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


AC T09072 XX ID T09072 XX DT 14.06.2006 (created); jag. DT 05.06.2015 (updated); msr. CO Copyright (C), QIAGEN. XX FA Smad3 XX SY Smad-3. XX OS mouse, Mus musculus OC eukaryota; animalia; metazoa; chordata; vertebrata; tetrapoda; mammalia; eutheria; rodentia; myomorpha; muridae; murinae XX GE G002404 Smad3. XX CL C0041; SMAD. XX SZ 425 AA; 48.1 kDa (cDNA) (calc.). XX SQ MSSILPFTPPIVKRLLGWKKGEQNGQEEKWCEKAVKSLVKKLKKTGQLDELEKAITTQNV SQ NTKCITIPRSLDGRLQVSHRKGLPHVIYCRLWRWPDLHSHHELRAMELCEFAFNMKKDEV SQ CVNPYHYQRVETPVLPPVLVPRHTEIPAEFPPLDDYSHSIPENTNFPAGIEPQSNIPETP SQ PPGYLSEDGETSDHQMNHSMDAGSPNLSPNPMSPAHNNLDLQPVTYCEPAFWCSISYYEL SQ NQRVGETFHASQPSMTVDGFTDPSNSERFCLGLLSNVNRNAAVELTRRHIGRGVRLYYIG SQ GEVFAECLSDSAIFVQSPNCNQRYGWHPATVCKIPPGCNLKIFNNQEFAALLAQSVNQGF SQ EAVYQLTRMCTIRMSFVKGWGAEYRRQTVTSTPCWIELHLNGPLQWLDKVLTQMGSPSIR SQ CSSVS XX SC translated from EMBL #AB008192 XX FT 1 145 MH1 domain [1]. FT 10 136 PS51075; MH1. FT 26 134 SM00523; dwAneu5. FT 28 131 PF03165; MH1 domain. FT 146 231 Linker region [1]. FT 226 403 PF03166; MH2 domain. FT 230 401 SM00524; DWB. FT 232 421 MH2 domain [1]. FT 232 425 PS51076; MH2. FT 422 425 SSXS motif [1]. XX IN T17460 IRF-3; Mammalia. IN T10783 Smad1; Mammalia. IN T24830 Smad2; Mammalia. IN T13998 Smad4; Mammalia. IN T04759 STAT1; human, Homo sapiens. XX MX M02794 V$SMAD3_03. MX M00701 V$SMAD3_Q6. MX M01888 V$SMAD3_Q6_01. MX M07429 V$SMAD3_Q6_02. MX M02898 V$SMAD4_04. MX M08897 V$SMAD_Q4. MX M00792 V$SMAD_Q6. MX M00974 V$SMAD_Q6_01. XX BS R09967. BS R25469. BS R68120. BS R68122. BS R37792. XX DR TRANSPATH: MO000082956. DR TRANSCOMPEL: C00557. DR TRANSCOMPEL: C00574. DR EMBL: AB008192; AB008192. DR UniProtKB: Q8BUN5; XX RN [1]; RE0015115. RX PUBMED: 10767528. RA Dick A., Mayr T., Bauer H., Meier A., Hammerschmidt M. RT Cloning and characterization of zebrafish smad2, smad3 and smad4 RL Gene 246:69-80 (2000). RN [2]; RE0015602. RX PUBMED: 10331191. RA Kano K., Notani A., Nam S. Y., Fujisawa M., Kurohmaru M., Hayashi Y. RT Cloning and studies of the mouse cDNA encoding Smad3 RL J. Vet. Med. Sci. 61:213-219 (1999). RN [3]; RE0015682. RX PUBMED: 10064594. RA Yang X., Letterio J. J., Lechleider R. J., Chen L., Hayman R., Gu H., Roberts A. B., Deng D. RT Targeted disruption of SMAD3 results in impaired mucosal immunity and diminished T cell responsiveness to TGF-beta RL EMBO J. 18:1280-1291 (1999). RN [4]; RE0015683. RX PUBMED: 10082515. RA Datto M. B., Frederick J. P., Pan L., Borton A. J., Zhuang Y., Wang X. F. RT Targeted disruption of Smad3 reveals an essential role in transforming growth factor beta-mediated signal transduction RL Mol. Cell. Biol. 19:2495-2504 (1999). RN [5]; RE0023194. RX PUBMED: 12145309. RA Norwitz E. R., Xu S., Xu J., Spiryda L. B., Park J. S., Jeong K. H., McGee E. A., Kaiser U. B. RT Direct binding of AP-1 (Fos/Jun) proteins to a SMAD binding element facilitates both gonadotropin-releasing hormone (GnRH)- and activin-mediated transcriptional activation of the mouse GnRH receptor gene. RL J. Biol. Chem. 277:37469-37478 (2002). RN [6]; RE0031943. RX PUBMED: 15241418. RA Matsuura I., Denissova N. G., Wang G., He D., Long J., Liu F. RT Cyclin-dependent kinases regulate the antiproliferative function of Smads. RL Nature 430:226-31 (2004). XX //