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NOT2_YEAST
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   03-AUG-2022, entry version 177.
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;
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 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. 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; P25655: CDC39; NbExp=7; IntAct=EBI-12153, EBI-12139;
CC       P06100; P34909: MOT2; NbExp=3; IntAct=EBI-12153, EBI-12174;
CC       P06100; P06102: NOT3; NbExp=2; IntAct=EBI-12153, EBI-12165;
CC       P06100; Q12514: NOT5; NbExp=6; 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}.
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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   PDBsum; 4BY6; -.
DR   AlphaFoldDB; P06100; -.
DR   SMR; P06100; -.
DR   BioGRID; 31900; 236.
DR   ComplexPortal; CPX-1800; CCR4-NOT mRNA deadenylase complex.
DR   DIP; DIP-590N; -.
DR   IntAct; P06100; 24.
DR   MINT; P06100; -.
DR   STRING; 4932.YDL165W; -.
DR   MaxQB; P06100; -.
DR   PaxDb; P06100; -.
DR   PRIDE; P06100; -.
DR   EnsemblFungi; YDL165W_mRNA; YDL165W; YDL165W.
DR   GeneID; 851389; -.
DR   KEGG; sce:YDL165W; -.
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   BioCyc; YEAST:G3O-29557-MON; -.
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 from RNA polymerase II promoter; IDA:SGD.
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 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; IPR040168; Not2/3/5.
DR   InterPro; IPR007282; NOT2/3/5_C.
DR   PANTHER; PTHR23326; PTHR23326; 1.
DR   Pfam; PF04153; NOT2_3_5; 1.
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
 
 
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