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TRANSFAC FACTOR TABLE, Release 2017.2 - public - 2017-06-30, (C) QIAGEN


AC T02441 XX ID T02441 XX DT 04.05.1998 (created); ili. DT 14.11.2014 (updated); mka. CO Copyright (C), QIAGEN. XX FA AML3 XX SY Acute myeloid leukemia 3 protein; CBF-alpha 1; CCAAT Binding Factor alpha1; Core-binding factor, alpha 1 subunit; Osf2; Osteoblast-specific transcription factor 2; PEBP2A1; PEBP2aA; Polyoma virus Enhancer Binding protein 2alphaA2; Runt-related transcription factor 2; RUNX2. XX OS rat, Rattus norvegicus OC eukaryota; animalia; metazoa; chordata; vertebrata; tetrapoda; mammalia; eutheria; rodentia; myomorpha; muridae; murinae XX GE G005057 Runx2. XX CL C0029; runt; 6.4.1.0.1. XX SF one of several possible splice variants (by homology with human and mouse genes); SF immunoreactive species of 45, 60 and 65 kDa in Western assay [1]; XX CP calvaria, metaphysis, epiphysis [1]. XX FF Treatment of cells with recombinant human FGF2 can increase the expression of the AML3 (both type I and type II isoforms) in rat osteosarcoma ROS17/2.8 cells [9]; FF major component of the osteoblast-specific complex of primary osteoblasts [1]; FF translational arrest of AML proteins cause decrease in alkaline phosphatase levels, osteocalcin levels, and a reduced number of mineralized nodules [1]; XX IN T00031 AP-1; rat, Rattus norvegicus. IN T06459 ATF-4; rat, Rattus norvegicus. IN T02452 Dlx-5; rat, Rattus norvegicus. IN T17666 FOXO1A; rat, Rattus norvegicus. IN T31203 HDAC3; rat, Rattus norvegicus. IN T01648 HES-1; rat, Rattus norvegicus. IN T04232 Smad2; rat, Rattus norvegicus. IN T00882 VDR; rat, Rattus norvegicus. IN T00885 VDR; human, Homo sapiens. XX MX M07276 V$AML3_Q3. MX M01856 V$AML3_Q6. MX M08866 V$AML_Q4. MX M00769 V$AML_Q6. MX M00731 V$OSF2_Q6. MX M00984 V$PEBP_Q6. XX BS R24058. BS R05004. BS R30358. BS R20435. BS R34780. BS R34782. BS R34783. BS R32880. BS R36137. BS R24512. BS R19712. BS R19732. BS R19740. BS R19708. BS R19710. BS R63723. BS R30361. BS R35638. BS R29522. BS R29526. BS R29528. BS R29529. BS R27666. BS R34778. BS R34587. BS R73181. BS R73178. BS R34580. BS R34583. BS R64888. BS R26778. BS R60388. BS R36136. XX DR TRANSPATH: MO000026425. DR TRANSCOMPEL: C00232. DR TRANSCOMPEL: C00397. DR UniProtKB: Q9Z2J9; RUN2_RAT. XX RN [1]; RE0006845. RX PUBMED: 9215522. RA Banerjee C., McCabe L. R., Choi J.-Y., Hiebert S. W., Stein J. L., Stein G. S., Lian J. B. RT Runt homology domain proteins in osteoblast differentiation: AML3/CBFA1 is a major component of a bone-specific complex RL J. Cell. Biochem. 66:1-8 (1997). RN [2]; RE0023220. RX PUBMED: 11274169. RA Hess J., Porte D., Munz C., Angel P. RT AP-1 and Cbfa/runt physically interact and regulate parathyroid hormone-dependent MMP13 expression in osteoblasts through a new osteoblast-specific element 2/AP-1 composite element. RL J. Biol. Chem. 276:20029-20038 (2001). RN [3]; RE0035651. RX PUBMED: 15456894. RA Hassan M. Q., Javed A., Morasso M. I., Karlin J., Montecino M., van Wijnen A. J., Stein G. S., Stein J. L., Lian J. B. RT Dlx3 transcriptional regulation of osteoblast differentiation: temporal recruitment of Msx2, Dlx3, and Dlx5 homeodomain proteins to chromatin of the osteocalcin gene. RL Mol. Cell. Biol. 24:9248-9261 (2004). RN [4]; RE0035892. RX PUBMED: 15292260. RA Schroeder T. M., Kahler R. A., Li X., Westendorf J. J. RT Histone deacetylase 3 interacts with runx2 to repress the osteocalcin promoter and regulate osteoblast differentiation. RL J. Biol. Chem. 279:41998-42007 (2004). RN [5]; RE0035930. RX PUBMED: 15456860. RA Paredes R., Arriagada G., Cruzat F., Villagra A., Olate J., Zaidi K., van Wijnen A., Lian J. B., Stein G. S., Stein J. L., Montecino M. RT Bone-specific transcription factor Runx2 interacts with the 1alpha,25-dihydroxyvitamin D3 receptor to up-regulate rat osteocalcin gene expression in osteoblastic cells. RL Mol. Cell. Biol. 24:8847-8861 (2004). RN [6]; RE0035990. RX PUBMED: 14982932. RA Selvamurugan N., Kwok S., Alliston T., Reiss M., Partridge N. C. RT Transforming growth factor-beta 1 regulation of collagenase-3 expression in osteoblastic cells by cross-talk between the Smad and MAPK signaling pathways and their components, Smad2 and Runx2. RL J. Biol. Chem. 279:19327-19334 (2004). RN [7]; RE0047240. RX PUBMED: 10801838. RA McCarthy T. L., Ji C., Chen Y., Kim K. K., Imagawa M., Ito Y., Centrella M. RT Runt domain factor (Runx)-dependent effects on CCAAT/ enhancer-binding protein delta expression and activity in osteoblasts RL J. Biol. Chem. 275:21746-53 (2000). RN [8]; RE0048867. RX PUBMED: 16195230. RA Shen Q., Christakos S. RT The vitamin D receptor, Runx2, and the Notch signaling pathway cooperate in the transcriptional regulation of osteopontin. RL J. Biol. Chem. 280:40589-40598 (2005). RN [9]; RE0048973. RX PUBMED: 12403780. RA Kim H. J., Kim J. H., Bae S. C., Choi J. Y., Kim H. J., Ryoo H. M. RT The protein kinase C pathway plays a central role in the fibroblast growth factor-stimulated expression and transactivation activity of Runx2. RL J. Biol. Chem. 278:319-326 (2003). XX //