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CYC8_SCHPO
ID   CYC8_SCHPO              Reviewed;        1102 AA.
AC   O60184; Q9USA6;
DT   30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=General transcriptional corepressor ssn6;
GN   Name=ssn6; ORFNames=SPBC23E6.09;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 633-836, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=ATCC 38364 / 968;
RX   PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA   Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA   Hiraoka Y.;
RT   "Large-scale screening of intracellular protein localization in living
RT   fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL   Genes Cells 5:169-190(2000).
RN   [3]
RP   FUNCTION, AND INTERACTION WITH TUP11 AND TUP12.
RX   PubMed=15632072; DOI=10.1128/mcb.25.2.716-727.2005;
RA   Fagerstroem-Billai F., Wright A.P.H.;
RT   "Functional comparison of the Tup11 and Tup12 transcriptional corepressors
RT   in fission yeast.";
RL   Mol. Cell. Biol. 25:716-727(2005).
RN   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-893; SER-895; SER-897;
RP   SER-898; SER-992; SER-1059 AND SER-1061, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=18257517; DOI=10.1021/pr7006335;
RA   Wilson-Grady J.T., Villen J., Gygi S.P.;
RT   "Phosphoproteome analysis of fission yeast.";
RL   J. Proteome Res. 7:1088-1097(2008).
CC   -!- FUNCTION: Acts as component of the ssn6-tup corepressor complexes,
CC       which are involved in the repression of many genes in a wide variety of
CC       physiological processes. May also be involved in the derepression of at
CC       least some target genes. The complex is recruited to target genes by
CC       interaction with DNA-bound transcriptional repressors. The complex
CC       recruits histone deacetylases to produce a repressive chromatin
CC       structure, interacts with hypoacetylated N-terminal tails of histones
CC       H3 and H4 that have been programmed for repression by the action of
CC       histone deacetylases and interferes directly with the transcriptional
CC       machinery by associating with the RNA polymerase II mediator complex
CC       (By similarity). {ECO:0000250, ECO:0000269|PubMed:15632072}.
CC   -!- SUBUNIT: Associates independently with tup11 and tup12 to form ssn6-tup
CC       corepressor complexes.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Nuclear dots.
CC   -!- SIMILARITY: Belongs to the CYC8/SSN6 family. {ECO:0000305}.
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DR   EMBL; CU329671; CAA18877.1; -; Genomic_DNA.
DR   EMBL; AB027911; BAA87215.1; -; Genomic_DNA.
DR   PIR; T39943; T39943.
DR   RefSeq; NP_596609.1; NM_001022530.2.
DR   AlphaFoldDB; O60184; -.
DR   SMR; O60184; -.
DR   BioGRID; 277181; 5.
DR   STRING; 4896.SPBC23E6.09.1; -.
DR   iPTMnet; O60184; -.
DR   MaxQB; O60184; -.
DR   PaxDb; O60184; -.
DR   PRIDE; O60184; -.
DR   EnsemblFungi; SPBC23E6.09.1; SPBC23E6.09.1:pep; SPBC23E6.09.
DR   GeneID; 2540656; -.
DR   KEGG; spo:SPBC23E6.09; -.
DR   PomBase; SPBC23E6.09; ssn6.
DR   VEuPathDB; FungiDB:SPBC23E6.09; -.
DR   eggNOG; KOG1124; Eukaryota.
DR   HOGENOM; CLU_006762_2_1_1; -.
DR   InParanoid; O60184; -.
DR   OMA; ETRVISW; -.
DR   Reactome; R-SPO-2559580; Oxidative Stress Induced Senescence.
DR   PRO; PR:O60184; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0000785; C:chromatin; IDA:PomBase.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0017053; C:transcription repressor complex; EXP:PomBase.
DR   GO; GO:0031490; F:chromatin DNA binding; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0003714; F:transcription corepressor activity; ISO:PomBase.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:PomBase.
DR   GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR   Gene3D; 1.25.40.10; -; 3.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR001440; TPR_1.
DR   InterPro; IPR019734; TPR_repeat.
DR   Pfam; PF00515; TPR_1; 1.
DR   Pfam; PF13181; TPR_8; 3.
DR   SMART; SM00028; TPR; 10.
DR   SUPFAM; SSF48452; SSF48452; 2.
DR   PROSITE; PS50005; TPR; 9.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW   TPR repeat; Transcription; Transcription regulation.
FT   CHAIN           1..1102
FT                   /note="General transcriptional corepressor ssn6"
FT                   /id="PRO_0000106418"
FT   REPEAT          334..367
FT                   /note="TPR 1"
FT   REPEAT          368..401
FT                   /note="TPR 2"
FT   REPEAT          402..435
FT                   /note="TPR 3"
FT   REPEAT          438..471
FT                   /note="TPR 4"
FT   REPEAT          475..508
FT                   /note="TPR 5"
FT   REPEAT          512..545
FT                   /note="TPR 6"
FT   REPEAT          584..617
FT                   /note="TPR 7"
FT   REPEAT          618..651
FT                   /note="TPR 8"
FT   REPEAT          652..686
FT                   /note="TPR 9"
FT   REGION          1..94
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          166..209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          739..764
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          808..1102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..187
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..209
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        808..865
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        866..883
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        884..906
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        924..971
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        972..987
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        988..1002
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1003..1048
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1055..1074
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         893
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         895
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         897
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         898
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         992
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         1059
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         1061
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
SQ   SEQUENCE   1102 AA;  121517 MW;  C5258D714C42FE7A CRC64;
     MPQSQVATAS PSQNAQPNHG MGSKVLSSDP NASLPPQTAY YASPLHANSV SLPPSHLPRS
     TLHPLLSQQQ QPAQQSPSLG PAQQNIQQPP SVSIASQPHY AEAIVPIQQV LQPQQYRQLP
     PNMVAATNAP QQHPQLQRMM PILSSNQPIQ QLPLPNQASP YIPVPLQQQQ QSQPQQQPQQ
     QQHQQPQQPQ PPQQPLQQQQ QQRQLHSGIQ QPVSTIVSQN GTYYSIPAVN HPMAGQPIAI
     APVPAPNQAA LPPIPPQALP ANGTPNTLAS PVTLPAANSA VQNAQPVPMT SSPAMAVVPQ
     NKTAATSTLA AQQGANVLPP NAPESVRHLI SLNEETWIQI GRLAELFDDQ DKALSAYESA
     LRQNPYSIPA MLQIATILRN REQFPLAIEY YQTILDCDPK QGEIWSALGH CYLMQDDLSR
     AYSAYRQALY HLKDPKDPKL WYGIGILYDR YGSHEHAEEA FMQCLRMDPN FEKVNEIYFR
     LGIIYKQQHK FAQSLELFRH ILDNPPKPLT VLDIYFQIGH VYEQRKEYKL AKEAYERVLA
     ETPNHAKVLQ QLGWLCHQQS SSFTNQDLAI QYLTKSLEAD DTDAQSWYLI GRCYVAQQKY
     NKAYEAYQQA VYRDGRNPTF WCSIGVLYYQ INQYQDALDA YSRAIRLNPY ISEVWYDLGT
     LYESCHNQIS DALDAYQRAA ELDPTNPHIK ARLQLLRGPN NEQHKIVNAP PSNVPNVQTA
     KYINQPGVPY SNVPVAQLSG NWQPPHLPQA QLPSATGQSG VVQQPYQTQP SVTNNNVATQ
     PVIASTVPVQ TAAPSSQTAV PQTIHQSNAF TPRGKHASGS RNSISSTKSP QHKLSDQPRS
     RNNSISNVSH RERSNSVSSK SRETRTSASN ESDPKKSTQR DSSKKLENST VVSGSPSSSS
     KSDAAKSIKP QKPEPALKPV EGTADPKSTK RNHQETEKTA DTDVSSTEPV KRQKTADVND
     DVGEEEVKQS VSEQVDSAQL TSEPKSESLP KSPEEKSDDT SNDVTTENTN DINGDSNMDN
     VATVDKSTDA VDTSTATVAA TTTTAEEELP QKESQERSSP SPENQDSTPL APKSVSPKQA
     ARTLDIDENY DDDEGEKETV SV
 
 
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