ID CNO10_HUMAN Reviewed; 744 AA. AC Q9H9A5; B7Z7L1; F8WAF2; Q9BU30; Q9H5J7; Q9H8X1; Q9H9W0; Q9HAH3; AC Q9UFJ2; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 10-APR-2019, entry version 160. DE RecName: Full=CCR4-NOT transcription complex subunit 10; GN Name=CNOT10; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 5 AND 6), RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 85-744 (ISOFORM 4), AND RP VARIANT SER-348. RC TISSUE=Embryo, and Testis; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., RA Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT RP SER-736. RC TISSUE=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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 482-744 (ISOFORM 1). RC TISSUE=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., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., 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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [7] RP IDENTIFICATION IN THE CCR4-NOT COMPLEX, AND COMPOSITION OF THE RP CCR4-NOT 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 [8] 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., RA Buerckstuemmer T., 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 [9] RP IDENTIFICATION IN THE CCR4-NOT COMPLEX. RX PubMed=23232451; DOI=10.4161/rna.23065; RA Mauxion F., Preve B., Seraphin B.; RT "C2ORF29/CNOT11 and CNOT10 form a new module of the CCR4-NOT RT complex."; RL RNA Biol. 10:267-276(2013). RN [10] RP FUNCTION. RX PubMed=23221646; DOI=10.1093/nar/gks1133; RA Farber V., Erben E., Sharma S., Stoecklin G., Clayton C.; RT "Trypanosome CNOT10 is essential for the integrity of the NOT RT deadenylase complex and for degradation of many mRNAs."; RL Nucleic Acids Res. 41:1211-1222(2013). RN [11] RP INTERACTION WITH CNOT11. RX PubMed=23303381; DOI=10.4161/rna.23018; RA Bawankar P., Loh B., Wohlbold L., Schmidt S., Izaurralde E.; RT "NOT10 and C2orf29/NOT11 form a conserved module of the CCR4-NOT RT complex that docks onto the NOT1 N-terminal domain."; RL RNA Biol. 10:228-244(2013). RN [12] 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). CC -!- FUNCTION: Component of the CCR4-NOT complex which is one of the CC major cellular mRNA deadenylases and is linked to various cellular CC processes including bulk mRNA degradation, miRNA-mediated CC repression, translational repression during translational CC initiation and general transcription regulation. Additional CC complex functions may be a consequence of its influence on mRNA CC expression. Is not required for association of CNOT7 to the CCR4- CC NOT complex. {ECO:0000269|PubMed:23221646}. CC -!- SUBUNIT: Component of the CCR4-NOT complex; distinct complexes CC seem to exist that differ in the participation of probably CC mutually exclusive catalytic subunits. CNOT10 and CNOT11 form a CC subcomplex docked to the CNOT1 scaffold. CC {ECO:0000269|PubMed:19558367, ECO:0000269|PubMed:23232451}. CC -!- INTERACTION: CC Q9UKZ1:CNOT11; NbExp=4; IntAct=EBI-1054261, EBI-2562014; CC Q9HCJ0:TNRC6C; NbExp=10; IntAct=EBI-1054261, EBI-6507625; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus CC {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; CC IsoId=Q9H9A5-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9H9A5-2; Sequence=VSP_030312; CC Name=3; CC IsoId=Q9H9A5-3; Sequence=VSP_030313; CC Name=4; CC IsoId=Q9H9A5-4; Sequence=VSP_030313, VSP_030314; CC Name=5; CC IsoId=Q9H9A5-5; Sequence=VSP_030311; CC Name=6; CC IsoId=Q9H9A5-6; Sequence=VSP_045557; CC Note=No experimental confirmation available.; CC -!- SIMILARITY: Belongs to the CNOT10 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB13876.1; Type=Erroneous initiation; 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; AK021695; BAB13876.1; ALT_INIT; mRNA. DR EMBL; AK022576; BAB14108.1; -; mRNA. DR EMBL; AK022952; BAB14327.1; -; mRNA. DR EMBL; AK023227; BAB14478.1; -; mRNA. DR EMBL; AK027026; BAB15629.1; -; mRNA. DR EMBL; AK302196; BAH13647.1; -; mRNA. DR EMBL; AC138972; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC139452; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471055; EAW64435.1; -; Genomic_DNA. DR EMBL; BC002928; AAH02928.1; -; mRNA. DR EMBL; BC002931; AAH02931.1; -; mRNA. DR EMBL; AL117639; CAB56027.2; -; mRNA. DR CCDS; CCDS2655.1; -. [Q9H9A5-1] DR CCDS; CCDS58821.1; -. [Q9H9A5-3] DR CCDS; CCDS58822.1; -. [Q9H9A5-6] DR RefSeq; NP_001243670.1; NM_001256741.1. [Q9H9A5-3] DR RefSeq; NP_001243671.1; NM_001256742.1. [Q9H9A5-6] DR RefSeq; NP_056257.1; NM_015442.2. [Q9H9A5-1] DR UniGene; Hs.444851; -. DR ProteinModelPortal; Q9H9A5; -. DR BioGrid; 117411; 52. DR CORUM; Q9H9A5; -. DR DIP; DIP-46839N; -. DR IntAct; Q9H9A5; 28. DR MINT; Q9H9A5; -. DR STRING; 9606.ENSP00000399862; -. DR iPTMnet; Q9H9A5; -. DR PhosphoSitePlus; Q9H9A5; -. DR BioMuta; CNOT10; -. DR DMDM; 74733982; -. DR EPD; Q9H9A5; -. DR jPOST; Q9H9A5; -. DR MaxQB; Q9H9A5; -. DR PaxDb; Q9H9A5; -. DR PeptideAtlas; Q9H9A5; -. DR PRIDE; Q9H9A5; -. DR ProteomicsDB; 81300; -. DR ProteomicsDB; 81301; -. [Q9H9A5-2] DR ProteomicsDB; 81302; -. [Q9H9A5-3] DR ProteomicsDB; 81303; -. [Q9H9A5-4] DR ProteomicsDB; 81304; -. [Q9H9A5-5] DR DNASU; 25904; -. DR Ensembl; ENST00000328834; ENSP00000330060; ENSG00000182973. [Q9H9A5-1] DR Ensembl; ENST00000331889; ENSP00000329376; ENSG00000182973. [Q9H9A5-3] DR Ensembl; ENST00000454516; ENSP00000399862; ENSG00000182973. [Q9H9A5-6] DR GeneID; 25904; -. DR KEGG; hsa:25904; -. DR UCSC; uc003cfc.2; human. [Q9H9A5-1] DR CTD; 25904; -. DR EuPathDB; HostDB:ENSG00000182973.18; -. DR GeneCards; CNOT10; -. DR HGNC; HGNC:23817; CNOT10. DR HPA; HPA035614; -. DR HPA; HPA041450; -. DR neXtProt; NX_Q9H9A5; -. DR PharmGKB; PA134862503; -. DR eggNOG; KOG2471; Eukaryota. DR eggNOG; ENOG410XQQJ; LUCA. DR GeneTree; ENSGT00390000001827; -. DR HOGENOM; HOG000111843; -. DR HOVERGEN; HBG077464; -. DR InParanoid; Q9H9A5; -. DR KO; K12607; -. DR OMA; SARTMML; -. DR OrthoDB; 249353at2759; -. DR PhylomeDB; Q9H9A5; -. DR TreeFam; TF323368; -. 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 ChiTaRS; CNOT10; human. DR GenomeRNAi; 25904; -. DR PRO; PR:Q9H9A5; -. DR Proteomes; UP000005640; Chromosome 3. DR Bgee; ENSG00000182973; Expressed in 151 organ(s), highest expression level in testis. DR ExpressionAtlas; Q9H9A5; baseline and differential. DR Genevisible; Q9H9A5; HS. DR GO; GO:0030014; C:CCR4-NOT complex; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome. DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProtKB-KW. DR GO; GO:0006402; P:mRNA catabolic process; IBA:GO_Central. DR GO; GO:0017148; P:negative regulation of translation; IBA:GO_Central. DR GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; TAS:Reactome. DR Gene3D; 1.25.40.10; -; 2. DR InterPro; IPR039740; CNOT10. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR InterPro; IPR019734; TPR_repeat. DR PANTHER; PTHR12979; PTHR12979; 1. DR SMART; SM00028; TPR; 4. DR SUPFAM; SSF48452; SSF48452; 3. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Coiled coil; Complete proteome; KW Cytoplasm; Nucleus; Polymorphism; Reference proteome; KW RNA-mediated gene silencing; Transcription; Transcription regulation; KW Translation regulation. FT INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330}. FT CHAIN 2 744 CCR4-NOT transcription complex subunit FT 10. FT /FTId=PRO_0000314579. FT COILED 74 107 {ECO:0000255}. FT MOD_RES 2 2 N-acetylalanine. FT {ECO:0000244|PubMed:19413330}. FT VAR_SEQ 1 293 Missing (in isoform 5). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_030311. FT VAR_SEQ 1 7 MAADKPA -> MKSIGVKTVKVCGSKSSVRIEGQPCSLGQS FT RRKVKLMGERSYTLSIGNGDYFWANKEMLWDYVQTLS (in FT isoform 6). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_045557. FT VAR_SEQ 144 144 Missing (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_030312. FT VAR_SEQ 505 532 SSKSHDGDKFIPAPPSSPLRKQELENLK -> R (in FT isoform 3 and isoform 4). FT {ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334}. FT /FTId=VSP_030313. FT VAR_SEQ 556 577 Missing (in isoform 4). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_030314. FT VARIANT 348 348 T -> S (in dbSNP:rs11558687). FT {ECO:0000269|PubMed:14702039}. FT /FTId=VAR_053982. FT VARIANT 736 736 P -> S (in dbSNP:rs17849684). FT {ECO:0000269|PubMed:15489334}. FT /FTId=VAR_037957. FT CONFLICT 5 5 K -> R (in Ref. 1; BAB14108). FT {ECO:0000305}. FT CONFLICT 52 52 C -> R (in Ref. 1; BAB14478). FT {ECO:0000305}. FT CONFLICT 270 270 V -> M (in Ref. 1; BAB13876). FT {ECO:0000305}. FT CONFLICT 478 478 D -> G (in Ref. 1; BAB14108). FT {ECO:0000305}. FT CONFLICT 509 509 H -> Y (in Ref. 1; BAB14108). FT {ECO:0000305}. FT CONFLICT 518 518 P -> L (in Ref. 1; BAH13647). FT {ECO:0000305}. FT CONFLICT 622 622 A -> T (in Ref. 1; BAB14478). FT {ECO:0000305}. SQ SEQUENCE 744 AA; 82310 MW; BA1984B71F0A1E7A CRC64; MAADKPADQG AEKHEGTGQS SGITDQEKEL STNAFQAFTS GNYDACLQHL ACLQDINKDD YKIILNTAVA EFFKSNQTTT DNLRQTLNQL KNQVHSAVEE MDGLDDVENS MLYYNQAVIL YHLRQYTEAI SVGEKLYQFI EPFEEKFAQA VCFLLVDLYI LTYQAEKALH LLAVLEKMIS QGNNNKNGKN ETGNNNNKDG SNHKAESGAL IEAAKSKIHQ YKVRAYIQMK SLKACKREIK SVMNTAGNSA PSLFLKSNFE YLRGNYRKAV KLLNSSNIAE HPGFMKTGEC LRCMFWNNLG CIHFAMSKHN LGIFYFKKAL QENDNVCAQL SAGSTDPGKK FSGRPMCTLL TNKRYELLYN CGIQLLHIGR PLAAFECLIE AVQVYHANPR LWLRLAECCI AANKGTSEQE TKGLPSKKGI VQSIVGQGYH RKIVLASQSI QNTVYNDGQS SAIPVASMEF AAICLRNALL LLPEEQQDPK QENGAKNSNQ LGGNTESSES SETCSSKSHD GDKFIPAPPS SPLRKQELEN LKCSILACSA YVALALGDNL MALNHADKLL QQPKLSGSLK FLGHLYAAEA LISLDRISDA ITHLNPENVT DVSLGISSNE QDQGSDKGEN EAMESSGKRA PQCYPSSVNS ARTVMLFNLG SAYCLRSEYD KARKCLHQAA SMIHPKEVPP EAILLAVYLE LQNGNTQLAL QIIKRNQLLP AVKTHSEVRK KPVFQPVHPI QPIQMPAFTT VQRK //