CNOT8_HUMAN
ID CNOT8_HUMAN Reviewed; 292 AA.
AC Q9UFF9; B0AZS3; B2RAR8; B7Z8R1; D3DQI8; O95709; Q7Z521; Q9H6Y1;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=CCR4-NOT transcription complex subunit 8;
DE EC=3.1.13.4;
DE AltName: Full=CAF1-like protein;
DE Short=CALIFp;
DE AltName: Full=CAF2;
DE AltName: Full=CCR4-associated factor 8;
DE AltName: Full=Caf1b;
GN Name=CNOT8; Synonyms=CALIF, POP2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT PRO-32.
RX PubMed=10036195; DOI=10.1006/geno.1998.5687;
RA Fidler C., Wainscoat J.S., Boultwood J.;
RT "The human POP2 gene: identification, sequencing, and mapping to the
RT critical region of the 5q- syndrome.";
RL Genomics 56:134-136(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH CNOT1 AND
RP CNOT3.
RX PubMed=10637334; DOI=10.1093/nar/28.3.809;
RA Albert T.K., Lemaire M., van Berkum N.L., Gentz R., Collart M.A.,
RA Timmers H.T.M.;
RT "Isolation and characterization of human orthologs of yeast CCR4-NOT
RT complex subunits.";
RL Nucleic Acids Res. 28:809-817(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Jiang C.L., Yu L., Ding J.B., Ge H.P., He H., Zhao S.Y.;
RT "Cloning and characterization of a new human cDNA homologous to murine
RT mCAF1 mRNA.";
RL Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Brain, Colon, Liver, and Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
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 [10]
RP INTERACTION WITH BTG1 AND BTG2.
RX PubMed=11136725; DOI=10.1074/jbc.m008201200;
RA Prevot D., Morel A.P., Voeltzel T., Rostan M.C., Rimokh R., Magaud J.P.,
RA Corbo L.;
RT "Relationships of the antiproliferative proteins BTG1 and BTG2 with CAF1,
RT the human homolog of a component of the yeast CCR4 transcriptional complex:
RT involvement in estrogen receptor alpha signaling pathway.";
RL J. Biol. Chem. 276:9640-9648(2001).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BTG2.
RX PubMed=12771185; DOI=10.1242/jcs.00480;
RA Morel A.-P., Sentis S., Bianchin C., Le Romancer M., Jonard L.,
RA Rostan M.-C., Rimokh R., Corbo L.;
RT "BTG2 antiproliferative protein interacts with the human CCR4 complex
RT existing in vivo in three cell-cycle-regulated forms.";
RL J. Cell Sci. 116:2929-2936(2003).
RN [12]
RP CATALYTIC ACTIVITY.
RX PubMed=15769875; DOI=10.1261/rna.7135305;
RA Bianchin C., Mauxion F., Sentis S., Seraphin B., Corbo L.;
RT "Conservation of the deadenylase activity of proteins of the Caf1 family in
RT human.";
RL RNA 11:487-494(2005).
RN [13]
RP IDENTIFICATION IN THE CCR4-NOT COMPLEX, AND COMPOSITION OF THE CCR4-NOT
RP COMPLEX.
RX PubMed=19558367; DOI=10.1042/bj20090500;
RA Lau N.C., Kolkman A., van Schaik F.M., Mulder K.W., Pijnappel W.W.,
RA Heck A.J., Timmers H.T.;
RT "Human Ccr4-Not complexes contain variable deadenylase subunits.";
RL Biochem. J. 422:443-453(2009).
RN [14]
RP FUNCTION.
RX PubMed=19605561; DOI=10.1091/mbc.e09-02-0146;
RA Aslam A., Mittal S., Koch F., Andrau J.C., Winkler G.S.;
RT "The Ccr4-NOT deadenylase subunits CNOT7 and CNOT8 have overlapping roles
RT and modulate cell proliferation.";
RL Mol. Biol. Cell 20:3840-3850(2009).
RN [15]
RP FUNCTION, AND MUTAGENESIS OF ASP-40 AND GLU-42.
RX PubMed=20065043; DOI=10.1128/mcb.01481-09;
RA Piao X., Zhang X., Wu L., Belasco J.G.;
RT "CCR4-NOT deadenylates mRNA associated with complexes in human cells.";
RL Mol. Cell. Biol. 30:1486-1494(2010).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP FUNCTION, AND INTERACTION WITH TOB1 AND BTG2.
RX PubMed=23236473; DOI=10.1371/journal.pone.0051331;
RA Doidge R., Mittal S., Aslam A., Winkler G.S.;
RT "The anti-proliferative activity of BTG/TOB proteins is mediated via the
RT Caf1a (CNOT7) and Caf1b (CNOT8) deadenylase subunits of the Ccr4-not
RT complex.";
RL PLoS ONE 7:E51331-E51331(2012).
CC -!- FUNCTION: Has 3'-5' poly(A) exoribonuclease activity for synthetic
CC poly(A) RNA substrate. Its function seems to be partially redundant
CC with that of CNOT7. Catalytic component of the CCR4-NOT complex which
CC is linked to various cellular processes including bulk mRNA
CC degradation, miRNA-mediated repression, translational repression during
CC translational initiation and general transcription regulation. During
CC miRNA-mediated repression the complex seems also to act as
CC translational repressor during translational initiation. Additional
CC complex functions may be a consequence of its influence on mRNA
CC expression. Associates with members of the BTG family such as TOB1 and
CC BTG2 and is required for their anti-proliferative activity.
CC {ECO:0000269|PubMed:12771185, ECO:0000269|PubMed:19605561,
CC ECO:0000269|PubMed:20065043, ECO:0000269|PubMed:23236473}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4;
CC Evidence={ECO:0000269|PubMed:15769875};
CC -!- SUBUNIT: Component of the CCR4-NOT complex; distinct complexes seem to
CC exist that differ in the participation of probably mutually exclusive
CC catalytic subunits; the complex contains two deadenylase subunits,
CC CNOT6 or CNOT6L, and CNOT7 or CNOT8. In the complex interacts directly
CC with CNOT1. Interacts with BTG1, BTG2 and TOB1. Interacts with BTG4 (By
CC similarity). {ECO:0000250|UniProtKB:Q9D8X5,
CC ECO:0000269|PubMed:10637334, ECO:0000269|PubMed:11136725,
CC ECO:0000269|PubMed:12771185, ECO:0000269|PubMed:19558367,
CC ECO:0000269|PubMed:23236473}.
CC -!- INTERACTION:
CC Q9UFF9; P62324: BTG1; NbExp=6; IntAct=EBI-742299, EBI-742279;
CC Q9UFF9; Q6IBC8: BTG1; NbExp=3; IntAct=EBI-742299, EBI-10250021;
CC Q9UFF9; P78543: BTG2; NbExp=5; IntAct=EBI-742299, EBI-1047576;
CC Q9UFF9; A5YKK6: CNOT1; NbExp=6; IntAct=EBI-742299, EBI-1222758;
CC Q9UFF9; Q9NZN8: CNOT2; NbExp=3; IntAct=EBI-742299, EBI-743033;
CC Q9UFF9; O75175: CNOT3; NbExp=3; IntAct=EBI-742299, EBI-743073;
CC Q9UFF9; Q9ULM6: CNOT6; NbExp=2; IntAct=EBI-742299, EBI-2104530;
CC Q9UFF9; Q96LI5: CNOT6L; NbExp=4; IntAct=EBI-742299, EBI-1046635;
CC Q9UFF9; Q86TB9: PATL1; NbExp=3; IntAct=EBI-742299, EBI-2562092;
CC Q9UFF9; Q14106: TOB2; NbExp=3; IntAct=EBI-742299, EBI-2562000;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12771185}. Nucleus
CC {ECO:0000269|PubMed:12771185}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9UFF9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UFF9-2; Sequence=VSP_055527;
CC Name=3;
CC IsoId=Q9UFF9-3; Sequence=VSP_055528;
CC -!- SIMILARITY: Belongs to the CAF1 family. {ECO:0000305}.
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DR EMBL; AF053318; AAD02685.1; -; mRNA.
DR EMBL; AF180476; AAF29830.1; -; mRNA.
DR EMBL; AF087844; AAP97157.1; -; mRNA.
DR EMBL; AL122045; CAB59181.1; -; mRNA.
DR EMBL; BT006857; AAP35503.1; -; mRNA.
DR EMBL; AK025358; BAB15119.1; -; mRNA.
DR EMBL; AK315864; BAF98755.1; -; mRNA.
DR EMBL; AK297381; BAH12567.1; -; mRNA.
DR EMBL; AK303775; BAH14047.1; -; mRNA.
DR EMBL; AK314317; BAG36965.1; -; mRNA.
DR EMBL; AK316221; BAH14592.1; -; mRNA.
DR EMBL; AK316269; BAH14640.1; -; mRNA.
DR EMBL; AC112169; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW61625.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61626.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61627.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW61628.1; -; Genomic_DNA.
DR EMBL; BC017366; AAH17366.1; -; mRNA.
DR CCDS; CCDS4329.1; -. [Q9UFF9-1]
DR CCDS; CCDS75361.1; -. [Q9UFF9-3]
DR CCDS; CCDS78074.1; -. [Q9UFF9-2]
DR PIR; T34529; T34529.
DR PIR; T52257; T52257.
DR RefSeq; NP_001288002.1; NM_001301073.1. [Q9UFF9-1]
DR RefSeq; NP_001288003.1; NM_001301074.1. [Q9UFF9-3]
DR RefSeq; NP_001288004.1; NM_001301075.1. [Q9UFF9-2]
DR RefSeq; NP_001288006.1; NM_001301077.1. [Q9UFF9-2]
DR RefSeq; NP_001288009.1; NM_001301080.1. [Q9UFF9-2]
DR RefSeq; NP_001288011.1; NM_001301082.1. [Q9UFF9-2]
DR RefSeq; NP_001288012.1; NM_001301083.1. [Q9UFF9-2]
DR RefSeq; NP_001288015.1; NM_001301086.1.
DR RefSeq; NP_004770.4; NM_004779.5. [Q9UFF9-1]
DR RefSeq; XP_005268584.1; XM_005268527.2. [Q9UFF9-3]
DR RefSeq; XP_011536008.1; XM_011537706.1. [Q9UFF9-2]
DR RefSeq; XP_011536010.1; XM_011537708.2. [Q9UFF9-2]
DR RefSeq; XP_016865537.1; XM_017010048.1. [Q9UFF9-1]
DR RefSeq; XP_016865538.1; XM_017010049.1. [Q9UFF9-1]
DR RefSeq; XP_016865539.1; XM_017010050.1. [Q9UFF9-1]
DR RefSeq; XP_016865540.1; XM_017010051.1. [Q9UFF9-1]
DR RefSeq; XP_016865541.1; XM_017010052.1. [Q9UFF9-3]
DR RefSeq; XP_016865542.1; XM_017010053.1. [Q9UFF9-3]
DR RefSeq; XP_016865543.1; XM_017010054.1. [Q9UFF9-3]
DR RefSeq; XP_016865544.1; XM_017010055.1. [Q9UFF9-3]
DR RefSeq; XP_016865545.1; XM_017010056.1. [Q9UFF9-3]
DR RefSeq; XP_016865546.1; XM_017010057.1. [Q9UFF9-2]
DR AlphaFoldDB; Q9UFF9; -.
DR SMR; Q9UFF9; -.
DR BioGRID; 114744; 74.
DR ComplexPortal; CPX-2535; CCR4-NOT mRNA deadenylase complex, CNOT6L-CNOT8 variant.
DR ComplexPortal; CPX-2849; CCR4-NOT mRNA deadenylase complex, CNOT6-CNOT8 variant.
DR CORUM; Q9UFF9; -.
DR DIP; DIP-29084N; -.
DR IntAct; Q9UFF9; 37.
DR MINT; Q9UFF9; -.
DR STRING; 9606.ENSP00000430493; -.
DR iPTMnet; Q9UFF9; -.
DR PhosphoSitePlus; Q9UFF9; -.
DR BioMuta; CNOT8; -.
DR DMDM; 15213949; -.
DR EPD; Q9UFF9; -.
DR jPOST; Q9UFF9; -.
DR MassIVE; Q9UFF9; -.
DR MaxQB; Q9UFF9; -.
DR PaxDb; Q9UFF9; -.
DR PeptideAtlas; Q9UFF9; -.
DR PRIDE; Q9UFF9; -.
DR ProteomicsDB; 2533; -.
DR ProteomicsDB; 6971; -.
DR ProteomicsDB; 84181; -. [Q9UFF9-1]
DR Antibodypedia; 28328; 281 antibodies from 28 providers.
DR DNASU; 9337; -.
DR Ensembl; ENST00000285896.11; ENSP00000285896.6; ENSG00000155508.14. [Q9UFF9-1]
DR Ensembl; ENST00000403027.6; ENSP00000384747.2; ENSG00000155508.14. [Q9UFF9-1]
DR Ensembl; ENST00000517876.5; ENSP00000430493.1; ENSG00000155508.14. [Q9UFF9-1]
DR Ensembl; ENST00000519404.5; ENSP00000430833.1; ENSG00000155508.14. [Q9UFF9-3]
DR Ensembl; ENST00000520671.5; ENSP00000428305.1; ENSG00000155508.14. [Q9UFF9-2]
DR Ensembl; ENST00000521450.5; ENSP00000431034.1; ENSG00000155508.14. [Q9UFF9-2]
DR Ensembl; ENST00000521583.5; ENSP00000429882.1; ENSG00000155508.14. [Q9UFF9-2]
DR Ensembl; ENST00000523698.5; ENSP00000428565.1; ENSG00000155508.14. [Q9UFF9-2]
DR GeneID; 9337; -.
DR KEGG; hsa:9337; -.
DR MANE-Select; ENST00000285896.11; ENSP00000285896.6; NM_001301073.2; NP_001288002.1.
DR UCSC; uc003lvu.4; human. [Q9UFF9-1]
DR CTD; 9337; -.
DR DisGeNET; 9337; -.
DR GeneCards; CNOT8; -.
DR HGNC; HGNC:9207; CNOT8.
DR HPA; ENSG00000155508; Low tissue specificity.
DR MIM; 603731; gene.
DR neXtProt; NX_Q9UFF9; -.
DR OpenTargets; ENSG00000155508; -.
DR PharmGKB; PA26679; -.
DR VEuPathDB; HostDB:ENSG00000155508; -.
DR eggNOG; KOG0304; Eukaryota.
DR GeneTree; ENSGT00390000000080; -.
DR HOGENOM; CLU_124749_0_0_1; -.
DR InParanoid; Q9UFF9; -.
DR OMA; HIREVWS; -.
DR OrthoDB; 931256at2759; -.
DR PhylomeDB; Q9UFF9; -.
DR TreeFam; TF314185; -.
DR PathwayCommons; Q9UFF9; -.
DR Reactome; R-HSA-429947; Deadenylation of mRNA.
DR Reactome; R-HSA-6804115; TP53 regulates transcription of additional cell cycle genes whose exact role in the p53 pathway remain uncertain.
DR SignaLink; Q9UFF9; -.
DR SIGNOR; Q9UFF9; -.
DR BioGRID-ORCS; 9337; 18 hits in 1082 CRISPR screens.
DR ChiTaRS; CNOT8; human.
DR GeneWiki; CNOT8; -.
DR GenomeRNAi; 9337; -.
DR Pharos; Q9UFF9; Tbio.
DR PRO; PR:Q9UFF9; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9UFF9; protein.
DR Bgee; ENSG00000155508; Expressed in secondary oocyte and 207 other tissues.
DR ExpressionAtlas; Q9UFF9; baseline and differential.
DR Genevisible; Q9UFF9; HS.
DR GO; GO:0030014; C:CCR4-NOT complex; IDA:UniProtKB.
DR GO; GO:0030015; C:CCR4-NOT core complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:GO_Central.
DR GO; GO:0000932; C:P-body; IBA:GO_Central.
DR GO; GO:0000175; F:3'-5'-exoribonuclease activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0043928; P:exonucleolytic catabolism of deadenylated mRNA; IDA:UniProtKB.
DR GO; GO:0035195; P:miRNA-mediated gene silencing; TAS:UniProtKB.
DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IC:ComplexPortal.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0061014; P:positive regulation of mRNA catabolic process; IMP:BHF-UCL.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 3.30.420.10; -; 1.
DR InterPro; IPR039637; CNOT7/CNOT8/Pop2.
DR InterPro; IPR027212; Cnot8.
DR InterPro; IPR006941; RNase_CAF1.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR10797; PTHR10797; 1.
DR PANTHER; PTHR10797:SF1; PTHR10797:SF1; 1.
DR Pfam; PF04857; CAF1; 2.
DR SUPFAM; SSF53098; SSF53098; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Exonuclease; Hydrolase; Metal-binding;
KW Nuclease; Nucleus; Reference proteome; Repressor; RNA-binding;
KW RNA-mediated gene silencing; Transcription; Transcription regulation;
KW Translation regulation.
FT CHAIN 1..292
FT /note="CCR4-NOT transcription complex subunit 8"
FT /id="PRO_0000212846"
FT BINDING 40
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 40
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 42
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 161
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..106
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055527"
FT VAR_SEQ 105..158
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055528"
FT VARIANT 32
FT /note="L -> P (in dbSNP:rs1139980)"
FT /evidence="ECO:0000269|PubMed:10036195"
FT /id="VAR_048751"
FT MUTAGEN 40
FT /note="D->A: Impairs deadenylation and decay of mRNAi-
FT targeted mRNA; when associated with A-42."
FT /evidence="ECO:0000269|PubMed:20065043"
FT MUTAGEN 42
FT /note="E->A: Impairs deadenylation and decay of mRNAi-
FT targeted mRNA; when associated with A-40."
FT /evidence="ECO:0000269|PubMed:20065043"
FT CONFLICT 99..105
FT /note="FKFNLTE -> CKLYLTV (in Ref. 3; AAP97157)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="K -> R (in Ref. 5; BAB15119)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="F -> L (in Ref. 1; AAD02685)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="F -> S (in Ref. 1; AAD02685)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 292 AA; 33540 MW; 81027A966E51AFDB CRC64;
MPAALVENSQ VICEVWASNL EEEMRKIREI VLSYSYIAMD TEFPGVVVRP IGEFRSSIDY
QYQLLRCNVD LLKIIQLGLT FTNEKGEYPS GINTWQFNFK FNLTEDMYSQ DSIDLLANSG
LQFQKHEEEG IDTLHFAELL MTSGVVLCDN VKWLSFHSGY DFGYMVKLLT DSRLPEEEHE
FFHILNLFFP SIYDVKYLMK SCKNLKGGLQ EVADQLDLQR IGRQHQAGSD SLLTGMAFFR
MKELFFEDSI DDAKYCGRLY GLGTGVAQKQ NEDVDSAQEK MSILAIINNM QQ
