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Database: UniProt
Entry: Q03347
LinkDB: Q03347
Original site: Q03347 
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   22-APR-2020, entry version 194.
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;
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}.
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   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   jPOST; Q03347; -.
DR   MaxQB; Q03347; -.
DR   PaxDb; Q03347; -.
DR   PeptideAtlas; Q03347; -.
DR   PRIDE; Q03347; -.
DR   MGI; MGI:99852; Runx1.
DR   eggNOG; KOG3982; Eukaryota.
DR   eggNOG; ENOG4111J4Y; LUCA.
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: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: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:0070491; F:repressing transcription factor binding; IPI: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 regulatory region sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR   GO; GO:0008134; F:transcription factor binding; ISO:MGI.
DR   GO; GO:0044212; F:transcription regulatory region DNA 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: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: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:0045892; P:negative regulation of transcription, DNA-templated; 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:0030854; P:positive regulation of granulocyte differentiation; ISS:UniProtKB.
DR   GO; GO:0032729; P:positive regulation of interferon-gamma production; IDA: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:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:0045595; P:regulation of cell differentiation; IBA:GO_Central.
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:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
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   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; 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          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          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   COMPBIAS        187..451
FT                   /note="Pro/Ser/Thr-rich"
FT   BINDING         112
FT                   /note="Chloride 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00399"
FT   BINDING         116
FT                   /note="Chloride 1; via amide nitrogen"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00399"
FT   BINDING         139
FT                   /note="Chloride 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00399"
FT   BINDING         170
FT                   /note="Chloride 2; via amide nitrogen"
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:0000244|PDB:1EAQ"
FT   TURN            59..61
FT                   /evidence="ECO:0000244|PDB:1EAQ"
FT   STRAND          62..64
FT                   /evidence="ECO:0000244|PDB:4L18"
FT   STRAND          70..72
FT                   /evidence="ECO:0000244|PDB:1EAQ"
FT   STRAND          77..80
FT                   /evidence="ECO:0000244|PDB:1EAQ"
FT   STRAND          90..95
FT                   /evidence="ECO:0000244|PDB:1EAQ"
FT   STRAND          102..109
FT                   /evidence="ECO:0000244|PDB:1EAQ"
FT   STRAND          112..115
FT                   /evidence="ECO:0000244|PDB:1EAQ"
FT   STRAND          117..119
FT                   /evidence="ECO:0000244|PDB:1EAQ"
FT   STRAND          121..125
FT                   /evidence="ECO:0000244|PDB:1EAQ"
FT   STRAND          128..130
FT                   /evidence="ECO:0000244|PDB:1EAQ"
FT   STRAND          146..152
FT                   /evidence="ECO:0000244|PDB:1EAQ"
FT   STRAND          154..156
FT                   /evidence="ECO:0000244|PDB:1EAQ"
FT   STRAND          158..161
FT                   /evidence="ECO:0000244|PDB:1EAQ"
FT   STRAND          166..171
FT                   /evidence="ECO:0000244|PDB:1EAQ"
FT   HELIX           194..203
FT                   /evidence="ECO:0000244|PDB:4L18"
FT   HELIX           205..210
FT                   /evidence="ECO:0000244|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
//
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