NOT3_YEAST
ID NOT3_YEAST Reviewed; 836 AA.
AC P06102; D6VVP4; Q6B233;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=General negative regulator of transcription subunit 3;
GN Name=NOT3; OrderedLocusNames=YIL038C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [3]
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 [4]
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 [5]
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 [6]
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 [7]
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 [8]
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).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450 AND SER-657, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-322, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450; SER-565 AND SER-657, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-303; SER-307; SER-446;
RP SER-450; SER-565; SER-569 AND THR-571, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [13]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-535, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Acts as component of the CCR4-NOT core complex, which in the
CC nucleus seems to be a general transcription factor, and in the
CC cytoplasm the major mRNA deadenylase involved in mRNA turnover. The NOT
CC protein subcomplex negatively regulates the basal and activated
CC transcription of many genes. Preferentially affects TC-type TATA
CC element-dependent transcription. Could directly or indirectly inhibit
CC component(s) of the general transcription machinery.
CC {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.
CC The core complex probably is part of a less characterized 1.9 MDa CCR4-
CC NOT complex. {ECO:0000269|PubMed:11733989, ECO:0000269|PubMed:9463387}.
CC -!- INTERACTION:
CC P06102; P53829: CAF40; NbExp=3; IntAct=EBI-12165, EBI-28306;
CC P06102; P06100: CDC36; NbExp=2; IntAct=EBI-12165, EBI-12153;
CC P06102; P25655: CDC39; NbExp=3; IntAct=EBI-12165, EBI-12139;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus.
CC -!- MISCELLANEOUS: Present with 2490 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CNOT2/3/5 family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be CDC39 (which is in fact NOT1).
CC {ECO:0000305|PubMed:3018676}.
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DR EMBL; Z46861; CAA86913.1; -; Genomic_DNA.
DR EMBL; X04289; CAA27837.1; -; Genomic_DNA.
DR EMBL; AY692897; AAT92916.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08510.1; -; Genomic_DNA.
DR PIR; S49940; S49940.
DR RefSeq; NP_012226.3; NM_001179388.3.
DR AlphaFoldDB; P06102; -.
DR SMR; P06102; -.
DR BioGRID; 34952; 256.
DR ComplexPortal; CPX-1800; CCR4-NOT mRNA deadenylase complex.
DR DIP; DIP-2256N; -.
DR IntAct; P06102; 45.
DR MINT; P06102; -.
DR STRING; 4932.YIL038C; -.
DR iPTMnet; P06102; -.
DR MaxQB; P06102; -.
DR PaxDb; P06102; -.
DR PRIDE; P06102; -.
DR TopDownProteomics; P06102; -.
DR EnsemblFungi; YIL038C_mRNA; YIL038C; YIL038C.
DR GeneID; 854773; -.
DR KEGG; sce:YIL038C; -.
DR SGD; S000001300; NOT3.
DR VEuPathDB; FungiDB:YIL038C; -.
DR eggNOG; KOG2150; Eukaryota.
DR HOGENOM; CLU_020483_0_0_1; -.
DR InParanoid; P06102; -.
DR OMA; IKTWAAG; -.
DR BioCyc; YEAST:G3O-31310-MON; -.
DR PRO; PR:P06102; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P06102; 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; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0000290; P:deadenylation-dependent decapping of nuclear-transcribed mRNA; IMP: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 from RNA polymerase II promoter; IDA:SGD.
DR GO; GO:0016567; P:protein ubiquitination; IMP:SGD.
DR Gene3D; 2.30.30.1020; -; 1.
DR InterPro; IPR038635; CCR4-NOT_su2/3/5_N_sf.
DR InterPro; IPR012270; CCR4-NOT_su3/5.
DR InterPro; IPR040168; Not2/3/5.
DR InterPro; IPR007282; NOT2/3/5_C.
DR InterPro; IPR007207; Not_N.
DR PANTHER; PTHR23326; PTHR23326; 1.
DR Pfam; PF04153; NOT2_3_5; 1.
DR Pfam; PF04065; Not3; 1.
DR PIRSF; PIRSF005290; NOT_su_3_5; 1.
PE 1: Evidence at protein level;
KW Activator; Coiled coil; Cytoplasm; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..836
FT /note="General negative regulator of transcription subunit
FT 3"
FT /id="PRO_0000198337"
FT REGION 252..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..391
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 513..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 36..68
FT /evidence="ECO:0000255"
FT COILED 119..195
FT /evidence="ECO:0000255"
FT COILED 255..292
FT /evidence="ECO:0000255"
FT COILED 803..831
FT /evidence="ECO:0000255"
FT COMPBIAS 265..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 565
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 569
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 571
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 657
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
FT CROSSLNK 535
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT CONFLICT 106
FT /note="I -> N (in Ref. 1; CAA86913)"
FT /evidence="ECO:0000305"
FT CONFLICT 593
FT /note="K -> R (in Ref. 4; AAT92916)"
FT /evidence="ECO:0000305"
FT CONFLICT 725
FT /note="Y -> C (in Ref. 1; CAA86913)"
FT /evidence="ECO:0000305"
FT CONFLICT 827..836
FT /note="KQLKQGKISV -> ETIETGKN (in Ref. 1; CAA86913)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 836 AA; 94403 MW; 69B76694FCC6846F CRC64;
MAHRKLQQEV DRVFKKINEG LEIFNSYYER HESCTNNPSQ KDKLESDLKR EVKKLQRLRE
QIKSWQSSPD IKDKDSLLDY RRSVEIAMEK YKAVEKASKE KAYSNISLKK SETLDPQERE
RRDISEYLSQ MIDELERQYD SLQVEIDKLL LLNKKKKTSS TTNDEKKEQY KRFQARYRWH
QQQMELALRL LANEELDPQD VKNVQDDINY FVESNQDPDF VEDETIYDGL NLQSNEAIAH
EVAQYFASQN AEDNNTSDAN ESLQDISKLS KKEQRKLERE AKKAAKLAAK NATGAAIPVA
GPSSTPSPVI PVADASKETE RSPSSSPIHN ATKPEEAVKT SIKSPRSSAD NLLPSLQKSP
SSATPETPTN VHTHIHQTPN GITGATTLKP ATLPAKPAGE LKWAVAASQA VEKDRKVTSA
SSTISNTSTK TPTTAAATTT SSNANSRIGS ALNTPKLSTS SLSLQPDNTG ASSSAATAAA
VLAAGAAAVH QNNQAFYRNM SSSHHPLVSL ATNPKSEHEV ATTVNQNGPE NTTKKVMEQK
EEESPEERNK LQVPTFGVFD DDFESDRDSE TEPEEEEQPS TPKYLSLEQR EAKTNEIKKE
FVSDFETLLL PSGVQEFIMS SELYNSQIES KITYKRSRDM CEISRLVEVP QGVNPPSPLD
AFRSTQQWDV MRCSLRDIII GSERLKEDSS SIYAKILENF RTLEMFSLFY NYYFAITPLE
REIAYKILNE RDWKVSKDGT MWFLRQGEVK FFNEICEVGD YKIFKLDDWT VIDKINFRLD
YSFLQPPVDT ASEVRDVSVD NNNVNDQSNV TLEQQKQEIS HGKQLLKQLK QGKISV
