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Gene Ontology Classifications
SMAD family member 3

Go Annotations as Summary Text (Tabular View) (GO Graph)

GO curators for mouse genes have assigned the following annotations to the gene product of Smad3. (This text reflects annotations as of Tuesday, May 26, 2015.)
Summary from NCBI RefSeq

[Summary is not available for the mouse gene. This summary is for the human ortholog.] The protein encoded by this gene belongs to the SMAD, a family of proteins similar to the gene products of the Drosophila gene 'mothers against decapentaplegic' (Mad) and the C. elegans gene Sma. SMAD proteins are signal transducers and transcriptional modulators that mediate multiple signaling pathways. This protein functions as a transcriptional modulator activated by transforming growth factor-beta and is thought to play a role in the regulation of carcinogenesis. [provided by RefSeq, Apr 2009]
Summary text based on GO annotations supported by experimental evidence in mouse
Summary text based on GO annotations supported by experimental evidence in other organisms
Summary text based on GO annotations supported by structural data
Summary text for additional MGI annotations
  1. Ashcroft GS et al. (2003) Role of Smad3 in the hormonal modulation of in vivo wound healing responses. Wound Repair Regen, 11:468-73. (PubMed:14617288)
  2. Ashcroft GS et al. (1999) Mice lacking Smad3 show accelerated wound healing and an impaired local inflammatory response [see comments] Nat Cell Biol, 1:260-6. (PubMed:10559937)
  3. Baburajendran N et al. (2011) Structural basis for the cooperative DNA recognition by Smad4 MH1 dimers. Nucleic Acids Res, 39:8213-22. (PubMed:21724602)
  4. Bailey JS et al. (2004) Activin regulation of the follicle-stimulating hormone beta-subunit gene involves Smads and the TALE homeodomain proteins Pbx1 and Prep1. Mol Endocrinol, 18:1158-70. (PubMed:14764653)
  5. Borton AJ et al. (2001) The loss of Smad3 results in a lower rate of bone formation and osteopenia through dysregulation of osteoblast differentiation and apoptosis. J Bone Miner Res, 16:1754-64. (PubMed:11585338)
  6. Chou YT et al. (2006) Cited2 modulates TGF-beta-mediated upregulation of MMP9. Oncogene, 25:5547-60. (PubMed:16619037)
  7. Dunn NR et al. (2004) Combinatorial activities of Smad2 and Smad3 regulate mesoderm formation and patterning in the mouse embryo. Development, 131:1717-28. (PubMed:15084457)
  8. Ellis LR et al. (2003) Interaction of Smads with collagen types I, III, and V. Biochem Biophys Res Commun, 310:1117-23. (PubMed:14559231)
  9. Ellsworth BS et al. (2003) The gonadotropin releasing hormone (GnRH) receptor activating sequence (GRAS) is a composite regulatory element that interacts with multiple classes of transcription factors including Smads, AP-1 and a forkhead DNA binding protein. Mol Cell Endocrinol, 206:93-111. (PubMed:12943993)
  10. Esguerra CV et al. (2007) Ttrap is an essential modulator of Smad3-dependent Nodal signaling during zebrafish gastrulation and left-right axis determination. Development, 134:4381-93. (PubMed:18039968)
  11. Kang JS et al. (2005) Repression of Runx2 function by TGF-beta through recruitment of class II histone deacetylases by Smad3. EMBO J, 24:2543-55. (PubMed:15990875)
  12. Kawakatsu M et al. (2011) Loss of Smad3 gives rise to poor soft callus formation and accelerates early fracture healing. Exp Mol Pathol, 90:107-15. (PubMed:21035443)
  13. Kojic S et al. (2010) A novel role for cardiac ankyrin repeat protein Ankrd1/CARP as a co-activator of the p53 tumor suppressor protein. Arch Biochem Biophys, 502:60-7. (PubMed:20599664)
  14. Labbe E et al. (1998) Smad2 and Smad3 positively and negatively regulate TGF beta-dependent transcription through the forkhead DNA-binding protein FAST2. Mol Cell, 2:109-20. (PubMed:9702197)
  15. Li Z et al. (2011) Response gene to complement 32 is essential for fibroblast activation in renal fibrosis. J Biol Chem, 286:41323-30. (PubMed:21990365)
  16. Liu D et al. (2001) TGF-beta inhibits muscle differentiation through functional repression of myogenic transcription factors by Smad3. Genes Dev, 15:2950-66. (PubMed:11711431)
  17. Liu W et al. (2006) Axin is a scaffold protein in TGF-beta signaling that promotes degradation of Smad7 by Arkadia. EMBO J, 25:1646-58. (PubMed:16601693)
  18. Liu Y et al. (2004) Smad2 and Smad3 coordinately regulate craniofacial and endodermal development. Dev Biol, 270:411-26. (PubMed:15183723)
  19. Mullen AC et al. (2011) Master transcription factors determine cell-type-specific responses to TGF-beta signaling. Cell, 147:565-76. (PubMed:22036565)
  20. Nishimura G et al. (2006) DeltaEF1 mediates TGF-beta signaling in vascular smooth muscle cell differentiation. Dev Cell, 11:93-104. (PubMed:16824956)
  21. Qiu P et al. (2005) Myocardin enhances Smad3-mediated transforming growth factor-beta1 signaling in a CArG box-independent manner: Smad-binding element is an important cis element for SM22alpha transcription in vivo. Circ Res, 97:983-91. (PubMed:16224064)
  22. Quinn ZA et al. (2001) Smad proteins function as co-modulators for MEF2 transcriptional regulatory proteins. Nucleic Acids Res, 29:732-42. (PubMed:11160896)
  23. Redshaw N et al. (2013) TGF-beta/Smad2/3 signaling directly regulates several miRNAs in mouse ES cells and early embryos. PLoS One, 8:e55186. (PubMed:23390484)
  24. Ring C et al. (2002) The role of a Williams-Beuren syndrome-associated helix-loop-helix domain-containing transcription factor in activin/nodal signaling. Genes Dev, 16:820-35. (PubMed:11937490)
  25. Sowa H et al. (2004) Menin is required for bone morphogenetic protein 2- and transforming growth factor beta-regulated osteoblastic differentiation through interaction with Smads and Runx2. J Biol Chem, 279:40267-75. (PubMed:15150273)
  26. Subramanian SV et al. (2004) Induction of vascular smooth muscle alpha-actin gene transcription in transforming growth factor beta1-activated myofibroblasts mediated by dynamic interplay between the Pur repressor proteins and Sp1/Smad coactivators. Mol Biol Cell, 15:4532-43. (PubMed:15282343)
  27. Symonds D et al. (2003) Smad 3 regulates proliferation of the mouse ovarian surface epithelium. Anat Rec A Discov Mol Cell Evol Biol, 273:681-6. (PubMed:12845704)
  28. Tang LY et al. (2011) Ablation of Smurf2 reveals an inhibition in TGF-beta signalling through multiple mono-ubiquitination of Smad3. EMBO J, 30:4777-89. (PubMed:22045334)
  29. Tang Y et al. (2003) Disruption of transforming growth factor-beta signaling in ELF beta-spectrin-deficient mice. Science, 299:574-7. (PubMed:12543979)
  30. Wang B et al. (2011) Transposon mutagenesis with coat color genotyping identifies an essential role for Skor2 in sonic hedgehog signaling and cerebellum development. Development, 138:4487-97. (PubMed:21937600)
  31. Warner DR et al. (2007) PRDM16/MEL1: a novel Smad binding protein expressed in murine embryonic orofacial tissue. Biochim Biophys Acta, 1773:814-20. (PubMed:17467076)
  32. Warner DR et al. (2004) Functional interaction between Smad, CREB binding protein, and p68 RNA helicase. Biochem Biophys Res Commun, 324:70-6. (PubMed:15464984)
  33. Wu G et al. (2007) The anaphase-promoting complex coordinates initiation of lens differentiation. Mol Biol Cell, 18:1018-29. (PubMed:17215516)
  34. Yang X et al. (1999) Targeted disruption of SMAD3 results in impaired mucosal immunity and diminished T cell responsiveness to TGF-beta. EMBO J, 18:1280-91. (PubMed:10064594)
  35. Zhang J et al. (2007) Essential function of HIPK2 in TGFbeta-dependent survival of midbrain dopamine neurons. Nat Neurosci, 10:77-86. (PubMed:17159989)
  36. Zieba A et al. (2012) Intercellular variation in signaling through the TGF-beta pathway and its relation to cell density and cell cycle phase. Mol Cell Proteomics, 11:M111.013482. (PubMed:22442258)

Go Annotations in Tabular Form (Text View) (GO Graph)

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Gene Ontology Evidence Code Abbreviations:

  EXP Inferred from experiment
  IAS Inferred from ancestral sequence
  IBA Inferred from biological aspect of ancestor
  IBD Inferred from biological aspect of descendant
  IC Inferred by curator
  IDA Inferred from direct assay
  IEA Inferred from electronic annotation
  IGI Inferred from genetic interaction
  IKR Inferred from key residues
  IMP Inferred from mutant phenotype
  IMR Inferred from missing residues
  IPI Inferred from physical interaction
  IRD Inferred from rapid divergence
  ISS Inferred from sequence or structural similarity
  ISO Inferred from sequence orthology
  ISA Inferred from sequence alignment
  ISM Inferred from sequence model
  NAS Non-traceable author statement
  ND No biological data available
  RCA Reviewed computational analysis
  TAS Traceable author statement


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