ID MTG16_HUMAN Reviewed; 653 AA. AC O75081; D3DX78; O60615; O60616; O60617; O75082; O75107; O75108; Q0P5Z6; AC Q6P5W6; DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 2. DT 24-JAN-2024, entry version 171. DE RecName: Full=Protein CBFA2T3; DE AltName: Full=MTG8-related protein 2; DE AltName: Full=Myeloid translocation gene on chromosome 16 protein; DE Short=hMTG16; DE AltName: Full=Zinc finger MYND domain-containing protein 4; GN Name=CBFA2T3; Synonyms=MTG16, MTGR2, ZMYND4; 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 [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), CHROMOSOMAL RP TRANSLOCATION WITH RUNX1, TISSUE SPECIFICITY, AND VARIANT GLY-429. RC TISSUE=Brain; RX PubMed=9596646; RA Gamou T., Kitamura E., Hosoda F., Shimuzu K., Hayashi Y., Nagase T., RA Yokoyama Y., Ohki M.; RT "The partner gene of AML1 in t(16;21) myeloid malignancies is a novel RT member of the MTG8(ETO) family."; RL Blood 91:4028-4037(1998). RN [2] 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung, and Pancreas; 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 128-297 AND 492-604, NUCLEOTIDE RP SEQUENCE [MRNA] OF 341-431, AND TISSUE SPECIFICITY. RC TISSUE=Brain; RX PubMed=9790752; DOI=10.1006/geno.1998.5429; RA Calabi F., Cilli V.; RT "CBFA2T1, a gene rearranged in human leukemia, is a member of a multigene RT family."; RL Genomics 52:332-341(1998). RN [5] RP CHROMOSOMAL TRANSLOCATION WITH RUNX1. RX PubMed=10995019; DOI=10.1038/sj.leu.2401885; RA Salomon-Nguyen F., Busson-Le Coniat M., Lafage Pochitaloff M., RA Mozziconacci J., Berger R., Bernard O.A.; RT "AML1-MTG16 fusion gene in therapy-related acute leukemia with RT t(16;21)(q24;q22): two new cases."; RL Leukemia 14:1704-1705(2000). RN [6] RP CHROMOSOMAL TRANSLOCATION WITH RUNX1. RX PubMed=11224496; RA La Starza R., Sambani C., Crescenzi B., Matteucci C., Martelli M.F., RA Mecucci C.; RT "AML1/MTG16 fusion gene from a t(16;21)(q24;q22) translocation in RT treatment-induced leukemia after breast cancer."; RL Haematologica 86:212-213(2001). RN [7] RP INTERACTION WITH HDAC1; HDAC2; HDAC3; HDAC6; HDAC8; NCOR1 AND NCOR2. RX PubMed=11533236; DOI=10.1128/mcb.21.19.6470-6483.2001; RA Amann J.M., Nip J., Strom D.K., Lutterbach B., Harada H., Lenny N., RA Downing J.R., Meyers S., Hiebert S.W.; RT "ETO, a target of t(8;21) in acute leukemia, makes distinct contacts with RT multiple histone deacetylases and binds mSin3A through its oligomerization RT domain."; RL Mol. Cell. Biol. 21:6470-6483(2001). RN [8] RP FUNCTION. RX PubMed=12183414; RA Kochetkova M., McKenzie O.L.D., Bais A.J., Martin J.M., Secker G.A., RA Seshadri R., Powell J.A., Hinze S.J., Gardner A.E., Spendlove H.E., RA O'Callaghan N.J., Cleton-Jansen A.-M., Cornelisse C., Whitmore S.A., RA Crawford J., Kremmidiotis G., Sutherland G.R., Callen D.F.; RT "CBFA2T3 (MTG16) is a putative breast tumor suppressor gene from the breast RT cancer loss of heterozygosity region at 16q24.3."; RL Cancer Res. 62:4599-4604(2002). RN [9] RP FUNCTION (ISOFORM 2), INTERACTION WITH PRKAR2A, MUTAGENESIS OF VAL-494, AND RP SUBCELLULAR LOCATION (ISOFORM 2). RX PubMed=11823486; DOI=10.4049/jimmunol.168.4.1590; RA Schillace R.V., Andrews S.F., Liberty G.A., Davey M.P., Carr D.W.; RT "Identification and characterization of myeloid translocation gene 16b as a RT novel a kinase anchoring protein in T lymphocytes."; RL J. Immunol. 168:1590-1599(2002). RN [10] RP ALTERNATIVE SPLICING (ISOFORMS 3 AND 4), SUBCELLULAR LOCATION, AND RP INTERACTION WITH CBFA2T2; HDAC1; HDAC3 AND RUNX1T1. RX PubMed=12242670; DOI=10.1038/sj.onc.1205882; RA Hoogeveen A.T., Rossetti S., Stoyanova V., Schonkeren J., Fenaroli A., RA Schiaffonati L., van Unen L., Sacchi N.; RT "The transcriptional corepressor MTG16a contains a novel nucleolar RT targeting sequence deranged in t(16; 21)-positive myeloid malignancies."; RL Oncogene 21:6703-6712(2002). RN [11] RP REVIEW. RX PubMed=12559562; DOI=10.1016/s0378-1119(02)01172-1; RA Davis J.N., McGhee L., Meyers S.; RT "The ETO (MTG8) gene family."; RL Gene 303:1-10(2003). RN [12] RP FUNCTION, INTERACTION WITH NCOR1, AND TISSUE SPECIFICITY. RX PubMed=15231665; DOI=10.1158/0008-5472.can-03-3689; RA Ibanez V., Sharma A., Buonamici S., Verma A., Kalakonda S., Wang J., RA Kadkol S., Saunthararajah Y.; RT "AML1-ETO decreases ETO-2 (MTG16) interactions with nuclear receptor RT corepressor, an effect that impairs granulocyte differentiation."; RL Cancer Res. 64:4547-4554(2004). RN [13] RP REVIEW. RX PubMed=15203199; DOI=10.1016/j.ygeno.2004.02.011; RA Rossetti S., Hoogeveen A.T., Sacchi N.; RT "The MTG proteins: chromatin repression players with a passion for RT networking."; RL Genomics 84:1-9(2004). RN [14] RP INTERACTION WITH PDE4A AND PDE7A. RX PubMed=15470020; DOI=10.4049/jimmunol.173.8.4806; RA Asirvatham A.L., Galligan S.G., Schillace R.V., Davey M.P., Vasta V., RA Beavo J.A., Carr D.W.; RT "A-kinase anchoring proteins interact with phosphodiesterases in T RT lymphocyte cell lines."; RL J. Immunol. 173:4806-4814(2004). RN [15] RP INDUCTION. RX PubMed=15676213; DOI=10.1016/j.exphem.2004.10.011; RA Lindberg S.R., Olsson A., Persson A.-M., Olsson I.; RT "The leukemia-associated ETO homologues are differently expressed during RT hematopoietic differentiation."; RL Exp. Hematol. 33:189-198(2005). RN [16] RP INTERACTION WITH AML1-MTG8/ETO. RX PubMed=16616331; DOI=10.1016/j.ccr.2006.03.012; RA Liu Y., Cheney M.D., Gaudet J.J., Chruszcz M., Lukasik S.M., Sugiyama D., RA Lary J., Cole J., Dauter Z., Minor W., Speck N.A., Bushweller J.H.; RT "The tetramer structure of the Nervy homology two domain, NHR2, is critical RT for AML1/ETO's activity."; RL Cancer Cell 9:249-260(2006). RN [17] RP INTERACTION WITH ERBB4. RX PubMed=16815842; DOI=10.1074/jbc.m603998200; RA Linggi B., Carpenter G.; RT "ErbB-4 s80 intracellular domain abrogates ETO2-dependent transcriptional RT repression."; RL J. Biol. Chem. 281:25373-25380(2006). RN [18] RP FUNCTION, AND INTERACTION WITH ZNF652. RX PubMed=16966434; DOI=10.1158/1541-7786.mcr-05-0249; RA Kumar R., Manning J., Spendlove H.E., Kremmidiotis G., McKirdy R., Lee J., RA Millband D.N., Cheney K.M., Stampfer M.R., Dwivedi P.P., Morris H.A., RA Callen D.F.; RT "ZNF652, a novel zinc finger protein, interacts with the putative breast RT tumor suppressor CBFA2T3 to repress transcription."; RL Mol. Cancer Res. 4:655-665(2006). RN [19] RP IDENTIFICATION BY 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 [20] RP INTERACTION WITH PLXNA1; PLXNA3 AND PRKAR1A. RX PubMed=20138877; DOI=10.1016/j.febslet.2010.02.007; RA Fiedler S.E., Schillace R.V., Daniels C.J., Andrews S.F., Carr D.W.; RT "Myeloid translocation gene 16b is a dual A-kinase anchoring protein that RT interacts selectively with plexins in a phospho-regulated manner."; RL FEBS Lett. 584:873-877(2010). RN [21] RP FUNCTION, AND INTERACTION WITH ZBTB4; ZBTB33 AND ZBTB38. RX PubMed=23251453; DOI=10.1371/journal.pone.0051205; RA Barrett C.W., Smith J.J., Lu L.C., Markham N., Stengel K.R., Short S.P., RA Zhang B., Hunt A.A., Fingleton B.M., Carnahan R.H., Engel M.E., Chen X., RA Beauchamp R.D., Wilson K.T., Hiebert S.W., Reynolds A.B., Williams C.S.; RT "Kaiso directs the transcriptional corepressor MTG16 to the Kaiso binding RT site in target promoters."; RL PLoS ONE 7:E51205-E51205(2012). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-457; SER-459 AND THR-479, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 [23] RP FUNCTION, AND REGIONS NHR2 AND NHR3. RX PubMed=23840896; DOI=10.1371/journal.pone.0068502; RA Kumar P., Sharoyko V.V., Spegel P., Gullberg U., Mulder H., Olsson I., RA Ajore R.; RT "The transcriptional co-repressor myeloid translocation gene 16 inhibits RT glycolysis and stimulates mitochondrial respiration."; RL PLoS ONE 8:E68502-E68502(2013). RN [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-637; SER-641 AND THR-650, 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 [25] RP FUNCTION, AND INTERACTION WITH HIF1A AND EGLN1. RX PubMed=25974097; DOI=10.1371/journal.pone.0123725; RA Kumar P., Gullberg U., Olsson I., Ajore R.; RT "Myeloid translocation gene-16 co-repressor promotes degradation of RT hypoxia-inducible factor 1."; RL PLoS ONE 10:E0123725-E0123725(2015). RN [26] RP VARIANTS [LARGE SCALE ANALYSIS] HIS-306; LYS-518 AND VAL-534. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Transcriptional corepressor which facilitates transcriptional CC repression via its association with DNA-binding transcription factors CC and recruitment of other corepressors and histone-modifying enzymes CC (PubMed:12559562, PubMed:15203199). Can repress the expression of MMP7 CC in a ZBTB33-dependent manner (PubMed:23251453). Reduces the protein CC levels and stability of the transcriptinal regulator HIF1A; interacts CC with EGLN1 and promotes the HIF1A prolyl hydroxylation-dependent CC ubiquitination and proteasomal degradation pathway (PubMed:25974097). CC Contributes to inhibition of glycolysis and stimulation of CC mitochondrial respiration by down-regulating the expression of CC glycolytic genes including PFKFB3, PFKFB4, PDK1, PFKP, LDHA and HK1 CC which are direct targets of HIF1A (PubMed:23840896, PubMed:25974097). CC Regulates the proliferation and the differentiation of erythroid CC progenitors by repressing the expression of TAL1 target genes (By CC similarity). Plays a role in granulocyte differentiation CC (PubMed:15231665). {ECO:0000250|UniProtKB:O54972, CC ECO:0000269|PubMed:12183414, ECO:0000269|PubMed:15231665, CC ECO:0000269|PubMed:16966434, ECO:0000269|PubMed:23251453, CC ECO:0000269|PubMed:23840896, ECO:0000269|PubMed:25974097, CC ECO:0000303|PubMed:12559562, ECO:0000303|PubMed:15203199}. CC -!- FUNCTION: Isoform 2 functions as an A-kinase-anchoring protein CC (PubMed:11823486). {ECO:0000269|PubMed:11823486}. CC -!- SUBUNIT: Homooligomer. Homotetramerization is mediated by nervy CC homology region 2 (NRH2) (By similarity). Can interact with RUNX1T1 and CC CBFA2T2; heterotetramerization between members of the CBFA2T family is CC proposed (PubMed:12242670). Component of a TAL-1 complex composed at CC least of CBFA2T3, LDB1, TAL1 and TCF3 (By similarity). Interacts with CC ERBB4, HDAC1, HDAC2, HDAC3, HDAC6, HDAC8, NCOR1, NCOR2, and ZNF652. CC According to PubMed:12242670, may not interact with HDAC6. Interacts CC with PLXNA1, PLXNA3 and PRKAR1A. Isoform 2 interacts with PRKAR2A, CC PDE7A and probably PDE4A. Interacts with ZBTB4, ZBTB38 and ZBTB33. CC Interacts with HIF1A and EGLN1. Interacts with the AML1-MTG8/ETO fusion CC protein. {ECO:0000250|UniProtKB:O54972, ECO:0000250|UniProtKB:Q06455, CC ECO:0000269|PubMed:11533236, ECO:0000269|PubMed:11823486, CC ECO:0000269|PubMed:12242670, ECO:0000269|PubMed:15231665, CC ECO:0000269|PubMed:15470020, ECO:0000269|PubMed:16616331, CC ECO:0000269|PubMed:16815842, ECO:0000269|PubMed:16966434, CC ECO:0000269|PubMed:20138877, ECO:0000269|PubMed:23251453, CC ECO:0000269|PubMed:25974097}. CC -!- INTERACTION: CC O75081; P51805: PLXNA3; NbExp=2; IntAct=EBI-1190217, EBI-7135904; CC O75081; Q9Y2D9: ZNF652; NbExp=2; IntAct=EBI-1190217, EBI-1190229; CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus, nucleolus. Note=The RUNX1- CC CBFA2T3 fusion protein localizes to the nucleoplasm. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus, nucleoplasm CC {ECO:0000269|PubMed:11823486}. Golgi apparatus membrane CC {ECO:0000269|PubMed:11823486}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; Synonyms=CBFA2T3A, MTG16a; CC IsoId=O75081-1; Sequence=Displayed; CC Name=2; Synonyms=CBFA2T3B, MTG16b; CC IsoId=O75081-2; Sequence=VSP_028620, VSP_028624; CC Name=3; Synonyms=MTG16c; CC IsoId=O75081-4; Sequence=VSP_028621; CC Name=4; Synonyms=MTG16HEL; CC IsoId=O75081-5; Sequence=VSP_028622, VSP_028623; CC -!- TISSUE SPECIFICITY: Widely expressed with higher expression in heart, CC pancreas, skeletal muscle, spleen, thymus and peripheral blood CC leukocytes. Expressed in hematopoietic cells (at protein level). CC {ECO:0000269|PubMed:15231665, ECO:0000269|PubMed:9596646, CC ECO:0000269|PubMed:9790752}. CC -!- INDUCTION: Down-regulated by all-trans retinoic acid (ATRA). CC {ECO:0000269|PubMed:15676213}. CC -!- DOMAIN: Nervy homology region 2 (NHR2) mediates homo- and possibly CC heterotypic oligomerization by forming a four-helix bundle tetrameric CC structure. {ECO:0000250|UniProtKB:Q06455}. CC -!- DISEASE: Note=A chromosomal aberration involving CBFA2T3 is found in CC therapy-related myeloid malignancies. Translocation t(16;21)(q24;q22) CC that forms a RUNX1-CBFA2T3 fusion protein. CC {ECO:0000269|PubMed:10995019, ECO:0000269|PubMed:11224496, CC ECO:0000269|PubMed:9596646}. CC -!- SIMILARITY: Belongs to the CBFA2T family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH62624.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305}; CC Sequence=BAA31276.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=BAA31277.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/428/CBFA2T3"; 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; AB010419; BAA29061.1; -; mRNA. DR EMBL; AB010420; BAA29062.1; -; mRNA. DR EMBL; AB013286; BAA31276.1; ALT_SEQ; Genomic_DNA. DR EMBL; AB013286; BAA31277.1; ALT_SEQ; Genomic_DNA. DR EMBL; CH471184; EAW66748.1; -; Genomic_DNA. DR EMBL; CH471184; EAW66752.1; -; Genomic_DNA. DR EMBL; BC047019; AAH47019.1; -; mRNA. DR EMBL; BC062624; AAH62624.1; ALT_SEQ; mRNA. DR EMBL; AF052217; AAC64701.1; -; Genomic_DNA. DR EMBL; AF052216; AAC64701.1; JOINED; Genomic_DNA. DR EMBL; AF052215; AAC64702.1; -; Genomic_DNA. DR EMBL; AF052213; AAC64702.1; JOINED; Genomic_DNA. DR EMBL; AF052214; AAC64702.1; JOINED; Genomic_DNA. DR EMBL; AF052220; AAC64698.1; -; mRNA. DR CCDS; CCDS10972.1; -. [O75081-1] DR CCDS; CCDS10973.1; -. [O75081-2] DR RefSeq; NP_005178.4; NM_005187.5. [O75081-1] DR RefSeq; NP_787127.1; NM_175931.2. [O75081-2] DR AlphaFoldDB; O75081; -. DR BMRB; O75081; -. DR SMR; O75081; -. DR BioGRID; 107311; 83. DR DIP; DIP-48898N; -. DR IntAct; O75081; 17. DR MINT; O75081; -. DR STRING; 9606.ENSP00000268679; -. DR iPTMnet; O75081; -. DR PhosphoSitePlus; O75081; -. DR BioMuta; CBFA2T3; -. DR EPD; O75081; -. DR jPOST; O75081; -. DR MassIVE; O75081; -. DR MaxQB; O75081; -. DR PaxDb; 9606-ENSP00000268679; -. DR PeptideAtlas; O75081; -. DR ProteomicsDB; 49745; -. [O75081-1] DR ProteomicsDB; 49746; -. [O75081-2] DR ProteomicsDB; 49747; -. [O75081-4] DR ProteomicsDB; 49748; -. [O75081-5] DR Pumba; O75081; -. DR Antibodypedia; 30813; 158 antibodies from 27 providers. DR DNASU; 863; -. DR Ensembl; ENST00000268679.9; ENSP00000268679.4; ENSG00000129993.15. [O75081-1] DR Ensembl; ENST00000327483.9; ENSP00000332122.5; ENSG00000129993.15. [O75081-2] DR GeneID; 863; -. DR KEGG; hsa:863; -. DR MANE-Select; ENST00000268679.9; ENSP00000268679.4; NM_005187.6; NP_005178.4. DR UCSC; uc002fml.3; human. [O75081-1] DR AGR; HGNC:1537; -. DR CTD; 863; -. DR DisGeNET; 863; -. DR GeneCards; CBFA2T3; -. DR HGNC; HGNC:1537; CBFA2T3. DR HPA; ENSG00000129993; Tissue enhanced (brain, lymphoid tissue). DR MalaCards; CBFA2T3; -. DR MIM; 603870; gene. DR neXtProt; NX_O75081; -. DR OpenTargets; ENSG00000129993; -. DR Orphanet; 329469; Acute megakaryoblastic leukemia without Down syndrome. DR PharmGKB; PA26113; -. DR VEuPathDB; HostDB:ENSG00000129993; -. DR eggNOG; ENOG502QTD6; Eukaryota. DR GeneTree; ENSGT00950000183176; -. DR HOGENOM; CLU_022077_2_0_1; -. DR InParanoid; O75081; -. DR OMA; RASDPFY; -. DR OrthoDB; 5314634at2759; -. DR PhylomeDB; O75081; -. DR TreeFam; TF106303; -. DR PathwayCommons; O75081; -. DR SignaLink; O75081; -. DR SIGNOR; O75081; -. DR BioGRID-ORCS; 863; 29 hits in 1158 CRISPR screens. DR ChiTaRS; CBFA2T3; human. DR GeneWiki; CBFA2T3; -. DR GenomeRNAi; 863; -. DR Pharos; O75081; Tbio. DR PRO; PR:O75081; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; O75081; Protein. DR Bgee; ENSG00000129993; Expressed in endometrium epithelium and 121 other cell types or tissues. DR ExpressionAtlas; O75081; baseline and differential. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central. DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro. DR GO; GO:0030851; P:granulocyte differentiation; IDA:MGI. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0045820; P:negative regulation of glycolytic process; IDA:UniProtKB. DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB. DR GO; GO:1903715; P:regulation of aerobic respiration; IDA:UniProtKB. DR GO; GO:0001666; P:response to hypoxia; IDA:UniProtKB. DR Gene3D; 6.10.140.2220; -; 1. DR Gene3D; 6.10.250.230; -; 1. DR Gene3D; 1.20.120.1110; TAFH/NHR1 domain; 1. DR InterPro; IPR013289; CBFA2T1/2/3. DR InterPro; IPR013292; CBFA2T3. DR InterPro; IPR014896; NHR2. DR InterPro; IPR037249; TAFH/NHR1_dom_sf. DR InterPro; IPR003894; TAFH_NHR1. DR InterPro; IPR002893; Znf_MYND. DR PANTHER; PTHR10379; MTG8 ETO EIGHT TWENTY ONE PROTEIN; 1. DR PANTHER; PTHR10379:SF6; PROTEIN CBFA2T3; 1. DR Pfam; PF08788; NHR2; 1. DR Pfam; PF07531; TAFH; 1. DR Pfam; PF01753; zf-MYND; 1. DR PRINTS; PR01875; ETOFAMILY. DR PRINTS; PR01878; MTG16PROTEIN. DR SMART; SM00549; TAFH; 1. DR SUPFAM; SSF144232; HIT/MYND zinc finger-like; 1. DR SUPFAM; SSF158553; TAFH domain-like; 1. DR PROSITE; PS51119; TAFH; 1. DR PROSITE; PS01360; ZF_MYND_1; 1. DR PROSITE; PS50865; ZF_MYND_2; 1. DR Genevisible; O75081; HS. PE 1: Evidence at protein level; KW Alternative splicing; Chromosomal rearrangement; Coiled coil; KW Differentiation; Golgi apparatus; Membrane; Metal-binding; Nucleus; KW Phosphoprotein; Reference proteome; Repressor; Transcription; KW Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1..653 FT /note="Protein CBFA2T3" FT /id="PRO_0000307173" FT DOMAIN 171..266 FT /note="TAFH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00440" FT ZN_FING 556..592 FT /note="MYND-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134" FT REGION 1..435 FT /note="Mediates localization to the nucleus" FT /evidence="ECO:0000250" FT REGION 1..430 FT /note="Mediates interaction with PDE7A (in isoform 2)" FT REGION 1..127 FT /note="Required for nucleolar targeting (in isoform 1)" FT REGION 1..109 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 145..242 FT /note="Interaction with ZBTB33" FT /evidence="ECO:0000269|PubMed:23251453" FT REGION 176..268 FT /note="Interaction with HIF1A" FT /evidence="ECO:0000269|PubMed:25974097" FT REGION 284..342 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 394..412 FT /note="Nervy homology region 2 (NHR2); essential for down- FT regulation of PFKFB3, PFKFB4 and PDK1 expression" FT /evidence="ECO:0000269|PubMed:23840896" FT REGION 434..472 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 485..533 FT /note="Nervy homology region 3 (NHR3); essential for down- FT regulation of PFKFB3, PFKFB4 and PDK1 expression" FT /evidence="ECO:0000269|PubMed:23840896" FT REGION 485..506 FT /note="Mediates interaction with PRKAR2A" FT /evidence="ECO:0000269|PubMed:11823486" FT REGION 603..653 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 488..543 FT /evidence="ECO:0000255" FT COMPBIAS 10..30 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 75..90 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 286..314 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 434..449 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 638..653 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 556 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134" FT BINDING 559 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134" FT BINDING 567 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134" FT BINDING 570 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134" FT BINDING 576 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134" FT BINDING 580 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134" FT BINDING 588 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134" FT BINDING 592 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134" FT SITE 51..52 FT /note="Breakpoint for translocation to form type-1 RUNX1- FT CBFA2T3 fusion protein" FT SITE 127..128 FT /note="Breakpoint for translocation to form type-2 RUNX1- FT CBFA2T3 fusion protein" FT MOD_RES 457 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 459 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 479 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 637 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 641 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 650 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:24275569" FT VAR_SEQ 1..61 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:9596646" FT /id="VSP_028620" FT VAR_SEQ 51..127 FT /note="APVDRKAKASAMPDSPAEVKTQPRSTPPSMPPPPPAASQGATRPPSFTPHTH FT REDGPATLPHGRFHGCLKWSMVCLL -> V (in isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_028621" FT VAR_SEQ 51 FT /note="A -> GKPALAAAGAPALCTPGQADARPVLGPA (in isoform 4)" FT /evidence="ECO:0000305" FT /id="VSP_028622" FT VAR_SEQ 52..653 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000305" FT /id="VSP_028623" FT VAR_SEQ 102..126 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:9596646" FT /id="VSP_028624" FT VARIANT 306 FT /note="R -> H (in a colorectal cancer sample; somatic FT mutation; dbSNP:rs745972870)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035447" FT VARIANT 429 FT /note="E -> G (in dbSNP:rs1053526)" FT /evidence="ECO:0000269|PubMed:9596646" FT /id="VAR_035374" FT VARIANT 518 FT /note="E -> K (in a colorectal cancer sample; somatic FT mutation; dbSNP:rs774310781)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035448" FT VARIANT 534 FT /note="A -> V (in a colorectal cancer sample; somatic FT mutation; dbSNP:rs553618592)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035449" FT MUTAGEN 494 FT /note="V->P,A: Loss of interaction with PRKAR2A." FT /evidence="ECO:0000269|PubMed:11823486" FT CONFLICT 231 FT /note="F -> L (in Ref. 3; AAH47019)" FT /evidence="ECO:0000305" FT CONFLICT 295 FT /note="T -> S (in Ref. 4; AAC64702)" FT /evidence="ECO:0000305" FT CONFLICT 305 FT /note="D -> E (in Ref. 1; BAA29061)" FT /evidence="ECO:0000305" FT CONFLICT 370 FT /note="R -> P (in Ref. 4; AAC64698)" FT /evidence="ECO:0000305" FT CONFLICT 420 FT /note="L -> V (in Ref. 4; AAC64698)" FT /evidence="ECO:0000305" FT CONFLICT 542 FT /note="A -> D (in Ref. 4; AAC64701)" FT /evidence="ECO:0000305" SQ SEQUENCE 653 AA; 71192 MW; 0B72B602120FA5DE CRC64; MPASRLRDRA ASSASGSTCG SMSQTHPVLE SGLLASAGCS APRGPRKGGP APVDRKAKAS AMPDSPAEVK TQPRSTPPSM PPPPPAASQG ATRPPSFTPH THREDGPATL PHGRFHGCLK WSMVCLLMNG SSHSPTAING APCTPNGFSN GPATSSTASL STQHLPPACG ARQLSKLKRF LTTLQQFGSD ISPEIGERVR TLVLGLVNST LTIEEFHSKL QEATNFPLRP FVIPFLKANL PLLQRELLHC ARLAKQTPAQ YLAQHEQLLL DASASSPIDS SELLLEVNEN GKRRTPDRTK ENGSDRDPLH PEHLSKRPCT LNPAQRYSPS NGPPQPTPPP HYRLEDIAMA HHFRDAYRHP DPRELRERHR PLVVPGSRQE EVIDHKLTER EWAEEWKHLN NLLNCIMDMV EKTRRSLTVL RRCQEADREE LNHWARRYSD AEDTKKGPAP AAARPRSSSA GPEGPQLDVP REFLPRTLTG YVPEDIWRKA EEAVNEVKRQ AMSELQKAVS DAERKAHELI TTERAKMERA LAEAKRQASE DALTVINQQE DSSESCWNCG RKASETCSGC NAARYCGSFC QHRDWEKHHH VCGQSLQGPT AVVADPVPGP PEAAHSLGPS LPVGAASPSE AGSAGPSRPG SPSPPGPLDT VPR //