NOT4_YEAST
ID NOT4_YEAST Reviewed; 587 AA.
AC P34909; D3DLX3;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=General negative regulator of transcription subunit 4;
DE AltName: Full=Modulator of transcription 2;
GN Name=MOT2; Synonyms=CCL1, NOT4, SIG1, SSF1; OrderedLocusNames=YER068W;
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=8039500; DOI=10.1002/j.1460-2075.1994.tb06604.x;
RA Leberer E., Dignard D., Harcus D., Whiteway M., Thomas D.Y.;
RT "Molecular characterization of SIG1, a Saccharomyces cerevisiae gene
RT involved in negative regulation of G-protein-mediated signal
RT transduction.";
RL EMBO J. 13:3050-3064(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=8164669; DOI=10.1128/mcb.14.5.3139-3149.1994;
RA Cade R.M., Errede B.;
RT "MOT2 encodes a negative regulator of gene expression that affects basal
RT expression of pheromone-responsive genes in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 14:3139-3149(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=8164670; DOI=10.1128/mcb.14.5.3150-3157.1994;
RA Irie K., Yamaguchi K., Kawase K., Matsumoto K.;
RT "The yeast MOT2 gene encodes a putative zinc finger protein that serves as
RT a global negative regulator affecting expression of several categories of
RT genes, including mating-pheromone-responsive genes.";
RL Mol. Cell. Biol. 14:3150-3157(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169868;
RA Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E.,
RA Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E.,
RA Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S.,
RA Hyman R.W., Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D.,
RA Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y.,
RA Botstein D., Davis R.W.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome V.";
RL Nature 387:78-81(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 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 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-310 AND SER-312, 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 [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-310; SER-312; THR-326 AND
RP SER-360, AND IDENTIFICATION BY MASS 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 [14]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-270, 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. In
CC the complex interacts with NOT1. The core complex probably is part of a
CC less characterized 1.9 MDa CCR4-NOT complex.
CC {ECO:0000269|PubMed:10490603, ECO:0000269|PubMed:11733989,
CC ECO:0000269|PubMed:9463387}.
CC -!- INTERACTION:
CC P34909; P53829: CAF40; NbExp=5; IntAct=EBI-12174, EBI-28306;
CC P34909; P31384: CCR4; NbExp=3; IntAct=EBI-12174, EBI-4396;
CC P34909; P06100: CDC36; NbExp=3; IntAct=EBI-12174, EBI-12153;
CC P34909; P25655: CDC39; NbExp=8; IntAct=EBI-12174, EBI-12139;
CC P34909; Q12514: NOT5; NbExp=3; IntAct=EBI-12174, EBI-12184;
CC P34909; P39008: POP2; NbExp=3; IntAct=EBI-12174, EBI-13629;
CC P34909; Q01939: RPT6; NbExp=2; IntAct=EBI-12174, EBI-13914;
CC P34909; P15731: UBC4; NbExp=2; IntAct=EBI-12174, EBI-19735;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus.
CC -!- MISCELLANEOUS: Present with 4280 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; M96736; AAC37413.1; -; Genomic_DNA.
DR EMBL; L26309; AAB00326.1; -; Unassigned_DNA.
DR EMBL; U18813; AAB64604.1; -; Genomic_DNA.
DR EMBL; BK006939; DAA07727.1; -; Genomic_DNA.
DR PIR; A56015; A56015.
DR RefSeq; NP_010991.3; NM_001178959.3.
DR PDB; 5AIE; X-ray; 2.80 A; A=30-83.
DR PDB; 5AJD; X-ray; 3.62 A; B/D/F/H/J/L=418-477.
DR PDBsum; 5AIE; -.
DR PDBsum; 5AJD; -.
DR AlphaFoldDB; P34909; -.
DR SMR; P34909; -.
DR BioGRID; 36811; 200.
DR ComplexPortal; CPX-1800; CCR4-NOT mRNA deadenylase complex.
DR DIP; DIP-2255N; -.
DR IntAct; P34909; 25.
DR MINT; P34909; -.
DR STRING; 4932.YER068W; -.
DR iPTMnet; P34909; -.
DR MaxQB; P34909; -.
DR PaxDb; P34909; -.
DR PRIDE; P34909; -.
DR EnsemblFungi; YER068W_mRNA; YER068W; YER068W.
DR GeneID; 856799; -.
DR KEGG; sce:YER068W; -.
DR SGD; S000000870; MOT2.
DR VEuPathDB; FungiDB:YER068W; -.
DR eggNOG; KOG2068; Eukaryota.
DR GeneTree; ENSGT00940000174608; -.
DR HOGENOM; CLU_028046_0_0_1; -.
DR InParanoid; P34909; -.
DR OMA; DSFNKRE; -.
DR BioCyc; YEAST:G3O-30242-MON; -.
DR PRO; PR:P34909; -.
DR Proteomes; UP000002311; Chromosome V.
DR RNAct; P34909; protein.
DR GO; GO:0030014; C:CCR4-NOT complex; IBA:GO_Central.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:SGD.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IBA:GO_Central.
DR GO; GO:0031087; P:deadenylation-independent decapping of nuclear-transcribed mRNA; IMP:SGD.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IC:ComplexPortal.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IDA:SGD.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IGI:SGD.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:SGD.
DR GO; GO:0016567; P:protein ubiquitination; IDA:SGD.
DR CDD; cd16618; mRING-HC-C4C4_CNOT4; 1.
DR CDD; cd12438; RRM_CNOT4; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR034261; CNOT4_RRM.
DR InterPro; IPR039780; Mot2.
DR InterPro; IPR039515; NOT4_mRING-HC-C4C4.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12603; PTHR12603; 1.
DR SMART; SM00361; RRM_1; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Coiled coil; Cytoplasm; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW RNA-binding; Transcription; Transcription regulation; Ubl conjugation;
KW Zinc; Zinc-finger.
FT CHAIN 1..587
FT /note="General negative regulator of transcription subunit
FT 4"
FT /id="PRO_0000081681"
FT DOMAIN 137..228
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT ZN_FING 33..78
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 229..256
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 370..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 94..128
FT /evidence="ECO:0000255"
FT COMPBIAS 370..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 310
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 326
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CROSSLNK 270
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT TURN 34..36
FT /evidence="ECO:0007829|PDB:5AIE"
FT TURN 42..46
FT /evidence="ECO:0007829|PDB:5AIE"
FT HELIX 58..66
FT /evidence="ECO:0007829|PDB:5AIE"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:5AIE"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:5AIE"
SQ SEQUENCE 587 AA; 65354 MW; 8847084BD9BF48B7 CRC64;
MMNPHVQENL QAIHNALSNF DTSFLSEDEE DYCPLCIEPM DITDKNFFPC PCGYQICQFC
YNNIRQNPEL NGRCPACRRK YDDENVRYVT LSPEELKMER AKLARKEKER KHREKERKEN
EYTNRKHLSG TRVIQKNLVY VVGINPPVPY EEVAPTLKSE KYFGQYGKIN KIVVNRKTPH
SNNTTSEHYH HHSPGYGVYI TFGSKDDAAR CIAQVDGTYM DGRLIKAAYG TTKYCSSYLR
GLPCPNPNCM FLHEPGEEAD SFNKRELHNK QQAQQQSGGT AFTRSGIHNN ISTSTAGSNT
NLLSENFTGT PSPAAMRAQL HHDSHTNAGT PVLTPAPVPA GSNPWGVTQS ATPVTSINLS
KNSSSINLPT LNDSLGHHTT PTTENTITST TTTTNTNATS HSHGSKKKQS LAAEEYKDPY
DALGNAVDFL DARLHSLSNY QKRPISIKSN IIDEETYKKY PSLFSWDKIE ASKKSDNTLA
NKLVEILAIK PIDYTASVVQ FLQSVNVGVN DNITITDNTK TPTQPIRLQT VSQQIQPPLN
VSTPPPGIFG PQHKVPIQQQ QMGDTSSRNS SDLLNQLING RKIIAGN
