SSN8_YEAST
ID SSN8_YEAST Reviewed; 323 AA.
AC P47821; D6W1F3;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=RNA polymerase II holoenzyme cyclin-like subunit;
DE AltName: Full=Suppressor of RNA polymerase B 11;
GN Name=SSN8; Synonyms=GIG3, NUT9, SRB11, UME3; OrderedLocusNames=YNL025C;
GN ORFNames=N2805;
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 [GENOMIC DNA], FUNCTION, AND INTERACTION WITH SSN3.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7877695; DOI=10.1038/374193a0;
RA Liao S.-M., Zhang J., Jeffery D.A., Koleske A.J., Thompson C.M., Chao D.M.,
RA Viljoen M., van Vuuren H.J.J., Young R.A.;
RT "A kinase-cyclin pair in the RNA polymerase II holoenzyme.";
RL Nature 374:193-196(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RA Smith J.B., Mallory M.J., Strich R.;
RT "UME3, a new C-type cyclin involved in the developmental switch between
RT meiotic and mitotic cell division in S. cerevisiae.";
RL Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7732022; DOI=10.1073/pnas.92.9.4006;
RA Kuchin S., Yeghiayan P., Carlson M.;
RT "Cyclin-dependent protein kinase and cyclin homologs SSN3 and SSN8
RT contribute to transcriptional control in yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:4006-4010(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [5]
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 [6]
RP FUNCTION, AND INTERACTION WITH SSN3.
RX PubMed=9702190; DOI=10.1016/s1097-2765(00)80112-4;
RA Hengartner C.J., Myer V.E., Liao S.-M., Wilson C.J., Koh S.S., Young R.A.;
RT "Temporal regulation of RNA polymerase II by Srb10 and Kin28 cyclin-
RT dependent kinases.";
RL Mol. Cell 2:43-53(1998).
RN [7]
RP INTERACTION WITH MED1 AND MED4, FUNCTION OF THE MEDIATOR COMPLEX, AND
RP INTERACTION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
RX PubMed=11555651; DOI=10.1074/jbc.m105961200;
RA Kang J.S., Kim S.H., Hwang M.S., Han S.J., Lee Y.C., Kim Y.-J.;
RT "The structural and functional organization of the yeast mediator
RT complex.";
RL J. Biol. Chem. 276:42003-42010(2001).
RN [8]
RP FUNCTION, AND INTERACTION WITH SSN3.
RX PubMed=11226276; DOI=10.1073/pnas.041611198;
RA Zaman Z., Ansari A.Z., Koh S.S., Young R., Ptashne M.;
RT "Interaction of a transcriptional repressor with the RNA polymerase II
RT holoenzyme plays a crucial role in repression.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:2550-2554(2001).
RN [9]
RP IDENTIFICATION IN THE SRB8-11 COMPLEX, AND FUNCTION OF THE SRB8-11 COMPLEX.
RX PubMed=12200444; DOI=10.1074/jbc.m207195200;
RA Borggrefe T., Davis R., Erdjument-Bromage H., Tempst P., Kornberg R.D.;
RT "A complex of the Srb8, -9, -10, and -11 transcriptional regulatory
RT proteins from yeast.";
RL J. Biol. Chem. 277:44202-44207(2002).
RN [10]
RP INTERACTION WITH ASK10.
RX PubMed=14555478; DOI=10.1128/ec.2.5.962-970.2003;
RA Cohen T.J., Lee K., Rutkowski L.H., Strich R.;
RT "Ask10p mediates the oxidative stress-induced destruction of the
RT Saccharomyces cerevisiae C-type cyclin Ume3p/Srb11p.";
RL Eukaryot. Cell 2:962-970(2003).
RN [11]
RP FUNCTION.
RX PubMed=12520306; DOI=10.1038/nature01243;
RA Nelson C., Goto S., Lund K., Hung W., Sadowski I.;
RT "Srb10/Cdk8 regulates yeast filamentous growth by phosphorylating the
RT transcription factor Ste12.";
RL Nature 421:187-190(2003).
RN [12]
RP TOPOLOGY OF THE MEDIATOR COMPLEX.
RX PubMed=15477388; DOI=10.1093/nar/gkh878;
RA Guglielmi B., van Berkum N.L., Klapholz B., Bijma T., Boube M.,
RA Boschiero C., Bourbon H.-M., Holstege F.C.P., Werner M.;
RT "A high resolution protein interaction map of the yeast Mediator complex.";
RL Nucleic Acids Res. 32:5379-5391(2004).
RN [13]
RP FUNCTION OF THE MEDIATOR COMPLEX.
RX PubMed=16076843; DOI=10.1074/jbc.m506067200;
RA Nair D., Kim Y., Myers L.C.;
RT "Mediator and TFIIH govern carboxyl-terminal domain-dependent transcription
RT in yeast extracts.";
RL J. Biol. Chem. 280:33739-33748(2005).
RN [14]
RP FUNCTION.
RX PubMed=16109375; DOI=10.1016/j.molcel.2005.06.033;
RA van de Peppel J., Kettelarij N., van Bakel H., Kockelkorn T.T.J.P.,
RA van Leenen D., Holstege F.C.P.;
RT "Mediator expression profiling epistasis reveals a signal transduction
RT pathway with antagonistic submodules and highly specific downstream
RT targets.";
RL Mol. Cell 19:511-522(2005).
RN [15]
RP FUNCTION OF THE SRB8-11 COMPLEX.
RX PubMed=15601835; DOI=10.1128/mcb.25.1.114-123.2005;
RA Larschan E., Winston F.;
RT "The Saccharomyces cerevisiae Srb8-Srb11 complex functions with the SAGA
RT complex during Gal4-activated transcription.";
RL Mol. Cell. Biol. 25:114-123(2005).
RN [16]
RP FUNCTION.
RX PubMed=15687503; DOI=10.1073/pnas.0409671102;
RA Ansari A.Z., Ogirala A., Ptashne M.;
RT "Transcriptional activating regions target attached substrates to a cyclin-
RT dependent kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:2346-2349(2005).
RN [17]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16630888; DOI=10.1016/j.molcel.2006.03.023;
RA Andrau J.-C., van de Pasch L., Lijnzaad P., Bijma T., Koerkamp M.G.,
RA van de Peppel J., Werner M., Holstege F.C.P.;
RT "Genome-wide location of the coactivator mediator: binding without
RT activation and transient Cdk8 interaction on DNA.";
RL Mol. Cell 22:179-192(2006).
CC -!- FUNCTION: Component of the SRB8-11 complex. The SRB8-11 complex is a
CC regulatory module of the Mediator complex which is itself involved in
CC regulation of basal and activated RNA polymerase II-dependent
CC transcription. The SRB8-11 complex may be involved in the
CC transcriptional repression of a subset of genes regulated by Mediator.
CC It may inhibit the association of the Mediator complex with RNA
CC polymerase II to form the holoenzyme complex. The SRB8-11 complex
CC phosphorylates the C-terminal domain (CTD) of the largest subunit of
CC RNA polymerase II RPB1 at serines 2 and 5. The SSN3/SRB10 and
CC SSN8/SRB11 kinase-cyclin pair may also positively and negatively
CC regulate numerous transcriptional activators in response to changes in
CC nutritional and physiological conditions. {ECO:0000269|PubMed:11226276,
CC ECO:0000269|PubMed:11555651, ECO:0000269|PubMed:12200444,
CC ECO:0000269|PubMed:12520306, ECO:0000269|PubMed:15601835,
CC ECO:0000269|PubMed:15687503, ECO:0000269|PubMed:16076843,
CC ECO:0000269|PubMed:16109375, ECO:0000269|PubMed:16630888,
CC ECO:0000269|PubMed:7877695, ECO:0000269|PubMed:9702190}.
CC -!- SUBUNIT: Component of the SRB8-11 complex which consists of SRB8,
CC SSN2/SRB9, SSN3/SRB10 and SSN8/SRB11. The SRB8-11 complex associates
CC with the Mediator complex. The SSN3/SRB10 and SSN8/SRB11 kinase-cyclin
CC pair also associate with the RNA polymerase II holoenzyme. Interacts
CC with ASK10. {ECO:0000269|PubMed:11226276, ECO:0000269|PubMed:11555651,
CC ECO:0000269|PubMed:12200444, ECO:0000269|PubMed:14555478,
CC ECO:0000269|PubMed:7877695, ECO:0000269|PubMed:9702190}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16630888}.
CC -!- SIMILARITY: Belongs to the cyclin family. Cyclin C subfamily.
CC {ECO:0000305}.
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DR EMBL; U20221; AAA69820.1; -; Genomic_DNA.
DR EMBL; U16248; AAA64270.1; -; Genomic_DNA.
DR EMBL; U20635; AAA85714.1; -; Genomic_DNA.
DR EMBL; Z71301; CAA95887.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10519.1; -; Genomic_DNA.
DR PIR; S59373; S59373.
DR RefSeq; NP_014373.3; NM_001182864.3.
DR PDB; 7KPV; EM; 3.80 A; B=1-323.
DR PDB; 7KPX; EM; 4.40 A; B=1-323.
DR PDBsum; 7KPV; -.
DR PDBsum; 7KPX; -.
DR AlphaFoldDB; P47821; -.
DR SMR; P47821; -.
DR BioGRID; 35801; 401.
DR ComplexPortal; CPX-1853; CKM complex.
DR DIP; DIP-2007N; -.
DR IntAct; P47821; 35.
DR MINT; P47821; -.
DR STRING; 4932.YNL025C; -.
DR iPTMnet; P47821; -.
DR MaxQB; P47821; -.
DR PaxDb; P47821; -.
DR PRIDE; P47821; -.
DR EnsemblFungi; YNL025C_mRNA; YNL025C; YNL025C.
DR GeneID; 855706; -.
DR KEGG; sce:YNL025C; -.
DR SGD; S000004970; SSN8.
DR VEuPathDB; FungiDB:YNL025C; -.
DR eggNOG; KOG0794; Eukaryota.
DR GeneTree; ENSGT00940000167379; -.
DR HOGENOM; CLU_034754_2_1_1; -.
DR InParanoid; P47821; -.
DR OMA; MSGSYWT; -.
DR BioCyc; YEAST:G3O-33063-MON; -.
DR PRO; PR:P47821; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P47821; protein.
DR GO; GO:1990508; C:CKM complex; IPI:ComplexPortal.
DR GO; GO:0016592; C:mediator complex; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IDA:SGD.
DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:SGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0000411; P:positive regulation of transcription by galactose; IMP:SGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:SGD.
DR GO; GO:0010673; P:positive regulation of transcription from RNA polymerase II promoter involved in meiotic cell cycle; IMP:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IDA:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00043; CYCLIN; 1.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR043198; Cyclin/Ssn8.
DR InterPro; IPR006671; Cyclin_N.
DR InterPro; IPR028367; CyclinC/Ssn8.
DR PANTHER; PTHR10026; PTHR10026; 1.
DR PANTHER; PTHR10026:SF7; PTHR10026:SF7; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR SMART; SM00385; CYCLIN; 2.
DR SUPFAM; SSF47954; SSF47954; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Cyclin; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..323
FT /note="RNA polymerase II holoenzyme cyclin-like subunit"
FT /id="PRO_0000080428"
FT DOMAIN 45..176
FT /note="Cyclin N-terminal"
SQ SEQUENCE 323 AA; 37791 MW; 2BA16A3374CCF207 CRC64;
MSGSFWTSTQ RHHWQYTKAS LAKERQKLWL LECQLFPQGL NIVMDSKQNG IEQSITKNIP
ITHRDLHYDK DYNLRIYCYF LIMKLGRRLN IRQYALATAH IYLSRFLIKA SVREINLYML
VTTCVYLACK VEECPQYIRT LVSEARTLWP EFIPPDPTKV TEFEFYLLEE LESYLIVHHP
YQSLKQIVQV LKQPPFQITL SSDDLQNCWS LINDSYINDV HLLYPPHIIA VACLFITISI
HGKPTKGSSL ASAASEAIRD PKNSSSPVQI AFNRFMAESL VDLEEVMDTI QEQITLYDHW
DKYHEQWIKF LLHTLYLRPA SAI
