ID MTG8R_HUMAN Reviewed; 604 AA. AC O43439; B2RAE6; F8W6D7; Q5TGE4; Q5TGE5; Q5TGE6; Q5TGE7; Q8IWF3; Q96B06; AC Q96L00; Q9H436; Q9UJP8; Q9UJP9; Q9UP24; DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 24-JAN-2024, entry version 191. DE RecName: Full=Protein CBFA2T2; DE AltName: Full=ETO homologous on chromosome 20; DE AltName: Full=MTG8-like protein; DE AltName: Full=MTG8-related protein 1; DE AltName: Full=Myeloid translocation-related protein 1; DE AltName: Full=p85; GN Name=CBFA2T2; Synonyms=EHT, MTGR1; 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 2), AND TISSUE SPECIFICITY. RX PubMed=9787195; RA Fracchiolla N.S., Colombo G., Finelli P., Maiolo A.T., Neri A.; RT "EHT, a new member of the MTG8/ETO gene family, maps on 20q11 region and is RT deleted in acute myeloid leukemias."; RL Blood 92:3481-3484(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, RP PHOSPHORYLATION, AND INTERACTION WITH AML1-MTG8/ETO. RC TISSUE=Leukemia; RX PubMed=9447981; DOI=10.1128/mcb.18.2.846; RA Kitabayashi I., Ida K., Morohoshi F., Yokoyama A., Mitsuhashi N., RA Shimizu K., Nomura N., Hayashi Y., Ohki M.; RT "The AML1-MTG8 leukemic fusion protein forms a complex with a novel member RT of the MTG8(ETO/CDR) family, MTGR1."; RL Mol. Cell. Biol. 18:846-858(1998). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 2), AND RP TISSUE SPECIFICITY. RC TISSUE=Leukemia; RX PubMed=10675041; DOI=10.1016/s0378-1119(99)00481-3; RA Morohoshi F., Mitani S., Mitsuhashi N., Kitabayashi I., Takahashi E., RA Suzuki M., Munakata N., Ohki M.; RT "Structure and expression pattern of a human MTG8/ETO family gene, MTGR1."; RL Gene 241:287-295(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 1-532 (ISOFORM 5). RC TISSUE=Brain, and Hippocampus; 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 GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [6] 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 [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4). RC TISSUE=Eye, Ovary, and Prostate; 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 [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 22-604 (ISOFORMS 1/4/5), ALTERNATIVE RP SPLICING, AND TISSUE SPECIFICITY. RC TISSUE=Fetal brain, and Retina; 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 [9] RP INTERACTION WITH CBFA2T3. 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 [10] RP INTERACTION WITH RUNX1T1 AND CBFA2T3. RX PubMed=14703694; DOI=10.1046/j.0902-4441.2003.00166.x; RA Lindberg S.R., Olsson A., Persson A.M., Olsson I.; RT "Interactions between the leukaemia-associated ETO homologues of nuclear RT repressor proteins."; RL Eur. J. Haematol. 71:439-447(2003). 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 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 [13] 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 [14] 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 [15] RP CHROMOSOMAL TRANSLOCATION WITH RUNX1. RX PubMed=20520637; DOI=10.1038/leu.2010.106; RA Guastadisegni M.C., Lonoce A., Impera L., Di Terlizzi F., Fugazza G., RA Aliano S., Grasso R., Cluzeau T., Raynaud S., Rocchi M., Storlazzi C.T.; RT "CBFA2T2 and C20orf112: two novel fusion partners of RUNX1 in acute myeloid RT leukemia."; RL Leukemia 24:1516-1519(2010). RN [16] RP IDENTIFICATION BY 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 [17] RP IDENTIFICATION BY 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 [18] RP FUNCTION. 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 [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33; SER-264; SER-409 AND RP SER-577, AND 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 [20] 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 [21] RP CHROMOSOMAL TRANSLOCATION WITH PAX5. RX PubMed=26115422; DOI=10.1111/bjh.13543; RA Stasevich I., Inglott S., Austin N., Chatters S., Chalker J., Addy D., RA Dryden C., Ancliff P., Ford A., Williams O., Kempski H.; RT "PAX5 alterations in genetically unclassified childhood Precursor B-cell RT acute lymphoblastic leukaemia."; RL Br. J. Haematol. 171:263-272(2015). RN [22] RP FUNCTION, AND INTERACTION WITH PRDM14. RX PubMed=27281218; DOI=10.1038/nature18004; RA Tu S., Narendra V., Yamaji M., Vidal S.E., Rojas L.A., Wang X., Kim S.Y., RA Garcia B.A., Tuschl T., Stadtfeld M., Reinberg D.; RT "Co-repressor CBFA2T2 regulates pluripotency and germline development."; RL Nature 534:387-390(2016). RN [23] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-38 AND LYS-449, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). 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). Via association with PRDM14 is CC involved in regulation of embryonic stem cell (ESC) pluripotency CC (PubMed:27281218). Involved in primordial germ cell (PCG) formation. CC Stabilizes PRDM14 and OCT4 on chromatin in a homooligomerization- CC dependent manner (By similarity). Can repress the expression of MMP7 in CC a ZBTB33-dependent manner (PubMed:23251453). May function as a complex CC with the chimeric protein RUNX1/AML1-CBFA2T1/MTG8 (AML1-MTG8/ETO fusion CC protein) which is produced in acute myeloid leukemia with the CC chromosomal translocation t(8;21). May thus be involved in the CC repression of AML1-dependent transcription and the induction of G- CC CSF/CSF3-dependent cell growth. May be a tumor suppressor gene CC candidate involved in myeloid tumors with the deletion of the 20q11 CC region. Through heteromerization with CBFA2T3/MTG16 may be involved in CC regulation of the proliferation and the differentiation of erythroid CC progenitors by repressing the expression of TAL1 target genes (By CC similarity). Required for the maintenance of the secretory cell lineage CC in the small intestine. Can inhibit Notch signaling probably by CC association with RBPJ and may be involved in GFI1-mediated Paneth cell CC differentiation (By similarity). {ECO:0000250|UniProtKB:O70374, CC ECO:0000269|PubMed:23251453, ECO:0000303|PubMed:12559562, CC ECO:0000303|PubMed:15203199}. CC -!- SUBUNIT: Homooligomer. Homotetramerization is mediated by nervy CC homology region 2 (By similarity). Can interact with RUNX1T1/CBFA2T1 CC and CBFA2T3/MTG16; heterotetramerization between members of the CBFA2T CC family is proposed (PubMed:12242670, PubMed:14703694, PubMed:16616331). CC Forms a heterooligomer with the AML1-MTG8/ETO fusion protein CC (PubMed:9447981). Interacts with PRDM14 (PubMed:27281218). Interacts CC with RBPJ, GFI1, TCF4. Interacts with TAL1 and CBFA2T3/MTG16; the CC heteromer with CBFA2T3/MTG16 may function in repression of TAL1 (By CC similarity). {ECO:0000250|UniProtKB:O70374, CC ECO:0000250|UniProtKB:Q06455, ECO:0000269|PubMed:12242670, CC ECO:0000269|PubMed:14703694, ECO:0000269|PubMed:16616331, CC ECO:0000269|PubMed:27281218, ECO:0000269|PubMed:9447981, ECO:0000305}. CC -!- INTERACTION: CC O43439; Q99750: MDFI; NbExp=4; IntAct=EBI-748628, EBI-724076; CC O43439; Q9P0J1: PDP1; NbExp=3; IntAct=EBI-748628, EBI-2861634; CC O43439; Q9GZV8: PRDM14; NbExp=12; IntAct=EBI-748628, EBI-3957793; CC O43439; P17987: TCP1; NbExp=3; IntAct=EBI-748628, EBI-356553; CC O43439-4; O95429: BAG4; NbExp=3; IntAct=EBI-11954144, EBI-2949658; CC O43439-4; Q9Y592-2: CEP83; NbExp=3; IntAct=EBI-11954144, EBI-11123098; CC O43439-4; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-11954144, EBI-14069005; CC O43439-4; Q52LG2: KRTAP13-2; NbExp=3; IntAct=EBI-11954144, EBI-11953846; CC O43439-4; P43360: MAGEA6; NbExp=3; IntAct=EBI-11954144, EBI-1045155; CC O43439-4; Q9BSU1: PHAF1; NbExp=3; IntAct=EBI-11954144, EBI-946080; CC O43439-4; Q9GZV8: PRDM14; NbExp=6; IntAct=EBI-11954144, EBI-3957793; CC O43439-4; Q9NQX0: PRDM6; NbExp=3; IntAct=EBI-11954144, EBI-11320284; CC O43439-4; Q9BRV8: SIKE1; NbExp=3; IntAct=EBI-11954144, EBI-1773646; CC O43439-4; O60504: SORBS3; NbExp=3; IntAct=EBI-11954144, EBI-741237; CC O43439-4; P15884-3: TCF4; NbExp=3; IntAct=EBI-11954144, EBI-13636688; CC O43439-4; Q96GY0: ZC2HC1A; NbExp=3; IntAct=EBI-11954144, EBI-5458880; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; Synonyms=MTGR1b; CC IsoId=O43439-1; Sequence=Displayed; CC Name=2; Synonyms=MTGR1a, EHT; CC IsoId=O43439-2; Sequence=VSP_008121; CC Name=3; CC IsoId=O43439-3; Sequence=VSP_008121, VSP_008123, VSP_008124; CC Name=4; CC IsoId=O43439-4; Sequence=VSP_008122; CC Name=5; CC IsoId=O43439-5; Sequence=VSP_047410; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in fetal and adult tissues. CC Highly expressed in adult brain, heart, lung, kidney, lymph node, CC appendix, thymus, testis, uterus, small intestine, prostate and thymus. CC {ECO:0000269|PubMed:10675041, ECO:0000269|PubMed:9447981, CC ECO:0000269|PubMed:9787195, ECO:0000269|PubMed:9790752}. 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 CBFA2T2 is found in CC childhood precursor B-cell acute lymphoblastic leukemia (pre-B ALL). CC Translocation t(9;20)(p13;q11) with PAX5. CC {ECO:0000269|PubMed:26115422}. CC -!- DISEASE: Note=A chromosomal aberration involving CBFA2T2 is found in CC acute myeloid leukemia. Translocation t(20;21)(q11;q22) with CC RUNX1/AML1. {ECO:0000269|PubMed:20520637}. CC -!- SIMILARITY: Belongs to the CBFA2T family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC19378.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AK307887; 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; AF039200; AAC17499.1; -; mRNA. DR EMBL; AF068266; AAC19378.1; ALT_INIT; mRNA. DR EMBL; AF013970; AAC39841.1; -; mRNA. DR EMBL; AF069747; AAD02825.1; -; mRNA. DR EMBL; AF076461; AAD41221.1; -; Genomic_DNA. DR EMBL; AF076452; AAD41221.1; JOINED; Genomic_DNA. DR EMBL; AF076453; AAD41221.1; JOINED; Genomic_DNA. DR EMBL; AF076454; AAD41221.1; JOINED; Genomic_DNA. DR EMBL; AF076455; AAD41221.1; JOINED; Genomic_DNA. DR EMBL; AF076456; AAD41221.1; JOINED; Genomic_DNA. DR EMBL; AF076457; AAD41221.1; JOINED; Genomic_DNA. DR EMBL; AF076458; AAD41221.1; JOINED; Genomic_DNA. DR EMBL; AF076459; AAD41221.1; JOINED; Genomic_DNA. DR EMBL; AF076460; AAD41221.1; JOINED; Genomic_DNA. DR EMBL; AK307887; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AK314159; BAG36843.1; -; mRNA. DR EMBL; AL034421; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL121906; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL162505; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471077; EAW76311.1; -; Genomic_DNA. DR EMBL; BC015066; AAH15066.1; -; mRNA. DR EMBL; BC016298; AAH16298.2; -; mRNA. DR EMBL; BC040344; AAH40344.1; -; mRNA. DR EMBL; AF052210; AAC64699.1; -; mRNA. DR CCDS; CCDS13221.1; -. [O43439-1] DR CCDS; CCDS46590.1; -. [O43439-5] DR RefSeq; NP_001028171.1; NM_001032999.2. [O43439-5] DR RefSeq; NP_001034798.1; NM_001039709.1. [O43439-2] DR RefSeq; NP_005084.1; NM_005093.3. [O43439-1] DR RefSeq; XP_011527403.1; XM_011529101.2. DR RefSeq; XP_011527405.1; XM_011529103.2. DR RefSeq; XP_016883610.1; XM_017028121.1. DR AlphaFoldDB; O43439; -. DR SMR; O43439; -. DR BioGRID; 114586; 44. DR DIP; DIP-38274N; -. DR IntAct; O43439; 39. DR MINT; O43439; -. DR STRING; 9606.ENSP00000262653; -. DR iPTMnet; O43439; -. DR MetOSite; O43439; -. DR PhosphoSitePlus; O43439; -. DR BioMuta; CBFA2T2; -. DR EPD; O43439; -. DR jPOST; O43439; -. DR MassIVE; O43439; -. DR MaxQB; O43439; -. DR PaxDb; 9606-ENSP00000262653; -. DR PeptideAtlas; O43439; -. DR ProteomicsDB; 29761; -. DR ProteomicsDB; 48949; -. [O43439-1] DR ProteomicsDB; 48950; -. [O43439-2] DR ProteomicsDB; 48951; -. [O43439-3] DR ProteomicsDB; 48952; -. [O43439-4] DR Pumba; O43439; -. DR Antibodypedia; 10684; 311 antibodies from 33 providers. DR DNASU; 9139; -. DR Ensembl; ENST00000342704.11; ENSP00000345810.6; ENSG00000078699.22. [O43439-5] DR Ensembl; ENST00000344201.7; ENSP00000341865.3; ENSG00000078699.22. [O43439-3] DR Ensembl; ENST00000346541.7; ENSP00000262653.7; ENSG00000078699.22. [O43439-1] DR Ensembl; ENST00000359606.3; ENSP00000352622.3; ENSG00000078699.22. [O43439-4] DR Ensembl; ENST00000375279.6; ENSP00000364428.2; ENSG00000078699.22. [O43439-1] DR Ensembl; ENST00000397800.5; ENSP00000380902.1; ENSG00000078699.22. [O43439-2] DR Ensembl; ENST00000492345.5; ENSP00000433270.1; ENSG00000078699.22. [O43439-2] DR GeneID; 9139; -. DR KEGG; hsa:9139; -. DR MANE-Select; ENST00000342704.11; ENSP00000345810.6; NM_001032999.3; NP_001028171.1. [O43439-5] DR UCSC; uc002wze.2; human. [O43439-1] DR AGR; HGNC:1536; -. DR CTD; 9139; -. DR DisGeNET; 9139; -. DR GeneCards; CBFA2T2; -. DR HGNC; HGNC:1536; CBFA2T2. DR HPA; ENSG00000078699; Low tissue specificity. DR MIM; 603672; gene. DR neXtProt; NX_O43439; -. DR OpenTargets; ENSG00000078699; -. DR PharmGKB; PA26112; -. DR VEuPathDB; HostDB:ENSG00000078699; -. DR eggNOG; ENOG502QTD6; Eukaryota. DR GeneTree; ENSGT00950000183176; -. DR HOGENOM; CLU_092254_0_0_1; -. DR InParanoid; O43439; -. DR OMA; WKHLDHX; -. DR OrthoDB; 5314634at2759; -. DR PhylomeDB; O43439; -. DR TreeFam; TF106303; -. DR PathwayCommons; O43439; -. DR Reactome; R-HSA-9827857; Specification of primordial germ cells. DR SignaLink; O43439; -. DR BioGRID-ORCS; 9139; 17 hits in 1158 CRISPR screens. DR ChiTaRS; CBFA2T2; human. DR GeneWiki; CBFA2T2; -. DR GenomeRNAi; 9139; -. DR Pharos; O43439; Tbio. DR PRO; PR:O43439; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; O43439; Protein. DR Bgee; ENSG00000078699; Expressed in buccal mucosa cell and 206 other cell types or tissues. DR ExpressionAtlas; O43439; baseline and differential. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB. DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro. DR GO; GO:0060575; P:intestinal epithelial cell differentiation; IEA:Ensembl. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0010977; P:negative regulation of neuron projection development; ISS:UniProtKB. DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; IEA:Ensembl. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl. DR GO; GO:0010976; P:positive regulation of neuron projection development; 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; IPR013291; MTGR1. 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:SF13; PROTEIN CBFA2T2; 1. DR Pfam; PF08788; NHR2; 1. DR Pfam; PF07531; TAFH; 1. DR Pfam; PF01753; zf-MYND; 1. DR PRINTS; PR01875; ETOFAMILY. DR PRINTS; PR01877; MTGR1PROTEIN. 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; O43439; HS. PE 1: Evidence at protein level; KW Alternative splicing; Coiled coil; Isopeptide bond; Metal-binding; Nucleus; KW Phosphoprotein; Reference proteome; Repressor; Transcription; KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..604 FT /note="Protein CBFA2T2" FT /id="PRO_0000218301" FT DOMAIN 113..208 FT /note="TAFH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00440" FT ZN_FING 507..543 FT /note="MYND-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134" FT REGION 25..105 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 107..215 FT /note="Interaction with PRDM14" FT /evidence="ECO:0000250|UniProtKB:O70374" FT REGION 229..265 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 331..377 FT /note="Nervy homology region 2 (NHR2)" FT /evidence="ECO:0000305" FT REGION 397..427 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 435..484 FT /note="Nervy homology region 3 (NHR3)" FT /evidence="ECO:0000305" FT REGION 547..604 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 451..491 FT /evidence="ECO:0000255" FT COMPBIAS 45..60 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 64..105 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 233..254 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 403..427 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 570..604 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 507 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134" FT BINDING 510 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134" FT BINDING 518 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134" FT BINDING 521 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134" FT BINDING 527 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134" FT BINDING 531 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134" FT BINDING 539 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134" FT BINDING 543 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134" FT SITE 20..21 FT /note="Breakpoint for translocation to form RUNX1-CBFA2T2 FT in acute myeloid leukemia" FT /evidence="ECO:0000269|PubMed:20520637" FT MOD_RES 33 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 264 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 409 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 577 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 38 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 449 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1..29 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:9787195" FT /id="VSP_008121" FT VAR_SEQ 1..21 FT /note="MAKESGISLKEIQVLARQWKV -> MVGVPGAAAFQL (in isoform FT 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_047410" FT VAR_SEQ 1..20 FT /note="MAKESGISLKEIQVLARQWK -> MGFHHVGQARLELLTSGDLPALASQRAG FT IT (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_008122" FT VAR_SEQ 240..292 FT /note="RREENSFDRDTIAPEPPAKRVCTISPAPRHSPALTVPLMNPGGQFHPTPPPL FT Q -> SCIIHLKSMGVASRHEYFSGTLQMPAHPVRNSTLENLWVDCSRSLRSTVLPFP FT (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_008123" FT VAR_SEQ 293..604 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_008124" FT CONFLICT 31 FT /note="P -> H (in Ref. 7; AAH15066)" FT /evidence="ECO:0000305" FT CONFLICT 266 FT /note="A -> V (in Ref. 4; AK307887)" FT /evidence="ECO:0000305" SQ SEQUENCE 604 AA; 67133 MW; 1E55618844908169 CRC64; MAKESGISLK EIQVLARQWK VGPEKRVPAM PGSPVEVKIQ SRSSPPTMPP LPPINPGGPR PVSFTPTALS NGINHSPPTL NGAPSPPQRF SNGPASSTSS ALTNQQLPAT CGARQLSKLK RFLTTLQQFG NDISPEIGEK VRTLVLALVN STVTIEEFHC KLQEATNFPL RPFVIPFLKA NLPLLQRELL HCARAAKQTP SQYLAQHEHL LLNTSIASPA DSSELLMEVH GNGKRPSPER REENSFDRDT IAPEPPAKRV CTISPAPRHS PALTVPLMNP GGQFHPTPPP LQHYTLEDIA TSHLYREPNK MLEHREVRDR HHSLGLNGGY QDELVDHRLT EREWADEWKH LDHALNCIME MVEKTRRSMA VLRRCQESDR EELNYWKRRY NENTELRKTG TELVSRQHSP GSADSLSNDS QREFNSRPGT GYVPVEFWKK TEEAVNKVKI QAMSEVQKAV AEAEQKAFEV IATERARMEQ TIADVKRQAA EDAFLVINEQ EESTENCWNC GRKASETCSG CNIARYCGSF CQHKDWERHH RLCGQNLHGQ SPHGQGRPLL PVGRGSSARS ADCSVPSPAL DKTSATTSRS STPASVTAID TNGL //