CNOT9_MOUSE
ID CNOT9_MOUSE Reviewed; 299 AA.
AC Q9JKY0;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=CCR4-NOT transcription complex subunit 9 {ECO:0000312|MGI:MGI:1928902};
DE AltName: Full=Cell differentiation protein RQCD1 homolog;
DE Short=Rcd-1;
DE AltName: Full=EPO-induced protein FL10;
GN Name=Cnot9 {ECO:0000312|MGI:MGI:1928902}; Synonyms=Rcd1, Rqcd1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Erythroleukemia;
RX PubMed=10880228; DOI=10.1006/cyto.2000.0686;
RA Gregory R.C. Jr., Lord K.A., Panek L.B., Gaines P., Dillon S.B.,
RA Wojchowski D.M.;
RT "Subtraction cloning and initial characterization of novel EPO-immediate
RT response genes.";
RL Cytokine 12:845-857(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, INDUCTION, IDENTIFICATION IN A COMPLEX WITH ATF2 BOUND TO TARGET
RP DNA, AND INTERACTION WITH ATF2; RARA; RARB; RARG; RXRA; RXRB AND RXRG.
RX PubMed=12356739; DOI=10.1093/emboj/cdf521;
RA Hiroi N., Ito T., Yamamoto H., Ochiya T., Jinno S., Okayama H.;
RT "Mammalian Rcd1 is a novel transcriptional cofactor that mediates retinoic
RT acid-induced cell differentiation.";
RL EMBO J. 21:5235-5244(2002).
RN [5]
RP FUNCTION, INTERACTION WITH MYB, INDUCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15209511; DOI=10.1021/bi035857y;
RA Haas M., Siegert M., Schuermann A., Sodeik B., Wolfes H.;
RT "c-Myb protein interacts with Rcd-1, a component of the CCR4 transcription
RT mediator complex.";
RL Biochemistry 43:8152-8159(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH NANOS2.
RX PubMed=20133598; DOI=10.1073/pnas.0908664107;
RA Suzuki A., Igarashi K., Aisaki K., Kanno J., Saga Y.;
RT "NANOS2 interacts with the CCR4-NOT deadenylation complex and leads to
RT suppression of specific RNAs.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:3594-3599(2010).
CC -!- FUNCTION: Component of the CCR4-NOT complex which is one of the major
CC cellular mRNA deadenylases and is linked to various cellular processes
CC including bulk mRNA degradation, miRNA-mediated repression,
CC translational repression during translational initiation and general
CC transcription regulation. Additional complex functions may be a
CC consequence of its influence on mRNA expression. Involved in down-
CC regulation of MYB- and JUN-dependent transcription. May play a role in
CC cell differentiation. Required for retinoic acid-induced
CC differentiation of F9 teratocarcinoma cells. Does not bind DNA by
CC itself. Enhances ligand-dependent transcriptional activity of nuclear
CC hormone receptors. May play a role in cell differentiation.
CC {ECO:0000269|PubMed:12356739, ECO:0000269|PubMed:15209511}.
CC -!- SUBUNIT: Homodimer. Component of the CCR4-NOT complex; distinct
CC complexes seem to exist that differ in the participation of probably
CC mutually exclusive catalytic subunits. Interacts with MYB, ATF2, RARA,
CC RARB, RARG, RXRA, RXRB and RXRG. Identified in a complex with ATF2
CC bound to target DNA. Interacts with NANOS2. Directly interacts with
CC ZNF335 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15209511}. Cytoplasm,
CC P-body {ECO:0000269|PubMed:20133598}. Note=NANOS2 promotes its
CC localization to P-body. {ECO:0000269|PubMed:20133598}.
CC -!- TISSUE SPECIFICITY: Detected at low levels in bone marrow and thymus.
CC {ECO:0000269|PubMed:10880228}.
CC -!- INDUCTION: Up-regulated by EPO and EGF. Transiently up-regulated by
CC retinoic acid in F9 teratocarcinoma cells.
CC {ECO:0000269|PubMed:10880228, ECO:0000269|PubMed:12356739,
CC ECO:0000269|PubMed:15209511}.
CC -!- SIMILARITY: Belongs to the CNOT9 family. {ECO:0000305}.
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DR EMBL; AF221849; AAF61701.1; -; mRNA.
DR EMBL; AK005025; BAB23752.1; -; mRNA.
DR EMBL; BC050898; AAH50898.1; -; mRNA.
DR EMBL; BC051948; AAH51948.1; -; mRNA.
DR CCDS; CCDS35615.1; -.
DR RefSeq; NP_067358.1; NM_021383.5.
DR AlphaFoldDB; Q9JKY0; -.
DR SMR; Q9JKY0; -.
DR BioGRID; 208377; 4.
DR DIP; DIP-34266N; -.
DR IntAct; Q9JKY0; 7.
DR MINT; Q9JKY0; -.
DR STRING; 10090.ENSMUSP00000084466; -.
DR PhosphoSitePlus; Q9JKY0; -.
DR EPD; Q9JKY0; -.
DR MaxQB; Q9JKY0; -.
DR PaxDb; Q9JKY0; -.
DR PeptideAtlas; Q9JKY0; -.
DR PRIDE; Q9JKY0; -.
DR ProteomicsDB; 279125; -.
DR Antibodypedia; 51420; 127 antibodies from 24 providers.
DR DNASU; 58184; -.
DR Ensembl; ENSMUST00000087215; ENSMUSP00000084466; ENSMUSG00000026174.
DR GeneID; 58184; -.
DR KEGG; mmu:58184; -.
DR UCSC; uc007bmf.2; mouse.
DR CTD; 9125; -.
DR MGI; MGI:1928902; Cnot9.
DR VEuPathDB; HostDB:ENSMUSG00000026174; -.
DR eggNOG; KOG3036; Eukaryota.
DR GeneTree; ENSGT00390000001225; -.
DR HOGENOM; CLU_039962_2_0_1; -.
DR InParanoid; Q9JKY0; -.
DR OMA; SAWMHQQ; -.
DR OrthoDB; 1129961at2759; -.
DR PhylomeDB; Q9JKY0; -.
DR TreeFam; TF105734; -.
DR Reactome; R-MMU-429947; Deadenylation of mRNA.
DR Reactome; R-MMU-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
DR BioGRID-ORCS; 58184; 14 hits in 71 CRISPR screens.
DR ChiTaRS; Cnot9; mouse.
DR PRO; PR:Q9JKY0; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9JKY0; protein.
DR Bgee; ENSMUSG00000026174; Expressed in dorsal pancreas and 260 other tissues.
DR Genevisible; Q9JKY0; MM.
DR GO; GO:0030014; C:CCR4-NOT complex; ISS:UniProtKB.
DR GO; GO:0030015; C:CCR4-NOT core complex; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005154; F:epidermal growth factor receptor binding; ISO:MGI.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISS:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IDA:MGI.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:InterPro.
DR GO; GO:0033147; P:negative regulation of intracellular estrogen receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; IBA:GO_Central.
DR GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; ISO:MGI.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:MGI.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR007216; CNOT9.
DR PANTHER; PTHR12262:SF0; PTHR12262:SF0; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Cytoplasm; Nucleus; Reference proteome; Repressor;
KW RNA-mediated gene silencing; Transcription; Transcription regulation;
KW Translation regulation.
FT CHAIN 1..299
FT /note="CCR4-NOT transcription complex subunit 9"
FT /id="PRO_0000327227"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q92600"
SQ SEQUENCE 299 AA; 33601 MW; A4CA5DBE2E88DDA3 CRC64;
MHSLATAAPV PTALAQVDRE KIYQWINELS SPETRENALL ELSKKRESVP DLAPMLWHSF
GTIAALLQEI VNIYPSINPP TLTAHQSNRV CNALALLQCV ASHPETRSAF LAAHIPLFLY
PFLHTVSKTR PFEYLRLTSL GVIGALVKTD EQEVINFLLT TEIIPLCLRI MESGSELSKT
VATFILQKIL LDDTGLAYIC QTYERFSHVA MILGKMVLQL SKEPSARLLK HVVRCYLRLS
DNPRAREALR QCLPDQLKDT TFAQVLKDDT TTKRWLAQLV KNLQEGQVTD PRGIPLPPQ
