GGEGEVEEEE GETRCICGEL DTPDDSGFFI QCEQCSSWQH GYCVSITQDN APDKYWCEQC
RPELHQLFTT DTGEARSIYK PVQEKRRQSR RKARSAAASK SHAANEAEKS PRNTSNTDDN
VDDIGDEEDE VEDEASAVAL AKDGNTRSSR RRRRNSMDDA STDQYSLDPG DSDKKLLDRK
RATFMAREEK QYQRMLEKAL KESRRTSHQE DPESYENDAD IYQGDTDNHN GTTRLQTDVM
LTEGKPDSVT NDDMKESLRP SKEQSMEKTN DVEKEASQEK ESSTGSAQDT EKTDEPILPL
TSISSSEDDS RKASSRGSKR VSKPARKGNR TRRSNTSSDT NQNRRSADIG TDKPVKPRLP
PQRTSLNEMR RRVSAILEFI SRTQWELSED QSDREEFVRF VENQHFVEKV DTIYNGYNES
LSMMDDLTRE LLLWEKKYSN NTNAIQ
