RUNX1_HUMAN
ID RUNX1_HUMAN Reviewed; 453 AA.
AC Q01196; A8MV94; B2RMS4; D3DSG1; O60472; O60473; O76047; O76089; Q13081;
AC Q13755; Q13756; Q13757; Q13758; Q13759; Q15341; Q15343; Q16122; Q16284;
AC Q16285; Q16286; Q16346; Q16347; Q92479;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 3.
DT 03-AUG-2022, entry version 249.
DE RecName: Full=Runt-related transcription factor 1;
DE AltName: Full=Acute myeloid leukemia 1 protein;
DE AltName: Full=Core-binding factor subunit alpha-2;
DE Short=CBF-alpha-2;
DE AltName: Full=Oncogene AML-1;
DE AltName: Full=Polyomavirus enhancer-binding protein 2 alpha B subunit;
DE Short=PEA2-alpha B;
DE Short=PEBP2-alpha B;
DE AltName: Full=SL3-3 enhancer factor 1 alpha B subunit;
DE AltName: Full=SL3/AKV core-binding factor alpha B subunit;
GN Name=RUNX1; Synonyms=AML1, CBFA2;
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].
RA Ahn M.-Y., Bae S.C., Zhang Y.W., Shigesada K., Ito Y.;
RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM AML-1C).
RC TISSUE=Leukocyte;
RX PubMed=1720541; DOI=10.1073/pnas.88.23.10431;
RA Miyoshi H., Shimizu K., Kozu T., Maseki N., Kaneko Y., Ohki M.;
RT "t(8;21) breakpoints on chromosome 21 in acute myeloid leukemia are
RT clustered within a limited region of a single gene, AML1.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:10431-10434(1991).
RN [3]
RP ALTERNATIVE PRODUCTS, AND CHROMOSOMAL TRANSLOCATION WITH EAP.
RX PubMed=7533526; DOI=10.1002/gcc.2870110405;
RA Sacchi N., Nisson P.E., Watkins P.C., Faustinella F., Wijsman J.,
RA Hagemeijer A.;
RT "AML1 fusion transcripts in t(3;21) positive leukemia: evidence of
RT molecular heterogeneity and usage of splicing sites frequently involved in
RT the generation of normal AML1 transcripts.";
RL Genes Chromosomes Cancer 11:226-236(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM AML-1E), AND CHROMOSOMAL TRANSLOCATION
RP WITH ETO.
RX PubMed=8490181;
RA Nucifora G., Birn D.J., Espinosa R. III, Erickson P., Lebeau M.M.,
RA Roulston D., McKeithan T.W., Drabkin H., Rowley J.D.;
RT "Involvement of the AML1 gene in the t(3;21) in therapy-related leukemia
RT and in chronic myeloid leukemia in blast crisis.";
RL Blood 81:2728-2734(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM AML-1A).
RC TISSUE=Monocyte;
RX PubMed=7835892; DOI=10.1006/geno.1994.1519;
RA Levanon D., Negreanu V., Bernstein Y., Bar-Am I., Avivi L., Groner Y.;
RT "AML1, AML2, and AML3, the human members of the runt domain gene-family:
RT cDNA structure, expression, and chromosomal localization.";
RL Genomics 23:425-432(1994).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS AML-1B; AML-1A; AML-1G AND AML-1L).
RX PubMed=7651838; DOI=10.1093/nar/23.14.2762;
RA Miyoshi H., Ohira M., Shimizu K., Mitani K., Hirai H., Imai T.,
RA Yokoyama K., Soeda E., Ohki M.;
RT "Alternative splicing and genomic structure of the AML1 gene involved in
RT acute myeloid leukemia.";
RL Nucleic Acids Res. 23:2762-2769(1995).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM AML-1G).
RC TISSUE=B-cell;
RX PubMed=7891692; DOI=10.1128/mcb.15.4.1974;
RA Meyers S., Lenny N., Hiebert S.W.;
RT "The t(8;21) fusion protein interferes with AML-1B-dependent
RT transcriptional activation.";
RL Mol. Cell. Biol. 15:1974-1982(1995).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM AML-1L), AND FUNCTION (ISOFORM AML-1L).
RX PubMed=9199349; DOI=10.1128/mcb.17.7.4133;
RA Zhang Y.-W., Bae S.-C., Huang G., Fu Y.-X., Lu J., Ahn M.-Y., Kanno Y.,
RA Kanno T., Ito Y.;
RT "A novel transcript encoding an N-terminally truncated AML1/PEBP2 alphaB
RT protein interferes with transactivation and blocks granulocytic
RT differentiation of 32Dcl3 myeloid cells.";
RL Mol. Cell. Biol. 17:4133-4145(1997).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [10]
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 [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM AML-1G).
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 [12]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-177, AND CHROMOSOMAL TRANSLOCATION WITH
RP MECOM IN CHRONIC MYELOCYTIC LEUKEMIA.
RX PubMed=8313895; DOI=10.1002/j.1460-2075.1994.tb06288.x;
RA Mitani K., Ogawa S., Tanaka T., Miyoshi H., Kurokawa M., Mano H.,
RA Yazaki Y., Ohki M., Hirai H.;
RT "Generation of the AML1-EVI-1 fusion gene in the t(3;21)(q26;q22) causes
RT blastic crisis in chronic myelocytic leukemia.";
RL EMBO J. 13:504-510(1994).
RN [13]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-90 (ISOFORMS AML-1H AND AML-1I).
RX PubMed=8700862; DOI=10.1073/pnas.93.5.1935;
RA Ghozi M.C., Bernstein Y., Negreanu V., Levanon D., Groner Y.;
RT "Expression of the human acute myeloid leukemia gene AML1 is regulated by
RT two promoter regions.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:1935-1940(1996).
RN [14]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 440-453, AND ALTERNATIVE
RP SPLICING.
RC TISSUE=Monocyte;
RX PubMed=8634147; DOI=10.1089/dna.1996.15.175;
RA Levanon D., Bernstein Y., Negreanu V., Ghozi M.C., Bar-Am I., Aloya R.,
RA Goldenberg D., Lotem J., Groner Y.;
RT "A large variety of alternatively spliced and differentially expressed
RT mRNAs are encoded by the human acute myeloid leukemia gene AML1.";
RL DNA Cell Biol. 15:175-185(1996).
RN [15]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19, AND ALTERNATIVE SPLICING
RP (ISOFORM AML-1G).
RA Blechschmidt K., Rump A., Nordsiek G., Drescher B., Weber J., Rosenthal A.;
RT "Sequencing and analysis of 960 kb between AML1 and CBR1 on chromosome
RT 21q22.2.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [16]
RP SIMILARITY TO RUNT.
RX PubMed=1560822; DOI=10.1038/356484b0;
RA Daga A., Tighe J.E., Calabi F.;
RT "Leukaemia/Drosophila homology.";
RL Nature 356:484-484(1992).
RN [17]
RP ENHANCER CORE BINDING SEQUENCE.
RX PubMed=8413232; DOI=10.1128/mcb.13.10.6336-6345.1993;
RA Meyers S., Downing J.R., Hiebert S.W.;
RT "Identification of AML-1 and the (8;21) translocation protein (AML-1/ETO)
RT as sequence-specific DNA-binding proteins: the runt homology domain is
RT required for DNA binding and protein-protein interactions.";
RL Mol. Cell. Biol. 13:6336-6345(1993).
RN [18]
RP INTERACTION WITH ALYREF/THOC4.
RX PubMed=9119228; DOI=10.1101/gad.11.5.640;
RA Bruhn L., Munnerlyn A., Grosschedl R.;
RT "ALY, a context-dependent coactivator of LEF-1 and AML-1, is required for
RT TCRalpha enhancer function.";
RL Genes Dev. 11:640-653(1997).
RN [19]
RP CHROMOSOMAL TRANSLOCATION WITH CBFA2T3.
RX PubMed=9596646;
RA Gamou T., Kitamura E., Hosoda F., Shimuzu K., Hayashi Y., Nagase T.,
RA Yokoyama Y., Ohki M.;
RT "The partner gene of AML1 in t(16;21) myeloid malignancies is a novel
RT member of the MTG8(ETO) family.";
RL Blood 91:4028-4037(1998).
RN [20]
RP INTERACTION WITH TLE1.
RX PubMed=9751710; DOI=10.1073/pnas.95.20.11590;
RA Levanon D., Goldstein R.E., Bernstein Y., Tang H., Goldenberg D.,
RA Stifani S., Paroush Z., Groner Y.;
RT "Transcriptional repression by AML1 and LEF-1 is mediated by the
RT TLE/Groucho corepressors.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:11590-11595(1998).
RN [21]
RP FUNCTION, AND INTERACTION WITH ELF1; ELF2; ELF4 AND SPI1.
RX PubMed=10207087; DOI=10.1128/mcb.19.5.3635;
RA Mao S., Frank R.C., Zhang J., Miyazaki Y., Nimer S.D.;
RT "Functional and physical interactions between AML1 proteins and an ETS
RT protein, MEF: implications for the pathogenesis of t(8;21)-positive
RT leukemias.";
RL Mol. Cell. Biol. 19:3635-3644(1999).
RN [22]
RP INTERACTION WITH KAT6A, AND PHOSPHORYLATION.
RX PubMed=11742995; DOI=10.1093/emboj/20.24.7184;
RA Kitabayashi I., Aikawa Y., Nguyen L.A., Yokoyama A., Ohki M.;
RT "Activation of AML1-mediated transcription by MOZ and inhibition by the
RT MOZ-CBP fusion protein.";
RL EMBO J. 20:7184-7196(2001).
RN [23]
RP INTERACTION WITH KAT6B, AND FUNCTION.
RX PubMed=11965546; DOI=10.1038/sj.onc.1205367;
RA Pelletier N., Champagne N., Stifani S., Yang X.-J.;
RT "MOZ and MORF histone acetyltransferases interact with the Runt-domain
RT transcription factor Runx2.";
RL Oncogene 21:2729-2740(2002).
RN [24]
RP INTERACTION WITH SUV39H1, AND METHYLATION.
RX PubMed=12917624; DOI=10.1038/sj.onc.1206600;
RA Chakraborty S., Sinha K.K., Senyuk V., Nucifora G.;
RT "SUV39H1 interacts with AML1 and abrogates AML1 transactivity. AML1 is
RT methylated in vivo.";
RL Oncogene 22:5229-5237(2003).
RN [25]
RP FUNCTION, AND INTERACTION WITH ELF2.
RX PubMed=14970218; DOI=10.1074/jbc.m309074200;
RA Cho J.-Y., Akbarali Y., Zerbini L.F., Gu X., Boltax J., Wang Y.,
RA Oettgen P., Zhang D.-E., Libermann T.A.;
RT "Isoforms of the Ets transcription factor NERF/ELF-2 physically interact
RT with AML1 and mediate opposing effects on AML1-mediated transcription of
RT the B cell-specific blk gene.";
RL J. Biol. Chem. 279:19512-19522(2004).
RN [26]
RP INTERACTION WITH SUV39H1.
RX PubMed=16652147; DOI=10.1038/sj.onc.1209591;
RA Reed-Inderbitzin E., Moreno-Miralles I., Vanden-Eynden S.K., Xie J.,
RA Lutterbach B., Durst-Goodwin K.L., Luce K.S., Irvin B.J., Cleary M.L.,
RA Brandt S.J., Hiebert S.W.;
RT "RUNX1 associates with histone deacetylases and SUV39H1 to repress
RT transcription.";
RL Oncogene 25:5777-5786(2006).
RN [27]
RP FUNCTION IN MYELOID DIFFERENTIATION, AND INTERACTION WITH CDK6.
RX PubMed=17431401; DOI=10.1038/sj.emboj.7601675;
RA Fujimoto T., Anderson K., Jacobsen S.E., Nishikawa S.I., Nerlov C.;
RT "Cdk6 blocks myeloid differentiation by interfering with Runx1 DNA binding
RT and Runx1-C/EBPalpha interaction.";
RL EMBO J. 26:2361-2370(2007).
RN [28]
RP CHROMOSOMAL TRANSLOCATION WITH MACROD1.
RX PubMed=17532767; DOI=10.1111/j.1600-0609.2007.00858.x;
RA Imagama S., Abe A., Suzuki M., Hayakawa F., Katsumi A., Emi N., Kiyoi H.,
RA Naoe T.;
RT "LRP16 is fused to RUNX1 in monocytic leukemia cell line with
RT t(11;21)(q13;q22).";
RL Eur. J. Haematol. 79:25-31(2007).
RN [29]
RP FUNCTION, AND INTERACTION WITH FOXP3.
RX PubMed=17377532; DOI=10.1038/nature05673;
RA Ono M., Yaguchi H., Ohkura N., Kitabayashi I., Nagamura Y., Nomura T.,
RA Miyachi Y., Tsukada T., Sakaguchi S.;
RT "Foxp3 controls regulatory T-cell function by interacting with
RT AML1/Runx1.";
RL Nature 446:685-689(2007).
RN [30]
RP PHOSPHORYLATION AT SER-249; THR-273 AND SER-276 BY HIPK2, VARIANT GLN-174,
RP AND MUTAGENESIS OF SER-67; LYS-83; GLY-108; SER-249; THR-273 AND SER-276.
RX PubMed=18695000; DOI=10.1182/blood-2008-01-134122;
RA Wee H.-J., Voon D.C.-C., Bae S.-C., Ito Y.;
RT "PEBP2-beta/CBF-beta-dependent phosphorylation of RUNX1 and p300 by HIPK2:
RT implications for leukemogenesis.";
RL Blood 112:3777-3787(2008).
RN [31]
RP INTERACTION WITH YAP1.
RX PubMed=18280240; DOI=10.1016/j.molcel.2007.12.022;
RA Levy D., Adamovich Y., Reuven N., Shaul Y.;
RT "Yap1 phosphorylation by c-Abl is a critical step in selective activation
RT of proapoptotic genes in response to DNA damage.";
RL Mol. Cell 29:350-361(2008).
RN [32]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14 AND SER-21, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [33]
RP INTERACTION WITH CBFB, AND MUTAGENESIS OF MET-106; ALA-107 AND SER-140.
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 [34]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14; SER-249; SER-266; SER-268
RP AND SER-276, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [35]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-24 AND LYS-43, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [36]
RP CHROMOSOMAL TRANSLOCATION WITH CBFA2T2.
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 [37]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14; SER-21; SER-193; SER-212
RP AND THR-296, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [38]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212 AND SER-435, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [39]
RP INDUCTION.
RX PubMed=25134913; DOI=10.1007/s00018-014-1704-2;
RA Lu B., Sun X., Chen Y., Jin Q., Liang Q., Liu S., Li Y., Zhou Y., Li W.,
RA Huang Z.;
RT "Novel function of PITH domain-containing 1 as an activator of internal
RT ribosomal entry site to enhance RUNX1 expression and promote megakaryocyte
RT differentiation.";
RL Cell. Mol. Life Sci. 72:821-832(2015).
RN [40]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 59-173 IN COMPLEX WITH CBFB.
RX PubMed=10856244; DOI=10.1093/emboj/19.12.3004;
RA Warren A.J., Bravo J., Williams R.L., Rabbitts T.H.;
RT "Structural basis for the heterodimeric interaction between the acute
RT leukaemia-associated transcription factors AML1 and CBFbeta.";
RL EMBO J. 19:3004-3015(2000).
RN [41]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 54-243 IN COMPLEX WITH CBFB AND
RP DNA, AND MUTAGENESIS OF ARG-80; LYS-83; THR-84; ARG-135; ARG-139; ARG-142;
RP LYS-167; THR-169; ASP-171; ARG-174 AND ARG-177.
RX PubMed=11276260; DOI=10.1038/86264;
RA Bravo J., Li Z., Speck N.A., Warren A.J.;
RT "The leukemia-associated AML1 (Runx1) -- CBF beta complex functions as a
RT DNA-induced molecular clamp.";
RL Nat. Struct. Biol. 8:371-378(2001).
RN [42]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 61-174 IN COMPLEX WITH DNA.
RX PubMed=12377125; DOI=10.1016/s0969-2126(02)00853-5;
RA Bartfeld D., Shimon L., Couture G.C., Rabinovich D., Frolow F., Levanon D.,
RA Groner Y., Shakked Z.;
RT "DNA recognition by the RUNX1 transcription factor is mediated by an
RT allosteric transition in the RUNT domain and by DNA bending.";
RL Structure 10:1395-1407(2002).
RN [43]
RP STRUCTURE BY NMR OF 53-178, AND MUTAGENESIS OF ALA-107 AND GLY-108.
RX PubMed=10404214; DOI=10.1038/10658;
RA Nagata T., Gupta V., Sorce D., Kim W.-Y., Sali A., Chait B.T.,
RA Shigesada K., Ito Y., Werner M.H.;
RT "Immunoglobulin motif DNA recognition and heterodimerization of the
RT PEBP2/CBF Runt domain.";
RL Nat. Struct. Biol. 6:615-619(1999).
RN [44]
RP STRUCTURE BY NMR OF 61-175 IN COMPLEX WITH DNA.
RX PubMed=10545320; DOI=10.1016/s0969-2126(00)80058-1;
RA Berardi M.J., Sun C., Zehr M., Abildgaard F., Peng J., Speck N.A.,
RA Bushweller J.H.;
RT "The Ig fold of the core binding factor alpha Runt domain is a member of a
RT family of structurally and functionally related Ig-fold DNA-binding
RT domains.";
RL Structure 7:1247-1256(1999).
RN [45]
RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 46-185, AND CHLORIDE-BINDING.
RX PubMed=12217689; DOI=10.1016/s0022-2836(02)00702-7;
RA Baeckstroem S., Wolf-Watz M., Grundstroem C., Haerd T., Grundstroem T.,
RA Sauer U.H.;
RT "The RUNX1 Runt domain at 1.25A resolution: a structural switch and
RT specifically bound chloride ions modulate DNA binding.";
RL J. Mol. Biol. 322:259-272(2002).
RN [46]
RP REVIEW ON AML1 TRANSLOCATIONS.
RX PubMed=7795214;
RA Nucifora G., Rowley J.D.;
RT "AML1 and the 8;21 and 3;21 translocations in acute and chronic myeloid
RT leukemia.";
RL Blood 86:1-14(1995).
RN [47]
RP CHROMOSOMAL TRANSLOCATION WITH MTG8/ETO 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 [48]
RP CHROMOSOMAL TRANSLOCATION WITH MTG8/ETO 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 [49]
RP CHROMOSOMAL TRANSLOCATION WITH MTG8/ETO IN AML-M2.
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 [50]
RP CHROMOSOMAL TRANSLOCATION WITH EAP IN MYELODYSPLASIA.
RC TISSUE=Peripheral blood;
RX PubMed=8395054; DOI=10.1073/pnas.90.16.7784;
RA Nucifora G., Begy C.R., Erickson P., Drabkin H.A., Rowley J.D.;
RT "The 3;21 translocation in myelodysplasia results in a fusion transcript
RT between the AML1 gene and the gene for EAP, a highly conserved protein
RT associated with the Epstein-Barr virus small RNA EBER 1.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:7784-7788(1993).
RN [51]
RP CHROMOSOMAL TRANSLOCATION WITH MTG8/ETO IN AML-M2.
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 [52]
RP CHROMOSOMAL TRANSLOCATION WITH TEL IN ACUTE LYMPHOBLASTIC LEUKEMIA (ALL).
RX PubMed=7780150;
RA Romana S.P., Mauchauffe M., le Coniat M., Chumakov I., le Paslier D.,
RA Berger R., Bernard O.A.;
RT "The t(12;21) of acute lymphoblastic leukemia results in a tel-AML1 gene
RT fusion.";
RL Blood 85:3662-3670(1995).
RN [53]
RP CHROMOSOMAL TRANSLOCATION WITH MTG8/ETO 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 [54]
RP CHROMOSOMAL TRANSLOCATION WITH TEL IN ACUTE LYMPHOBLASTIC LEUKEMIA (ALL).
RX PubMed=7761424; DOI=10.1073/pnas.92.11.4917;
RA Golub T.R., Barker G.F., Bohlander S.K., Hiebert S.W., Ward D.C.,
RA Bray-Ward P., Morgan E., Raimondi S.C., Rowley J.D., Gilliland D.G.;
RT "Fusion of the TEL gene on 12p13 to the AML1 gene on 21q22 in acute
RT lymphoblastic leukemia.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:4917-4921(1995).
RN [55]
RP VARIANTS FPDMM GLN-139 AND GLN-174.
RX PubMed=10508512; DOI=10.1038/13793;
RA Song W.-J., Sullivan M.G., Legare R.D., Hutchings S., Tan X., Kufrin D.,
RA Ratajczak J., Resende I.C., Haworth C., Hock R., Loh M., Felix C.,
RA Roy D.-C., Busque L., Kurnit D., Willman C., Gewirtz A.M., Speck N.A.,
RA Bushweller J.H., Li F.P., Gardiner K., Poncz M., Maris J.M.,
RA Gilliland D.G.;
RT "Haploinsufficiency of CBFA2 causes familial thrombocytopenia with
RT propensity to develop acute myelogenous leukaemia.";
RL Nat. Genet. 23:166-175(1999).
RN [56]
RP CHROMOSOMAL REARRANGEMENT.
RX PubMed=18925961; DOI=10.1186/1471-2407-8-299;
RA Gelsi-Boyer V., Trouplin V., Adelaide J., Aceto N., Remy V., Pinson S.,
RA Houdayer C., Arnoulet C., Sainty D., Bentires-Alj M., Olschwang S., Vey N.,
RA Mozziconacci M.-J., Birnbaum D., Chaffanet M.;
RT "Genome profiling of chronic myelomonocytic leukemia: frequent alterations
RT of RAS and RUNX1 genes.";
RL BMC Cancer 8:299-299(2008).
RN [57]
RP INTERACTION WITH DPF2.
RX PubMed=28533407; DOI=10.1073/pnas.1700328114;
RA Huber F.M., Greenblatt S.M., Davenport A.M., Martinez C., Xu Y., Vu L.P.,
RA Nimer S.D., Hoelz A.;
RT "Histone-binding of DPF2 mediates its repressive role in myeloid
RT differentiation.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:6016-6021(2017).
CC -!- FUNCTION: Forms the heterodimeric complex core-binding factor (CBF)
CC with CBFB. RUNX members modulate the transcription of their target
CC genes through recognizing the core consensus binding sequence 5'-
CC TGTGGT-3', or very rarely, 5'-TGCGGT-3', within their regulatory
CC regions via their runt domain, while CBFB is a non-DNA-binding
CC regulatory subunit that allosterically enhances the sequence-specific
CC DNA-binding capacity of RUNX. The heterodimers bind to the core site of
CC a number of enhancers and promoters, including murine leukemia virus,
CC polyomavirus enhancer, T-cell receptor enhancers, LCK, IL3 and GM-CSF
CC promoters (Probable). Essential for the development of normal
CC hematopoiesis (PubMed:17431401). Acts synergistically with ELF4 to
CC transactivate the IL-3 promoter and with ELF2 to transactivate the BLK
CC promoter (PubMed:10207087, PubMed:14970218). Inhibits KAT6B-dependent
CC transcriptional activation (By similarity). Involved in lineage
CC commitment of immature T cell precursors. CBF complexes repress ZBTB7B
CC transcription factor during cytotoxic (CD8+) T cell development. They
CC bind to RUNX-binding sequence within the ZBTB7B locus acting as
CC transcriptional silencer and allowing for cytotoxic T cell
CC differentiation. CBF complexes binding to the transcriptional silencer
CC is essential for recruitment of nuclear protein complexes that catalyze
CC epigenetic modifications to establish epigenetic ZBTB7B silencing (By
CC similarity). Controls the anergy and suppressive function of regulatory
CC T-cells (Treg) by associating with FOXP3. Activates the expression of
CC IL2 and IFNG and down-regulates the expression of TNFRSF18, IL2RA and
CC CTLA4, in conventional T-cells (PubMed:17377532). Positively regulates
CC the expression of RORC in T-helper 17 cells (By similarity).
CC {ECO:0000250|UniProtKB:Q03347, ECO:0000269|PubMed:10207087,
CC ECO:0000269|PubMed:11965546, ECO:0000269|PubMed:14970218,
CC ECO:0000269|PubMed:17377532, ECO:0000269|PubMed:17431401, ECO:0000305}.
CC -!- FUNCTION: Isoform AML-1G shows higher binding activities for target
CC genes and binds TCR-beta-E2 and RAG-1 target site with threefold higher
CC affinity than other isoforms. It is less effective in the context of
CC neutrophil terminal differentiation. {ECO:0000250|UniProtKB:Q03347}.
CC -!- FUNCTION: Isoform AML-1L interferes with the transactivation activity
CC of RUNX1. {ECO:0000269|PubMed:9199349}.
CC -!- SUBUNIT: Heterodimer with CBFB. RUNX1 binds DNA as a monomer and
CC through the Runt domain. DNA-binding is increased by
CC heterodimerization. Isoform AML-1L can neither bind DNA nor
CC heterodimerize. Interacts with TLE1 and ALYREF/THOC4 (PubMed:9119228,
CC PubMed:9751710). Interacts with ELF1, ELF2 and SPI1 (PubMed:10207087).
CC Interacts via its Runt domain with the ELF4 N-terminal region
CC (PubMed:10207087). Interaction with ELF2 isoform 2 (NERF-1a) may act to
CC repress RUNX1-mediated transactivation (PubMed:14970218). Interacts
CC with KAT6A and KAT6B (PubMed:11742995, PubMed:11965546). Interacts with
CC SUV39H1, leading to abrogation of transactivating and DNA-binding
CC properties of RUNX1 (PubMed:12917624, PubMed:16652147). Interacts with
CC YAP1 (PubMed:18280240). Interacts with HIPK2 (By similarity).
CC Interaction with CDK6 prevents myeloid differentiation, reducing its
CC transcription transactivation activity. Found in a complex with PRMT5,
CC RUNX1 and CBFB. Interacts with FOXP3 (PubMed:17377532). Interacts with
CC TBX21 (By similarity). Interacts with DPF2 (PubMed:28533407).
CC {ECO:0000250|UniProtKB:Q03347, ECO:0000269|PubMed:10207087,
CC ECO:0000269|PubMed:10545320, ECO:0000269|PubMed:10856244,
CC ECO:0000269|PubMed:11276260, ECO:0000269|PubMed:11742995,
CC ECO:0000269|PubMed:11965546, ECO:0000269|PubMed:12377125,
CC ECO:0000269|PubMed:12917624, ECO:0000269|PubMed:14970218,
CC ECO:0000269|PubMed:16652147, ECO:0000269|PubMed:17377532,
CC ECO:0000269|PubMed:17431401, ECO:0000269|PubMed:18280240,
CC ECO:0000269|PubMed:28533407, ECO:0000269|PubMed:9119228,
CC ECO:0000269|PubMed:9751710}.
CC -!- INTERACTION:
CC Q01196; Q13951: CBFB; NbExp=3; IntAct=EBI-925904, EBI-718750;
CC Q01196; Q00534: CDK6; NbExp=5; IntAct=EBI-925904, EBI-295663;
CC Q01196; Q15723: ELF2; NbExp=2; IntAct=EBI-925904, EBI-956941;
CC Q01196; Q9H2X6: HIPK2; NbExp=4; IntAct=EBI-925904, EBI-348345;
CC Q01196; P52926: HMGA2; NbExp=2; IntAct=EBI-925904, EBI-912511;
CC Q01196; P17542: TAL1; NbExp=3; IntAct=EBI-925904, EBI-1753878;
CC Q01196; P46937: YAP1; NbExp=3; IntAct=EBI-925904, EBI-1044059;
CC Q01196-1; Q04724: TLE1; NbExp=4; IntAct=EBI-925940, EBI-711424;
CC Q01196-1; P59633: 3b; Xeno; NbExp=6; IntAct=EBI-925940, EBI-25489004;
CC Q01196-1; P16371: gro; Xeno; NbExp=4; IntAct=EBI-925940, EBI-153866;
CC Q01196-2; Q04724: TLE1; NbExp=3; IntAct=EBI-925944, EBI-711424;
CC Q01196-8; O95817: BAG3; NbExp=3; IntAct=EBI-12001422, EBI-747185;
CC Q01196-8; O95429: BAG4; NbExp=3; IntAct=EBI-12001422, EBI-2949658;
CC Q01196-8; Q13951: CBFB; NbExp=3; IntAct=EBI-12001422, EBI-718750;
CC Q01196-8; O75909-2: CCNK; NbExp=3; IntAct=EBI-12001422, EBI-12010594;
CC Q01196-8; Q8WU58: FAM222B; NbExp=3; IntAct=EBI-12001422, EBI-2807642;
CC Q01196-8; Q96EF6: FBXO17; NbExp=3; IntAct=EBI-12001422, EBI-2510157;
CC Q01196-8; Q96CN9: GCC1; NbExp=3; IntAct=EBI-12001422, EBI-746252;
CC Q01196-8; O14964: HGS; NbExp=3; IntAct=EBI-12001422, EBI-740220;
CC Q01196-8; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-12001422, EBI-10271199;
CC Q01196-8; Q7RTU3: OLIG3; NbExp=3; IntAct=EBI-12001422, EBI-10225049;
CC Q01196-8; P09234: SNRPC; NbExp=3; IntAct=EBI-12001422, EBI-766589;
CC Q01196-8; Q15562-2: TEAD2; NbExp=3; IntAct=EBI-12001422, EBI-9370956;
CC Q01196-8; Q15561: TEAD4; NbExp=5; IntAct=EBI-12001422, EBI-747736;
CC Q01196-8; Q96M29: TEKT5; NbExp=3; IntAct=EBI-12001422, EBI-10239812;
CC Q01196-8; A5D8V6: VPS37C; NbExp=3; IntAct=EBI-12001422, EBI-2559305;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=11;
CC Comment=Additional isoforms seem to exist.;
CC Name=AML-1B;
CC IsoId=Q01196-1; Sequence=Displayed;
CC Name=AML-1A;
CC IsoId=Q01196-2; Sequence=VSP_005929;
CC Name=AML-1C;
CC IsoId=Q01196-3; Sequence=VSP_005926, VSP_005927;
CC Name=AML-1E;
CC IsoId=Q01196-4; Sequence=VSP_005928;
CC Name=AML-1FA;
CC IsoId=Q01196-5; Sequence=VSP_005923, VSP_005924;
CC Name=AML-1FB;
CC IsoId=Q01196-6; Sequence=VSP_005921, VSP_005922;
CC Name=AML-1FC;
CC IsoId=Q01196-7; Sequence=VSP_005920, VSP_005925;
CC Name=AML-1G;
CC IsoId=Q01196-8; Sequence=VSP_005917;
CC Name=AML-1H;
CC IsoId=Q01196-9; Sequence=VSP_005916;
CC Name=AML-1I;
CC IsoId=Q01196-10; Sequence=VSP_005918;
CC Name=AML-1L; Synonyms=AML1-delta N;
CC IsoId=Q01196-11; Sequence=VSP_005919;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined except brain and
CC heart. Highest levels in thymus, bone marrow and peripheral blood.
CC -!- INDUCTION: Up-regulated by phorbol myristate acetate (PMA).
CC {ECO:0000269|PubMed:25134913}.
CC -!- DOMAIN: A proline/serine/threonine rich region at the C-terminus is
CC necessary for transcriptional activation of target genes.
CC -!- PTM: Phosphorylated in its C-terminus upon IL-6 treatment.
CC Phosphorylation enhances interaction with KAT6A.
CC -!- PTM: Methylated. {ECO:0000269|PubMed:12917624}.
CC -!- PTM: Phosphorylated in Ser-249 Thr-273 and Ser-276 by HIPK2 when
CC associated with CBFB and DNA. This phosphorylation promotes subsequent
CC EP300 phosphorylation. {ECO:0000269|PubMed:18695000}.
CC -!- DISEASE: Note=A chromosomal aberration involving RUNX1/AML1 is a cause
CC of M2 type acute myeloid leukemia (AML-M2). Translocation
CC t(8;21)(q22;q22) with RUNX1T1.
CC -!- DISEASE: Note=A chromosomal aberration involving RUNX1/AML1 is a cause
CC of therapy-related myelodysplastic syndrome (T-MDS). Translocation
CC t(3;21)(q26;q22) with EAP or MECOM.
CC -!- DISEASE: Note=A chromosomal aberration involving RUNX1/AML1 is a cause
CC of chronic myelogenous leukemia (CML). Translocation t(3;21)(q26;q22)
CC with EAP or MECOM.
CC -!- DISEASE: Note=A chromosomal aberration involving RUNX1/AML1 is found in
CC childhood acute lymphoblastic leukemia (ALL). Translocation
CC t(12;21)(p13;q22) with TEL. The translocation fuses the 3'-end of TEL
CC to the alternate 5'-exon of AML-1H.
CC -!- DISEASE: Note=A chromosomal aberration involving RUNX1 is found in
CC acute leukemia. Translocation t(11,21)(q13;q22) that forms a MACROD1-
CC RUNX1 fusion protein.
CC -!- DISEASE: Familial platelet disorder with associated myeloid malignancy
CC (FPDMM) [MIM:601399]: Autosomal dominant disease characterized by
CC qualitative and quantitative platelet defects, and propensity to
CC develop acute myelogenous leukemia. {ECO:0000269|PubMed:10508512}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- DISEASE: Note=A chromosomal aberration involving RUNX1/AML1 is found in
CC therapy-related myeloid malignancies. Translocation t(16;21)(q24;q22)
CC that forms a RUNX1-CBFA2T3 fusion protein.
CC -!- DISEASE: Note=A chromosomal aberration involving RUNX1/AML1 is a cause
CC of chronic myelomonocytic leukemia. Inversion inv(21)(q21;q22) with
CC USP16.
CC -!- DISEASE: Note=A chromosomal aberration involving RUNX1/AML1 is found in
CC acute myeloid leukemia. Translocation t(20;21)(q11;q22) with CBFA2T2.
CC {ECO:0000269|PubMed:20520637}.
CC -!- CAUTION: The fusion of AML1 with EAP in T-MDS induces a change of
CC reading frame in the latter resulting in 17 AA unrelated to those of
CC EAP. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC05246.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAC05247.1; Type=Erroneous initiation; Note=Extended 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/AML1ID52.html";
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DR EMBL; L34598; AAA51720.1; -; mRNA.
DR EMBL; D43967; BAA07902.1; -; mRNA.
DR EMBL; D10570; BAA01426.1; -; mRNA.
DR EMBL; S76345; AAB33729.1; -; mRNA.
DR EMBL; S76346; AAB33730.1; -; mRNA.
DR EMBL; S76350; AAB33731.1; -; mRNA.
DR EMBL; S60998; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; X79549; CAA56092.1; -; mRNA.
DR EMBL; D43968; BAA07903.1; -; mRNA.
DR EMBL; D43969; BAA07904.1; -; mRNA.
DR EMBL; U19601; AAB51691.1; -; mRNA.
DR EMBL; L21756; AAA03086.1; ALT_TERM; mRNA.
DR EMBL; S69002; AAB29907.1; ALT_TERM; mRNA.
DR EMBL; D13979; BAA03089.1; -; mRNA.
DR EMBL; D14822; BAA03559.1; ALT_TERM; mRNA.
DR EMBL; D14823; BAA03560.1; ALT_TERM; mRNA.
DR EMBL; S78158; AAB34819.2; ALT_TERM; mRNA.
DR EMBL; S78159; AAB34820.2; ALT_TERM; mRNA.
DR EMBL; S50186; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; S78496; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; S74092; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; X90979; CAA62466.1; -; mRNA.
DR EMBL; X90976; CAA62464.1; -; mRNA.
DR EMBL; D89790; BAA14022.1; -; mRNA.
DR EMBL; D89788; BAA14020.1; -; mRNA.
DR EMBL; D89789; BAA14021.1; -; mRNA.
DR EMBL; AP000330; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000331; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000332; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000333; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000334; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF015262; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471079; EAX09769.1; -; Genomic_DNA.
DR EMBL; CH471079; EAX09770.1; -; Genomic_DNA.
DR EMBL; BC136380; AAI36381.1; -; mRNA.
DR EMBL; BC136381; AAI36382.1; -; mRNA.
DR EMBL; BC144053; AAI44054.1; -; mRNA.
DR EMBL; AF025841; AAC05246.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF025841; AAC05247.1; ALT_INIT; Genomic_DNA.
DR EMBL; AJ229043; CAA13070.1; -; Genomic_DNA.
DR CCDS; CCDS13639.1; -. [Q01196-8]
DR CCDS; CCDS42922.1; -. [Q01196-1]
DR CCDS; CCDS46646.1; -. [Q01196-3]
DR PIR; I39443; I39443.
DR PIR; S57842; S57842.
DR RefSeq; NP_001001890.1; NM_001001890.2. [Q01196-1]
DR RefSeq; NP_001116079.1; NM_001122607.1. [Q01196-3]
DR RefSeq; NP_001745.2; NM_001754.4. [Q01196-8]
DR RefSeq; XP_005261125.1; XM_005261068.3. [Q01196-10]
DR RefSeq; XP_011528068.1; XM_011529766.2. [Q01196-8]
DR PDB; 1CMO; NMR; -; A=52-178.
DR PDB; 1CO1; NMR; -; A=61-175.
DR PDB; 1E50; X-ray; 2.60 A; A/C/E/G/Q/R=50-183.
DR PDB; 1H9D; X-ray; 2.60 A; A/C=50-183.
DR PDB; 1LJM; X-ray; 2.50 A; A/B=51-181.
DR PDBsum; 1CMO; -.
DR PDBsum; 1CO1; -.
DR PDBsum; 1E50; -.
DR PDBsum; 1H9D; -.
DR PDBsum; 1LJM; -.
DR AlphaFoldDB; Q01196; -.
DR SMR; Q01196; -.
DR BioGRID; 107309; 248.
DR CORUM; Q01196; -.
DR DIP; DIP-36773N; -.
DR ELM; Q01196; -.
DR IntAct; Q01196; 41.
DR MINT; Q01196; -.
DR STRING; 9606.ENSP00000300305; -.
DR BindingDB; Q01196; -.
DR GlyGen; Q01196; 3 sites, 2 O-linked glycans (3 sites).
DR iPTMnet; Q01196; -.
DR MetOSite; Q01196; -.
DR PhosphoSitePlus; Q01196; -.
DR BioMuta; RUNX1; -.
DR DMDM; 215274205; -.
DR EPD; Q01196; -.
DR jPOST; Q01196; -.
DR MassIVE; Q01196; -.
DR MaxQB; Q01196; -.
DR PaxDb; Q01196; -.
DR PeptideAtlas; Q01196; -.
DR PRIDE; Q01196; -.
DR ProteomicsDB; 57927; -. [Q01196-1]
DR ProteomicsDB; 57928; -. [Q01196-10]
DR ProteomicsDB; 57929; -. [Q01196-11]
DR ProteomicsDB; 57930; -. [Q01196-2]
DR ProteomicsDB; 57931; -. [Q01196-3]
DR ProteomicsDB; 57932; -. [Q01196-4]
DR ProteomicsDB; 57933; -. [Q01196-5]
DR ProteomicsDB; 57934; -. [Q01196-6]
DR ProteomicsDB; 57935; -. [Q01196-7]
DR ProteomicsDB; 57936; -. [Q01196-8]
DR ProteomicsDB; 57937; -. [Q01196-9]
DR Antibodypedia; 935; 1139 antibodies from 46 providers.
DR DNASU; 861; -.
DR Ensembl; ENST00000300305.7; ENSP00000300305.3; ENSG00000159216.19. [Q01196-8]
DR Ensembl; ENST00000344691.8; ENSP00000340690.4; ENSG00000159216.19. [Q01196-1]
DR Ensembl; ENST00000358356.9; ENSP00000351123.5; ENSG00000159216.19. [Q01196-3]
DR Ensembl; ENST00000437180.5; ENSP00000409227.1; ENSG00000159216.19. [Q01196-8]
DR Ensembl; ENST00000675419.1; ENSP00000501943.1; ENSG00000159216.19. [Q01196-8]
DR GeneID; 861; -.
DR KEGG; hsa:861; -.
DR MANE-Select; ENST00000675419.1; ENSP00000501943.1; NM_001754.5; NP_001745.2. [Q01196-8]
DR UCSC; uc002yuh.3; human. [Q01196-1]
DR CTD; 861; -.
DR DisGeNET; 861; -.
DR GeneCards; RUNX1; -.
DR GeneReviews; RUNX1; -.
DR HGNC; HGNC:10471; RUNX1.
DR HPA; ENSG00000159216; Low tissue specificity.
DR MalaCards; RUNX1; -.
DR MIM; 151385; gene.
DR MIM; 601399; phenotype.
DR neXtProt; NX_Q01196; -.
DR OpenTargets; ENSG00000159216; -.
DR Orphanet; 102724; Acute myeloid leukemia with t(8;21)(q22;q22) translocation.
DR Orphanet; 98850; Aggressive systemic mastocytosis.
DR Orphanet; 585877; B-lymphoblastic leukemia/lymphoma with recurrent genetic abnormality.
DR Orphanet; 521; Chronic myeloid leukemia.
DR Orphanet; 71290; Familial platelet disorder with associated myeloid malignancy.
DR PharmGKB; PA34884; -.
DR VEuPathDB; HostDB:ENSG00000159216; -.
DR eggNOG; KOG3982; Eukaryota.
DR GeneTree; ENSGT00940000159255; -.
DR HOGENOM; CLU_032910_1_0_1; -.
DR InParanoid; Q01196; -.
DR OMA; PRVNHST; -.
DR OrthoDB; 562214at2759; -.
DR PhylomeDB; Q01196; -.
DR TreeFam; TF321496; -.
DR PathwayCommons; Q01196; -.
DR Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation.
DR Reactome; R-HSA-549127; Organic cation transport.
DR Reactome; R-HSA-8877330; RUNX1 and FOXP3 control the development of regulatory T lymphocytes (Tregs).
DR Reactome; R-HSA-8931987; RUNX1 regulates estrogen receptor mediated transcription.
DR Reactome; R-HSA-8934593; Regulation of RUNX1 Expression and Activity.
DR Reactome; R-HSA-8935964; RUNX1 regulates expression of components of tight junctions.
DR Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-HSA-8939242; RUNX1 regulates transcription of genes involved in differentiation of keratinocytes.
DR Reactome; R-HSA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR Reactome; R-HSA-8939245; RUNX1 regulates transcription of genes involved in BCR signaling.
DR Reactome; R-HSA-8939246; RUNX1 regulates transcription of genes involved in differentiation of myeloid cells.
DR Reactome; R-HSA-8939247; RUNX1 regulates transcription of genes involved in interleukin signaling.
DR Reactome; R-HSA-8939256; RUNX1 regulates transcription of genes involved in WNT signaling.
DR Reactome; R-HSA-8941333; RUNX2 regulates genes involved in differentiation of myeloid cells.
DR Reactome; R-HSA-8951936; RUNX3 regulates p14-ARF.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR Reactome; R-HSA-9616222; Transcriptional regulation of granulopoiesis.
DR SignaLink; Q01196; -.
DR SIGNOR; Q01196; -.
DR BioGRID-ORCS; 861; 63 hits in 1107 CRISPR screens.
DR ChiTaRS; RUNX1; human.
DR EvolutionaryTrace; Q01196; -.
DR GeneWiki; RUNX1; -.
DR GenomeRNAi; 861; -.
DR Pharos; Q01196; Tbio.
DR PRO; PR:Q01196; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; Q01196; protein.
DR Bgee; ENSG00000159216; Expressed in olfactory segment of nasal mucosa and 170 other tissues.
DR ExpressionAtlas; Q01196; baseline and differential.
DR Genevisible; Q01196; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0016513; C:core-binding factor complex; TAS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0001223; F:transcription coactivator binding; IPI:UniProtKB.
DR GO; GO:0001222; F:transcription corepressor binding; IPI:UniProtKB.
DR GO; GO:0061026; P:cardiac muscle tissue regeneration; ISS:BHF-UCL.
DR GO; GO:0002062; P:chondrocyte differentiation; IBA:GO_Central.
DR GO; GO:0071425; P:hematopoietic stem cell proliferation; TAS:UniProtKB.
DR GO; GO:0030097; P:hemopoiesis; IDA:UniProtKB.
DR GO; GO:0030099; P:myeloid cell differentiation; IDA:UniProtKB.
DR GO; GO:0002573; P:myeloid leukocyte differentiation; IMP:ARUK-UCL.
DR GO; GO:0043371; P:negative regulation of CD4-positive, alpha-beta T cell differentiation; ISS:UniProtKB.
DR GO; GO:0030853; P:negative regulation of granulocyte differentiation; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0001503; P:ossification; IBA:GO_Central.
DR GO; GO:0048935; P:peripheral nervous system neuron development; TAS:BHF-UCL.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0043378; P:positive regulation of CD8-positive, alpha-beta T cell differentiation; ISS:UniProtKB.
DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; ISS:BHF-UCL.
DR GO; GO:1903055; P:positive regulation of extracellular matrix organization; ISS:BHF-UCL.
DR GO; GO:0030854; P:positive regulation of granulocyte differentiation; IMP:UniProtKB.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0060043; P:regulation of cardiac muscle cell proliferation; ISS:BHF-UCL.
DR GO; GO:0045595; P:regulation of cell differentiation; IBA:GO_Central.
DR GO; GO:1905203; P:regulation of connective tissue replacement; ISS:BHF-UCL.
DR GO; GO:0010755; P:regulation of plasminogen activation; ISS:BHF-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 2.60.40.720; -; 1.
DR Gene3D; 4.10.770.10; -; 1.
DR InterPro; IPR000040; AML1_Runt.
DR InterPro; IPR008967; p53-like_TF_DNA-bd.
DR InterPro; IPR012346; p53/RUNT-type_TF_DNA-bd_sf.
DR InterPro; IPR013524; Runt_dom.
DR InterPro; IPR027384; Runx_central_dom_sf.
DR InterPro; IPR013711; RunxI_C_dom.
DR InterPro; IPR016554; TF_Runt-rel_RUNX.
DR PANTHER; PTHR11950; PTHR11950; 1.
DR Pfam; PF00853; Runt; 1.
DR Pfam; PF08504; RunxI; 1.
DR PIRSF; PIRSF009374; TF_Runt-rel_RUNX; 1.
DR PRINTS; PR00967; ONCOGENEAML1.
DR SUPFAM; SSF49417; SSF49417; 1.
DR PROSITE; PS51062; RUNT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing; Chloride;
KW Chromosomal rearrangement; Disease variant; DNA-binding; Methylation;
KW Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..453
FT /note="Runt-related transcription factor 1"
FT /id="PRO_0000174655"
FT DOMAIN 50..178
FT /note="Runt"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00399"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..84
FT /note="Interaction with DNA"
FT REGION 135..143
FT /note="Interaction with DNA"
FT REGION 168..177
FT /note="Interaction with DNA"
FT REGION 171..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..371
FT /note="Interaction with KAT6A"
FT /evidence="ECO:0000269|PubMed:11742995"
FT REGION 307..400
FT /note="Interaction with KAT6B"
FT /evidence="ECO:0000250"
FT REGION 362..402
FT /note="Interaction with FOXP3"
FT /evidence="ECO:0000269|PubMed:17377532"
FT REGION 404..445
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 112
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="1"
FT BINDING 116
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="1"
FT BINDING 139
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="2"
FT BINDING 170
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="2"
FT SITE 177..178
FT /note="Breakpoint for translocation to form AML1-EMV-1 (or
FT AML1-EAP) in CML and T-MDS, to form AML1-MTG8 (ETO) in AML-
FT M2, to form AML1-CBFA2T3 in therapy-related myeloid
FT malignancies, to form AML1-MECOM in CML and to form type I
FT MACROD1-RUNX1 fusion protein"
FT SITE 241..242
FT /note="Breakpoint for translocation to form AML1-EAP in T-
FT MDS and CML, to form type II MACROD1-RUNX1 fusion protein
FT and to form RUNX1-CBFA2T2 in acute myeloid leukemia"
FT /evidence="ECO:0000269|PubMed:20520637"
FT MOD_RES 14
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 24
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 43
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 249
FT /note="Phosphoserine; by HIPK2"
FT /evidence="ECO:0000269|PubMed:18695000,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 273
FT /note="Phosphothreonine; by HIPK2"
FT /evidence="ECO:0000269|PubMed:18695000"
FT MOD_RES 276
FT /note="Phosphoserine; by HIPK2"
FT /evidence="ECO:0000269|PubMed:18695000,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 296
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 435
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..105
FT /note="Missing (in isoform AML-1L)"
FT /evidence="ECO:0000303|PubMed:7651838,
FT ECO:0000303|PubMed:9199349"
FT /id="VSP_005919"
FT VAR_SEQ 1..5
FT /note="MRIPV -> MASDSIFESFPSYPQCFMRECILGMNPSRDVH (in
FT isoform AML-1G)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:7651838, ECO:0000303|PubMed:7891692"
FT /id="VSP_005917"
FT VAR_SEQ 1..5
FT /note="MRIPV -> MNPSRDVH (in isoform AML-1H)"
FT /evidence="ECO:0000305"
FT /id="VSP_005916"
FT VAR_SEQ 1..5
FT /note="MRIPV -> MPAAPRGPAQGEAAARTRSR (in isoform AML-1I)"
FT /evidence="ECO:0000305"
FT /id="VSP_005918"
FT VAR_SEQ 137..242
FT /note="VGRSGRGKSFTLTITVFTNPPQVATYHRAIKITVDGPREPRRHRQKLDDQTK
FT PGSLSFSERLSELEQLRRTAMRVSPHHPAPTPNPRASLNHSTAFNPQPQSQMQD -> V
FT DGPREPRRHRQKLDDQTKPGSLSFSERLSELEQLRRTAMRVSPHHPAPTPNPRASLNHS
FT TAFNPQPQSQMQDTRQIQPSPPWSYDQSYQYLGSIASPSVHPATPI (in isoform
FT AML-1FC)"
FT /evidence="ECO:0000305"
FT /id="VSP_005920"
FT VAR_SEQ 178..224
FT /note="RHRQKLDDQTKPGSLSFSERLSELEQLRRTAMRVSPHHPAPTPNPRA -> S
FT KCIHLGLVHPPGWYTLQAGILRDHVSDSLGSTFPPGGWQAPVKPKS (in isoform
FT AML-1FA)"
FT /evidence="ECO:0000305"
FT /id="VSP_005923"
FT VAR_SEQ 178..188
FT /note="RHRQKLDDQTK -> NSLTWPRYPHI (in isoform AML-1FB)"
FT /evidence="ECO:0000305"
FT /id="VSP_005921"
FT VAR_SEQ 189..453
FT /note="Missing (in isoform AML-1FB)"
FT /evidence="ECO:0000305"
FT /id="VSP_005922"
FT VAR_SEQ 225..453
FT /note="Missing (in isoform AML-1FA)"
FT /evidence="ECO:0000305"
FT /id="VSP_005924"
FT VAR_SEQ 242..250
FT /note="DTRQIQPSP -> EEDTAPWRC (in isoform AML-1C)"
FT /evidence="ECO:0000303|PubMed:1720541"
FT /id="VSP_005926"
FT VAR_SEQ 243..453
FT /note="Missing (in isoform AML-1FC)"
FT /evidence="ECO:0000305"
FT /id="VSP_005925"
FT VAR_SEQ 251..453
FT /note="Missing (in isoform AML-1C)"
FT /evidence="ECO:0000303|PubMed:1720541"
FT /id="VSP_005927"
FT VAR_SEQ 258..453
FT /note="Missing (in isoform AML-1E)"
FT /evidence="ECO:0000303|PubMed:8490181"
FT /id="VSP_005928"
FT VAR_SEQ 440..453
FT /note="APSARLEEAVWRPY -> GGASCSRQARRDPGPWARTPSWGRGRPTDRISL
FT (in isoform AML-1A)"
FT /evidence="ECO:0000303|PubMed:7651838,
FT ECO:0000303|PubMed:7835892"
FT /id="VSP_005929"
FT VARIANT 139
FT /note="R -> Q (in FPDMM; dbSNP:rs1060499616)"
FT /evidence="ECO:0000269|PubMed:10508512"
FT /id="VAR_012128"
FT VARIANT 174
FT /note="R -> Q (in FPDMM; impaired phosphorylation;
FT dbSNP:rs74315450)"
FT /evidence="ECO:0000269|PubMed:10508512,
FT ECO:0000269|PubMed:18695000"
FT /id="VAR_012129"
FT VARIANT 431
FT /note="S -> R (in dbSNP:rs1055308)"
FT /id="VAR_013177"
FT VARIANT 433
FT /note="S -> R (in dbSNP:rs1055309)"
FT /id="VAR_013178"
FT MUTAGEN 67
FT /note="S->R: Loss of heterodimerization and reduced EP300
FT phosphorylation induction."
FT /evidence="ECO:0000269|PubMed:18695000"
FT MUTAGEN 80
FT /note="R->A: Strongly reduces DNA-binding."
FT /evidence="ECO:0000269|PubMed:11276260"
FT MUTAGEN 83
FT /note="K->A: Strongly reduces DNA-binding."
FT /evidence="ECO:0000269|PubMed:11276260,
FT ECO:0000269|PubMed:18695000"
FT MUTAGEN 83
FT /note="K->E: Strongly reduces DNA-binding, impaired
FT phosphorylation and reduced EP300 phosphorylation
FT induction."
FT /evidence="ECO:0000269|PubMed:11276260,
FT ECO:0000269|PubMed:18695000"
FT MUTAGEN 84
FT /note="T->A: No effect on DNA binding."
FT /evidence="ECO:0000269|PubMed:11276260"
FT MUTAGEN 106
FT /note="M->V: Disrupts interaction of AML1-MTG8/ETO with
FT CBFB, no effect on AML1-MTG8/ETO-mediated transformation
FT activity."
FT /evidence="ECO:0000269|PubMed:19202074"
FT MUTAGEN 107
FT /note="A->T: Loss of heterodimerization. Disrupts
FT interactionof AML1-MTG8/ETO with CBFB, no effect on AML1-
FT MTG8/ETO-mediated transformation activity."
FT /evidence="ECO:0000269|PubMed:10404214,
FT ECO:0000269|PubMed:19202074"
FT MUTAGEN 108
FT /note="G->R: Loss of heterodimerization and impaired
FT phosphorylation."
FT /evidence="ECO:0000269|PubMed:10404214,
FT ECO:0000269|PubMed:18695000"
FT MUTAGEN 135
FT /note="R->A: Strongly reduces DNA-binding."
FT /evidence="ECO:0000269|PubMed:11276260"
FT MUTAGEN 139
FT /note="R->A: Strongly reduces DNA-binding."
FT /evidence="ECO:0000269|PubMed:11276260"
FT MUTAGEN 140
FT /note="S->G: Disrupts AML1-MTG8/ETO DNA-binding, decreases
FT AML1-MTG8/ETO transforming activity."
FT /evidence="ECO:0000269|PubMed:19202074"
FT MUTAGEN 142
FT /note="R->A: Strongly reduces DNA-binding."
FT /evidence="ECO:0000269|PubMed:11276260"
FT MUTAGEN 145..453
FT /note="Missing: No DNA-binding."
FT MUTAGEN 167
FT /note="K->A: Reduces DNA-binding."
FT /evidence="ECO:0000269|PubMed:11276260"
FT MUTAGEN 169
FT /note="T->A: Strongly reduces DNA-binding."
FT /evidence="ECO:0000269|PubMed:11276260"
FT MUTAGEN 171
FT /note="D->A: Strongly reduces DNA-binding."
FT /evidence="ECO:0000269|PubMed:11276260"
FT MUTAGEN 174
FT /note="R->A: Strongly reduces DNA-binding."
FT /evidence="ECO:0000269|PubMed:11276260"
FT MUTAGEN 177
FT /note="R->A: Strongly reduces DNA-binding."
FT /evidence="ECO:0000269|PubMed:11276260"
FT MUTAGEN 249
FT /note="S->A: Reduced phosphorylation."
FT /evidence="ECO:0000269|PubMed:18695000"
FT MUTAGEN 273
FT /note="T->A: Reduced phosphorylation; when associated with
FT A-276."
FT /evidence="ECO:0000269|PubMed:18695000"
FT MUTAGEN 276
FT /note="S->A: Reduced phosphorylation; when associated with
FT A-273."
FT /evidence="ECO:0000269|PubMed:18695000"
FT CONFLICT 412
FT /note="S -> F (in Ref. 1; AAA51720)"
FT /evidence="ECO:0000305"
FT HELIX 54..57
FT /evidence="ECO:0007829|PDB:1CMO"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:1LJM"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:1LJM"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:1LJM"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:1CMO"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:1LJM"
FT STRAND 102..108
FT /evidence="ECO:0007829|PDB:1LJM"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:1H9D"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:1LJM"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:1LJM"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:1LJM"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:1LJM"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:1E50"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:1LJM"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:1LJM"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:1CMO"
SQ SEQUENCE 453 AA; 48737 MW; 4F1F193A7CADDBAB CRC64;
MRIPVDASTS RRFTPPSTAL SPGKMSEALP LGAPDAGAAL AGKLRSGDRS MVEVLADHPG
ELVRTDSPNF LCSVLPTHWR CNKTLPIAFK VVALGDVPDG TLVTVMAGND ENYSAELRNA
TAAMKNQVAR FNDLRFVGRS GRGKSFTLTI TVFTNPPQVA TYHRAIKITV DGPREPRRHR
QKLDDQTKPG SLSFSERLSE LEQLRRTAMR VSPHHPAPTP NPRASLNHST AFNPQPQSQM
QDTRQIQPSP PWSYDQSYQY LGSIASPSVH PATPISPGRA SGMTTLSAEL SSRLSTAPDL
TAFSDPRQFP ALPSISDPRM HYPGAFTYSP TPVTSGIGIG MSAMGSATRY HTYLPPPYPG
SSQAQGGPFQ ASSPSYHLYY GASAGSYQFS MVGGERSPPR ILPPCTNAST GSALLNPSLP
NQSDVVEAEG SHSNSPTNMA PSARLEEAVW RPY
