ID CNOT2_HUMAN Reviewed; 540 AA. AC Q9NZN8; Q9H3E0; Q9NSX5; Q9NWR6; Q9P028; DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 192. DE RecName: Full=CCR4-NOT transcription complex subunit 2; DE AltName: Full=CCR4-associated factor 2; GN Name=CNOT2; Synonyms=CDC36, NOT2; ORFNames=HSPC131, MSTP046; 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), INTERACTION WITH CNOT1, AND TISSUE RP SPECIFICITY. 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Heart; RA Liu B., Liu Y.Q., Wang X.Y., Zhao B., Sheng H., Zhao X.W., Liu S., Xu Y.Y., RA Ye J., Song L., Gao Y., Zhang C.L., Zhang J., Wei Y.J., Cao H.Q., Zhao Y., RA Liu L.S., Ding J.F., Gao R.L., Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C., RA Zhao M.S., Hui R.T.; RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Umbilical cord blood; RX PubMed=11042152; DOI=10.1101/gr.140200; RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.; RT "Cloning and functional analysis of cDNAs with open reading frames for 300 RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor RT cells."; RL Genome Res. 10:1546-1560(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4). RC TISSUE=Fetal kidney, and Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lymph, and Skin; 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 [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-377. RA Bi A., Yu L., Zhang M., Fan Y., Zhang Q., Zhao Y., Gao J., Zhao S.; RT "Separation and molecular cloning of a novel human cDNA fragment coding a RT protein without homologs."; RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases. RN [8] RP FUNCTION, AND DOMAIN. RX PubMed=14707134; DOI=10.1074/jbc.m311747200; RA Zwartjes C.G., Jayne S., van den Berg D.L., Timmers H.T.; RT "Repression of promoter activity by CNOT2, a subunit of the transcription RT regulatory Ccr4-not complex."; RL J. Biol. Chem. 279:10848-10854(2004). RN [9] RP FUNCTION, AND INTERACTION WITH NCOR1; NCOR2; HDAC3 AND GPS2. RX PubMed=16712523; DOI=10.1042/bj20060406; RA Jayne S., Zwartjes C.G., van Schaik F.M., Timmers H.T.; RT "Involvement of the SMRT/NCoR-HDAC3 complex in transcriptional repression RT by the CNOT2 subunit of the human Ccr4-Not complex."; RL Biochem. J. 398:461-467(2006). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the RT kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-93; SER-126 AND SER-165, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(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, INTERACTION WITH CNOT3, AND SUBCELLULAR LOCATION. RX PubMed=21299754; DOI=10.1111/j.1365-2443.2011.01492.x; RA Ito K., Inoue T., Yokoyama K., Morita M., Suzuki T., Yamamoto T.; RT "CNOT2 depletion disrupts and inhibits the CCR4-NOT deadenylase complex and RT induces apoptotic cell death."; RL Genes Cells 16:368-379(2011). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [19] RP FUNCTION, AND DEVELOPMENTAL STAGE. RX PubMed=22367759; DOI=10.1002/stem.1070; RA Zheng X., Dumitru R., Lackford B.L., Freudenberg J.M., Singh A.P., RA Archer T.K., Jothi R., Hu G.; RT "Cnot1, Cnot2, and Cnot3 maintain mouse and human ESC identity and inhibit RT extraembryonic differentiation."; RL Stem Cells 30:910-922(2012). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165 AND SER-242, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-165 AND SER-274, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [22] RP INVOLVEMENT IN IDNADFS. RX PubMed=31145527; DOI=10.1002/ajmg.a.61217; RA Alesi V., Loddo S., Cali F., Orlando V., Genovese S., Ferretti D., RA Calacci C., Calvieri G., Falasca R., Ulgheri L., Drago F., Dallapiccola B., RA Baban A., Novelli A.; RT "A heterozygous, intragenic deletion of CNOT2 recapitulates the phenotype RT of 12q15 deletion syndrome."; RL Am. J. Med. Genet. A 179:1615-1621(2019). RN [23] RP VARIANT IDNADFS 316-LYS--PHE-540 DEL. RX PubMed=31512373; DOI=10.1002/ajmg.a.61356; RA Uehara T., Tsuchihashi T., Yamada M., Suzuki H., Takenouchi T., Kosaki K.; RT "CNOT2 haploinsufficiency causes a neurodevelopmental disorder with RT characteristic facial features."; RL Am. J. Med. Genet. A 179:2506-2509(2019). 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. Required for the CCR4- CC NOT complex structural integrity. Can repress transcription and may CC link the CCR4-NOT complex to transcriptional regulation; the repressive CC function may specifically involve the N-Cor repressor complex CC containing HDAC3, NCOR1 and NCOR2. Involved in the maintenance of CC embryonic stem (ES) cell identity. {ECO:0000269|PubMed:14707134, CC ECO:0000269|PubMed:16712523, ECO:0000269|PubMed:21299754, CC ECO:0000269|PubMed:22367759}. 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. In the complex interacts directly with CNOT3. CC Interacts with NCOR1, NCOR2. HDAC3 and GPS2. CC {ECO:0000269|PubMed:10637334, ECO:0000269|PubMed:16712523, CC ECO:0000269|PubMed:19558367, ECO:0000269|PubMed:21299754}. CC -!- INTERACTION: CC Q9NZN8; Q96C12: ARMC5; NbExp=3; IntAct=EBI-743033, EBI-6425121; CC Q9NZN8; P41182: BCL6; NbExp=3; IntAct=EBI-743033, EBI-765407; CC Q9NZN8; Q9HBH7: BEX1; NbExp=3; IntAct=EBI-743033, EBI-7162175; CC Q9NZN8; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-743033, EBI-10175300; CC Q9NZN8; Q9H5F2: CFAP68; NbExp=3; IntAct=EBI-743033, EBI-718615; CC Q9NZN8; Q9H1P6: CIMIP1; NbExp=3; IntAct=EBI-743033, EBI-12155483; CC Q9NZN8; A5YKK6: CNOT1; NbExp=5; IntAct=EBI-743033, EBI-1222758; CC Q9NZN8; O75175: CNOT3; NbExp=10; IntAct=EBI-743033, EBI-743073; CC Q9NZN8; Q96LI5: CNOT6L; NbExp=2; IntAct=EBI-743033, EBI-1046635; CC Q9NZN8; Q9UFF9: CNOT8; NbExp=3; IntAct=EBI-743033, EBI-742299; CC Q9NZN8; P33240: CSTF2; NbExp=3; IntAct=EBI-743033, EBI-711360; CC Q9NZN8; F2Z2M7: GALNT10; NbExp=3; IntAct=EBI-743033, EBI-23893155; CC Q9NZN8; Q8N6F7: GCSAM; NbExp=3; IntAct=EBI-743033, EBI-10267082; CC Q9NZN8; Q13098-7: GPS1; NbExp=3; IntAct=EBI-743033, EBI-10983983; CC Q9NZN8; O75031: HSF2BP; NbExp=3; IntAct=EBI-743033, EBI-7116203; CC Q9NZN8; Q9H019: MTFR1L; NbExp=3; IntAct=EBI-743033, EBI-2824497; CC Q9NZN8; P0CG20: PRR35; NbExp=3; IntAct=EBI-743033, EBI-11986293; CC Q9NZN8; P28070: PSMB4; NbExp=3; IntAct=EBI-743033, EBI-603350; CC Q9NZN8; P63244: RACK1; NbExp=3; IntAct=EBI-743033, EBI-296739; CC Q9NZN8; Q13207: TBX2; NbExp=3; IntAct=EBI-743033, EBI-2853051; CC Q9NZN8; Q9BXF9: TEKT3; NbExp=3; IntAct=EBI-743033, EBI-8644516; CC Q9NZN8; Q9HCJ0: TNRC6C; NbExp=4; IntAct=EBI-743033, EBI-6507625; CC Q9NZN8; Q15911-2: ZFHX3; NbExp=3; IntAct=EBI-743033, EBI-10237226; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21299754}. Nucleus CC {ECO:0000305|PubMed:21299754}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=Q9NZN8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NZN8-2; Sequence=VSP_009912; CC Name=3; CC IsoId=Q9NZN8-3; Sequence=VSP_009913; CC Name=4; CC IsoId=Q9NZN8-4; Sequence=VSP_009915, VSP_009916; CC Name=5; CC IsoId=Q9NZN8-5; Sequence=VSP_009914; CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in brain, heart, CC thymus, spleen, kidney, liver, small intestine, placenta, lung and CC peripheral blood leukocytes. {ECO:0000269|PubMed:10637334}. CC -!- DEVELOPMENTAL STAGE: Expressed in embryonic stem (ES) cells. CC {ECO:0000269|PubMed:22367759}. CC -!- DISEASE: Intellectual developmental disorder with nasal speech, CC dysmorphic facies, and variable skeletal anomalies (IDNADFS) CC [MIM:618608]: An autosomal dominant disorder characterized by delayed CC development, speech delay with nasal speech, and characteristic facial CC features including upslanted palpebral fissures, anteverted nares, a CC thin upper lip, and micrognathia. Some patients may have skeletal CC anomalies, such as brachydactyly, toe syndactyly and flat feet. CC {ECO:0000269|PubMed:31145527, ECO:0000269|PubMed:31512373}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- MISCELLANEOUS: [Isoform 3]: May be due to an intron retention. CC {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 4]: May be due to an intron retention. CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the CNOT2/3/5 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAF29095.1; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=AAQ13426.1; Type=Frameshift; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF180473; AAF29827.1; -; mRNA. DR EMBL; AF113226; AAG39297.1; -; mRNA. DR EMBL; AF161480; AAF29095.1; ALT_FRAME; mRNA. DR EMBL; AK000662; BAA91313.1; -; mRNA. DR EMBL; AL137674; CAB70869.1; -; mRNA. DR EMBL; BX641116; CAE46054.1; -; mRNA. DR EMBL; BC002597; AAH02597.1; -; mRNA. DR EMBL; BC011826; AAH11826.1; -; mRNA. DR EMBL; AF044215; AAQ13426.1; ALT_FRAME; mRNA. DR CCDS; CCDS31857.1; -. [Q9NZN8-1] DR PIR; T46494; T46494. DR RefSeq; NP_001186231.1; NM_001199302.1. [Q9NZN8-1] DR RefSeq; NP_001186232.1; NM_001199303.1. [Q9NZN8-1] DR RefSeq; NP_055330.1; NM_014515.5. [Q9NZN8-1] DR RefSeq; XP_011536701.1; XM_011538399.1. DR PDB; 4C0D; X-ray; 3.20 A; B=344-540. DR PDB; 4C0F; X-ray; 2.40 A; A/B/C/D=429-540. DR PDB; 5FU6; X-ray; 2.90 A; B/E=350-540. DR PDB; 5FU7; X-ray; 3.10 A; B/F=350-540. DR PDBsum; 4C0D; -. DR PDBsum; 4C0F; -. DR PDBsum; 5FU6; -. DR PDBsum; 5FU7; -. DR AlphaFoldDB; Q9NZN8; -. DR SMR; Q9NZN8; -. DR BioGRID; 110910; 180. DR ComplexPortal; CPX-2522; CCR4-NOT mRNA deadenylase complex, CNOT6L-CNOT7 variant. 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 ComplexPortal; CPX-707; CCR4-NOT mRNA deadenylase complex, CNOT6-CNOT7 variant. DR CORUM; Q9NZN8; -. DR DIP; DIP-42656N; -. DR IntAct; Q9NZN8; 92. DR MINT; Q9NZN8; -. DR STRING; 9606.ENSP00000229195; -. DR ChEMBL; CHEMBL4105920; -. DR GlyCosmos; Q9NZN8; 2 sites, 1 glycan. DR GlyGen; Q9NZN8; 10 sites, 1 O-linked glycan (10 sites). DR iPTMnet; Q9NZN8; -. DR MetOSite; Q9NZN8; -. DR PhosphoSitePlus; Q9NZN8; -. DR BioMuta; CNOT2; -. DR DMDM; 46396017; -. DR EPD; Q9NZN8; -. DR jPOST; Q9NZN8; -. DR MassIVE; Q9NZN8; -. DR MaxQB; Q9NZN8; -. DR PaxDb; 9606-ENSP00000229195; -. DR PeptideAtlas; Q9NZN8; -. DR ProteomicsDB; 83462; -. [Q9NZN8-1] DR ProteomicsDB; 83463; -. [Q9NZN8-2] DR ProteomicsDB; 83464; -. [Q9NZN8-3] DR ProteomicsDB; 83465; -. [Q9NZN8-4] DR ProteomicsDB; 83466; -. [Q9NZN8-5] DR Pumba; Q9NZN8; -. DR Antibodypedia; 17029; 503 antibodies from 33 providers. DR DNASU; 4848; -. DR Ensembl; ENST00000229195.8; ENSP00000229195.3; ENSG00000111596.14. [Q9NZN8-1] DR Ensembl; ENST00000418359.7; ENSP00000412091.3; ENSG00000111596.14. [Q9NZN8-1] DR Ensembl; ENST00000551043.5; ENSP00000449260.1; ENSG00000111596.14. [Q9NZN8-1] DR Ensembl; ENST00000551483.5; ENSP00000448883.1; ENSG00000111596.14. [Q9NZN8-3] DR GeneID; 4848; -. DR KEGG; hsa:4848; -. DR MANE-Select; ENST00000229195.8; ENSP00000229195.3; NM_014515.7; NP_055330.1. DR UCSC; uc001svv.4; human. [Q9NZN8-1] DR AGR; HGNC:7878; -. DR CTD; 4848; -. DR DisGeNET; 4848; -. DR GeneCards; CNOT2; -. DR HGNC; HGNC:7878; CNOT2. DR HPA; ENSG00000111596; Low tissue specificity. DR MalaCards; CNOT2; -. DR MIM; 604909; gene. DR MIM; 618608; phenotype. DR neXtProt; NX_Q9NZN8; -. DR OpenTargets; ENSG00000111596; -. DR Orphanet; 289513; 12q15q21.1 microdeletion syndrome. DR PharmGKB; PA26673; -. DR VEuPathDB; HostDB:ENSG00000111596; -. DR eggNOG; KOG2151; Eukaryota. DR GeneTree; ENSGT00390000001285; -. DR HOGENOM; CLU_033275_1_0_1; -. DR InParanoid; Q9NZN8; -. DR OMA; DYHDESL; -. DR OrthoDB; 20932at2759; -. DR PhylomeDB; Q9NZN8; -. DR TreeFam; TF313102; -. DR PathwayCommons; Q9NZN8; -. 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 Reactome; R-HSA-9820841; M-decay: degradation of maternal mRNAs by maternally stored factors. DR SignaLink; Q9NZN8; -. DR SIGNOR; Q9NZN8; -. DR BioGRID-ORCS; 4848; 311 hits in 1167 CRISPR screens. DR ChiTaRS; CNOT2; human. DR GeneWiki; CNOT2; -. DR GenomeRNAi; 4848; -. DR Pharos; Q9NZN8; Tbio. DR PRO; PR:Q9NZN8; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q9NZN8; Protein. DR Bgee; ENSG00000111596; Expressed in oocyte and 215 other cell types or tissues. DR ExpressionAtlas; Q9NZN8; baseline and differential. 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:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; NAS:UniProtKB. DR GO; GO:0000932; C:P-body; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0003712; F:transcription coregulator activity; TAS:UniProtKB. DR GO; GO:0001222; F:transcription corepressor binding; IDA:UniProtKB. DR GO; GO:0033147; P:negative regulation of intracellular estrogen receptor signaling pathway; IMP:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IBA:GO_Central. DR GO; GO:0010606; P:positive regulation of cytoplasmic mRNA processing body assembly; IMP:UniProtKB. DR GO; GO:2000036; P:regulation of stem cell population maintenance; IMP:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; NAS:UniProtKB. DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW. DR GO; GO:0031047; P:regulatory ncRNA-mediated gene silencing; IEA:UniProtKB-KW. DR GO; GO:0001829; P:trophectodermal cell differentiation; IEA:Ensembl. DR Gene3D; 2.30.30.1020; CCR4-NOT complex subunit 2/3/5, C-terminal domain; 1. DR IDEAL; IID00503; -. DR InterPro; IPR038635; CCR4-NOT_su2/3/5_C_sf. DR InterPro; IPR040168; Not2/3/5. DR InterPro; IPR007282; NOT2/3/5_C. DR PANTHER; PTHR23326; CCR4 NOT-RELATED; 1. DR PANTHER; PTHR23326:SF3; CCR4-NOT TRANSCRIPTION COMPLEX SUBUNIT 2; 1. DR Pfam; PF04153; NOT2_3_5_C; 1. DR Genevisible; Q9NZN8; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytoplasm; Developmental protein; KW Disease variant; Intellectual disability; Nucleus; Phosphoprotein; KW Reference proteome; Repressor; RNA-mediated gene silencing; Transcription; KW Transcription regulation; Translation regulation. FT CHAIN 1..540 FT /note="CCR4-NOT transcription complex subunit 2" FT /id="PRO_0000198331" FT REGION 96..126 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 276..342 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 437..540 FT /note="Repressor domain" FT COMPBIAS 96..125 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 287..335 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 93 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 126 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332" FT MOD_RES 157 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8C5L3" FT MOD_RES 165 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 169 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q8C5L3" FT MOD_RES 242 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 274 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT VAR_SEQ 1..349 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_009913" FT VAR_SEQ 1..175 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_009912" FT VAR_SEQ 229..278 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_009914" FT VAR_SEQ 465..475 FT /note="FNRDWRYHKEE -> YVQSILITFVL (in isoform 4)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_009915" FT VAR_SEQ 476..540 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:17974005" FT /id="VSP_009916" FT VARIANT 316..540 FT /note="Missing (in IDNADFS)" FT /evidence="ECO:0000269|PubMed:31512373" FT /id="VAR_083417" FT VARIANT 460 FT /note="A -> T (in dbSNP:rs11178192)" FT /id="VAR_048750" FT HELIX 357..366 FT /evidence="ECO:0007829|PDB:5FU6" FT HELIX 371..373 FT /evidence="ECO:0007829|PDB:4C0D" FT TURN 376..378 FT /evidence="ECO:0007829|PDB:5FU6" FT HELIX 382..385 FT /evidence="ECO:0007829|PDB:5FU6" FT HELIX 396..398 FT /evidence="ECO:0007829|PDB:5FU6" FT TURN 410..412 FT /evidence="ECO:0007829|PDB:5FU6" FT HELIX 419..421 FT /evidence="ECO:0007829|PDB:5FU6" FT HELIX 424..427 FT /evidence="ECO:0007829|PDB:5FU6" FT HELIX 429..432 FT /evidence="ECO:0007829|PDB:4C0F" FT HELIX 436..438 FT /evidence="ECO:0007829|PDB:4C0F" FT HELIX 441..449 FT /evidence="ECO:0007829|PDB:4C0F" FT HELIX 453..466 FT /evidence="ECO:0007829|PDB:4C0F" FT STRAND 470..472 FT /evidence="ECO:0007829|PDB:4C0F" FT TURN 473..476 FT /evidence="ECO:0007829|PDB:4C0F" FT STRAND 477..481 FT /evidence="ECO:0007829|PDB:4C0F" FT STRAND 488..490 FT /evidence="ECO:0007829|PDB:4C0F" FT STRAND 492..503 FT /evidence="ECO:0007829|PDB:4C0F" FT TURN 504..507 FT /evidence="ECO:0007829|PDB:4C0F" FT STRAND 508..517 FT /evidence="ECO:0007829|PDB:4C0F" FT HELIX 518..520 FT /evidence="ECO:0007829|PDB:4C0F" FT HELIX 537..539 FT /evidence="ECO:0007829|PDB:4C0F" SQ SEQUENCE 540 AA; 59738 MW; 7183890F033E3B83 CRC64; MVRTDGHTLS EKRNYQVTNS MFGASRKKFV EGVDSDYHDE NMYYSQSSMF PHRSEKDMLA SPSTSGQLSQ FGASLYGQQS ALGLPMRGMS NNTPQLNRSL SQGTQLPSHV TPTTGVPTMS LHTPPSPSRG ILPMNPRNMM NHSQVGQGIG IPSRTNSMSS SGLGSPNRSS PSIICMPKQQ PSRQPFTVNS MSGFGMNRNQ AFGMNNSLSS NIFNGTDGSE NVTGLDLSDF PALADRNRRE GSGNPTPLIN PLAGRAPYVG MVTKPANEQS QDFSIHNEDF PALPGSSYKD PTSSNDDSKS NLNTSGKTTS STDGPKFPGD KSSTTQNNNQ QKKGIQVLPD GRVTNIPQGM VTDQFGMIGL LTFIRAAETD PGMVHLALGS DLTTLGLNLN SPENLYPKFA SPWASSPCRP QDIDFHVPSE YLTNIHIRDK LAAIKLGRYG EDLLFYLYYM NGGDVLQLLA AVELFNRDWR YHKEERVWIT RAPGMEPTMK TNTYERGTYY FFDCLNWRKV AKEFHLEYDK LEERPHLPST FNYNPAQQAF //