ID RUNX2_MOUSE Reviewed; 607 AA.
AC Q08775; O35183; Q08776; Q9JLN0; Q9QUQ6; Q9QY29; Q9R0U4; Q9Z2J7;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2001, sequence version 2.
DT 24-JAN-2024, entry version 218.
DE RecName: Full=Runt-related transcription factor 2 {ECO:0000312|MGI:MGI:99829};
DE AltName: Full=Acute myeloid leukemia 3 protein;
DE AltName: Full=Core-binding factor subunit alpha-1;
DE Short=CBF-alpha-1;
DE AltName: Full=Oncogene AML-3;
DE AltName: Full=Osteoblast-specific transcription factor 2;
DE Short=OSF-2;
DE AltName: Full=Polyomavirus enhancer-binding protein 2 alpha A subunit;
DE Short=PEA2-alpha A;
DE Short=PEBP2-alpha A {ECO:0000303|PubMed:9238031};
DE AltName: Full=SL3-3 enhancer factor 1 alpha A subunit;
DE AltName: Full=SL3/AKV core-binding factor alpha A subunit;
GN Name=Runx2;
GN Synonyms=Aml3, Cbfa1 {ECO:0000303|PubMed:9182762},
GN Osf2 {ECO:0000312|MGI:MGI:99829}, Pebp2a {ECO:0000303|PubMed:9238031};
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] (ISOFORMS 3 AND 4).
RX PubMed=8341710; DOI=10.1073/pnas.90.14.6859;
RA Ogawa E., Maruyama M., Kagoshima H., Inuzuka M., Lu J., Satake M.,
RA Shigesada K., Ito Y.;
RT "PEBP2/PEA2 represents a family of transcription factors homologous to the
RT products of the Drosophila runt gene and the human AML1 gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:6859-6863(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND DEVELOPMENTAL STAGE (ISOFORM
RP 2).
RC STRAIN=C57BL/6J; TISSUE=Osteoblast;
RX PubMed=9182762; DOI=10.1016/s0092-8674(00)80257-3;
RA Ducy P., Zhang R., Geoffroy V., Ridall A.L., Karsenty G.;
RT "Osf2/Cbfa1: a transcriptional activator of osteoblast differentiation.";
RL Cell 89:747-754(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4; 5; 6; 7; 8 AND 9).
RC STRAIN=CD2-MYC;
RX PubMed=9238031; DOI=10.1073/pnas.94.16.8646;
RA Stewart M., Terry A., Hu M., O'Hara M., Blyth K., Baxter E., Cameron E.,
RA Onions D.E., Neil J.C.;
RT "Proviral insertions induce the expression of bone-specific isoforms of
RT PEBP2alphaA (CBFA1): evidence for a new myc collaborating oncogene.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:8646-8651(1997).
RN [4]
RP PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 2 AND 6), AND
RP ALTERNATIVE SPLICING.
RX PubMed=9651525; DOI=10.1016/s0378-1119(98)00227-3;
RA Xiao Z.S., Thomas R., Hinson T.K., Quarles L.D.;
RT "Genomic structure and isoform expression of the mouse, rat and human
RT Cbfa1/Osf2 transcription factor.";
RL Gene 214:187-197(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-98 (ISOFORMS 1 AND 2).
RX PubMed=10524201; DOI=10.1016/s0167-4781(99)00113-x;
RA Fujiwara M., Tagashira S., Harada H., Ogawa S., Katsumata T., Nakatsuka M.,
RA Komori T., Takada H.;
RT "Isolation and characterization of the distal promoter region of mouse
RT Cbfa1.";
RL Biochim. Biophys. Acta 1446:265-272(1999).
RN [6]
RP PROTEIN SEQUENCE OF 263-277 AND 305-319.
RX PubMed=8386878; DOI=10.1006/viro.1993.1262;
RA Ogawa E., Inuzuka M., Maruyama M., Satake M., Naito-Fujimoto M., Ito Y.,
RA Shigesada K.;
RT "Molecular cloning and characterization of PEBP2 beta, the heterodimeric
RT partner of a novel Drosophila runt-related DNA binding protein PEBP2
RT alpha.";
RL Virology 194:314-331(1993).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-35.
RC STRAIN=129;
RA Chi X.-Z., Bae S.-C.;
RT "Analysis of the two PEBP2aA/cbfa1 promoter regions.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION.
RX PubMed=9182763; DOI=10.1016/s0092-8674(00)80258-5;
RA Komori T., Yagi H., Nomura S., Yamaguchi A., Sasaki K., Deguchi K.,
RA Shimizu Y., Bronson R.T., Gao Y.-H., Inada M., Sato M., Okamoto R.,
RA Kitamura Y., Yoshiki S., Kishimoto T.;
RT "Targeted disruption of Cbfa1 results in a complete lack of bone formation
RT owing to maturational arrest of osteoblasts.";
RL Cell 89:755-764(1997).
RN [9]
RP PHOSPHORYLATION.
RX PubMed=10660618; DOI=10.1074/jbc.275.6.4453;
RA Xiao G., Jiang D., Thomas P., Benson M.D., Guan K., Karsenty G.,
RA Franceschi R.T.;
RT "MAPK pathways activate and phosphorylate the osteoblast-specific
RT transcription factor, Cbfa1.";
RL J. Biol. Chem. 275:4453-4459(2000).
RN [10]
RP INTERACTION WITH IFI204.
RX PubMed=15557274; DOI=10.1074/jbc.m412604200;
RA Liu C.-J., Chang E., Yu J., Carlson C.S., Prazak L., Yu X.-P., Ding B.,
RA Lengyel P., Di Cesare P.E.;
RT "The interferon-inducible p204 protein acts as a transcriptional
RT coactivator of Cbfa1 and enhances osteoblast differentiation.";
RL J. Biol. Chem. 280:2788-2796(2005).
RN [11]
RP INTERACTION WITH SATB2.
RX PubMed=16751105; DOI=10.1016/j.cell.2006.05.012;
RA Dobreva G., Chahrour M., Dautzenberg M., Chirivella L., Kanzler B.,
RA Farinas I., Karsenty G., Grosschedl R.;
RT "SATB2 is a multifunctional determinant of craniofacial patterning and
RT osteoblast differentiation.";
RL Cell 125:971-986(2006).
RN [12]
RP INTERACTION WITH HIVEP3.
RX PubMed=16728642; DOI=10.1126/science.1126313;
RA Jones D.C., Wein M.N., Oukka M., Hofstaetter J.G., Glimcher M.J.,
RA Glimcher L.H.;
RT "Regulation of adult bone mass by the zinc finger adapter protein Schnurri-
RT 3.";
RL Science 312:1223-1227(2006).
RN [13]
RP INTERACTION WITH DDX5 (ISOFORM 3).
RX PubMed=17960593; DOI=10.1002/jcb.21526;
RA Jensen E.D., Niu L., Caretti G., Nicol S.M., Teplyuk N., Stein G.S.,
RA Sartorelli V., van Wijnen A.J., Fuller-Pace F.V., Westendorf J.J.;
RT "p68 (Ddx5) interacts with Runx2 and regulates osteoblast
RT differentiation.";
RL J. Cell. Biochem. 103:1438-1451(2008).
RN [14]
RP FUNCTION, PHOSPHORYLATION BY HIPK3, AND INTERACTION WITH HIPK3.
RX PubMed=20484411; DOI=10.1210/me.2010-0029;
RA Sierra O.L., Towler D.A.;
RT "Runx2 trans-activation mediated by the MSX2-interacting nuclear target
RT requires homeodomain interacting protein kinase-3.";
RL Mol. Endocrinol. 24:1478-1497(2010).
RN [15]
RP INTERACTION WITH TMEM119.
RX PubMed=21239498; DOI=10.1074/jbc.m110.179127;
RA Hisa I., Inoue Y., Hendy G.N., Canaff L., Kitazawa R., Kitazawa S.,
RA Komori T., Sugimoto T., Seino S., Kaji H.;
RT "Parathyroid hormone-responsive Smad3-related factor, Tmem119, promotes
RT osteoblast differentiation and interacts with the bone morphogenetic
RT protein-Runx2 pathway.";
RL J. Biol. Chem. 286:9787-9796(2011).
RN [16]
RP INTERACTION WITH FOXO1.
RX PubMed=21471200; DOI=10.1074/jbc.m110.197905;
RA Yang S., Xu H., Yu S., Cao H., Fan J., Ge C., Fransceschi R.T., Dong H.H.,
RA Xiao G.;
RT "Foxo1 mediates insulin-like growth factor 1 (IGF1)/insulin regulation of
RT osteocalcin expression by antagonizing Runx2 in osteoblasts.";
RL J. Biol. Chem. 286:19149-19158(2011).
RN [17]
RP DEVELOPMENTAL STAGE.
RX PubMed=24028588; DOI=10.1111/eos.12078;
RA Feng X.Y., Zhao Y.M., Wang W.J., Ge L.H.;
RT "Msx1 regulates proliferation and differentiation of mouse dental
RT mesenchymal cells in culture.";
RL Eur. J. Oral Sci. 121:412-420(2013).
RN [18]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-353, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [19]
RP DEVELOPMENTAL STAGE.
RX PubMed=29148101; DOI=10.1111/eos.12390;
RA Feng X.Y., Wu X.S., Wang J.S., Zhang C.M., Wang S.L.;
RT "Homeobox protein MSX-1 inhibits expression of bone morphogenetic protein
RT 2, bone morphogenetic protein 4, and lymphoid enhancer-binding factor 1 via
RT Wnt/beta-catenin signaling to prevent differentiation of dental mesenchymal
RT cells during the late bell stage.";
RL Eur. J. Oral Sci. 126:1-12(2018).
RN [20]
RP INTERACTION WITH IPO7, SUBCELLULAR LOCATION, AND INDUCTION BY ODONTOBLASTIC
RP AND OSTEOBLASTIC DIFFERENTIATION.
RX PubMed=35922041; DOI=10.1093/stmcls/sxac055;
RA Zhang Y., Zhang H., Xiao Z., Yuan G., Yang G.;
RT "IPO7 Promotes Odontoblastic Differentiation and Inhibits Osteoblastic
RT Differentiation Through Regulation of RUNX2 Expression and Translocation.";
RL Stem Cells 40:1020-1030(2022).
CC -!- FUNCTION: Transcription factor involved in osteoblastic differentiation
CC and skeletal morphogenesis. Essential for the maturation of osteoblasts
CC and both intramembranous and endochondral ossification. CBF binds to
CC the core site, 5'-PYGPYGGT-3', of a number of enhancers and promoters,
CC including murine leukemia virus, polyomavirus enhancer, T-cell receptor
CC enhancers, osteocalcin, osteopontin, bone sialoprotein, alpha 1(I)
CC collagen, LCK, IL-3 and GM-CSF promoters. Inhibits KAT6B-dependent
CC transcriptional activation (By similarity). In osteoblasts, supports
CC transcription activation: synergizes with SPEN/MINT to enhance FGFR2-
CC mediated activation of the osteocalcin FGF-responsive element (OCFRE).
CC {ECO:0000250, ECO:0000269|PubMed:20484411, ECO:0000269|PubMed:9182763}.
CC -!- SUBUNIT: Heterodimer of an alpha and a beta subunit. The alpha subunit
CC binds DNA as a monomer and through the Runt domain. DNA-binding is
CC increased by heterodimerization. Interacts with XRCC6 (Ku70) and XRCC5
CC (Ku80). Interacts with CCNB1, KAT6A and KAT6B (By similarity).
CC Interacts with HIVEP3. Interacts with IFI204. Interaction with SATB2;
CC the interaction results in enhanced DNA binding and transactivation by
CC these transcription factors. Binds to HIPK3. Interacts with FOXO1 (via
CC a C-terminal region); the interaction inhibits RUNX2 transcriptional
CC activity towards BGLAP. Interacts with FOXP3 (By similarity). Interacts
CC with TMEM119 (PubMed:21239498). Interacts with OLFM2 (By similarity).
CC Interacts with IPO7; the interaction inhibits RUNX2 nuclear
CC translocation in osteoblasts (PubMed:35922041).
CC {ECO:0000250|UniProtKB:Q13950, ECO:0000250|UniProtKB:Q9Z2J9,
CC ECO:0000269|PubMed:15557274, ECO:0000269|PubMed:16728642,
CC ECO:0000269|PubMed:16751105, ECO:0000269|PubMed:20484411,
CC ECO:0000269|PubMed:21239498, ECO:0000269|PubMed:21471200,
CC ECO:0000269|PubMed:35922041}.
CC -!- SUBUNIT: [Isoform 3]: Interacts with DDX5.
CC {ECO:0000269|PubMed:17960593}.
CC -!- INTERACTION:
CC Q08775; Q6NZM9: Hdac4; NbExp=3; IntAct=EBI-903354, EBI-646397;
CC Q08775; Q9D030: Twist2; NbExp=2; IntAct=EBI-903354, EBI-2903190;
CC Q08775; P25976: Ubtf; NbExp=4; IntAct=EBI-903354, EBI-7364139;
CC Q08775; Q6AYI1: Ddx5; Xeno; NbExp=2; IntAct=EBI-903354, EBI-931635;
CC Q08775-3; P17844: DDX5; Xeno; NbExp=2; IntAct=EBI-6119991, EBI-351962;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:35922041}. Cytoplasm
CC {ECO:0000269|PubMed:35922041}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q08775-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q08775-2; Sequence=VSP_005941;
CC Name=3; Synonyms=PEBP2-alpha A1;
CC IsoId=Q08775-3; Sequence=VSP_005940, VSP_005942;
CC Name=4; Synonyms=PEBP2-alpha A2;
CC IsoId=Q08775-4; Sequence=VSP_005940, VSP_005942, VSP_005944,
CC VSP_005945;
CC Name=5; Synonyms=G1;
CC IsoId=Q08775-5; Sequence=VSP_005939;
CC Name=6; Synonyms=G2;
CC IsoId=Q08775-6; Sequence=VSP_005939, VSP_005943;
CC Name=7; Synonyms=U1;
CC IsoId=Q08775-7; Sequence=VSP_005939, VSP_005946, VSP_005948;
CC Name=8; Synonyms=Y1;
CC IsoId=Q08775-8; Sequence=VSP_005939, VSP_005947;
CC Name=9; Synonyms=Y2;
CC IsoId=Q08775-9; Sequence=VSP_005939, VSP_005943, VSP_005947;
CC -!- TISSUE SPECIFICITY: Found in thymus and testis, T-cell lines but not in
CC B-cell lines. Isoform 2 is exclusively found in bone, particularly in
CC osteoblasts; isoforms 3 and 4 are expressed in T-cell lines; isoforms
CC 5, 6, 7, 8 and 9 can be found in osteoblasts and osteosarcoma cell
CC lines.
CC -!- DEVELOPMENTAL STAGE: Expressed in early bell stage dental mesenchymal
CC cells at 15.5 dpc (at protein level) (PubMed:24028588). Expressed in
CC bell stage dental mesenchymal cells at 17.5 dpc (PubMed:29148101).
CC {ECO:0000269|PubMed:24028588, ECO:0000269|PubMed:29148101}.
CC -!- DEVELOPMENTAL STAGE: [Isoform 2]: Expression occurs early during
CC skeletal development and is restricted to cells of the mesenchymal
CC condensations and of the osteoblast lineage at 12.5 dpc.
CC {ECO:0000269|PubMed:9182762}.
CC -!- INDUCTION: Induced during the early stages of odontoblastic
CC differentiation in dental papilla cells (PubMed:35922041). Induced
CC during osteoblastic differentiation (PubMed:35922041).
CC {ECO:0000269|PubMed:35922041}.
CC -!- DOMAIN: A proline/serine/threonine rich region at the C-terminus is
CC necessary for transcriptional activation of target genes and contains
CC the phosphorylation sites.
CC -!- PTM: Phosphorylated; probably by MAP kinases (MAPK). Phosphorylation by
CC HIPK3 is required for the SPEN/MINT and FGF2 transactivation during
CC osteoblastic differentiation. Phosphorylation at Ser-537 by CDK1
CC promotes endothelial cell proliferation required for tumor angiogenesis
CC probably by facilitating cell cycle progression (By similarity).
CC {ECO:0000250}.
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DR EMBL; D14636; BAA03485.1; -; mRNA.
DR EMBL; D14637; BAA03486.1; -; mRNA.
DR EMBL; AF010284; AAB65409.1; -; mRNA.
DR EMBL; AF005936; AAB82419.1; -; mRNA.
DR EMBL; AF053948; AAC77440.1; -; Genomic_DNA.
DR EMBL; AF053951; AAC78623.1; -; mRNA.
DR EMBL; AF053956; AAC78626.1; -; mRNA.
DR EMBL; AF134836; AAF22568.1; -; Genomic_DNA.
DR EMBL; AF134836; AAF22569.1; -; Genomic_DNA.
DR EMBL; AB013129; BAA85345.1; -; Genomic_DNA.
DR EMBL; AB013129; BAA85346.1; -; Genomic_DNA.
DR EMBL; AH009404; AAF73290.1; -; Genomic_DNA.
DR CCDS; CCDS37624.2; -. [Q08775-5]
DR PIR; A48233; A48233.
DR RefSeq; NP_001139510.1; NM_001146038.2. [Q08775-5]
DR RefSeq; NP_001258556.1; NM_001271627.1. [Q08775-5]
DR RefSeq; NP_033950.2; NM_009820.5. [Q08775-5]
DR RefSeq; XP_006523607.1; XM_006523544.2.
DR RefSeq; XP_006523608.1; XM_006523545.2.
DR AlphaFoldDB; Q08775; -.
DR BMRB; Q08775; -.
DR SMR; Q08775; -.
DR BioGRID; 198518; 23.
DR CORUM; Q08775; -.
DR DIP; DIP-36316N; -.
DR ELM; Q08775; -.
DR IntAct; Q08775; 12.
DR MINT; Q08775; -.
DR STRING; 10090.ENSMUSP00000109201; -.
DR ChEMBL; CHEMBL1681609; -.
DR GlyGen; Q08775; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q08775; -.
DR PhosphoSitePlus; Q08775; -.
DR SwissPalm; Q08775; -.
DR EPD; Q08775; -.
DR MaxQB; Q08775; -.
DR PaxDb; 10090-ENSMUSP00000109202; -.
DR PeptideAtlas; Q08775; -.
DR ProteomicsDB; 256652; -. [Q08775-1]
DR ProteomicsDB; 256653; -. [Q08775-2]
DR ProteomicsDB; 256654; -. [Q08775-3]
DR ProteomicsDB; 256655; -. [Q08775-4]
DR ProteomicsDB; 256656; -. [Q08775-5]
DR ProteomicsDB; 256657; -. [Q08775-6]
DR ProteomicsDB; 256658; -. [Q08775-7]
DR ProteomicsDB; 256659; -. [Q08775-8]
DR ProteomicsDB; 256660; -. [Q08775-9]
DR Pumba; Q08775; -.
DR Antibodypedia; 3645; 1063 antibodies from 45 providers.
DR DNASU; 12393; -.
DR Ensembl; ENSMUST00000113571.10; ENSMUSP00000109201.4; ENSMUSG00000039153.18. [Q08775-5]
DR Ensembl; ENSMUST00000159943.8; ENSMUSP00000124918.2; ENSMUSG00000039153.18. [Q08775-5]
DR Ensembl; ENSMUST00000160673.8; ENSMUSP00000123743.2; ENSMUSG00000039153.18. [Q08775-2]
DR Ensembl; ENSMUST00000238400.2; ENSMUSP00000158748.2; ENSMUSG00000039153.18. [Q08775-8]
DR GeneID; 12393; -.
DR KEGG; mmu:12393; -.
DR UCSC; uc008cpy.3; mouse. [Q08775-6]
DR UCSC; uc008cqa.3; mouse. [Q08775-1]
DR AGR; MGI:99829; -.
DR CTD; 860; -.
DR MGI; MGI:99829; Runx2.
DR VEuPathDB; HostDB:ENSMUSG00000039153; -.
DR eggNOG; KOG3982; Eukaryota.
DR GeneTree; ENSGT00940000160171; -.
DR HOGENOM; CLU_032910_0_2_1; -.
DR InParanoid; Q08775; -.
DR OrthoDB; 2881451at2759; -.
DR PhylomeDB; Q08775; -.
DR Reactome; R-MMU-8878166; Transcriptional regulation by RUNX2. [Q08775-5]
DR Reactome; R-MMU-8939902; Regulation of RUNX2 expression and activity. [Q08775-5]
DR Reactome; R-MMU-8940973; RUNX2 regulates osteoblast differentiation. [Q08775-5]
DR Reactome; R-MMU-8941326; RUNX2 regulates bone development. [Q08775-5]
DR BioGRID-ORCS; 12393; 5 hits in 80 CRISPR screens.
DR ChiTaRS; Runx2; mouse.
DR PRO; PR:Q08775; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q08775; Protein.
DR Bgee; ENSMUSG00000039153; Expressed in head bone and 283 other cell types or tissues.
DR ExpressionAtlas; Q08775; baseline and differential.
DR Genevisible; Q08775; MM.
DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0043425; F:bHLH transcription factor binding; IPI:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:MGI.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IMP:ARUK-UCL.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA: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:MGI.
DR GO; GO:0140296; F:general transcription initiation factor binding; ISO:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0019904; F:protein domain specific binding; IPI:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0030509; P:BMP signaling pathway; IMP:BHF-UCL.
DR GO; GO:0030282; P:bone mineralization; IDA:MGI.
DR GO; GO:0048469; P:cell maturation; IMP:MGI.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0002063; P:chondrocyte development; IMP:MGI.
DR GO; GO:0002062; P:chondrocyte differentiation; IMP:MGI.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IGI:MGI.
DR GO; GO:0035115; P:embryonic forelimb morphogenesis; IMP:MGI.
DR GO; GO:0001958; P:endochondral ossification; IMP:MGI.
DR GO; GO:0050673; P:epithelial cell proliferation; IMP:MGI.
DR GO; GO:0010467; P:gene expression; IDA:MGI.
DR GO; GO:0030097; P:hemopoiesis; IBA:GO_Central.
DR GO; GO:0036076; P:ligamentous ossification; IGI:MGI.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IMP:MGI.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IMP:MGI.
DR GO; GO:0001503; P:ossification; IBA:GO_Central.
DR GO; GO:0002076; P:osteoblast development; IGI:MGI.
DR GO; GO:0001649; P:osteoblast differentiation; IDA:MGI.
DR GO; GO:0002051; P:osteoblast fate commitment; IGI:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IGI:MGI.
DR GO; GO:0032332; P:positive regulation of chondrocyte differentiation; IMP:MGI.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:MGI.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IMP:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:MGI.
DR GO; GO:0045778; P:positive regulation of ossification; ISO:MGI.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IDA:MGI.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045595; P:regulation of cell differentiation; IBA:GO_Central.
DR GO; GO:0040036; P:regulation of fibroblast growth factor receptor signaling pathway; IMP:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IDA:MGI.
DR GO; GO:0042487; P:regulation of odontogenesis of dentin-containing tooth; IMP:MGI.
DR GO; GO:0030278; P:regulation of ossification; IMP:MGI.
DR GO; GO:0045667; P:regulation of osteoblast differentiation; IDA:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:1904383; P:response to sodium phosphate; IDA:MGI.
DR GO; GO:0001501; P:skeletal system development; IMP:MGI.
DR GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
DR GO; GO:0060395; P:SMAD protein signal transduction; ISO:MGI.
DR GO; GO:0007224; P:smoothened signaling pathway; IMP:MGI.
DR GO; GO:0048863; P:stem cell differentiation; IDA:MGI.
DR GO; GO:0072089; P:stem cell proliferation; IMP:MGI.
DR GO; GO:0030217; P:T cell differentiation; IDA: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 PANTHER; PTHR11950; RUNT RELATED; 1.
DR PANTHER; PTHR11950:SF7; RUNT-RELATED TRANSCRIPTION FACTOR 2; 1.
DR Pfam; PF00853; Runt; 1.
DR Pfam; PF08504; RunxI; 1.
DR PRINTS; PR00967; ONCOGENEAML1.
DR SUPFAM; SSF81995; beta-sandwich domain of Sec23/24; 1.
DR SUPFAM; SSF49417; p53-like transcription factors; 1.
DR PROSITE; PS51062; RUNT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Differentiation;
KW Direct protein sequencing; DNA-binding; Isopeptide bond; Methylation;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..607
FT /note="Runt-related transcription factor 2"
FT /id="PRO_0000174660"
FT DOMAIN 187..315
FT /note="Runt"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00399"
FT REGION 1..88
FT /note="Interaction with IFI204"
FT /evidence="ECO:0000269|PubMed:15557274"
FT REGION 100..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..258
FT /note="Required for interaction with FOXO1"
FT /evidence="ECO:0000269|PubMed:21471200"
FT REGION 307..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..525
FT /note="Interaction with KAT6A"
FT /evidence="ECO:0000250"
FT REGION 460..554
FT /note="Interaction with KAT6B"
FT /evidence="ECO:0000250"
FT REGION 548..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..359
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 353
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 537
FT /note="Phosphoserine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q13950"
FT CROSSLNK 324
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13950"
FT VAR_SEQ 1..98
FT /note="MLHSPHKQPQNHKCGANFLQEDCKKALAFKWLISAGHYQPPRPTESVSALTT
FT VHAGIFKAASSIYNRGHKFYLEKKGGTMASNSLFSAVTPCQQSFFW -> MRIPV (in
FT isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:8341710,
FT ECO:0000303|PubMed:9238031"
FT /id="VSP_005940"
FT VAR_SEQ 1..79
FT /note="Missing (in isoform 5, isoform 6, isoform 7, isoform
FT 8 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:9238031"
FT /id="VSP_005939"
FT VAR_SEQ 47..57
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9182762,
FT ECO:0000303|PubMed:9238031"
FT /id="VSP_005941"
FT VAR_SEQ 156
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:8341710,
FT ECO:0000303|PubMed:9238031"
FT /id="VSP_005942"
FT VAR_SEQ 316..373
FT /note="Missing (in isoform 6 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:9238031"
FT /id="VSP_005943"
FT VAR_SEQ 399..400
FT /note="PS -> LS (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:8341710,
FT ECO:0000303|PubMed:9238031"
FT /id="VSP_005944"
FT VAR_SEQ 401..607
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:8341710,
FT ECO:0000303|PubMed:9238031"
FT /id="VSP_005945"
FT VAR_SEQ 427..439
FT /note="DDDTATSDFCLWP -> GFCGTTTTTTTKL (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:9238031"
FT /id="VSP_005946"
FT VAR_SEQ 428..607
FT /note="DDTATSDFCLWPSSLSKKSQAGASELGPFSDPRQFPSISSLTESRFSNPRMH
FT YPATFTYTPPVTSGMSLGMSATTHYHTYLPPPYPGSSQSQSGPFQTSSTPYLYYGTSSA
FT SYQFPMVPGGDRSPSRMVPPCTTTSNGSTLLNPNLPNQNDGVDADGSHSSSPTVLNSSG
FT RMDESVWRPY -> SEPSTLDSQSSTTLFLSSEEPGPSTAALPSPSSSCEPQPFSPSPM
FT LPPLLQPLSTASTVPAPCVPRRTGLYTIVTSSPEAAPHLVDWMPSCPTATSPGVRGKDH
FT ERPQTMMAPAPALASERGHSQHAGPARDDHAEHPGTSPKPCAPPAAAATLEASVGDILV
FT ELRTMNGHLDIIAKALTKLASSLVPQSQPVPEAPDAN (in isoform 8 and
FT isoform 9)"
FT /evidence="ECO:0000303|PubMed:9238031"
FT /id="VSP_005947"
FT VAR_SEQ 440..607
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:9238031"
FT /id="VSP_005948"
FT CONFLICT 266
FT /note="A -> S (in Ref. 4; AAC78626)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="G -> S (in Ref. 4; AAC78626)"
FT /evidence="ECO:0000305"
FT CONFLICT 373
FT /note="D -> N (in Ref. 4; AAC78626)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="R -> T (in Ref. 4; AAC78626)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="M -> L (in Ref. 4; AAC78626)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="P -> L (in Ref. 4; AAC78626)"
FT /evidence="ECO:0000305"
FT CONFLICT 472
FT /note="R -> P (in Ref. 4; AAC78626)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 607 AA; 66205 MW; E87A4497ED19EE0E CRC64;
MLHSPHKQPQ NHKCGANFLQ EDCKKALAFK WLISAGHYQP PRPTESVSAL TTVHAGIFKA
ASSIYNRGHK FYLEKKGGTM ASNSLFSAVT PCQQSFFWDP STSRRFSPPS SSLQPGKMSD
VSPVVAAQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQEAAA AAAAAAAAAA AAAAAVPRLR
PPHDNRTMVE IIADHPAELV RTDSPNFLCS VLPSHWRCNK TLPVAFKVVA LGEVPDGTVV
TVMAGNDENY SAELRNASAV MKNQVARFND LRFVGRSGRG KSFTLTITVF TNPPQVATYH
RAIKVTVDGP REPRRHRQKL DDSKPSLFSD RLSDLGRIPH PSMRVGVPPQ NPRPSLNSAP
SPFNPQGQSQ ITDPRQAQSS PPWSYDQSYP SYLSQMTSPS IHSTTPLSST RGTGLPAITD
VPRRISDDDT ATSDFCLWPS SLSKKSQAGA SELGPFSDPR QFPSISSLTE SRFSNPRMHY
PATFTYTPPV TSGMSLGMSA TTHYHTYLPP PYPGSSQSQS GPFQTSSTPY LYYGTSSASY
QFPMVPGGDR SPSRMVPPCT TTSNGSTLLN PNLPNQNDGV DADGSHSSSP TVLNSSGRMD
ESVWRPY
//
