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
