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}, Osf2 GN {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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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. DR Genevisible; Q08775; MM. 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 //