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Runt-related transcription factor 1 (Acute myeloid leukemia 1 protein) (Core-binding factor subunit alpha-2) (CBF-alpha-2) (Oncogene AML-1) (Polyomavirus enhancer-binding protein 2 alpha B subunit) (PEA2-alpha B) (PEBP2-alpha B) (SL3-3 enhancer factor 1 alpha B subunit) (SL3/AKV core-binding factor alpha B subunit)

 RUNX1_HUMAN             Reviewed;         453 AA.
Q01196; A8MV94; B2RMS4; D3DSG1; O60472; O60473; O76047; O76089;
Q13081; Q13755; Q13756; Q13757; Q13758; Q13759; Q15341; Q15343;
Q16122; Q16284; Q16285; Q16286; Q16346; Q16347; Q92479;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
25-NOV-2008, sequence version 3.
22-NOV-2017, entry version 217.
RecName: Full=Runt-related transcription factor 1;
AltName: Full=Acute myeloid leukemia 1 protein;
AltName: Full=Core-binding factor subunit alpha-2;
Short=CBF-alpha-2;
AltName: Full=Oncogene AML-1;
AltName: Full=Polyomavirus enhancer-binding protein 2 alpha B subunit;
Short=PEA2-alpha B;
Short=PEBP2-alpha B;
AltName: Full=SL3-3 enhancer factor 1 alpha B subunit;
AltName: Full=SL3/AKV core-binding factor alpha B subunit;
Name=RUNX1; Synonyms=AML1, CBFA2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Ahn M.-Y., Bae S.C., Zhang Y.W., Shigesada K., Ito Y.;
Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM AML-1C).
TISSUE=Leukocyte;
PubMed=1720541; DOI=10.1073/pnas.88.23.10431;
Miyoshi H., Shimizu K., Kozu T., Maseki N., Kaneko Y., Ohki M.;
"t(8;21) breakpoints on chromosome 21 in acute myeloid leukemia are
clustered within a limited region of a single gene, AML1.";
Proc. Natl. Acad. Sci. U.S.A. 88:10431-10434(1991).
[3]
ALTERNATIVE PRODUCTS, AND CHROMOSOMAL TRANSLOCATION WITH EAP.
PubMed=7533526; DOI=10.1002/gcc.2870110405;
Sacchi N., Nisson P.E., Watkins P.C., Faustinella F., Wijsman J.,
Hagemeijer A.;
"AML1 fusion transcripts in t(3;21) positive leukemia: evidence of
molecular heterogeneity and usage of splicing sites frequently
involved in the generation of normal AML1 transcripts.";
Genes Chromosomes Cancer 11:226-236(1994).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM AML-1E), AND CHROMOSOMAL
TRANSLOCATION WITH ETO.
PubMed=8490181;
Nucifora G., Birn D.J., Espinosa R. III, Erickson P., Lebeau M.M.,
Roulston D., McKeithan T.W., Drabkin H., Rowley J.D.;
"Involvement of the AML1 gene in the t(3;21) in therapy-related
leukemia and in chronic myeloid leukemia in blast crisis.";
Blood 81:2728-2734(1993).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM AML-1A).
TISSUE=Monocyte;
PubMed=7835892; DOI=10.1006/geno.1994.1519;
Levanon D., Negreanu V., Bernstein Y., Bar-Am I., Avivi L., Groner Y.;
"AML1, AML2, and AML3, the human members of the runt domain gene-
family: cDNA structure, expression, and chromosomal localization.";
Genomics 23:425-432(1994).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS AML-1B; AML-1A; AML-1G AND
AML-1L).
PubMed=7651838; DOI=10.1093/nar/23.14.2762;
Miyoshi H., Ohira M., Shimizu K., Mitani K., Hirai H., Imai T.,
Yokoyama K., Soeda E., Ohki M.;
"Alternative splicing and genomic structure of the AML1 gene involved
in acute myeloid leukemia.";
Nucleic Acids Res. 23:2762-2769(1995).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM AML-1G).
TISSUE=B-cell;
PubMed=7891692; DOI=10.1128/MCB.15.4.1974;
Meyers S., Lenny N., Hiebert S.W.;
"The t(8;21) fusion protein interferes with AML-1B-dependent
transcriptional activation.";
Mol. Cell. Biol. 15:1974-1982(1995).
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM AML-1L).
PubMed=9199349; DOI=10.1128/MCB.17.7.4133;
Zhang Y.-W., Bae S.-C., Huang G., Fu Y.-X., Lu J., Ahn M.-Y.,
Kanno Y., Kanno T., Ito Y.;
"A novel transcript encoding an N-terminally truncated AML1/PEBP2
alphaB protein interferes with transactivation and blocks granulocytic
differentiation of 32Dcl3 myeloid cells.";
Mol. Cell. Biol. 17:4133-4145(1997).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10830953; DOI=10.1038/35012518;
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T.,
Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y.,
Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K.,
Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D.,
Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W.,
Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S.,
Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E.,
Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P.,
Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H.,
Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E.,
Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F.,
Lehrach H., Reinhardt R., Yaspo M.-L.;
"The DNA sequence of human chromosome 21.";
Nature 405:311-319(2000).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM AML-1G).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-177, AND CHROMOSOMAL TRANSLOCATION
WITH MECOM IN CHRONIC MYELOCYTIC LEUKEMIA.
PubMed=8313895;
Mitani K., Ogawa S., Tanaka T., Miyoshi H., Kurokawa M., Mano H.,
Yazaki Y., Ohki M., Hirai H.;
"Generation of the AML1-EVI-1 fusion gene in the t(3;21)(q26;q22)
causes blastic crisis in chronic myelocytic leukemia.";
EMBO J. 13:504-510(1994).
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-90 (ISOFORMS AML-1H AND
AML-1I).
PubMed=8700862; DOI=10.1073/pnas.93.5.1935;
Ghozi M.C., Bernstein Y., Negreanu V., Levanon D., Groner Y.;
"Expression of the human acute myeloid leukemia gene AML1 is regulated
by two promoter regions.";
Proc. Natl. Acad. Sci. U.S.A. 93:1935-1940(1996).
[14]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 440-453, AND ALTERNATIVE
SPLICING.
TISSUE=Monocyte;
PubMed=8634147; DOI=10.1089/dna.1996.15.175;
Levanon D., Bernstein Y., Negreanu V., Ghozi M.C., Bar-Am I.,
Aloya R., Goldenberg D., Lotem J., Groner Y.;
"A large variety of alternatively spliced and differentially expressed
mRNAs are encoded by the human acute myeloid leukemia gene AML1.";
DNA Cell Biol. 15:175-185(1996).
[15]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19, AND ALTERNATIVE SPLICING
(ISOFORM AML-1G).
Blechschmidt K., Rump A., Nordsiek G., Drescher B., Weber J.,
Rosenthal A.;
"Sequencing and analysis of 960 kb between AML1 and CBR1 on chromosome
21q22.2.";
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
[16]
SIMILARITY TO RUNT.
PubMed=1560822; DOI=10.1038/356484b0;
Daga A., Tighe J.E., Calabi F.;
"Leukaemia/Drosophila homology.";
Nature 356:484-484(1992).
[17]
ENHANCER CORE BINDING SEQUENCE.
PubMed=8413232; DOI=10.1128/MCB.13.10.6336;
Meyers S., Downing J.R., Hiebert S.W.;
"Identification of AML-1 and the (8;21) translocation protein (AML-
1/ETO) as sequence-specific DNA-binding proteins: the runt homology
domain is required for DNA binding and protein-protein interactions.";
Mol. Cell. Biol. 13:6336-6345(1993).
[18]
INTERACTION WITH ALYREF/THOC4.
PubMed=9119228; DOI=10.1101/gad.11.5.640;
Bruhn L., Munnerlyn A., Grosschedl R.;
"ALY, a context-dependent coactivator of LEF-1 and AML-1, is required
for TCRalpha enhancer function.";
Genes Dev. 11:640-653(1997).
[19]
CHROMOSOMAL TRANSLOCATION WITH CBFA2T3.
PubMed=9596646;
Gamou T., Kitamura E., Hosoda F., Shimuzu K., Hayashi Y., Nagase T.,
Yokoyama Y., Ohki M.;
"The partner gene of AML1 in t(16;21) myeloid malignancies is a novel
member of the MTG8(ETO) family.";
Blood 91:4028-4037(1998).
[20]
INTERACTION WITH TLE1.
PubMed=9751710; DOI=10.1073/pnas.95.20.11590;
Levanon D., Goldstein R.E., Bernstein Y., Tang H., Goldenberg D.,
Stifani S., Paroush Z., Groner Y.;
"Transcriptional repression by AML1 and LEF-1 is mediated by the
TLE/Groucho corepressors.";
Proc. Natl. Acad. Sci. U.S.A. 95:11590-11595(1998).
[21]
FUNCTION, AND INTERACTION WITH ELF1; ELF2; ELF4 AND SPI1.
PubMed=10207087; DOI=10.1128/MCB.19.5.3635;
Mao S., Frank R.C., Zhang J., Miyazaki Y., Nimer S.D.;
"Functional and physical interactions between AML1 proteins and an ETS
protein, MEF: implications for the pathogenesis of t(8;21)-positive
leukemias.";
Mol. Cell. Biol. 19:3635-3644(1999).
[22]
INTERACTION WITH KAT6A, AND PHOSPHORYLATION.
PubMed=11742995; DOI=10.1093/emboj/20.24.7184;
Kitabayashi I., Aikawa Y., Nguyen L.A., Yokoyama A., Ohki M.;
"Activation of AML1-mediated transcription by MOZ and inhibition by
the MOZ-CBP fusion protein.";
EMBO J. 20:7184-7196(2001).
[23]
INTERACTION WITH KAT6B, AND FUNCTION.
PubMed=11965546; DOI=10.1038/sj.onc.1205367;
Pelletier N., Champagne N., Stifani S., Yang X.-J.;
"MOZ and MORF histone acetyltransferases interact with the Runt-domain
transcription factor Runx2.";
Oncogene 21:2729-2740(2002).
[24]
INTERACTION WITH SUV39H1, AND METHYLATION.
PubMed=12917624; DOI=10.1038/sj.onc.1206600;
Chakraborty S., Sinha K.K., Senyuk V., Nucifora G.;
"SUV39H1 interacts with AML1 and abrogates AML1 transactivity. AML1 is
methylated in vivo.";
Oncogene 22:5229-5237(2003).
[25]
FUNCTION, AND INTERACTION WITH ELF2.
PubMed=14970218; DOI=10.1074/jbc.M309074200;
Cho J.-Y., Akbarali Y., Zerbini L.F., Gu X., Boltax J., Wang Y.,
Oettgen P., Zhang D.-E., Libermann T.A.;
"Isoforms of the Ets transcription factor NERF/ELF-2 physically
interact with AML1 and mediate opposing effects on AML1-mediated
transcription of the B cell-specific blk gene.";
J. Biol. Chem. 279:19512-19522(2004).
[26]
INTERACTION WITH SUV39H1.
PubMed=16652147; DOI=10.1038/sj.onc.1209591;
Reed-Inderbitzin E., Moreno-Miralles I., Vanden-Eynden S.K., Xie J.,
Lutterbach B., Durst-Goodwin K.L., Luce K.S., Irvin B.J., Cleary M.L.,
Brandt S.J., Hiebert S.W.;
"RUNX1 associates with histone deacetylases and SUV39H1 to repress
transcription.";
Oncogene 25:5777-5786(2006).
[27]
FUNCTION IN MYELOID DIFFERENTIATION, AND INTERACTION WITH CDK6.
PubMed=17431401; DOI=10.1038/sj.emboj.7601675;
Fujimoto T., Anderson K., Jacobsen S.E., Nishikawa S.I., Nerlov C.;
"Cdk6 blocks myeloid differentiation by interfering with Runx1 DNA
binding and Runx1-C/EBPalpha interaction.";
EMBO J. 26:2361-2370(2007).
[28]
CHROMOSOMAL TRANSLOCATION WITH MACROD1.
PubMed=17532767; DOI=10.1111/j.1600-0609.2007.00858.x;
Imagama S., Abe A., Suzuki M., Hayakawa F., Katsumi A., Emi N.,
Kiyoi H., Naoe T.;
"LRP16 is fused to RUNX1 in monocytic leukemia cell line with
t(11;21)(q13;q22).";
Eur. J. Haematol. 79:25-31(2007).
[29]
FUNCTION, AND INTERACTION WITH FOXP3.
PubMed=17377532; DOI=10.1038/nature05673;
Ono M., Yaguchi H., Ohkura N., Kitabayashi I., Nagamura Y., Nomura T.,
Miyachi Y., Tsukada T., Sakaguchi S.;
"Foxp3 controls regulatory T-cell function by interacting with
AML1/Runx1.";
Nature 446:685-689(2007).
[30]
PHOSPHORYLATION AT SER-249; THR-273 AND SER-276 BY HIPK2, VARIANT
GLN-174, AND MUTAGENESIS OF SER-67; LYS-83; GLY-108; SER-249; THR-273
AND SER-276.
PubMed=18695000; DOI=10.1182/blood-2008-01-134122;
Wee H.-J., Voon D.C.-C., Bae S.-C., Ito Y.;
"PEBP2-beta/CBF-beta-dependent phosphorylation of RUNX1 and p300 by
HIPK2: implications for leukemogenesis.";
Blood 112:3777-3787(2008).
[31]
INTERACTION WITH YAP1.
PubMed=18280240; DOI=10.1016/j.molcel.2007.12.022;
Levy D., Adamovich Y., Reuven N., Shaul Y.;
"Yap1 phosphorylation by c-Abl is a critical step in selective
activation of proapoptotic genes in response to DNA damage.";
Mol. Cell 29:350-361(2008).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14 AND SER-21, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[33]
INTERACTION WITH CBFB, AND MUTAGENESIS OF MET-106; ALA-107 AND
SER-140.
PubMed=19202074; DOI=10.1073/pnas.0810558106;
Kwok C., Zeisig B.B., Qiu J., Dong S., So C.W.;
"Transforming activity of AML1-ETO is independent of CBFbeta and ETO
interaction but requires formation of homo-oligomeric complexes.";
Proc. Natl. Acad. Sci. U.S.A. 106:2853-2858(2009).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14; SER-249; SER-266;
SER-268 AND SER-276, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[35]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-24 AND LYS-43, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[36]
CHROMOSOMAL TRANSLOCATION WITH CBFA2T2.
PubMed=20520637; DOI=10.1038/leu.2010.106;
Guastadisegni M.C., Lonoce A., Impera L., Di Terlizzi F., Fugazza G.,
Aliano S., Grasso R., Cluzeau T., Raynaud S., Rocchi M.,
Storlazzi C.T.;
"CBFA2T2 and C20orf112: two novel fusion partners of RUNX1 in acute
myeloid leukemia.";
Leukemia 24:1516-1519(2010).
[37]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14; SER-21; SER-193;
SER-212 AND THR-296, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[38]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-212 AND SER-435, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[39]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 59-173 IN COMPLEX WITH CBFB.
PubMed=10856244; DOI=10.1093/emboj/19.12.3004;
Warren A.J., Bravo J., Williams R.L., Rabbitts T.H.;
"Structural basis for the heterodimeric interaction between the acute
leukaemia-associated transcription factors AML1 and CBFbeta.";
EMBO J. 19:3004-3015(2000).
[40]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 54-243 IN COMPLEX WITH CBFB
AND DNA, AND MUTAGENESIS OF ARG-80; LYS-83; THR-84; ARG-135; ARG-139;
ARG-142; LYS-167; THR-169; ASP-171; ARG-174 AND ARG-177.
PubMed=11276260; DOI=10.1038/86264;
Bravo J., Li Z., Speck N.A., Warren A.J.;
"The leukemia-associated AML1 (Runx1) -- CBF beta complex functions as
a DNA-induced molecular clamp.";
Nat. Struct. Biol. 8:371-378(2001).
[41]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 61-174 IN COMPLEX WITH DNA.
PubMed=12377125; DOI=10.1016/S0969-2126(02)00853-5;
Bartfeld D., Shimon L., Couture G.C., Rabinovich D., Frolow F.,
Levanon D., Groner Y., Shakked Z.;
"DNA recognition by the RUNX1 transcription factor is mediated by an
allosteric transition in the RUNT domain and by DNA bending.";
Structure 10:1395-1407(2002).
[42]
STRUCTURE BY NMR OF 53-178, AND MUTAGENESIS OF ALA-107 AND GLY-108.
PubMed=10404214; DOI=10.1038/10658;
Nagata T., Gupta V., Sorce D., Kim W.-Y., Sali A., Chait B.T.,
Shigesada K., Ito Y., Werner M.H.;
"Immunoglobulin motif DNA recognition and heterodimerization of the
PEBP2/CBF Runt domain.";
Nat. Struct. Biol. 6:615-619(1999).
[43]
STRUCTURE BY NMR OF 61-175 IN COMPLEX WITH DNA.
PubMed=10545320; DOI=10.1016/S0969-2126(00)80058-1;
Berardi M.J., Sun C., Zehr M., Abildgaard F., Peng J., Speck N.A.,
Bushweller J.H.;
"The Ig fold of the core binding factor alpha Runt domain is a member
of a family of structurally and functionally related Ig-fold DNA-
binding domains.";
Structure 7:1247-1256(1999).
[44]
X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 46-185, AND
CHLORIDE-BINDING.
PubMed=12217689; DOI=10.1016/S0022-2836(02)00702-7;
Baeckstroem S., Wolf-Watz M., Grundstroem C., Haerd T.,
Grundstroem T., Sauer U.H.;
"The RUNX1 Runt domain at 1.25A resolution: a structural switch and
specifically bound chloride ions modulate DNA binding.";
J. Mol. Biol. 322:259-272(2002).
[45]
REVIEW ON AML1 TRANSLOCATIONS.
PubMed=7795214;
Nucifora G., Rowley J.D.;
"AML1 and the 8;21 and 3;21 translocations in acute and chronic
myeloid leukemia.";
Blood 86:1-14(1995).
[46]
CHROMOSOMAL TRANSLOCATION WITH MTG8/ETO IN AML-M2.
PubMed=1423235; DOI=10.1016/0165-4608(92)90384-K;
Nisson P.E., Watkins P.C., Sacchi N.;
"Transcriptionally active chimeric gene derived from the fusion of the
AML1 gene and a novel gene on chromosome 8 in t(8;21) leukemic
cells.";
Cancer Genet. Cytogenet. 63:81-88(1992).
[47]
CHROMOSOMAL TRANSLOCATION WITH MTG8/ETO IN AML-M2.
PubMed=8353289;
Kozu T., Miyoshi H., Shimizu K., Maseki N., Kaneko Y., Asou H.,
Kamada N., Ohki M.;
"Junctions of the AML1/MTG8(ETO) fusion are constant in t(8;21) acute
myeloid leukemia detected by reverse transcription polymerase chain
reaction.";
Blood 82:1270-1276(1993).
[48]
CHROMOSOMAL TRANSLOCATION WITH MTG8/ETO IN AML-M2.
PubMed=8334990;
Miyoshi H., Kozu T., Shimizu K., Enomoto K., Maseki N., Kaneko Y.,
Kamada N., Ohki M.;
"The t(8;21) translocation in acute myeloid leukemia results in
production of an AML1-MTG8 fusion transcript.";
EMBO J. 12:2715-2721(1993).
[49]
CHROMOSOMAL TRANSLOCATION WITH EAP IN MYELODYSPLASIA.
TISSUE=Peripheral blood;
PubMed=8395054; DOI=10.1073/pnas.90.16.7784;
Nucifora G., Begy C.R., Erickson P., Drabkin H.A., Rowley J.D.;
"The 3;21 translocation in myelodysplasia results in a fusion
transcript between the AML1 gene and the gene for EAP, a highly
conserved protein associated with the Epstein-Barr virus small RNA
EBER 1.";
Proc. Natl. Acad. Sci. U.S.A. 90:7784-7788(1993).
[50]
CHROMOSOMAL TRANSLOCATION WITH MTG8/ETO IN AML-M2.
PubMed=7919324;
Tighe J.E., Calabi F.;
"Alternative, out-of-frame runt/MTG8 transcripts are encoded by the
derivative (8) chromosome in the t(8;21) of acute myeloid leukemia
M2.";
Blood 84:2115-2121(1994).
[51]
CHROMOSOMAL TRANSLOCATION WITH TEL IN ACUTE LYMPHOBLASTIC LEUKEMIA
(ALL).
PubMed=7780150;
Romana S.P., Mauchauffe M., le Coniat M., Chumakov I., le Paslier D.,
Berger R., Bernard O.A.;
"The t(12;21) of acute lymphoblastic leukemia results in a tel-AML1
gene fusion.";
Blood 85:3662-3670(1995).
[52]
CHROMOSOMAL TRANSLOCATION WITH MTG8/ETO IN AML-M2.
PubMed=7541640; DOI=10.1002/gcc.2870130105;
Era T., Asou N., Kunisada T., Yamasaki H., Asou H., Kamada N.,
Nishikawa S., Yamaguchi K., Takatsuki K.;
"Identification of two transcripts of AML1/ETO-fused gene in t(8;21)
leukemic cells and expression of wild-type ETO gene in hematopoietic
cells.";
Genes Chromosomes Cancer 13:25-33(1995).
[53]
CHROMOSOMAL TRANSLOCATION WITH TEL IN ACUTE LYMPHOBLASTIC LEUKEMIA
(ALL).
PubMed=7761424; DOI=10.1073/pnas.92.11.4917;
Golub T.R., Barker G.F., Bohlander S.K., Hiebert S.W., Ward D.C.,
Bray-Ward P., Morgan E., Raimondi S.C., Rowley J.D., Gilliland D.G.;
"Fusion of the TEL gene on 12p13 to the AML1 gene on 21q22 in acute
lymphoblastic leukemia.";
Proc. Natl. Acad. Sci. U.S.A. 92:4917-4921(1995).
[54]
VARIANTS FPDMM GLN-139 AND GLN-174.
PubMed=10508512; DOI=10.1038/13793;
Song W.-J., Sullivan M.G., Legare R.D., Hutchings S., Tan X.,
Kufrin D., Ratajczak J., Resende I.C., Haworth C., Hock R., Loh M.,
Felix C., Roy D.-C., Busque L., Kurnit D., Willman C., Gewirtz A.M.,
Speck N.A., Bushweller J.H., Li F.P., Gardiner K., Poncz M.,
Maris J.M., Gilliland D.G.;
"Haploinsufficiency of CBFA2 causes familial thrombocytopenia with
propensity to develop acute myelogenous leukaemia.";
Nat. Genet. 23:166-175(1999).
[55]
CHROMOSOMAL REARRANGEMENT.
PubMed=18925961; DOI=10.1186/1471-2407-8-299;
Gelsi-Boyer V., Trouplin V., Adelaide J., Aceto N., Remy V.,
Pinson S., Houdayer C., Arnoulet C., Sainty D., Bentires-Alj M.,
Olschwang S., Vey N., Mozziconacci M.-J., Birnbaum D., Chaffanet M.;
"Genome profiling of chronic myelomonocytic leukemia: frequent
alterations of RAS and RUNX1 genes.";
BMC Cancer 8:299-299(2008).
-!- FUNCTION: CBF binds to the core site, 5'-PYGPYGGT-3', of a number
of enhancers and promoters, including murine leukemia virus,
polyomavirus enhancer, T-cell receptor enhancers, LCK, IL-3 and
GM-CSF promoters. The alpha subunit binds DNA and appears to have
a role in the development of normal hematopoiesis. Isoform AML-1L
interferes with the transactivation activity of RUNX1. Acts
synergistically with ELF4 to transactivate the IL-3 promoter and
with ELF2 to transactivate the mouse BLK promoter. Inhibits KAT6B-
dependent transcriptional activation. Controls the anergy and
suppressive function of regulatory T-cells (Treg) by associating
with FOXP3. Activates the expression of IL2 and IFNG and down-
regulates the expression of TNFRSF18, IL2RA and CTLA4, in
conventional T-cells (PubMed:17377532). Positively regulates the
expression of RORC in T-helper 17 cells (By similarity).
{ECO:0000250|UniProtKB:Q03347, ECO:0000269|PubMed:10207087,
ECO:0000269|PubMed:11965546, ECO:0000269|PubMed:14970218,
ECO:0000269|PubMed:17377532, ECO:0000269|PubMed:17431401}.
-!- SUBUNIT: Heterodimer with CBFB. RUNX1 binds DNA as a monomer and
through the Runt domain. DNA-binding is increased by
heterodimerization. Isoform AML-1L can neither bind DNA nor
heterodimerize. Interacts with TLE1 and ALYREF/THOC4. Interacts
with ELF1, ELF2 and SPI1. Interacts via its Runt domain with the
ELF4 N-terminal region. Interaction with ELF2 isoform 2 (NERF-1a)
may act to repress RUNX1-mediated transactivation. Interacts with
KAT6A and KAT6B. Interacts with SUV39H1, leading to abrogation of
transactivating and DNA-binding properties of RUNX1. Interacts
with YAP1. Interacts with HIPK2 (By similarity). Interaction with
CDK6 prevents myeloid differentiation, reducing its transcription
transactivation activity. Found in a complex with PRMT5, RUNX1 AND
CBFB. Interacts with FOXP3. Interacts with TBX21 (By similarity).
{ECO:0000250|UniProtKB:Q03347, ECO:0000269|PubMed:10207087,
ECO:0000269|PubMed:10545320, ECO:0000269|PubMed:10856244,
ECO:0000269|PubMed:11276260, ECO:0000269|PubMed:11742995,
ECO:0000269|PubMed:11965546, ECO:0000269|PubMed:12377125,
ECO:0000269|PubMed:12917624, ECO:0000269|PubMed:14970218,
ECO:0000269|PubMed:16652147, ECO:0000269|PubMed:17377532,
ECO:0000269|PubMed:17431401, ECO:0000269|PubMed:18280240,
ECO:0000269|PubMed:9119228, ECO:0000269|PubMed:9751710}.
-!- INTERACTION:
Q13951:CBFB; NbExp=3; IntAct=EBI-925904, EBI-718750;
Q00534:CDK6; NbExp=5; IntAct=EBI-925904, EBI-295663;
Q15723:ELF2; NbExp=2; IntAct=EBI-925904, EBI-956941;
P16371:gro (xeno); NbExp=4; IntAct=EBI-925940, EBI-153866;
Q9H2X6:HIPK2; NbExp=4; IntAct=EBI-925904, EBI-348345;
P17542:TAL1; NbExp=3; IntAct=EBI-925904, EBI-1753878;
Q04724:TLE1; NbExp=4; IntAct=EBI-925940, EBI-711424;
P46937:YAP1; NbExp=3; IntAct=EBI-925904, EBI-1044059;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=11;
Comment=Additional isoforms seem to exist.;
Name=AML-1B;
IsoId=Q01196-1; Sequence=Displayed;
Name=AML-1A;
IsoId=Q01196-2; Sequence=VSP_005929;
Name=AML-1C;
IsoId=Q01196-3; Sequence=VSP_005926, VSP_005927;
Name=AML-1E;
IsoId=Q01196-4; Sequence=VSP_005928;
Name=AML-1FA;
IsoId=Q01196-5; Sequence=VSP_005923, VSP_005924;
Name=AML-1FB;
IsoId=Q01196-6; Sequence=VSP_005921, VSP_005922;
Name=AML-1FC;
IsoId=Q01196-7; Sequence=VSP_005920, VSP_005925;
Name=AML-1G;
IsoId=Q01196-8; Sequence=VSP_005917;
Name=AML-1H;
IsoId=Q01196-9; Sequence=VSP_005916;
Name=AML-1I;
IsoId=Q01196-10; Sequence=VSP_005918;
Name=AML-1L; Synonyms=AML1-delta N;
IsoId=Q01196-11; Sequence=VSP_005919;
-!- TISSUE SPECIFICITY: Expressed in all tissues examined except brain
and heart. Highest levels in thymus, bone marrow and peripheral
blood.
-!- DOMAIN: A proline/serine/threonine rich region at the C-terminus
is necessary for transcriptional activation of target genes.
-!- PTM: Phosphorylated in its C-terminus upon IL-6 treatment.
Phosphorylation enhances interaction with KAT6A.
-!- PTM: Methylated. {ECO:0000269|PubMed:12917624}.
-!- PTM: Phosphorylated in Ser-249 Thr-273 and Ser-276 by HIPK2 when
associated with CBFB and DNA. This phosphorylation promotes
subsequent EP300 phosphorylation. {ECO:0000269|PubMed:18695000}.
-!- DISEASE: Note=A chromosomal aberration involving RUNX1/AML1 is a
cause of M2 type acute myeloid leukemia (AML-M2). Translocation
t(8;21)(q22;q22) with RUNX1T1.
-!- DISEASE: Note=A chromosomal aberration involving RUNX1/AML1 is a
cause of therapy-related myelodysplastic syndrome (T-MDS).
Translocation t(3;21)(q26;q22) with EAP or MECOM.
-!- DISEASE: Note=A chromosomal aberration involving RUNX1/AML1 is a
cause of chronic myelogenous leukemia (CML). Translocation
t(3;21)(q26;q22) with EAP or MECOM.
-!- DISEASE: Note=A chromosomal aberration involving RUNX1/AML1 is
found in childhood acute lymphoblastic leukemia (ALL).
Translocation t(12;21)(p13;q22) with TEL. The translocation fuses
the 3'-end of TEL to the alternate 5'-exon of AML-1H.
-!- DISEASE: Note=A chromosomal aberration involving RUNX1 is found in
acute leukemia. Translocation t(11,21)(q13;q22) that forms a
MACROD1-RUNX1 fusion protein.
-!- DISEASE: Familial platelet disorder with associated myeloid
malignancy (FPDMM) [MIM:601399]: Autosomal dominant disease
characterized by qualitative and quantitative platelet defects,
and propensity to develop acute myelogenous leukemia.
{ECO:0000269|PubMed:10508512}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Note=A chromosomal aberration involving RUNX1/AML1 is
found in therapy-related myeloid malignancies. Translocation
t(16;21)(q24;q22) that forms a RUNX1-CBFA2T3 fusion protein.
-!- DISEASE: Note=A chromosomal aberration involving RUNX1/AML1 is a
cause of chronic myelomonocytic leukemia. Inversion
inv(21)(q21;q22) with USP16.
-!- DISEASE: Note=A chromosomal aberration involving RUNX1/AML1 is
found in acute myeloid leukemia. Translocation t(20;21)(q11;q22)
with CBFA2T2. {ECO:0000269|PubMed:20520637}.
-!- CAUTION: The fusion of AML1 with EAP in T-MDS induces a change of
reading frame in the latter resulting in 17 AA unrelated to those
of EAP. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC05246.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
Sequence=AAC05247.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/AML1ID52.html";
-----------------------------------------------------------------------
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EMBL; L34598; AAA51720.1; -; mRNA.
EMBL; D43967; BAA07902.1; -; mRNA.
EMBL; D10570; BAA01426.1; -; mRNA.
EMBL; S76345; AAB33729.1; -; mRNA.
EMBL; S76346; AAB33730.1; -; mRNA.
EMBL; S76350; AAB33731.1; -; mRNA.
EMBL; S60998; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; X79549; CAA56092.1; -; mRNA.
EMBL; D43968; BAA07903.1; -; mRNA.
EMBL; D43969; BAA07904.1; -; mRNA.
EMBL; U19601; AAB51691.1; -; mRNA.
EMBL; L21756; AAA03086.1; ALT_TERM; mRNA.
EMBL; S69002; AAB29907.1; ALT_TERM; mRNA.
EMBL; D13979; BAA03089.1; -; mRNA.
EMBL; D14822; BAA03559.1; ALT_TERM; mRNA.
EMBL; D14823; BAA03560.1; ALT_TERM; mRNA.
EMBL; S78158; AAB34819.2; ALT_TERM; mRNA.
EMBL; S78159; AAB34820.2; ALT_TERM; mRNA.
EMBL; S50186; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; S78496; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; S74092; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; X90979; CAA62466.1; -; mRNA.
EMBL; X90976; CAA62464.1; -; mRNA.
EMBL; D89790; BAA14022.1; -; mRNA.
EMBL; D89788; BAA14020.1; -; mRNA.
EMBL; D89789; BAA14021.1; -; mRNA.
EMBL; AP000330; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP000331; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP000332; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP000333; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP000334; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF015262; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471079; EAX09769.1; -; Genomic_DNA.
EMBL; CH471079; EAX09770.1; -; Genomic_DNA.
EMBL; BC136380; AAI36381.1; -; mRNA.
EMBL; BC136381; AAI36382.1; -; mRNA.
EMBL; BC144053; AAI44054.1; -; mRNA.
EMBL; AF025841; AAC05246.1; ALT_INIT; Genomic_DNA.
EMBL; AF025841; AAC05247.1; ALT_INIT; Genomic_DNA.
EMBL; AJ229043; CAA13070.1; -; Genomic_DNA.
CCDS; CCDS13639.1; -. [Q01196-8]
CCDS; CCDS42922.1; -. [Q01196-1]
CCDS; CCDS46646.1; -. [Q01196-3]
PIR; I39443; I39443.
PIR; S57842; S57842.
RefSeq; NP_001001890.1; NM_001001890.2. [Q01196-1]
RefSeq; NP_001116079.1; NM_001122607.1. [Q01196-3]
RefSeq; NP_001745.2; NM_001754.4. [Q01196-8]
RefSeq; XP_005261125.1; XM_005261068.3. [Q01196-10]
RefSeq; XP_011528068.1; XM_011529766.2. [Q01196-8]
UniGene; Hs.149261; -.
UniGene; Hs.612648; -.
UniGene; Hs.705364; -.
PDB; 1CMO; NMR; -; A=52-178.
PDB; 1CO1; NMR; -; A=61-175.
PDB; 1E50; X-ray; 2.60 A; A/C/E/G/Q/R=50-183.
PDB; 1H9D; X-ray; 2.60 A; A/C=50-183.
PDB; 1LJM; X-ray; 2.50 A; A/B=51-181.
PDBsum; 1CMO; -.
PDBsum; 1CO1; -.
PDBsum; 1E50; -.
PDBsum; 1H9D; -.
PDBsum; 1LJM; -.
ProteinModelPortal; Q01196; -.
SMR; Q01196; -.
BioGrid; 107309; 81.
CORUM; Q01196; -.
DIP; DIP-36773N; -.
ELM; Q01196; -.
IntAct; Q01196; 34.
MINT; MINT-153610; -.
STRING; 9606.ENSP00000300305; -.
BindingDB; Q01196; -.
iPTMnet; Q01196; -.
PhosphoSitePlus; Q01196; -.
BioMuta; RUNX1; -.
DMDM; 215274205; -.
EPD; Q01196; -.
MaxQB; Q01196; -.
PaxDb; Q01196; -.
PeptideAtlas; Q01196; -.
PRIDE; Q01196; -.
Ensembl; ENST00000300305; ENSP00000300305; ENSG00000159216. [Q01196-8]
Ensembl; ENST00000344691; ENSP00000340690; ENSG00000159216. [Q01196-1]
Ensembl; ENST00000358356; ENSP00000351123; ENSG00000159216. [Q01196-3]
Ensembl; ENST00000437180; ENSP00000409227; ENSG00000159216. [Q01196-8]
GeneID; 861; -.
KEGG; hsa:861; -.
UCSC; uc002yuh.3; human. [Q01196-1]
CTD; 861; -.
DisGeNET; 861; -.
EuPathDB; HostDB:ENSG00000159216.18; -.
GeneCards; RUNX1; -.
HGNC; HGNC:10471; RUNX1.
HPA; HPA004176; -.
HPA; HPA037912; -.
MalaCards; RUNX1; -.
MIM; 151385; gene.
MIM; 601399; phenotype.
neXtProt; NX_Q01196; -.
OpenTargets; ENSG00000159216; -.
Orphanet; 102724; 'Acute myeloid leukemia with t(8;21)(q22;q22) translocation'.
Orphanet; 521; Chronic myeloid leukemia.
Orphanet; 71290; Familial platelet syndrome with predisposition to acute myelogenous leukemia.
Orphanet; 248340; Isolated delta-storage pool disease.
Orphanet; 99860; Precursor B-cell acute lymphoblastic leukemia.
PharmGKB; PA34884; -.
eggNOG; KOG3982; Eukaryota.
eggNOG; ENOG4111J4Y; LUCA.
GeneTree; ENSGT00390000016964; -.
HOVERGEN; HBG060268; -.
InParanoid; Q01196; -.
KO; K08367; -.
OMA; QSYPYLG; -.
OrthoDB; EOG091G0CXB; -.
PhylomeDB; Q01196; -.
TreeFam; TF321496; -.
Reactome; R-HSA-549127; Organic cation transport.
Reactome; R-HSA-8877330; RUNX1 and FOXP3 control the development of regulatory T lymphocytes (Tregs).
Reactome; R-HSA-8931987; RUNX1 regulates estrogen receptor mediated transcription.
Reactome; R-HSA-8934593; Regulation of RUNX1 Expression and Activity.
Reactome; R-HSA-8935964; RUNX1 regulates expression of components of tight junctions.
Reactome; R-HSA-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
Reactome; R-HSA-8939242; RUNX1 regulates transcription of genes involved in differentiation of keratinocytes.
Reactome; R-HSA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
Reactome; R-HSA-8939245; RUNX1 regulates transcription of genes involved in BCR signaling.
Reactome; R-HSA-8939246; RUNX1 regulates transcription of genes involved in differentiation of myeloid cells.
Reactome; R-HSA-8939247; RUNX1 regulates transcription of genes involved in interleukin signaling.
Reactome; R-HSA-8939256; RUNX1 regulates transcription of genes involved in WNT signaling.
Reactome; R-HSA-8941333; RUNX2 regulates genes involved in differentiation of myeloid cells.
Reactome; R-HSA-8951936; RUNX3 regulates p14-ARF.
SignaLink; Q01196; -.
SIGNOR; Q01196; -.
ChiTaRS; RUNX1; human.
EvolutionaryTrace; Q01196; -.
GeneWiki; RUNX1; -.
GenomeRNAi; 861; -.
PRO; PR:Q01196; -.
Proteomes; UP000005640; Chromosome 21.
Bgee; ENSG00000159216; -.
ExpressionAtlas; Q01196; baseline and differential.
Genevisible; Q01196; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:InterPro.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0001047; F:core promoter binding; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0000975; F:regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IDA:UniProtKB.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; IDA:NTNU_SB.
GO; GO:0002062; P:chondrocyte differentiation; IBA:GO_Central.
GO; GO:0071425; P:hematopoietic stem cell proliferation; TAS:UniProtKB.
GO; GO:0030097; P:hemopoiesis; IDA:UniProtKB.
GO; GO:0030099; P:myeloid cell differentiation; IDA:UniProtKB.
GO; GO:0030853; P:negative regulation of granulocyte differentiation; IMP:UniProtKB.
GO; GO:0001503; P:ossification; IBA:GO_Central.
GO; GO:0048935; P:peripheral nervous system neuron development; TAS:BHF-UCL.
GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
GO; GO:0030854; P:positive regulation of granulocyte differentiation; IMP:UniProtKB.
GO; GO:0032743; P:positive regulation of interleukin-2 production; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0050855; P:regulation of B cell receptor signaling pathway; TAS:Reactome.
GO; GO:2000810; P:regulation of bicellular tight junction assembly; TAS:Reactome.
GO; GO:0001959; P:regulation of cytokine-mediated signaling pathway; TAS:Reactome.
GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; TAS:Reactome.
GO; GO:0033146; P:regulation of intracellular estrogen receptor signaling pathway; TAS:Reactome.
GO; GO:0045616; P:regulation of keratinocyte differentiation; TAS:Reactome.
GO; GO:0045652; P:regulation of megakaryocyte differentiation; TAS:Reactome.
GO; GO:0045637; P:regulation of myeloid cell differentiation; TAS:Reactome.
GO; GO:0045589; P:regulation of regulatory T cell differentiation; TAS:Reactome.
GO; GO:0030111; P:regulation of Wnt signaling pathway; TAS:Reactome.
Gene3D; 2.60.40.720; -; 1.
Gene3D; 4.10.770.10; -; 1.
InterPro; IPR000040; AML1_Runt.
InterPro; IPR008967; p53-like_TF_DNA-bd.
InterPro; IPR012346; p53/RUNT-type_TF_DNA-bd_sf.
InterPro; IPR013524; Runt_dom.
InterPro; IPR027384; Runx_central_dom_sf.
InterPro; IPR013711; RunxI_C_dom.
InterPro; IPR016554; TF_Runt-rel_RUNX.
PANTHER; PTHR11950; PTHR11950; 1.
Pfam; PF00853; Runt; 1.
Pfam; PF08504; RunxI; 1.
PIRSF; PIRSF009374; TF_Runt-rel_RUNX; 1.
PRINTS; PR00967; ONCOGENEAML1.
SUPFAM; SSF49417; SSF49417; 1.
PROSITE; PS51062; RUNT; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing; Chloride;
Chromosomal rearrangement; Complete proteome; Disease mutation;
DNA-binding; Methylation; Nucleus; Phosphoprotein; Polymorphism;
Proto-oncogene; Reference proteome; Repressor; Transcription;
Transcription regulation.
CHAIN 1 453 Runt-related transcription factor 1.
/FTId=PRO_0000174655.
DOMAIN 50 178 Runt. {ECO:0000255|PROSITE-
ProRule:PRU00399}.
REGION 80 84 Interaction with DNA.
REGION 135 143 Interaction with DNA.
REGION 168 177 Interaction with DNA.
REGION 291 371 Interaction with KAT6A.
{ECO:0000269|PubMed:11742995}.
REGION 307 400 Interaction with KAT6B. {ECO:0000250}.
REGION 362 402 Interaction with FOXP3.
{ECO:0000269|PubMed:17377532}.
COMPBIAS 187 453 Pro/Ser/Thr-rich.
BINDING 112 112 Chloride 1.
BINDING 116 116 Chloride 1; via amide nitrogen.
BINDING 139 139 Chloride 2.
BINDING 170 170 Chloride 2; via amide nitrogen.
SITE 177 178 Breakpoint for translocation to form
AML1-EMV-1 (or AML1-EAP) in CML and T-
MDS, to form AML1-MTG8 (ETO) in AML-M2,
to form AML1-CBFA2T3 in therapy-related
myeloid malignancies, to form AML1-MECOM
in CML and to form type I MACROD1-RUNX1
fusion protein.
SITE 241 242 Breakpoint for translocation to form
AML1-EAP in T-MDS and CML, to form type
II MACROD1-RUNX1 fusion protein and to
form RUNX1-CBFA2T2 in acute myeloid
leukemia. {ECO:0000269|PubMed:20520637}.
MOD_RES 14 14 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 21 21 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 24 24 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 43 43 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 193 193 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 212 212 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 249 249 Phosphoserine; by HIPK2.
{ECO:0000244|PubMed:19690332,
ECO:0000269|PubMed:18695000}.
MOD_RES 266 266 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 268 268 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 273 273 Phosphothreonine; by HIPK2.
{ECO:0000269|PubMed:18695000}.
MOD_RES 276 276 Phosphoserine; by HIPK2.
{ECO:0000244|PubMed:19690332,
ECO:0000269|PubMed:18695000}.
MOD_RES 296 296 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 435 435 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 105 Missing (in isoform AML-1L).
{ECO:0000303|PubMed:7651838,
ECO:0000303|PubMed:9199349}.
/FTId=VSP_005919.
VAR_SEQ 1 5 MRIPV -> MASDSIFESFPSYPQCFMRECILGMNPSRDVH
(in isoform AML-1G).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7651838,
ECO:0000303|PubMed:7891692}.
/FTId=VSP_005917.
VAR_SEQ 1 5 MRIPV -> MNPSRDVH (in isoform AML-1H).
{ECO:0000305}.
/FTId=VSP_005916.
VAR_SEQ 1 5 MRIPV -> MPAAPRGPAQGEAAARTRSR (in isoform
AML-1I). {ECO:0000305}.
/FTId=VSP_005918.
VAR_SEQ 137 242 VGRSGRGKSFTLTITVFTNPPQVATYHRAIKITVDGPREPR
RHRQKLDDQTKPGSLSFSERLSELEQLRRTAMRVSPHHPAP
TPNPRASLNHSTAFNPQPQSQMQD -> VDGPREPRRHRQK
LDDQTKPGSLSFSERLSELEQLRRTAMRVSPHHPAPTPNPR
ASLNHSTAFNPQPQSQMQDTRQIQPSPPWSYDQSYQYLGSI
ASPSVHPATPI (in isoform AML-1FC).
{ECO:0000305}.
/FTId=VSP_005920.
VAR_SEQ 178 224 RHRQKLDDQTKPGSLSFSERLSELEQLRRTAMRVSPHHPAP
TPNPRA -> SKCIHLGLVHPPGWYTLQAGILRDHVSDSLG
STFPPGGWQAPVKPKS (in isoform AML-1FA).
{ECO:0000305}.
/FTId=VSP_005923.
VAR_SEQ 178 188 RHRQKLDDQTK -> NSLTWPRYPHI (in isoform
AML-1FB). {ECO:0000305}.
/FTId=VSP_005921.
VAR_SEQ 189 453 Missing (in isoform AML-1FB).
{ECO:0000305}.
/FTId=VSP_005922.
VAR_SEQ 225 453 Missing (in isoform AML-1FA).
{ECO:0000305}.
/FTId=VSP_005924.
VAR_SEQ 242 250 DTRQIQPSP -> EEDTAPWRC (in isoform AML-
1C). {ECO:0000303|PubMed:1720541}.
/FTId=VSP_005926.
VAR_SEQ 243 453 Missing (in isoform AML-1FC).
{ECO:0000305}.
/FTId=VSP_005925.
VAR_SEQ 251 453 Missing (in isoform AML-1C).
{ECO:0000303|PubMed:1720541}.
/FTId=VSP_005927.
VAR_SEQ 258 453 Missing (in isoform AML-1E).
{ECO:0000303|PubMed:8490181}.
/FTId=VSP_005928.
VAR_SEQ 440 453 APSARLEEAVWRPY -> GGASCSRQARRDPGPWARTPSWG
RGRPTDRISL (in isoform AML-1A).
{ECO:0000303|PubMed:7651838,
ECO:0000303|PubMed:7835892}.
/FTId=VSP_005929.
VARIANT 139 139 R -> Q (in FPDMM).
{ECO:0000269|PubMed:10508512}.
/FTId=VAR_012128.
VARIANT 174 174 R -> Q (in FPDMM; impaired
phosphorylation; dbSNP:rs74315450).
{ECO:0000269|PubMed:10508512,
ECO:0000269|PubMed:18695000}.
/FTId=VAR_012129.
VARIANT 431 431 S -> R (in dbSNP:rs1055308).
/FTId=VAR_013177.
VARIANT 433 433 S -> R (in dbSNP:rs1055309).
/FTId=VAR_013178.
MUTAGEN 67 67 S->R: Loss of heterodimerization and
reduced EP300 phosphorylation induction.
{ECO:0000269|PubMed:18695000}.
MUTAGEN 80 80 R->A: Strongly reduces DNA-binding.
{ECO:0000269|PubMed:11276260}.
MUTAGEN 83 83 K->A: Strongly reduces DNA-binding.
{ECO:0000269|PubMed:11276260,
ECO:0000269|PubMed:18695000}.
MUTAGEN 83 83 K->E: Strongly reduces DNA-binding,
impaired phosphorylation and reduced
EP300 phosphorylation induction.
{ECO:0000269|PubMed:11276260,
ECO:0000269|PubMed:18695000}.
MUTAGEN 84 84 T->A: No effect on DNA binding.
{ECO:0000269|PubMed:11276260}.
MUTAGEN 106 106 M->V: Disrupts interaction of AML1-
MTG8/ETO with CBFB, no effect on AML1-
MTG8/ETO-mediated transformation
activity. {ECO:0000269|PubMed:19202074}.
MUTAGEN 107 107 A->T: Loss of heterodimerization.
Disrupts interactionof AML1-MTG8/ETO with
CBFB, no effect on AML1-MTG8/ETO-mediated
transformation activity.
{ECO:0000269|PubMed:10404214,
ECO:0000269|PubMed:19202074}.
MUTAGEN 108 108 G->R: Loss of heterodimerization and
impaired phosphorylation.
{ECO:0000269|PubMed:10404214,
ECO:0000269|PubMed:18695000}.
MUTAGEN 135 135 R->A: Strongly reduces DNA-binding.
{ECO:0000269|PubMed:11276260}.
MUTAGEN 139 139 R->A: Strongly reduces DNA-binding.
{ECO:0000269|PubMed:11276260}.
MUTAGEN 140 140 S->G: Disrupts AML1-MTG8/ETO DNA-binding,
decreases AML1-MTG8/ETO transforming
activity. {ECO:0000269|PubMed:19202074}.
MUTAGEN 142 142 R->A: Strongly reduces DNA-binding.
{ECO:0000269|PubMed:11276260}.
MUTAGEN 145 453 Missing: No DNA-binding.
MUTAGEN 167 167 K->A: Reduces DNA-binding.
{ECO:0000269|PubMed:11276260}.
MUTAGEN 169 169 T->A: Strongly reduces DNA-binding.
{ECO:0000269|PubMed:11276260}.
MUTAGEN 171 171 D->A: Strongly reduces DNA-binding.
{ECO:0000269|PubMed:11276260}.
MUTAGEN 174 174 R->A: Strongly reduces DNA-binding.
{ECO:0000269|PubMed:11276260}.
MUTAGEN 177 177 R->A: Strongly reduces DNA-binding.
{ECO:0000269|PubMed:11276260}.
MUTAGEN 249 249 S->A: Reduced phosphorylation.
{ECO:0000269|PubMed:18695000}.
MUTAGEN 273 273 T->A: Reduced phosphorylation; when
associated with A-276.
{ECO:0000269|PubMed:18695000}.
MUTAGEN 276 276 S->A: Reduced phosphorylation; when
associated with A-273.
{ECO:0000269|PubMed:18695000}.
CONFLICT 412 412 S -> F (in Ref. 1; AAA51720).
{ECO:0000305}.
HELIX 54 57 {ECO:0000244|PDB:1CMO}.
STRAND 62 64 {ECO:0000244|PDB:1LJM}.
STRAND 70 73 {ECO:0000244|PDB:1LJM}.
STRAND 77 80 {ECO:0000244|PDB:1LJM}.
STRAND 82 84 {ECO:0000244|PDB:1CMO}.
STRAND 90 93 {ECO:0000244|PDB:1LJM}.
STRAND 102 108 {ECO:0000244|PDB:1LJM}.
STRAND 110 114 {ECO:0000244|PDB:1H9D}.
STRAND 117 119 {ECO:0000244|PDB:1LJM}.
STRAND 121 123 {ECO:0000244|PDB:1LJM}.
STRAND 128 130 {ECO:0000244|PDB:1LJM}.
STRAND 146 152 {ECO:0000244|PDB:1LJM}.
STRAND 154 156 {ECO:0000244|PDB:1E50}.
STRAND 158 161 {ECO:0000244|PDB:1LJM}.
STRAND 166 171 {ECO:0000244|PDB:1LJM}.
HELIX 175 177 {ECO:0000244|PDB:1CMO}.
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


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