NOT5_YEAST
ID NOT5_YEAST Reviewed; 560 AA.
AC Q12514; D6W476;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=General negative regulator of transcription subunit 5;
GN Name=NOT5; OrderedLocusNames=YPR072W; ORFNames=YP9499.27;
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].
RC STRAIN=ATCC 204511 / S288c / AB972;
RA Couch J.;
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(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=9511744; DOI=10.1016/s0378-1119(97)00605-7;
RA Oberholzer U., Collart M.A.;
RT "Characterization of NOT5 that encodes a new component of the Not protein
RT complex.";
RL Gene 207:61-69(1998).
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 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 [8]
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 [9]
RP INTERACTION WITH NOT2.
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 [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-306 AND SER-377, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-377, AND IDENTIFICATION BY
RP 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-306 AND SER-377, AND
RP 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-338, 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 and NOT2. 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 Q12514; P53829: CAF40; NbExp=3; IntAct=EBI-12184, EBI-28306;
CC Q12514; P06100: CDC36; NbExp=6; IntAct=EBI-12184, EBI-12153;
CC Q12514; P25655: CDC39; NbExp=6; IntAct=EBI-12184, EBI-12139;
CC Q12514; P34909: MOT2; NbExp=3; IntAct=EBI-12184, EBI-12174;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus.
CC -!- MISCELLANEOUS: Present with 5110 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the CNOT2/3/5 family. {ECO:0000305}.
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DR EMBL; U51033; AAB68123.1; -; Genomic_DNA.
DR EMBL; Z71255; CAA94980.1; -; Genomic_DNA.
DR EMBL; Z49219; CAA89189.1; -; Genomic_DNA.
DR EMBL; AY692887; AAT92906.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11492.1; -; Genomic_DNA.
DR PIR; S54093; S54093.
DR RefSeq; NP_015397.1; NM_001184169.1.
DR PDB; 4BY6; X-ray; 2.80 A; C/F=299-560.
DR PDB; 6TB3; EM; 2.80 A; BW=2-113.
DR PDBsum; 4BY6; -.
DR PDBsum; 6TB3; -.
DR AlphaFoldDB; Q12514; -.
DR SMR; Q12514; -.
DR BioGRID; 36245; 78.
DR ComplexPortal; CPX-1800; CCR4-NOT mRNA deadenylase complex.
DR DIP; DIP-2257N; -.
DR IntAct; Q12514; 24.
DR MINT; Q12514; -.
DR STRING; 4932.YPR072W; -.
DR iPTMnet; Q12514; -.
DR MaxQB; Q12514; -.
DR PaxDb; Q12514; -.
DR PRIDE; Q12514; -.
DR EnsemblFungi; YPR072W_mRNA; YPR072W; YPR072W.
DR GeneID; 856186; -.
DR KEGG; sce:YPR072W; -.
DR SGD; S000006276; NOT5.
DR VEuPathDB; FungiDB:YPR072W; -.
DR eggNOG; KOG2150; Eukaryota.
DR GeneTree; ENSGT00390000014743; -.
DR HOGENOM; CLU_013819_3_0_1; -.
DR InParanoid; Q12514; -.
DR OMA; YHYQGTY; -.
DR BioCyc; YEAST:G3O-34219-MON; -.
DR PRO; PR:Q12514; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12514; 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:0031087; P:deadenylation-independent 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 GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; 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; 2.
DR PIRSF; PIRSF005290; NOT_su_3_5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Coiled coil; Cytoplasm; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..560
FT /note="General negative regulator of transcription subunit
FT 5"
FT /id="PRO_0000198338"
FT REGION 212..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 3..26
FT /evidence="ECO:0000255"
FT COILED 37..71
FT /evidence="ECO:0000255"
FT COILED 124..177
FT /evidence="ECO:0000255"
FT COMPBIAS 212..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..290
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 306
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT CROSSLNK 338
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
FT TURN 348..351
FT /evidence="ECO:0007829|PDB:4BY6"
FT HELIX 353..355
FT /evidence="ECO:0007829|PDB:4BY6"
FT HELIX 356..364
FT /evidence="ECO:0007829|PDB:4BY6"
FT HELIX 367..370
FT /evidence="ECO:0007829|PDB:4BY6"
FT HELIX 378..389
FT /evidence="ECO:0007829|PDB:4BY6"
FT HELIX 394..397
FT /evidence="ECO:0007829|PDB:4BY6"
FT TURN 459..462
FT /evidence="ECO:0007829|PDB:4BY6"
FT HELIX 464..469
FT /evidence="ECO:0007829|PDB:4BY6"
FT HELIX 474..483
FT /evidence="ECO:0007829|PDB:4BY6"
FT HELIX 488..501
FT /evidence="ECO:0007829|PDB:4BY6"
FT STRAND 504..506
FT /evidence="ECO:0007829|PDB:4BY6"
FT TURN 507..509
FT /evidence="ECO:0007829|PDB:4BY6"
FT STRAND 512..515
FT /evidence="ECO:0007829|PDB:4BY6"
FT STRAND 532..535
FT /evidence="ECO:0007829|PDB:4BY6"
FT TURN 537..540
FT /evidence="ECO:0007829|PDB:4BY6"
FT STRAND 542..545
FT /evidence="ECO:0007829|PDB:4BY6"
FT HELIX 554..556
FT /evidence="ECO:0007829|PDB:4BY6"
SQ SEQUENCE 560 AA; 65855 MW; 073137119B3E92BC CRC64;
MSQRKLQQDI DKLLKKVKEG IEDFDDIYEK FQSTDPSNSS HREKLESDLK REIKKLQKHR
DQIKTWLSKE DVKDKQSVLM TNRRLIENGM ERFKSVEKLM KTKQFSKEAL TNPDIIKDPK
ELKKRDQVLF IHDCLDELQK QLEQYEAQEN EEQTERHEFH IANLENILKK LQNNEMDPEP
VEEFQDDIKY YVENNDDPDF IEYDTIYEDM GCEIQPSSSN NEAPKEGNNQ TSLSSIRSSK
KQERSPKKKA PQRDVSISDR ATTPIAPGVE SASQSISSTP TPVSTDTPLH TVKDDSIKFD
NSTLGTPTTH VSMKKKESEN DSEQQLNFPP DRTDEIRKTI QHDVETNAAF QNPLFNDELK
YWLDSKRYLM QPLQEMSPKM VSQLESSLLN CPDSLDADSP CLYTKPLSLP HPTSIFFPNE
PIRFVYPYDV PLNLTNNEND TDNKFGKDSK AKSKKDDDIY SRTSLARIFM KFDLDTLFFI
FYHYQGSYEQ FLAARELFKN RNWLFNKVDR CWYYKEIEKL PPGMGKSEEE SWRYFDYKKS
WLARRCGNDF VYNEEDFEKL
