ID RUNX1_MOUSE Reviewed; 451 AA.
AC Q03347; O08598; Q62049; Q9ESB9; Q9ET65;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 24-JAN-2024, entry version 208.
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, Pebp2ab;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Fibroblast;
RX PubMed=8437866;
RA Bae S.-C., Yamaguchi-Iwai Y., Ogawa E., Maruyama M., Inuzuka M.,
RA Kagoshima H., Shigesada K., Satake M., Ito Y.;
RT "Isolation of PEBP2 alpha B cDNA representing the mouse homolog of human
RT acute myeloid leukemia gene, AML1.";
RL Oncogene 8:809-814(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Fibroblast;
RX PubMed=8164679; DOI=10.1128/mcb.14.5.3242-3252.1994;
RA Bae S.-C., Ogawa E., Maruyama M., Oka H., Satake M., Shigesada K.,
RA Jenkins N.A., Gilbert D.J., Copeland N.G., Ito Y.;
RT "PEBP2 alpha B/mouse AML1 consists of multiple isoforms that possess
RT differential transactivation potentials.";
RL Mol. Cell. Biol. 14:3242-3252(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC STRAIN=BALB/cJ; TISSUE=Thymus;
RA Calabi F.;
RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
RX PubMed=10903914; DOI=10.1006/bbrc.2000.3112;
RA Tsuji K., Noda M.;
RT "Identification and expression of a novel 3'-exon of mouse
RT Runx1/Pebp2alphaB/Cbfa2/AML1 gene.";
RL Biochem. Biophys. Res. Commun. 274:171-176(2000).
RN [5]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RC STRAIN=129/Ola; TISSUE=Embryo;
RX PubMed=11243869; DOI=10.1006/bbrc.2001.4513;
RA Fujita Y., Nishimura M., Taniwaki M., Abe T., Okuda T.;
RT "Identification of an alternatively spliced form of the mouse AML1/RUNX1
RT gene transcript AML1c and its expression in early hematopoietic
RT development.";
RL Biochem. Biophys. Res. Commun. 281:1248-1255(2001).
RN [6]
RP PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM
RP 4), AND FUNCTION (ISOFORM 4).
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=11203699; DOI=10.1006/dbio.2000.9991;
RA Telfer J.C., Rothenberg E.V.;
RT "Expression and function of a stem cell promoter for the murine CBFalpha2
RT gene: distinct roles and regulation in natural killer and T cell
RT development.";
RL Dev. Biol. 229:363-382(2001).
RN [7]
RP FUNCTION IN LIVER HEMATOPOIESIS.
RX PubMed=8565077; DOI=10.1016/s0092-8674(00)80986-1;
RA Okuda T., van Deursen J., Hiebert S.W., Grosveld G., Downing J.R.;
RT "AML1, the target of multiple chromosomal translocations in human leukemia,
RT is essential for normal fetal liver hematopoiesis.";
RL Cell 84:321-330(1996).
RN [8]
RP FUNCTION, INTERACTION WITH FOXP3, AND SUBCELLULAR LOCATION.
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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP FUNCTION, AND INTERACTION WITH TBX21.
RX PubMed=21151104; DOI=10.1038/ni.1969;
RA Lazarevic V., Chen X., Shim J.H., Hwang E.S., Jang E., Bolm A.N., Oukka M.,
RA Kuchroo V.K., Glimcher L.H.;
RT "T-bet represses T(H)17 differentiation by preventing Runx1-mediated
RT activation of the gene encoding RORgammat.";
RL Nat. Immunol. 12:96-104(2011).
RN [11]
RP IDENTIFICATION IN A COMPLEX WITH PRMT5; RUNX1 AND CBFB.
RX PubMed=22193545; DOI=10.1038/cdd.2011.193;
RA Paul C., Sardet C., Fabbrizio E.;
RT "The histone- and PRMT5-associated protein COPR5 is required for myogenic
RT differentiation.";
RL Cell Death Differ. 19:900-908(2012).
RN [12]
RP FUNCTION IN NECROSIS AND HEMORRHAGING.
RX PubMed=8622955; DOI=10.1073/pnas.93.8.3444;
RA Wang Q., Stacy T., Binder M., Marin-Padilla M., Sharpe A.H., Speck N.A.;
RT "Disruption of the Cbfa2 gene causes necrosis and hemorrhaging in the
RT central nervous system and blocks definitive hematopoiesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:3444-3449(1996).
RN [13]
RP INTERACTION WITH HIPK2, PHOSPHORYLATION AT SER-249 AND SER-276 BY HIPK2,
RP AND MUTAGENESIS OF SER-249 AND SER-276.
RX PubMed=16917507; DOI=10.1038/sj.emboj.7601273;
RA Aikawa Y., Nguyen L.A., Isono K., Takakura N., Tagata Y., Schmitz M.L.,
RA Koseki H., Kitabayashi I.;
RT "Roles of HIPK1 and HIPK2 in AML1- and p300-dependent transcription,
RT hematopoiesis and blood vessel formation.";
RL EMBO J. 25:3955-3965(2006).
RN [14]
RP FUNCTION, AND MUTAGENESIS OF 447-VAL--TYR-451.
RX PubMed=18258917; DOI=10.1126/science.1151844;
RA Setoguchi R., Tachibana M., Naoe Y., Muroi S., Akiyama K., Tezuka C.,
RA Okuda T., Taniuchi I.;
RT "Repression of the transcription factor Th-POK by Runx complexes in
RT cytotoxic T cell development.";
RL Science 319:822-825(2008).
RN [15]
RP FUNCTION, AND MUTAGENESIS OF 447-VAL--TYR-451.
RX PubMed=23481257; DOI=10.1038/emboj.2013.47;
RA Tanaka H., Naito T., Muroi S., Seo W., Chihara R., Miyamoto C.,
RA Kominami R., Taniuchi I.;
RT "Epigenetic Thpok silencing limits the time window to choose CD4(+) helper-
RT lineage fate in the thymus.";
RL EMBO J. 32:1183-1194(2013).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 62-177 IN COMPLEX WITH CEBPB;
RP CBFB AND DNA.
RX PubMed=11375505; DOI=10.1107/s0907444901003900;
RA Tahirov T.H., Inoue-Bungo T., Sasaki M., Shiina M., Kimura K., Sato K.,
RA Kumasaka T., Yamamoto M., Kamiya N., Ogata K.;
RT "Crystallization and preliminary X-ray analyses of quaternary, ternary and
RT binary protein-DNA complexes with involvement of AML1/Runx-1/CBFalpha Runt
RT domain, CBFbeta and the C/EBPbeta bZip region.";
RL Acta Crystallogr. D 57:850-853(2001).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 60-182 IN COMPLEX WITH CEBPB;
RP CBFB AND DNA, AND MUTAGENESIS OF ARG-80; ASN-109; TYR-113; ARG-142;
RP LYS-144; THR-149; VAL-170; ASP-171; ARG-174 AND ARG-177.
RX PubMed=11257229; DOI=10.1016/s0092-8674(01)00271-9;
RA Tahirov T.H., Inoue-Bungo T., Morii H., Fujikawa A., Sasaki M., Kimura K.,
RA Shiina M., Sato K., Kumasaka T., Yamamoto M., Ishii S., Ogata K.;
RT "Structural analyses of DNA recognition by the AML1/Runx-1 Runt domain and
RT its allosteric control by CBFbeta.";
RL Cell 104:755-767(2001).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.25 ANGSTROMS) OF 60-173.
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).
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. Acts synergistically with ELF4 to transactivate the IL-3
CC promoter and with ELF2 to transactivate the BLK promoter. Inhibits
CC KAT6B-dependent transcriptional activation (By similarity). Involved in
CC lineage commitment of immature T cell precursors. CBF complexes repress
CC ZBTB7B transcription factor during cytotoxic (CD8+) T cell development.
CC They bind to RUNX-binding sequence within the ZBTB7B locus acting as
CC transcriptional silencer and allowing for cytotoxic T cell
CC differentiation (PubMed:18258917). CBF complexes binding to the
CC transcriptional silencer is essential for recruitment of nuclear
CC protein complexes that catalyze epigenetic modifications to establish
CC epigenetic ZBTB7B silencing (PubMed:23481257). Controls the anergy and
CC suppressive function of regulatory T-cells (Treg) by associating with
CC FOXP3. Activates the expression of IL2 and IFNG and down-regulates the
CC expression of TNFRSF18, IL2RA and CTLA4, in conventional T-cells
CC (PubMed:17377532). Positively regulates the expression of RORC in T-
CC helper 17 cells (PubMed:21151104). {ECO:0000250|UniProtKB:Q01196,
CC ECO:0000269|PubMed:17377532, ECO:0000269|PubMed:18258917,
CC ECO:0000269|PubMed:21151104, ECO:0000269|PubMed:23481257, ECO:0000305}.
CC -!- FUNCTION: Isoform 4 shows higher binding activities for target genes
CC 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:0000269|PubMed:11203699}.
CC -!- SUBUNIT: Heterodimer with CBFB. RUNX1 binds DNA as a monomer and
CC through the Runt domain. DNA-binding is increased by
CC heterodimerization. Interacts with TLE1 and ALYREF/THOC4. Interacts
CC with HIPK2, ELF1, ELF2 and SPI1. Interacts via its Runt domain with the
CC ELF4 N-terminal region. Interaction with ELF2 isoform 2 (NERF-1a) may
CC act to repress RUNX1-mediated transactivation. Interacts with KAT6A and
CC KAT6B. Interacts with SUV39H1, leading to abrogation of transactivating
CC and DNA-binding properties of RUNX1 (By similarity). Interacts with
CC YAP1. Interaction with CDK6 prevents myeloid differentiation, reducing
CC its transcription transactivation activity (By similarity). Found in a
CC complex with PRMT5, RUNX1 and CBFB. Interacts with FOXP3. Interacts
CC with TBX21 (PubMed:21151104). Interacts with DPF2 (By similarity).
CC {ECO:0000250|UniProtKB:Q01196, ECO:0000269|PubMed:11257229,
CC ECO:0000269|PubMed:11375505, ECO:0000269|PubMed:16917507,
CC ECO:0000269|PubMed:17377532, ECO:0000269|PubMed:21151104,
CC ECO:0000269|PubMed:22193545}.
CC -!- INTERACTION:
CC Q03347; Q99JB6: Foxp3; NbExp=5; IntAct=EBI-3863873, EBI-10956246;
CC Q03347; Q9JKD8: Tbx21; NbExp=3; IntAct=EBI-3863873, EBI-3863870;
CC Q03347; Q9JIZ5: Tfap4; NbExp=2; IntAct=EBI-3863873, EBI-15597718;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17377532}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=AML1-B, PEB2-alpha B1;
CC IsoId=Q03347-1; Sequence=Displayed;
CC Name=2; Synonyms=PEB2-alpha B2;
CC IsoId=Q03347-2; Sequence=VSP_005932, VSP_005933;
CC Name=3;
CC IsoId=Q03347-3; Sequence=VSP_005931, VSP_005934;
CC Name=4; Synonyms=AML1-C;
CC IsoId=Q03347-4; Sequence=VSP_005930;
CC Name=5;
CC IsoId=Q03347-5; Sequence=VSP_005935, VSP_005936;
CC -!- TISSUE SPECIFICITY: Isoform 4 is expressed at high levels in thymus,
CC spleen and T-cell lines and at lower levels in myeloid cell lines and
CC nonhematopoietic cells. Isoform 5 is expressed ubiquitously in lumbar
CC vertebrae, brain, kidney, heart, muscle, ovary and osteoblast-like cell
CC line MC3T3-E1.
CC -!- DEVELOPMENTAL STAGE: Differentially expressed during hematopoietic
CC differentiation. Isoform AML1-B is readily detectable in
CC undifferentiated embryonic stem (es) cells and peak expression is seen
CC on day 6 of differentiation, followed by a gradual decline thereafter.
CC Isoform AML1-C is undetectable in undifferentiated es cells, but is
CC gradually up-regulated along with differentiation and reaches its
CC highest levels on day 8 and this expression is maintained through day
CC 12. Isoform 5 is expressed at high levels at 6-8 dpc and then levels
CC decrease on 12 dpc. Isoform 4 expression is high throughout T-cell
CC development, declines with natural killer cell maturation, and appears
CC to be transiently reduced and then restored during B-cell development.
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 (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Methylated. {ECO:0000250}.
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:16917507}.
CC -!- DISEASE: Note=Mice with an Runx1 lacking the DNA-binding region are
CC found to die between embryonic days 11.5 to 12.5 due to hemorrhaging in
CC the central nervous system. This hemorrhaging is preceded by necrosis
CC and hematopoiesis is blocked (PubMed:8622955).
CC {ECO:0000269|PubMed:8622955}.
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DR EMBL; D26532; BAA05535.1; -; mRNA.
DR EMBL; D13802; BAA02960.1; -; mRNA.
DR EMBL; X97306; CAA65976.1; -; mRNA.
DR EMBL; AB046930; BAB08105.1; -; mRNA.
DR EMBL; AF345649; AAK29784.1; -; mRNA.
DR EMBL; AF193030; AAG32957.1; -; Genomic_DNA.
DR CCDS; CCDS28339.1; -. [Q03347-2]
DR CCDS; CCDS49916.1; -. [Q03347-1]
DR CCDS; CCDS49917.1; -. [Q03347-4]
DR PIR; A56017; A56017.
DR PDB; 1EAN; X-ray; 1.70 A; A=46-185.
DR PDB; 1EAO; X-ray; 1.40 A; A/B=46-185.
DR PDB; 1EAQ; X-ray; 1.25 A; A/B=46-185.
DR PDB; 1HJB; X-ray; 3.00 A; C/F=60-182.
DR PDB; 1HJC; X-ray; 2.65 A; A/D=60-182.
DR PDB; 1IO4; X-ray; 3.00 A; C=60-182.
DR PDB; 2J6W; X-ray; 2.60 A; A/B=46-185.
DR PDB; 3WTS; X-ray; 2.35 A; A/F=60-263.
DR PDB; 3WTT; X-ray; 2.35 A; A/F=60-263.
DR PDB; 3WTU; X-ray; 2.70 A; A/F=60-263.
DR PDB; 3WTV; X-ray; 2.70 A; A/F=60-263.
DR PDB; 3WTW; X-ray; 2.90 A; A/F=60-263.
DR PDB; 3WTX; X-ray; 2.80 A; A/F=60-263.
DR PDB; 3WTY; X-ray; 2.70 A; A/F=60-263.
DR PDB; 3WU1; X-ray; 2.40 A; A=55-177.
DR PDB; 4L0Y; X-ray; 2.50 A; A=1-242.
DR PDB; 4L0Z; X-ray; 2.70 A; A=1-242.
DR PDB; 4L18; X-ray; 2.30 A; A/E=48-214.
DR PDBsum; 1EAN; -.
DR PDBsum; 1EAO; -.
DR PDBsum; 1EAQ; -.
DR PDBsum; 1HJB; -.
DR PDBsum; 1HJC; -.
DR PDBsum; 1IO4; -.
DR PDBsum; 2J6W; -.
DR PDBsum; 3WTS; -.
DR PDBsum; 3WTT; -.
DR PDBsum; 3WTU; -.
DR PDBsum; 3WTV; -.
DR PDBsum; 3WTW; -.
DR PDBsum; 3WTX; -.
DR PDBsum; 3WTY; -.
DR PDBsum; 3WU1; -.
DR PDBsum; 4L0Y; -.
DR PDBsum; 4L0Z; -.
DR PDBsum; 4L18; -.
DR AlphaFoldDB; Q03347; -.
DR SMR; Q03347; -.
DR DIP; DIP-40723N; -.
DR ELM; Q03347; -.
DR IntAct; Q03347; 5.
DR MINT; Q03347; -.
DR STRING; 10090.ENSMUSP00000023673; -.
DR iPTMnet; Q03347; -.
DR PhosphoSitePlus; Q03347; -.
DR EPD; Q03347; -.
DR jPOST; Q03347; -.
DR MaxQB; Q03347; -.
DR PaxDb; 10090-ENSMUSP00000023673; -.
DR PeptideAtlas; Q03347; -.
DR ProteomicsDB; 256647; -. [Q03347-1]
DR ProteomicsDB; 256648; -. [Q03347-2]
DR ProteomicsDB; 256649; -. [Q03347-3]
DR ProteomicsDB; 256650; -. [Q03347-4]
DR ProteomicsDB; 256651; -. [Q03347-5]
DR AGR; MGI:99852; -.
DR MGI; MGI:99852; Runx1.
DR eggNOG; KOG3982; Eukaryota.
DR InParanoid; Q03347; -.
DR PhylomeDB; Q03347; -.
DR Reactome; R-MMU-549127; Organic cation transport.
DR Reactome; R-MMU-8877330; RUNX1 and FOXP3 control the development of regulatory T lymphocytes (Tregs).
DR Reactome; R-MMU-8931987; RUNX1 regulates estrogen receptor mediated transcription.
DR Reactome; R-MMU-8934593; Regulation of RUNX1 Expression and Activity.
DR Reactome; R-MMU-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Reactome; R-MMU-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-MMU-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR Reactome; R-MMU-8939245; RUNX1 regulates transcription of genes involved in BCR signaling.
DR Reactome; R-MMU-8939246; RUNX1 regulates transcription of genes involved in differentiation of myeloid cells.
DR Reactome; R-MMU-8939247; RUNX1 regulates transcription of genes involved in interleukin signaling.
DR Reactome; R-MMU-9018519; Estrogen-dependent gene expression.
DR ChiTaRS; Runx1; mouse.
DR EvolutionaryTrace; Q03347; -.
DR PRO; PR:Q03347; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q03347; Protein.
DR GO; GO:0005604; C:basement membrane; IDA:MGI.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0016513; C:core-binding factor complex; TAS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:ARUK-UCL.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISO:MGI.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
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; ISO:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0001223; F:transcription coactivator binding; ISO:MGI.
DR GO; GO:0001222; F:transcription corepressor binding; ISO:MGI.
DR GO; GO:0048266; P:behavioral response to pain; IMP:MGI.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IDA:MGI.
DR GO; GO:0007417; P:central nervous system development; IMP:MGI.
DR GO; GO:0002062; P:chondrocyte differentiation; IBA:GO_Central.
DR GO; GO:0060216; P:definitive hemopoiesis; IMP:MGI.
DR GO; GO:0035162; P:embryonic hemopoiesis; IMP:MGI.
DR GO; GO:0031069; P:hair follicle morphogenesis; IMP:MGI.
DR GO; GO:0030097; P:hemopoiesis; ISO:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0001889; P:liver development; IMP:MGI.
DR GO; GO:0030099; P:myeloid cell differentiation; ISO:MGI.
DR GO; GO:0002573; P:myeloid leukocyte differentiation; ISO:MGI.
DR GO; GO:0002318; P:myeloid progenitor cell differentiation; IMP:MGI.
DR GO; GO:0043371; P:negative regulation of CD4-positive, alpha-beta T cell differentiation; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB.
DR GO; GO:0030853; P:negative regulation of granulocyte differentiation; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0048666; P:neuron development; IMP:MGI.
DR GO; GO:0030182; P:neuron differentiation; IMP:MGI.
DR GO; GO:0048663; P:neuron fate commitment; IMP:MGI.
DR GO; GO:0001503; P:ossification; IBA:GO_Central.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:UniProtKB.
DR GO; GO:0043378; P:positive regulation of CD8-positive, alpha-beta T cell differentiation; IDA:UniProtKB.
DR GO; GO:1903431; P:positive regulation of cell maturation; IMP:MGI.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB.
DR GO; GO:0030854; P:positive regulation of granulocyte differentiation; ISS:UniProtKB.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; IMP:UniProtKB.
DR GO; GO:2000872; P:positive regulation of progesterone secretion; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0032729; P:positive regulation of type II interferon production; IDA:UniProtKB.
DR GO; GO:0045595; P:regulation of cell differentiation; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:MGI.
DR GO; GO:0071336; P:regulation of hair follicle cell proliferation; IMP:MGI.
DR GO; GO:0009966; P:regulation of signal transduction; IMP:MGI.
DR GO; GO:0002667; P:regulation of T cell anergy; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0032526; P:response to retinoic acid; IDA:BHF-UCL.
DR GO; GO:0001501; P:skeletal system development; IMP:MGI.
DR Gene3D; 2.60.40.720; -; 1.
DR InterPro; IPR000040; AML1_Runt.
DR InterPro; IPR008967; p53-like_TF_DNA-bd_sf.
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; RUNT RELATED; 1.
DR PANTHER; PTHR11950:SF40; RUNT-RELATED TRANSCRIPTION FACTOR 1; 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; p53-like transcription factors; 1.
DR PROSITE; PS51062; RUNT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing; DNA-binding;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..451
FT /note="Runt-related transcription factor 1"
FT /id="PRO_0000174656"
FT DOMAIN 50..178
FT /note="Runt"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00399"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..84
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 135..143
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 168..177
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250"
FT REGION 170..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 268..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..370
FT /note="Interaction with KAT6A"
FT /evidence="ECO:0000250"
FT REGION 307..399
FT /note="Interaction with KAT6B"
FT /evidence="ECO:0000250"
FT REGION 361..401
FT /note="Interaction with FOXP3"
FT /evidence="ECO:0000269|PubMed:17377532"
FT REGION 406..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..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 408..439
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 /evidence="ECO:0000255|PROSITE-ProRule:PRU00399"
FT BINDING 116
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00399"
FT BINDING 139
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00399"
FT BINDING 170
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00399"
FT MOD_RES 14
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q01196"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01196"
FT MOD_RES 24
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q01196"
FT MOD_RES 43
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q01196"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01196"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01196"
FT MOD_RES 249
FT /note="Phosphoserine; by HIPK2"
FT /evidence="ECO:0000269|PubMed:16917507"
FT MOD_RES 266
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01196"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01196"
FT MOD_RES 273
FT /note="Phosphothreonine; by HIPK2"
FT /evidence="ECO:0000250|UniProtKB:Q01196"
FT MOD_RES 276
FT /note="Phosphoserine; by HIPK2"
FT /evidence="ECO:0000269|PubMed:16917507"
FT MOD_RES 296
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q01196"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01196"
FT VAR_SEQ 1..5
FT /note="MRIPV -> MASDSIFESFPSYPQCFMR (in isoform 4)"
FT /evidence="ECO:0000305"
FT /id="VSP_005930"
FT VAR_SEQ 92..182
FT /note="VALGDVPDGTLVTVMAGNDENYSAELRNATAAMKNQVARFNDLRFVGRSGRG
FT KSFTLTITVFTNPPQVATYHRAIKITVDGPREPRRHRQK -> LLPEEGGGRSRWRSAD
FT GQSEPRGQRLRRLLKGAACSRSLWSFSLSLGWGGDAALPWRPSGGSASEVSKREFF
FT (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_005931"
FT VAR_SEQ 178
FT /note="R -> N (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8164679"
FT /id="VSP_005932"
FT VAR_SEQ 179..242
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8164679"
FT /id="VSP_005933"
FT VAR_SEQ 183..451
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_005934"
FT VAR_SEQ 242..303
FT /note="DARQIQPSPPWSYDQSYQYLGSITSSSVHPATPISPGRASGMTSLSAELSSR
FT LSTAPDLTAF -> KNPTEPTTLCLCWSPRRRKHRGCQAFLGALRELLKPRSISWEPNE
FT ENAVPSAEYLYSEKCGC (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_005935"
FT VAR_SEQ 304..451
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_005936"
FT MUTAGEN 80
FT /note="R->A: Interferes with DNA-binding."
FT /evidence="ECO:0000269|PubMed:11257229"
FT MUTAGEN 109
FT /note="N->A: Interferes with heterodimerization."
FT /evidence="ECO:0000269|PubMed:11257229"
FT MUTAGEN 113
FT /note="Y->A: Interferes with heterodimerization."
FT /evidence="ECO:0000269|PubMed:11257229"
FT MUTAGEN 142
FT /note="R->A: Interferes with DNA-binding."
FT /evidence="ECO:0000269|PubMed:11257229"
FT MUTAGEN 144
FT /note="K->M: Interferes with DNA-binding."
FT /evidence="ECO:0000269|PubMed:11257229"
FT MUTAGEN 149
FT /note="T->A: Interferes with heterodimerization."
FT /evidence="ECO:0000269|PubMed:11257229"
FT MUTAGEN 170
FT /note="V->A: No effect."
FT /evidence="ECO:0000269|PubMed:11257229"
FT MUTAGEN 171
FT /note="D->A: Interferes with DNA-binding."
FT /evidence="ECO:0000269|PubMed:11257229"
FT MUTAGEN 174
FT /note="R->A: Interferes with DNA-binding."
FT /evidence="ECO:0000269|PubMed:11257229"
FT MUTAGEN 177
FT /note="R->A: Interferes with DNA-binding."
FT /evidence="ECO:0000269|PubMed:11257229"
FT MUTAGEN 249
FT /note="S->A: Reduced phosphorylation."
FT /evidence="ECO:0000269|PubMed:16917507"
FT MUTAGEN 276
FT /note="S->A: Reduced phosphorylation."
FT /evidence="ECO:0000269|PubMed:16917507"
FT MUTAGEN 447..451
FT /note="Missing: Inhibits repression of ZBTB7B expression."
FT /evidence="ECO:0000269|PubMed:18258917,
FT ECO:0000269|PubMed:23481257"
FT CONFLICT 37..38
FT /note="GP -> A (in Ref. 3; CAA65976)"
FT /evidence="ECO:0000305"
FT HELIX 51..57
FT /evidence="ECO:0007829|PDB:1EAQ"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:1EAQ"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:4L18"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:1EAQ"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:1EAQ"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:1EAQ"
FT STRAND 102..109
FT /evidence="ECO:0007829|PDB:1EAQ"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:1EAQ"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:1EAQ"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:1EAQ"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:1EAQ"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:1EAQ"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:1EAQ"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:1EAQ"
FT STRAND 166..171
FT /evidence="ECO:0007829|PDB:1EAQ"
FT HELIX 194..203
FT /evidence="ECO:0007829|PDB:4L18"
FT HELIX 205..210
FT /evidence="ECO:0007829|PDB:4L0Z"
SQ SEQUENCE 451 AA; 48610 MW; 06B9E9BA01A6469C CRC64;
MRIPVDASTS RRFTPPSTAL SPGKMSEALP LGAPDGGPAL ASKLRSGDRS MVEVLADHPG
ELVRTDSPNF LCSVLPTHWR CNKTLPIAFK VVALGDVPDG TLVTVMAGND ENYSAELRNA
TAAMKNQVAR FNDLRFVGRS GRGKSFTLTI TVFTNPPQVA TYHRAIKITV DGPREPRRHR
QKLDDQTKPG SLSFSERLSE LEQLRRTAMR VSPHHPAPTP NPRASLNHST AFNPQPQSQM
QDARQIQPSP PWSYDQSYQY LGSITSSSVH PATPISPGRA SGMTSLSAEL SSRLSTAPDL
TAFGDPRQFP TLPSISDPRM HYPGAFTYSP PVTSGIGIGM SAMSSASRYH TYLPPPYPGS
SQAQAGPFQT GSPSYHLYYG ASAGSYQFSM VGGERSPPRI LPPCTNASTG AALLNPSLPS
QSDVVETEGS HSNSPTNMPP ARLEEAVWRP Y
//
