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 27-MAR-2024, entry version 179. 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; GN OrderedLocusNames=YNL025C; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 EMDB; EMD-22989; -. DR EMDB; EMD-22991; -. DR SMR; P47821; -. DR BioGRID; 35801; 421. 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; 4932-YNL025C; -. DR PeptideAtlas; P47821; -. DR EnsemblFungi; YNL025C_mRNA; YNL025C; YNL025C. DR GeneID; 855706; -. DR KEGG; sce:YNL025C; -. DR AGR; SGD:S000004970; -. 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; KVAHSQF; -. DR OrthoDB; 102875at2759; -. DR BioCyc; YEAST:G3O-33063-MONOMER; -. DR BioGRID-ORCS; 855706; 0 hits in 10 CRISPR screens. 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 CDD; cd20513; CYCLIN_CCNC_rpt1; 1. DR CDD; cd20546; CYCLIN_SpCG1C_ScCTK2-like_rpt2; 1. DR Gene3D; 1.10.472.10; Cyclin-like; 2. DR InterPro; IPR013763; Cyclin-like_dom. DR InterPro; IPR036915; Cyclin-like_sf. DR InterPro; IPR043198; Cyclin/Ssn8. DR InterPro; IPR006671; Cyclin_N. DR PANTHER; PTHR10026; CYCLIN; 1. DR PANTHER; PTHR10026:SF7; CYCLIN-C; 1. DR Pfam; PF00134; Cyclin_N; 1. DR PIRSF; PIRSF028758; Cyclin, C/H/G types; 1. DR SMART; SM00385; CYCLIN; 2. DR SUPFAM; SSF47954; Cyclin-like; 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 //