MTG8R_HUMAN
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 03-AUG-2022, entry version 183.
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};
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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. [O43439-4]
DR RefSeq; XP_011527405.1; XM_011529103.2. [O43439-2]
DR RefSeq; XP_016883610.1; XM_017028121.1. [O43439-2]
DR AlphaFoldDB; O43439; -.
DR SMR; O43439; -.
DR BioGRID; 114586; 41.
DR DIP; DIP-38274N; -.
DR IntAct; O43439; 40.
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; O43439; -.
DR PeptideAtlas; O43439; -.
DR PRIDE; 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 Antibodypedia; 10684; 292 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 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; ICGQGIH; -.
DR OrthoDB; 334242at2759; -.
DR PhylomeDB; O43439; -.
DR TreeFam; TF106303; -.
DR PathwayCommons; O43439; -.
DR SignaLink; O43439; -.
DR BioGRID-ORCS; 9139; 13 hits in 1078 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 205 other tissues.
DR ExpressionAtlas; O43439; baseline and differential.
DR Genevisible; O43439; HS.
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:0060575; P:intestinal epithelial cell differentiation; IEA:Ensembl.
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:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 1.20.120.1110; -; 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; PTHR10379; 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; SSF158553; SSF158553; 1.
DR PROSITE; PS51119; TAFH; 1.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
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
