ID NOT2_YEAST Reviewed; 191 AA. AC P06100; D6VRI6; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1988, sequence version 1. DT 02-SEP-2026, entry version 193. DE RecName: Full=General negative regulator of transcription subunit 2; DE AltName: Full=cell division cycle protein 36; GN Name=CDC36; Synonyms=DNA19, NOT2; OrderedLocusNames=YDL165W; 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]. RX PubMed=3018676; DOI=10.1093/nar/14.16.6681; RA Ferguson J., Ho J.-Y., Peterson T.A., Reed S.I.; RT "Nucleotide sequence of the yeast cell division cycle start genes CDC28, RT CDC36, CDC37, and CDC39, and a structural analysis of the predicted RT products."; RL Nucleic Acids Res. 14:6681-6697(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=3909103; DOI=10.1093/nar/13.23.8323; RA Barker D.G., White J.H.M., Johnston L.H.; RT "The nucleotide sequence of the DNA ligase gene (CDC9) from Saccharomyces RT cerevisiae: a gene which is cell-cycle regulated and induced in response to RT DNA damage."; RL Nucleic Acids Res. 13:8323-8337(1985). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=9169867; DOI=10.1038/387s075; RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., RA Mewes H.-W., Zollner A., Zaccaria P.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."; RL Nature 387:75-78(1997). RN [4] 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 [5] 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 [6] RP CHARACTERIZATION. RX PubMed=7926748; DOI=10.1101/gad.8.5.525; RA Collart M.A., Struhl K.; RT "NOT1(CDC39), NOT2(CDC36), NOT3, and NOT4 encode a global-negative RT regulator of transcription that differentially affects TATA-element RT utilization."; RL Genes Dev. 8:525-537(1994). RN [7] RP IDENTIFICATION IN THE CCR4-NOT CORE COMPLEX, AND FUNCTION OF THE CCR4-NOT RP CORE COMPLEX IN TRANSCRIPTIONAL REGULATION. RX PubMed=9463387; DOI=10.1093/emboj/17.4.1096; RA Liu H.Y., Badarinarayana V., Audino D.C., Rappsilber J., Mann M., RA Denis C.L.; RT "The NOT proteins are part of the CCR4 transcriptional complex and affect RT gene expression both positively and negatively."; RL EMBO J. 17:1096-1106(1998). RN [8] RP INTERACTION WITH NOT1. RX PubMed=10490603; DOI=10.1128/mcb.19.10.6642; RA Bai Y., Salvadore C., Chiang Y.C., Collart M.A., Liu H.Y., Denis C.L.; RT "The CCR4 and CAF1 proteins of the CCR4-NOT complex are physically and RT functionally separated from NOT2, NOT4, and NOT5."; RL Mol. Cell. Biol. 19:6642-6651(1999). RN [9] RP IDENTIFICATION IN THE CCR4-NOT CORE COMPLEX. RX PubMed=11733989; DOI=10.1006/jmbi.2001.5162; RA Chen J., Rappsilber J., Chiang Y.C., Russell P., Mann M., Denis C.L.; RT "Purification and characterization of the 1.0 MDa CCR4-NOT complex RT identifies two novel components of the complex."; RL J. Mol. Biol. 314:683-694(2001). RN [10] RP SUBCELLULAR LOCATION. RX PubMed=11889048; DOI=10.1093/emboj/21.6.1427; RA Tucker M., Staples R.R., Valencia-Sanchez M.A., Muhlrad D., Parker R.; RT "Ccr4p is the catalytic subunit of a Ccr4p/Pop2p/Notp mRNA deadenylase RT complex in Saccharomyces cerevisiae."; RL EMBO J. 21:1427-1436(2002). RN [11] RP INTERACTION WITH NOT5. RX PubMed=12215412; DOI=10.1016/s0022-2836(02)00707-6; RA Russell P., Benson J.D., Denis C.L.; RT "Characterization of mutations in NOT2 indicates that it plays an important RT role in maintaining the integrity of the CCR4-NOT complex."; RL J. Mol. Biol. 322:27-39(2002). RN [12] 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). CC -!- FUNCTION: Acts as a component of the CCR4-NOT core complex, which in CC the nucleus seems to be a general transcription factor, and in the CC cytoplasm the major mRNA deadenylase involved in mRNA turnover. NOT2 is CC required for the integrity of the complex. The NOT protein subcomplex CC negatively regulates the basal and activated transcription of many CC genes. Preferentially affects TC-type TATA element-dependent CC transcription. Could directly or indirectly inhibit component(s) of the CC general transcription machinery. {ECO:0000269|PubMed:9463387}. CC -!- SUBUNIT: Forms a NOT protein complex that comprises NOT1, NOT2, NOT3, CC NOT4 and NOT5. Subunit of the 1.0 MDa CCR4-NOT core complex that CC contains CCR4, CAF1, NOT1, NOT2, NOT3, NOT4, NOT5, CAF40 and CAF130. In CC the complex interacts with NOT1 and NOT5. The core complex probably is CC part of a less characterized 1.9 MDa CCR4-NOT complex. CC {ECO:0000269|PubMed:10490603, ECO:0000269|PubMed:11733989, CC ECO:0000269|PubMed:12215412, ECO:0000269|PubMed:9463387}. CC -!- INTERACTION: CC P06100; P53829: CAF40; NbExp=3; IntAct=EBI-12153, EBI-28306; CC P06100; P25655: CDC39; NbExp=8; IntAct=EBI-12153, EBI-12139; CC P06100; P34909: MOT2; NbExp=4; IntAct=EBI-12153, EBI-12174; CC P06100; P06102: NOT3; NbExp=3; IntAct=EBI-12153, EBI-12165; CC P06100; Q12514: NOT5; NbExp=7; IntAct=EBI-12153, EBI-12184; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11889048}. Nucleus CC {ECO:0000269|PubMed:11889048}. CC -!- MISCELLANEOUS: Present with 2120 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the CNOT2/3/5 family. {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; X04287; CAA27835.1; -; Genomic_DNA. DR EMBL; X03246; CAA27006.1; -; Genomic_DNA. DR EMBL; Z67750; CAA91581.1; -; Genomic_DNA. DR EMBL; Z74213; CAA98739.1; -; Genomic_DNA. DR EMBL; X68020; CAA48160.1; -; Genomic_DNA. DR EMBL; AY557644; AAS55970.1; -; Genomic_DNA. DR EMBL; BK006938; DAA11696.1; -; Genomic_DNA. DR PIR; S12304; RGBY36. DR RefSeq; NP_010116.1; NM_001180225.1. DR PDB; 4BY6; X-ray; 2.80 A; B/E=1-191. DR AlphaFoldDB; P06100; -. DR SMR; P06100; -. DR BioGRID; 31900; 251. DR ComplexPortal; CPX-1800; CCR4-NOT mRNA deadenylase complex. DR DIP; DIP-590N; -. DR FunCoup; P06100; 169. DR IntAct; P06100; 28. DR MINT; P06100; -. DR STRING; 4932.YDL165W; -. DR GlyGen; P06100; 1 site. DR iPTMnet; P06100; -. DR PaxDb; 4932-YDL165W; -. DR PeptideAtlas; P06100; -. DR EnsemblFungi; YDL165W_mRNA; YDL165W; YDL165W. DR GeneID; 851389; -. DR KEGG; sce:YDL165W; -. DR AGR; SGD:S000002324; -. DR SGD; S000002324; CDC36. DR VEuPathDB; FungiDB:YDL165W; -. DR eggNOG; KOG2151; Eukaryota. DR HOGENOM; CLU_033275_4_1_1; -. DR InParanoid; P06100; -. DR OMA; IFYMKPR; -. DR OrthoDB; 25391at2759; -. DR BioCyc; YEAST:G3O-29557-MONOMER; -. DR BioGRID-ORCS; 851389; 2 hits in 10 CRISPR screens. DR CD-CODE; A777E0F8; P-body. DR EvolutionaryTrace; P06100; -. DR PRO; PR:P06100; -. DR Proteomes; UP000002311; Chromosome IV. DR RNAct; P06100; protein. DR GO; GO:0030015; C:CCR4-NOT core complex; IPI:SGD. DR GO; GO:0005737; C:cytoplasm; IDA:SGD. DR GO; GO:0005634; C:nucleus; IDA:SGD. DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IMP:SGD. DR GO; GO:0031087; P:deadenylation-independent decapping of nuclear-transcribed mRNA; IMP:SGD. DR GO; GO:0000288; P:nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IDA:SGD. DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IDA:SGD. DR GO; GO:0032968; P:positive regulation of transcription elongation by RNA polymerase II; IDA:ComplexPortal. DR GO; GO:0016567; P:protein ubiquitination; IMP:SGD. DR GO; GO:0051726; P:regulation of cell cycle; IMP:SGD. DR GO; GO:0000749; P:response to pheromone triggering conjugation with cellular fusion; IMP:SGD. DR GO; GO:0006368; P:transcription elongation by RNA polymerase II; IMP:SGD. DR FunFam; 2.30.30.1020:FF:000012; CCR4-NOT transcriptional complex subunit; 1. DR Gene3D; 2.30.30.1020; CCR4-NOT complex subunit 2/3/5, C-terminal domain; 1. DR InterPro; IPR038635; CCR4-NOT_su2/3/5_C_sf. DR InterPro; IPR040168; Not2/3/5. DR InterPro; IPR007282; NOT2/3/5_C. DR PANTHER; PTHR23326; CCR4 NOT-RELATED; 1. DR Pfam; PF04153; NOT2_3_5_C; 1. DR PDBsum; 4BY6; -. PE 1: Evidence at protein level; KW 3D-structure; Activator; Cytoplasm; Nucleus; Reference proteome; Repressor; KW Transcription; Transcription regulation. FT CHAIN 1..191 FT /note="General negative regulator of transcription subunit FT 2" FT /id="PRO_0000198336" FT STRAND 7..9 FT /evidence="ECO:0007829|PDB:4BY6" FT HELIX 35..40 FT /evidence="ECO:0007829|PDB:4BY6" FT HELIX 53..55 FT /evidence="ECO:0007829|PDB:4BY6" FT STRAND 59..61 FT /evidence="ECO:0007829|PDB:4BY6" FT HELIX 76..78 FT /evidence="ECO:0007829|PDB:4BY6" FT HELIX 84..86 FT /evidence="ECO:0007829|PDB:4BY6" FT STRAND 88..91 FT /evidence="ECO:0007829|PDB:4BY6" FT TURN 97..99 FT /evidence="ECO:0007829|PDB:4BY6" FT HELIX 101..104 FT /evidence="ECO:0007829|PDB:4BY6" FT HELIX 109..118 FT /evidence="ECO:0007829|PDB:4BY6" FT HELIX 123..134 FT /evidence="ECO:0007829|PDB:4BY6" FT STRAND 138..140 FT /evidence="ECO:0007829|PDB:4BY6" FT TURN 141..144 FT /evidence="ECO:0007829|PDB:4BY6" FT STRAND 145..149 FT /evidence="ECO:0007829|PDB:4BY6" FT STRAND 161..172 FT /evidence="ECO:0007829|PDB:4BY6" FT TURN 173..176 FT /evidence="ECO:0007829|PDB:4BY6" FT STRAND 177..186 FT /evidence="ECO:0007829|PDB:4BY6" FT HELIX 187..189 FT /evidence="ECO:0007829|PDB:4BY6" SQ SEQUENCE 191 AA; 22363 MW; 7D0B69657F791371 CRC64; MEKFGLKALV PLLKLEDKEL SSTYDHSMTL GADLSSMLYS LGIPRDSQDH RVLDTFQSPW AETSRSEVEP RFFTPESFTN IPGVLQSTVT PPCFNSIQND QQRVALFQDE TLFFLFYKHP GTVIQELTYL ELRKRNWRYH KTLKAWLTKD PMMEPIVSAD GLSERGSYVF FDPQRWEKCQ RDFLLFYNAI M //