MTG8_HUMAN
ID MTG8_HUMAN Reviewed; 604 AA.
AC Q06455; B7Z4P4; E7EPN4; O14784; Q06456; Q14873; Q16239; Q16346; Q16347;
AC Q6IBL1; Q6NXH1; Q7Z4J5; Q92479; Q9BRZ0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 216.
DE RecName: Full=Protein CBFA2T1;
DE AltName: Full=Cyclin-D-related protein;
DE AltName: Full=Eight twenty one protein;
DE AltName: Full=Protein ETO;
DE AltName: Full=Protein MTG8;
DE AltName: Full=Zinc finger MYND domain-containing protein 2;
GN Name=RUNX1T1; Synonyms=AML1T1, CBFA2T1, CDR, ETO, MTG8, ZMYND2;
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 MTG8B), AND VARIANT AML1-MTG8/ETO
RP FUSION IN AML-M2.
RC TISSUE=Fetal brain;
RX PubMed=8334990; DOI=10.1002/j.1460-2075.1993.tb05933.x;
RA Miyoshi H., Kozu T., Shimizu K., Enomoto K., Maseki N., Kaneko Y.,
RA Kamada N., Ohki M.;
RT "The t(8;21) translocation in acute myeloid leukemia results in production
RT of an AML1-MTG8 fusion transcript.";
RL EMBO J. 12:2715-2721(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM MTG8B), AND ALTERNATIVE
RP SPLICING (ISOFORMS MTG8A-2 AND MTG8B-2).
RX PubMed=9661669; DOI=10.1016/s0378-1119(98)00141-3;
RA Wolford J.K., Prochazka M.;
RT "Structure and expression of the human MTG8/ETO gene.";
RL Gene 212:103-109(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM MTG8A).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [7]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Muscle;
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 [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 31-604.
RX PubMed=8137293;
RA Erickson P.F., Robinson M., Owens G., Drabkin H.A.;
RT "The ETO portion of acute myeloid leukemia t(8;21) fusion transcript
RT encodes a highly evolutionarily conserved putative transcription factor.";
RL Cancer Res. 54:1782-1786(1994).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 334-432, AND VARIANT AML1-MTG8/ETO
RP FUSION.
RX PubMed=7919324;
RA Tighe J.E., Calabi F.;
RT "Alternative, out-of-frame runt/MTG8 transcripts are encoded by the
RT derivative (8) chromosome in the t(8;21) of acute myeloid leukemia M2.";
RL Blood 84:2115-2121(1994).
RN [11]
RP INTERACTION WITH ATN1, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=10973986; DOI=10.1083/jcb.150.5.939;
RA Wood J.D., Nucifora F.C. Jr., Duan K., Zhang C., Wang J., Kim Y.,
RA Schilling G., Sacchi N., Liu J.M., Ross C.A.;
RT "Atrophin-1, the dentato-rubral and pallido-luysian atrophy gene product,
RT interacts with ETO/MTG8 in the nuclear matrix and represses
RT transcription.";
RL J. Cell Biol. 150:939-948(2000).
RN [12]
RP FUNCTION, AND INTERACTION WITH ZBTB16.
RX PubMed=10688654; DOI=10.1128/mcb.20.6.2075-2086.2000;
RA Melnick A.M., Westendorf J.J., Polinger A., Carlile G.W., Arai S.,
RA Ball H.J., Lutterbach B., Hiebert S.W., Licht J.D.;
RT "The ETO protein disrupted in t(8;21)-associated acute myeloid leukemia is
RT a corepressor for the promyelocytic leukemia zinc finger protein.";
RL Mol. Cell. Biol. 20:2075-2086(2000).
RN [13]
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 [14]
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 [15]
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 [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [17]
RP SUBUNIT.
RX PubMed=19202074; DOI=10.1073/pnas.0810558106;
RA Kwok C., Zeisig B.B., Qiu J., Dong S., So C.W.;
RT "Transforming activity of AML1-ETO is independent of CBFbeta and ETO
RT interaction but requires formation of homo-oligomeric complexes.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:2853-2858(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-417, AND
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 [19]
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 [20]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 335-403, SUBUNIT, NRH2 DOMAIN,
RP INTERACTION WITH HDAC1; HDAC2; HDAC3; TCF12; NCOR1; NCOR2; SIN3A; CBFA2T2
RP AND CBFA2T3, AND MUTAGENESIS OF LEU-345; LEU-357; LEU-360; LEU-361;
RP LEU-375; LEU-378 AND LEU-389.
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 [21]
RP STRUCTURE BY NMR OF 120-222, INTERACTION WITH TCF12, FUNCTION, AND
RP MUTAGENESIS OF LYS-125; LEU-126; ARG-128; PHE-129; ARG-178 AND PHE-184.
RX PubMed=16803958; DOI=10.1073/pnas.0603463103;
RA Plevin M.J., Zhang J., Guo C., Roeder R.G., Ikura M.;
RT "The acute myeloid leukemia fusion protein AML1-ETO targets E proteins via
RT a paired amphipathic helix-like TBP-associated factor homology domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:10242-10247(2006).
RN [22]
RP STRUCTURE BY NMR OF 510-559 IN COMPLEX WITH ZINC IONS AND NCOR2,
RP MUTAGENESIS OF HIS-547, AND INTERACTION WITH NCOR1 AND NCOR2.
RX PubMed=17560331; DOI=10.1016/j.ccr.2007.04.010;
RA Liu Y., Chen W., Gaudet J., Cheney M.D., Roudaia L., Cierpicki T.,
RA Klet R.C., Hartman K., Laue T.M., Speck N.A., Bushweller J.H.;
RT "Structural basis for recognition of SMRT/N-CoR by the MYND domain and its
RT contribution to AML1/ETO's activity.";
RL Cancer Cell 11:483-497(2007).
RN [23]
RP STRUCTURE BY NMR OF 119-225, INTERACTION WITH NCOR1 AND TCF12, MUTAGENESIS
RP OF PHE-129; PHE-136; GLN-170; THR-173; PHE-175 AND LEU-177, AND DOMAIN.
RX PubMed=17572682; DOI=10.1038/nsmb1258;
RA Wei Y., Liu S., Lausen J., Woodrell C., Cho S., Biris N., Kobayashi N.,
RA Wei Y., Yokoyama S., Werner M.H.;
RT "A TAF4-homology domain from the corepressor ETO is a docking platform for
RT positive and negative regulators of transcription.";
RL Nat. Struct. Mol. Biol. 14:653-661(2007).
RN [24]
RP STRUCTURE BY NMR OF 505-551.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of ZF-MYND domain of protein CBFA2TI (protein MTG8).";
RL Submitted (OCT-2006) to the PDB data bank.
RN [25]
RP X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS) OF 338-400 IN COMPLEX WITH TCF12,
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF LEU-345; 352-GLU-GLU-353; LEU-357;
RP LEU-360; LEU-361; LEU-375; LEU-378; 379-ARG--CYS-381 AND LEU-389.
RX PubMed=23812588; DOI=10.1038/nature12287;
RA Sun X.J., Wang Z., Wang L., Jiang Y., Kost N., Soong T.D., Chen W.Y.,
RA Tang Z., Nakadai T., Elemento O., Fischle W., Melnick A., Patel D.J.,
RA Nimer S.D., Roeder R.G.;
RT "A stable transcription factor complex nucleated by oligomeric AML1-ETO
RT controls leukaemogenesis.";
RL Nature 500:93-97(2013).
RN [26]
RP VARIANT AML1-MTG8/ETO FUSION IN AML-M2.
RX PubMed=7541640; DOI=10.1002/gcc.2870130105;
RA Era T., Asou N., Kunisada T., Yamasaki H., Asou H., Kamada N.,
RA Nishikawa S., Yamaguchi K., Takatsuki K.;
RT "Identification of two transcripts of AML1/ETO-fused gene in t(8;21)
RT leukemic cells and expression of wild-type ETO gene in hematopoietic
RT cells.";
RL Genes Chromosomes Cancer 13:25-33(1995).
RN [27]
RP VARIANT AML1-MTG8/ETO FUSION IN AML-M2.
RX PubMed=8353289;
RA Kozu T., Miyoshi H., Shimizu K., Maseki N., Kaneko Y., Asou H., Kamada N.,
RA Ohki M.;
RT "Junctions of the AML1/MTG8(ETO) fusion are constant in t(8;21) acute
RT myeloid leukemia detected by reverse transcription polymerase chain
RT reaction.";
RL Blood 82:1270-1276(1993).
RN [28]
RP VARIANT AML1-MTG8/ETO FUSION IN AML-M2.
RX PubMed=1423235; DOI=10.1016/0165-4608(92)90384-k;
RA Nisson P.E., Watkins P.C., Sacchi N.;
RT "Transcriptionally active chimeric gene derived from the fusion of the AML1
RT gene and a novel gene on chromosome 8 in t(8;21) leukemic cells.";
RL Cancer Genet. Cytogenet. 63:81-88(1992).
RN [29]
RP VARIANTS [LARGE SCALE ANALYSIS] TRP-386; TRP-395 AND VAL-471.
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, PubMed:10688654). Can repress the
CC expression of MMP7 in a ZBTB33-dependent manner (PubMed:23251453). Can
CC repress transactivation mediated by TCF12 (PubMed:16803958). Acts as a
CC negative regulator of adipogenesis (By similarity). The AML1-MTG8/ETO
CC fusion protein frequently found in leukemic cells is involved in
CC leukemogenesis and contributes to hematopoietic stem/progenitor cell
CC self-renewal (PubMed:23812588). {ECO:0000250|UniProtKB:Q61909,
CC ECO:0000269|PubMed:10688654, ECO:0000269|PubMed:10973986,
CC ECO:0000269|PubMed:16803958, ECO:0000269|PubMed:23251453,
CC ECO:0000269|PubMed:23812588, ECO:0000303|PubMed:12559562,
CC ECO:0000303|PubMed:15203199}.
CC -!- SUBUNIT: Homooligomer. Homotetramerization is mediated by nervy
CC homology region 2 (NRH2). Can interact with CBFA2T2 and CBFA2T3;
CC heterotetramerization between members of the CBFA2T family is proposed.
CC Interacts with TCF12, SIN3A, HDAC1, HDAC2, HDAC3, NCOR1, NCOR2.
CC Interacts with ATN1 (via its N-terminus); the interaction enhances the
CC transcriptional repression. Interacts (via its N-terminus) with ZBTB16;
CC the interaction increases the transcription repression activity of
CC ZBTB16 (PubMed:10688654). AML1-MTG8/ETO fusion protein interacts with
CC CBFB. AML1-MTG8/ETO is part of a stable transcription factor complex
CC AETFC in leukemic cells; AETFC formation seems to be involved in
CC recruitment of EP300. AML1-MTG8/ETO nervy homology region 2-mediated
CC oligomerization is proposed to be homotypic, required for AML1-
CC MTG8/ETO-mediated transformation of primary hematopoietic cells and is
CC required for AML1-MTG8/ETO interaction with TCF12.
CC {ECO:0000269|PubMed:10688654, ECO:0000269|PubMed:10973986,
CC ECO:0000269|PubMed:12242670, ECO:0000269|PubMed:16616331,
CC ECO:0000269|PubMed:16803958, ECO:0000269|PubMed:17560331,
CC ECO:0000269|PubMed:17572682, ECO:0000269|PubMed:19202074,
CC ECO:0000269|PubMed:23812588}.
CC -!- INTERACTION:
CC Q06455; O75376: NCOR1; NbExp=5; IntAct=EBI-743342, EBI-347233;
CC Q06455; P08047: SP1; NbExp=2; IntAct=EBI-743342, EBI-298336;
CC Q06455; Q9QX47: Son; Xeno; NbExp=4; IntAct=EBI-743342, EBI-643037;
CC Q06455-2; Q9P2A4: ABI3; NbExp=3; IntAct=EBI-11984663, EBI-742038;
CC Q06455-2; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-11984663, EBI-10173507;
CC Q06455-2; Q9BRR9: ARHGAP9; NbExp=3; IntAct=EBI-11984663, EBI-750254;
CC Q06455-2; Q86V38: ATN1; NbExp=3; IntAct=EBI-11984663, EBI-11954292;
CC Q06455-2; Q13490: BIRC2; NbExp=3; IntAct=EBI-11984663, EBI-514538;
CC Q06455-2; Q8NA61-2: CBY2; NbExp=3; IntAct=EBI-11984663, EBI-11524851;
CC Q06455-2; Q8NCU1: CCDC197; NbExp=3; IntAct=EBI-11984663, EBI-750686;
CC Q06455-2; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-11984663, EBI-396137;
CC Q06455-2; Q01850: CDR2; NbExp=3; IntAct=EBI-11984663, EBI-1181367;
CC Q06455-2; Q9Y592-2: CEP83; NbExp=3; IntAct=EBI-11984663, EBI-11123098;
CC Q06455-2; Q9Y2V7: COG6; NbExp=3; IntAct=EBI-11984663, EBI-3866319;
CC Q06455-2; Q8N684-3: CPSF7; NbExp=3; IntAct=EBI-11984663, EBI-11523759;
CC Q06455-2; Q05D60: DEUP1; NbExp=3; IntAct=EBI-11984663, EBI-748597;
CC Q06455-2; Q96C01: FAM136A; NbExp=3; IntAct=EBI-11984663, EBI-373319;
CC Q06455-2; Q8IZU1: FAM9A; NbExp=3; IntAct=EBI-11984663, EBI-8468186;
CC Q06455-2; Q9NSC5: HOMER3; NbExp=3; IntAct=EBI-11984663, EBI-748420;
CC Q06455-2; P14652: HOXB2; NbExp=3; IntAct=EBI-11984663, EBI-5329558;
CC Q06455-2; Q8IYA8: IHO1; NbExp=3; IntAct=EBI-11984663, EBI-8638439;
CC Q06455-2; Q6ZU52: KIAA0408; NbExp=5; IntAct=EBI-11984663, EBI-739493;
CC Q06455-2; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-11984663, EBI-14069005;
CC Q06455-2; Q9C075: KRT23; NbExp=3; IntAct=EBI-11984663, EBI-3211278;
CC Q06455-2; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-11984663, EBI-3044087;
CC Q06455-2; Q14525: KRT33B; NbExp=3; IntAct=EBI-11984663, EBI-1049638;
CC Q06455-2; Q92764: KRT35; NbExp=3; IntAct=EBI-11984663, EBI-1058674;
CC Q06455-2; Q3SY46: KRTAP13-3; NbExp=3; IntAct=EBI-11984663, EBI-10241252;
CC Q06455-2; Q3LI70: KRTAP19-6; NbExp=3; IntAct=EBI-11984663, EBI-12805508;
CC Q06455-2; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-11984663, EBI-11962084;
CC Q06455-2; Q9UBR4-2: LHX3; NbExp=3; IntAct=EBI-11984663, EBI-12039345;
CC Q06455-2; O60711: LPXN; NbExp=3; IntAct=EBI-11984663, EBI-744222;
CC Q06455-2; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-11984663, EBI-1216080;
CC Q06455-2; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-11984663, EBI-16439278;
CC Q06455-2; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-11984663, EBI-10172526;
CC Q06455-2; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-11984663, EBI-10172876;
CC Q06455-2; O43482: OIP5; NbExp=3; IntAct=EBI-11984663, EBI-536879;
CC Q06455-2; O75928-2: PIAS2; NbExp=5; IntAct=EBI-11984663, EBI-348567;
CC Q06455-2; Q9NRY6: PLSCR3; NbExp=3; IntAct=EBI-11984663, EBI-750734;
CC Q06455-2; Q9GZV8: PRDM14; NbExp=6; IntAct=EBI-11984663, EBI-3957793;
CC Q06455-2; Q9NQX0: PRDM6; NbExp=3; IntAct=EBI-11984663, EBI-11320284;
CC Q06455-2; P31321: PRKAR1B; NbExp=3; IntAct=EBI-11984663, EBI-2805516;
CC Q06455-2; Q9Y4B4: RAD54L2; NbExp=3; IntAct=EBI-11984663, EBI-948156;
CC Q06455-2; Q04864-2: REL; NbExp=3; IntAct=EBI-11984663, EBI-10829018;
CC Q06455-2; P78317: RNF4; NbExp=3; IntAct=EBI-11984663, EBI-2340927;
CC Q06455-2; Q8WWV3: RTN4IP1; NbExp=3; IntAct=EBI-11984663, EBI-743502;
CC Q06455-2; O60504: SORBS3; NbExp=3; IntAct=EBI-11984663, EBI-741237;
CC Q06455-2; Q8N0S2: SYCE1; NbExp=3; IntAct=EBI-11984663, EBI-6872807;
CC Q06455-2; Q969V4: TEKT1; NbExp=3; IntAct=EBI-11984663, EBI-10180409;
CC Q06455-2; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-11984663, EBI-1105213;
CC Q06455-2; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-11984663, EBI-2130429;
CC Q06455-2; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-11984663, EBI-2799833;
CC Q06455-2; Q9Y2W2: WBP11; NbExp=3; IntAct=EBI-11984663, EBI-714455;
CC Q06455-2; P98170: XIAP; NbExp=3; IntAct=EBI-11984663, EBI-517127;
CC Q06455-2; P26651: ZFP36; NbExp=3; IntAct=EBI-11984663, EBI-374248;
CC Q06455-2; Q8TF47: ZFP90; NbExp=3; IntAct=EBI-11984663, EBI-11419867;
CC Q06455-2; Q6P1L6: ZNF343; NbExp=3; IntAct=EBI-11984663, EBI-10252492;
CC Q06455-2; Q8N720: ZNF655; NbExp=3; IntAct=EBI-11984663, EBI-625509;
CC Q06455-2; Q7Z783; NbExp=3; IntAct=EBI-11984663, EBI-9088990;
CC Q06455-4; Q9P2A4: ABI3; NbExp=3; IntAct=EBI-10224192, EBI-742038;
CC Q06455-4; Q0VDD7: BRME1; NbExp=3; IntAct=EBI-10224192, EBI-741210;
CC Q06455-4; Q8NA61: CBY2; NbExp=3; IntAct=EBI-10224192, EBI-741724;
CC Q06455-4; Q8N684: CPSF7; NbExp=3; IntAct=EBI-10224192, EBI-746909;
CC Q06455-4; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-10224192, EBI-6942903;
CC Q06455-4; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-10224192, EBI-2349927;
CC Q06455-4; Q12929: EPS8; NbExp=3; IntAct=EBI-10224192, EBI-375576;
CC Q06455-4; Q14687: GSE1; NbExp=3; IntAct=EBI-10224192, EBI-372619;
CC Q06455-4; Q9NSC5: HOMER3; NbExp=3; IntAct=EBI-10224192, EBI-748420;
CC Q06455-4; Q8IYA8: IHO1; NbExp=3; IntAct=EBI-10224192, EBI-8638439;
CC Q06455-4; O60711: LPXN; NbExp=3; IntAct=EBI-10224192, EBI-744222;
CC Q06455-4; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-10224192, EBI-741037;
CC Q06455-4; P50222: MEOX2; NbExp=3; IntAct=EBI-10224192, EBI-748397;
CC Q06455-4; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-10224192, EBI-10172526;
CC Q06455-4; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-10224192, EBI-10172876;
CC Q06455-4; Q9GZV8: PRDM14; NbExp=3; IntAct=EBI-10224192, EBI-3957793;
CC Q06455-4; O43597: SPRY2; NbExp=3; IntAct=EBI-10224192, EBI-742487;
CC Q06455-4; O75558: STX11; NbExp=3; IntAct=EBI-10224192, EBI-714135;
CC Q06455-4; Q99081-3: TCF12; NbExp=2; IntAct=EBI-10224192, EBI-11952764;
CC Q06455-4; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-10224192, EBI-5235829;
CC Q06455-4; Q5VZL5: ZMYM4; NbExp=3; IntAct=EBI-10224192, EBI-2514659;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00440,
CC ECO:0000269|PubMed:10973986}. Note=Colocalizes with ATN1 in discrete
CC nuclear dots.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=MTG8B;
CC IsoId=Q06455-1; Sequence=Displayed;
CC Name=MTG8A;
CC IsoId=Q06455-2; Sequence=VSP_003327;
CC Name=3;
CC IsoId=Q06455-3; Sequence=VSP_044558;
CC Name=4;
CC IsoId=Q06455-4; Sequence=VSP_045442;
CC Name=MTG8B-2;
CC IsoId=Q06455-5; Sequence=VSP_058512, VSP_058513;
CC Name=MTG8A-2;
CC IsoId=Q06455-6; Sequence=VSP_003327, VSP_058512, VSP_058513;
CC -!- TISSUE SPECIFICITY: Most abundantly expressed in brain. Lower levels in
CC lung, heart, testis and ovary.
CC -!- DOMAIN: The TAFH domain mediates interaction with transcription
CC regulators. {ECO:0000269|PubMed:17572682}.
CC -!- DOMAIN: Nervy homology region 2 (NHR2) mediates homo- and possibly
CC heterotypic oligomerization by forming a four-helix bundle tetrameric
CC structure. {ECO:0000269|PubMed:16616331}.
CC -!- DISEASE: Note=A chromosomal aberration involving RUNX1T1 is a cause of
CC acute myeloid leukemia (AML-M2). Translocation t(8;21)(q22;q22) with
CC RUNX1/AML1. {ECO:0000269|PubMed:1423235, ECO:0000269|PubMed:7541640,
CC ECO:0000269|PubMed:8334990, ECO:0000269|PubMed:8353289}.
CC -!- SIMILARITY: Belongs to the CBFA2T family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH05850.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA03247.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ETOID26.html";
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DR EMBL; D14821; BAA03558.1; -; mRNA.
DR EMBL; D13979; BAA03089.1; ALT_SEQ; mRNA.
DR EMBL; D14289; BAA03247.1; ALT_INIT; mRNA.
DR EMBL; AF018282; AAC28932.1; -; Genomic_DNA.
DR EMBL; AF018271; AAC28932.1; JOINED; Genomic_DNA.
DR EMBL; AF018272; AAC28932.1; JOINED; Genomic_DNA.
DR EMBL; AF018273; AAC28932.1; JOINED; Genomic_DNA.
DR EMBL; AF018274; AAC28932.1; JOINED; Genomic_DNA.
DR EMBL; AF018275; AAC28932.1; JOINED; Genomic_DNA.
DR EMBL; AF018276; AAC28932.1; JOINED; Genomic_DNA.
DR EMBL; AF018277; AAC28932.1; JOINED; Genomic_DNA.
DR EMBL; AF018278; AAC28932.1; JOINED; Genomic_DNA.
DR EMBL; AF018279; AAC28932.1; JOINED; Genomic_DNA.
DR EMBL; AF018281; AAC28932.1; JOINED; Genomic_DNA.
DR EMBL; AF018282; AAC28931.1; -; Genomic_DNA.
DR EMBL; AF018270; AAC28931.1; JOINED; Genomic_DNA.
DR EMBL; AF018272; AAC28931.1; JOINED; Genomic_DNA.
DR EMBL; AF018273; AAC28931.1; JOINED; Genomic_DNA.
DR EMBL; AF018274; AAC28931.1; JOINED; Genomic_DNA.
DR EMBL; AF018275; AAC28931.1; JOINED; Genomic_DNA.
DR EMBL; AF018276; AAC28931.1; JOINED; Genomic_DNA.
DR EMBL; AF018277; AAC28931.1; JOINED; Genomic_DNA.
DR EMBL; AF018278; AAC28931.1; JOINED; Genomic_DNA.
DR EMBL; AF018279; AAC28931.1; JOINED; Genomic_DNA.
DR EMBL; AF018281; AAC28931.1; JOINED; Genomic_DNA.
DR EMBL; AF018283; AAC26143.1; -; mRNA.
DR EMBL; AK297616; BAH12630.1; -; mRNA.
DR EMBL; BT009871; AAP88873.1; -; mRNA.
DR EMBL; CR456792; CAG33073.1; -; mRNA.
DR EMBL; AC103680; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104339; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471060; EAW91685.1; -; Genomic_DNA.
DR EMBL; BC005850; AAH05850.1; ALT_INIT; mRNA.
DR EMBL; BC067078; AAH67078.2; -; mRNA.
DR EMBL; AF181450; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; D43638; BAA07755.1; -; mRNA.
DR EMBL; X79990; CAA56311.1; -; mRNA.
DR EMBL; S74096; AAB32126.1; -; Genomic_DNA.
DR EMBL; S74092; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; S78158; AAB34819.2; ALT_SEQ; mRNA.
DR EMBL; S78159; AAB34820.2; ALT_SEQ; mRNA.
DR EMBL; D14822; BAA03559.1; ALT_SEQ; mRNA.
DR EMBL; D14823; BAA03560.1; ALT_SEQ; mRNA.
DR EMBL; S50186; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS47891.1; -. [Q06455-2]
DR CCDS; CCDS56544.1; -. [Q06455-3]
DR CCDS; CCDS6256.1; -. [Q06455-1]
DR CCDS; CCDS6257.1; -. [Q06455-4]
DR PIR; A57784; A57784.
DR PIR; C57784; C57784.
DR RefSeq; NP_001185554.1; NM_001198625.1. [Q06455-2]
DR RefSeq; NP_001185555.1; NM_001198626.1. [Q06455-1]
DR RefSeq; NP_001185556.1; NM_001198627.1. [Q06455-1]
DR RefSeq; NP_001185557.1; NM_001198628.1. [Q06455-1]
DR RefSeq; NP_001185558.1; NM_001198629.1. [Q06455-1]
DR RefSeq; NP_001185559.1; NM_001198630.1. [Q06455-1]
DR RefSeq; NP_001185560.1; NM_001198631.1. [Q06455-1]
DR RefSeq; NP_001185561.1; NM_001198632.1. [Q06455-2]
DR RefSeq; NP_001185562.1; NM_001198633.1.
DR RefSeq; NP_001185563.1; NM_001198634.1. [Q06455-3]
DR RefSeq; NP_001185608.1; NM_001198679.1.
DR RefSeq; NP_004340.1; NM_004349.3. [Q06455-2]
DR RefSeq; NP_783552.1; NM_175634.2. [Q06455-1]
DR RefSeq; NP_783553.1; NM_175635.2. [Q06455-4]
DR RefSeq; NP_783554.1; NM_175636.2. [Q06455-4]
DR RefSeq; XP_006716739.1; XM_006716676.3. [Q06455-4]
DR RefSeq; XP_011515653.1; XM_011517351.2. [Q06455-1]
DR RefSeq; XP_011515654.1; XM_011517352.2. [Q06455-2]
DR RefSeq; XP_011515655.1; XM_011517353.2. [Q06455-4]
DR RefSeq; XP_016869420.1; XM_017013931.1.
DR RefSeq; XP_016869421.1; XM_017013932.1. [Q06455-2]
DR RefSeq; XP_016869422.1; XM_017013933.1. [Q06455-2]
DR RefSeq; XP_016869423.1; XM_017013934.1. [Q06455-4]
DR RefSeq; XP_016869424.1; XM_017013935.1. [Q06455-4]
DR RefSeq; XP_016869425.1; XM_017013936.1. [Q06455-4]
DR RefSeq; XP_016869426.1; XM_017013937.1. [Q06455-4]
DR PDB; 1WQ6; X-ray; 2.00 A; A/B=335-403.
DR PDB; 2DJ8; NMR; -; A=505-551.
DR PDB; 2H7B; NMR; -; A=120-222.
DR PDB; 2KNH; NMR; -; A=119-216.
DR PDB; 2KYG; NMR; -; C=437-467.
DR PDB; 2OD1; NMR; -; A=510-559.
DR PDB; 2ODD; NMR; -; A=510-559.
DR PDB; 2PP4; NMR; -; A=119-225.
DR PDB; 4JOL; X-ray; 2.91 A; A/B/C/D=338-400.
DR PDBsum; 1WQ6; -.
DR PDBsum; 2DJ8; -.
DR PDBsum; 2H7B; -.
DR PDBsum; 2KNH; -.
DR PDBsum; 2KYG; -.
DR PDBsum; 2OD1; -.
DR PDBsum; 2ODD; -.
DR PDBsum; 2PP4; -.
DR PDBsum; 4JOL; -.
DR AlphaFoldDB; Q06455; -.
DR BMRB; Q06455; -.
DR SMR; Q06455; -.
DR BioGRID; 107310; 111.
DR DIP; DIP-29401N; -.
DR ELM; Q06455; -.
DR IntAct; Q06455; 89.
DR MINT; Q06455; -.
DR STRING; 9606.ENSP00000402257; -.
DR GlyGen; Q06455; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q06455; -.
DR PhosphoSitePlus; Q06455; -.
DR BioMuta; RUNX1T1; -.
DR DMDM; 2498595; -.
DR EPD; Q06455; -.
DR jPOST; Q06455; -.
DR MassIVE; Q06455; -.
DR MaxQB; Q06455; -.
DR PaxDb; Q06455; -.
DR PeptideAtlas; Q06455; -.
DR PRIDE; Q06455; -.
DR ProteomicsDB; 17401; -.
DR ProteomicsDB; 58447; -. [Q06455-1]
DR ProteomicsDB; 58448; -. [Q06455-2]
DR ProteomicsDB; 69196; -.
DR Antibodypedia; 25672; 283 antibodies from 34 providers.
DR DNASU; 862; -.
DR Ensembl; ENST00000265814.4; ENSP00000265814.3; ENSG00000079102.16. [Q06455-1]
DR Ensembl; ENST00000360348.6; ENSP00000353504.2; ENSG00000079102.16. [Q06455-4]
DR Ensembl; ENST00000396218.5; ENSP00000379520.1; ENSG00000079102.16. [Q06455-2]
DR Ensembl; ENST00000422361.6; ENSP00000390137.2; ENSG00000079102.16. [Q06455-4]
DR Ensembl; ENST00000518844.5; ENSP00000430728.1; ENSG00000079102.16. [Q06455-2]
DR Ensembl; ENST00000520724.5; ENSP00000428742.2; ENSG00000079102.16. [Q06455-3]
DR Ensembl; ENST00000523629.5; ENSP00000428543.1; ENSG00000079102.16. [Q06455-1]
DR Ensembl; ENST00000613302.4; ENSP00000481799.1; ENSG00000079102.16. [Q06455-1]
DR Ensembl; ENST00000613886.4; ENSP00000478331.1; ENSG00000079102.16. [Q06455-2]
DR Ensembl; ENST00000614812.4; ENSP00000481315.1; ENSG00000079102.16. [Q06455-1]
DR Ensembl; ENST00000617740.4; ENSP00000481112.1; ENSG00000079102.16. [Q06455-1]
DR GeneID; 862; -.
DR KEGG; hsa:862; -.
DR UCSC; uc003yfc.3; human. [Q06455-1]
DR CTD; 862; -.
DR DisGeNET; 862; -.
DR GeneCards; RUNX1T1; -.
DR HGNC; HGNC:1535; RUNX1T1.
DR HPA; ENSG00000079102; Tissue enriched (brain).
DR MalaCards; RUNX1T1; -.
DR MIM; 133435; gene.
DR neXtProt; NX_Q06455; -.
DR OpenTargets; ENSG00000079102; -.
DR Orphanet; 102724; Acute myeloid leukemia with t(8;21)(q22;q22) translocation.
DR PharmGKB; PA26111; -.
DR VEuPathDB; HostDB:ENSG00000079102; -.
DR eggNOG; ENOG502QTD6; Eukaryota.
DR GeneTree; ENSGT00950000183176; -.
DR HOGENOM; CLU_022077_2_0_1; -.
DR InParanoid; Q06455; -.
DR OMA; SFQNRRH; -.
DR OrthoDB; 334242at2759; -.
DR PhylomeDB; Q06455; -.
DR TreeFam; TF106303; -.
DR PathwayCommons; Q06455; -.
DR SignaLink; Q06455; -.
DR SIGNOR; Q06455; -.
DR BioGRID-ORCS; 862; 15 hits in 1080 CRISPR screens.
DR ChiTaRS; RUNX1T1; human.
DR EvolutionaryTrace; Q06455; -.
DR GeneWiki; RUNX1T1; -.
DR GenomeRNAi; 862; -.
DR Pharos; Q06455; Tbio.
DR PRO; PR:Q06455; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q06455; protein.
DR Bgee; ENSG00000079102; Expressed in secondary oocyte and 198 other tissues.
DR ExpressionAtlas; Q06455; baseline and differential.
DR Genevisible; Q06455; HS.
DR GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI: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:0045599; P:negative regulation of fat cell differentiation; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 1.20.120.1110; -; 1.
DR IDEAL; IID00381; -.
DR InterPro; IPR013290; CBFA2T1.
DR InterPro; IPR013289; CBFA2T1/2/3.
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 PANTHER; PTHR10379:SF5; PTHR10379:SF5; 1.
DR Pfam; PF08788; NHR2; 1.
DR Pfam; PF07531; TAFH; 1.
DR Pfam; PF01753; zf-MYND; 1.
DR PRINTS; PR01875; ETOFAMILY.
DR PRINTS; PR01876; MTG8PROTEIN.
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 3D-structure; Alternative splicing; Chromosomal rearrangement; DNA-binding;
KW Metal-binding; Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..604
FT /note="Protein CBFA2T1"
FT /id="PRO_0000218299"
FT DOMAIN 120..215
FT /note="TAFH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00440"
FT ZN_FING 515..551
FT /note="MYND-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT REGION 32..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..383
FT /note="Important for oligomerization"
FT REGION 337..383
FT /note="Nervy homology region 2 (NHR2)"
FT /evidence="ECO:0000303|PubMed:12559562"
FT REGION 401..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 443..492
FT /note="Nervy homology region 3 (NHR3)"
FT /evidence="ECO:0000303|PubMed:12559562"
FT REGION 557..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 515
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="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 526
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 529
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 535
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="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 547
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 551
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT SITE 30..31
FT /note="Breakpoint for translocation to form AML1-MTG8 in
FT AML-M2"
FT /evidence="ECO:0000269|PubMed:8334990"
FT MOD_RES 41
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT VAR_SEQ 1..37
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4"
FT /id="VSP_045442"
FT VAR_SEQ 1..29
FT /note="MISVKRNTWRALSLVIGDCRKKGNFEYCQ -> MCHPDKAFTSDKLQCVFNE
FT YKAAVWVPPRPRPLSRAPLPE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044558"
FT VAR_SEQ 1..29
FT /note="MISVKRNTWRALSLVIGDCRKKGNFEYCQ -> MP (in isoform
FT MTG8A and isoform MTG8A-2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_003327"
FT VAR_SEQ 427
FT /note="D -> G (in isoform MTG8B-2 and isoform MTG8A-2)"
FT /evidence="ECO:0000303|PubMed:9661669"
FT /id="VSP_058512"
FT VAR_SEQ 428..604
FT /note="Missing (in isoform MTG8B-2 and isoform MTG8A-2)"
FT /evidence="ECO:0000303|PubMed:9661669"
FT /id="VSP_058513"
FT VARIANT 386
FT /note="R -> W (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs1301792645)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036321"
FT VARIANT 395
FT /note="R -> W (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs1448417558)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036322"
FT VARIANT 471
FT /note="A -> V (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs1462140811)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036323"
FT MUTAGEN 125
FT /note="K->A,D: Loss of interaction with TCF12."
FT /evidence="ECO:0000269|PubMed:16803958"
FT MUTAGEN 126
FT /note="L->A: Loss of interaction with TCF12."
FT /evidence="ECO:0000269|PubMed:16803958"
FT MUTAGEN 128
FT /note="R->D: Loss of interaction with TCF12."
FT /evidence="ECO:0000269|PubMed:16803958"
FT MUTAGEN 129
FT /note="F->A: Loss of interaction with TCF12."
FT /evidence="ECO:0000269|PubMed:16803958,
FT ECO:0000269|PubMed:17572682"
FT MUTAGEN 129
FT /note="F->K: Abolishes interaction with corepressor."
FT /evidence="ECO:0000269|PubMed:16803958,
FT ECO:0000269|PubMed:17572682"
FT MUTAGEN 136
FT /note="F->A: Abolishes interaction with corepressor."
FT /evidence="ECO:0000269|PubMed:17572682"
FT MUTAGEN 170
FT /note="Q->A: Abolishes interaction with corepressor."
FT /evidence="ECO:0000269|PubMed:17572682"
FT MUTAGEN 173
FT /note="T->Q: Abolishes interaction with corepressor."
FT /evidence="ECO:0000269|PubMed:17572682"
FT MUTAGEN 175
FT /note="F->A: Abolishes interaction with corepressor."
FT /evidence="ECO:0000269|PubMed:17572682"
FT MUTAGEN 177
FT /note="L->A: Abolishes interaction with corepressor."
FT /evidence="ECO:0000269|PubMed:17572682"
FT MUTAGEN 178
FT /note="R->A,D: Loss of interaction with TCF12."
FT /evidence="ECO:0000269|PubMed:16803958"
FT MUTAGEN 184
FT /note="F->A: Loss of interaction with TCF12."
FT /evidence="ECO:0000269|PubMed:16803958"
FT MUTAGEN 345
FT /note="L->E: Disrupts tetramerization, disrupts AML1-
FT MTG8/ETO interaction with TCF12, decreases AML1-MTG8/ETO
FT interaction with RUNX1T1, CBFA2T3 and CBFA2T2; when
FT associated with R-357; R-360; E-361; E-375; R-378 and R-
FT 389."
FT /evidence="ECO:0000269|PubMed:16616331,
FT ECO:0000269|PubMed:23812588"
FT MUTAGEN 352..353
FT /note="EE->AA: Decreases interaction with TCF12, no effect
FT on oligomerization. Impairs AML1-MTG8/ETO activity in
FT hematopoietic stem/progenitor cell self-renewal but no
FT effect in inhibiting differentiation; when associated with
FT 379-A--A-381."
FT /evidence="ECO:0000269|PubMed:23812588"
FT MUTAGEN 357
FT /note="L->R: Disrupts tetramerization, disrupts AML1-
FT MTG8/ETO interaction with TCF12, decreases AML1-MTG8/ETO
FT interaction with RUNX1T1, CBFA2T3 and CBFA2T2; when
FT associated with E-345; R-360; E- 61; E-375; R-378 and R-
FT 389."
FT /evidence="ECO:0000269|PubMed:16616331,
FT ECO:0000269|PubMed:23812588"
FT MUTAGEN 360
FT /note="L->R: Disrupts tetramerization, disrupts AML1-
FT MTG8/ETO interaction with TCF12, decreases AML1-MTG8/ETO
FT interaction with RUNX1T1, CBFA2T3 and CBFA2T2; when
FT associated with E-345; R-357; E-361; E-375; R-378 and R-
FT 389."
FT /evidence="ECO:0000269|PubMed:16616331,
FT ECO:0000269|PubMed:23812588"
FT MUTAGEN 361
FT /note="L->E: Disrupts tetramerization, disrupts AML1-
FT MTG8/ETO interaction with TCF12, decreases AML1-MTG8/ETO
FT interaction with RUNX1T1, CBFA2T3 and CBFA2T2; when
FT associated with E-345; R-357; R-360; E-375; R-378 and R-
FT 389."
FT /evidence="ECO:0000269|PubMed:16616331,
FT ECO:0000269|PubMed:23812588"
FT MUTAGEN 375
FT /note="L->E: Disrupts tetramerization, disrupts AML1-
FT MTG8/ETO interaction with TCF12, decreases AML1-MTG8/ETO
FT interaction with RUNX1T1, CBFA2T3 and CBFA2T2; when
FT associated with E-345; R-357; R-360; E-361; R-378 and R-
FT 389."
FT /evidence="ECO:0000269|PubMed:16616331,
FT ECO:0000269|PubMed:23812588"
FT MUTAGEN 378
FT /note="L->R: Disrupts tetramerization, disrupts AML1-
FT MTG8/ETO interaction with TCF12, decreases AML1-MTG8/ETO
FT interaction with RUNX1T1, CBFA2T3 and CBFA2T2 when
FT associated with E-345; R-357; R-360; E-361; E-375 and R-
FT 389."
FT /evidence="ECO:0000269|PubMed:16616331,
FT ECO:0000269|PubMed:23812588"
FT MUTAGEN 379..381
FT /note="RRC->AAA: Disrupts interaction with TCF12, no effect
FT on oligomerization. Impairs AML1-MTG8/ETO activity in
FT hematopoietic stem/progenitor cell self-renewal but no
FT effect in inhibiting differentiation; when associated with
FT 352-E-E-353."
FT /evidence="ECO:0000269|PubMed:23812588"
FT MUTAGEN 389
FT /note="L->R: Disrupts tetramerization, disrupts AML1-
FT MTG8/ETO interaction with TCF12, decreases AML1-MTG8/ETO
FT interaction with RUNX1T1, CBFA2T3 and CBFA2T2; when
FT associated with E-345; R-357; R-360; E-361; E-375 and R-
FT 378."
FT /evidence="ECO:0000269|PubMed:16616331,
FT ECO:0000269|PubMed:23812588"
FT MUTAGEN 547
FT /note="H->A: Causes unfolding of the MYND-type zinc finger
FT domain."
FT /evidence="ECO:0000269|PubMed:17560331"
FT CONFLICT 455
FT /note="E -> G (in Ref. 3; BAH12630)"
FT /evidence="ECO:0000305"
FT CONFLICT 506
FT /note="N -> S (in Ref. 3; BAH12630)"
FT /evidence="ECO:0000305"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:2H7B"
FT HELIX 125..135
FT /evidence="ECO:0007829|PDB:2H7B"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:2H7B"
FT HELIX 142..156
FT /evidence="ECO:0007829|PDB:2H7B"
FT HELIX 162..172
FT /evidence="ECO:0007829|PDB:2H7B"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:2H7B"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:2H7B"
FT HELIX 182..186
FT /evidence="ECO:0007829|PDB:2H7B"
FT HELIX 189..199
FT /evidence="ECO:0007829|PDB:2H7B"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:2H7B"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:2H7B"
FT HELIX 347..399
FT /evidence="ECO:0007829|PDB:1WQ6"
FT HELIX 444..465
FT /evidence="ECO:0007829|PDB:2KYG"
FT STRAND 512..514
FT /evidence="ECO:0007829|PDB:2ODD"
FT STRAND 516..518
FT /evidence="ECO:0007829|PDB:2DJ8"
FT STRAND 524..526
FT /evidence="ECO:0007829|PDB:2ODD"
FT TURN 527..529
FT /evidence="ECO:0007829|PDB:2DJ8"
FT STRAND 533..536
FT /evidence="ECO:0007829|PDB:2DJ8"
FT HELIX 537..542
FT /evidence="ECO:0007829|PDB:2DJ8"
FT HELIX 544..547
FT /evidence="ECO:0007829|PDB:2DJ8"
FT TURN 548..550
FT /evidence="ECO:0007829|PDB:2DJ8"
SQ SEQUENCE 604 AA; 67566 MW; C3D2452F96E65679 CRC64;
MISVKRNTWR ALSLVIGDCR KKGNFEYCQD RTEKHSTMPD SPVDVKTQSR LTPPTMPPPP
TTQGAPRTSS FTPTTLTNGT SHSPTALNGA PSPPNGFSNG PSSSSSSSLA NQQLPPACGA
RQLSKLKRFL TTLQQFGNDI SPEIGERVRT LVLGLVNSTL TIEEFHSKLQ EATNFPLRPF
VIPFLKANLP LLQRELLHCA RLAKQNPAQY LAQHEQLLLD ASTTSPVDSS ELLLDVNENG
KRRTPDRTKE NGFDREPLHS EHPSKRPCTI SPGQRYSPNN GLSYQPNGLP HPTPPPPQHY
RLDDMAIAHH YRDSYRHPSH RDLRDRNRPM GLHGTRQEEM IDHRLTDREW AEEWKHLDHL
LNCIMDMVEK TRRSLTVLRR CQEADREELN YWIRRYSDAE DLKKGGGSSS SHSRQQSPVN
PDPVALDAHR EFLHRPASGY VPEEIWKKAE EAVNEVKRQA MTELQKAVSE AERKAHDMIT
TERAKMERTV AEAKRQAAED ALAVINQQED SSESCWNCGR KASETCSGCN TARYCGSFCQ
HKDWEKHHHI CGQTLQAQQQ GDTPAVSSSV TPNSGAGSPM DTPPAATPRS TTPGTPSTIE
TTPR
