Sequence Detail

ID/Version

Q8BUN5 O09144 Q93002 O35273 Q8BX84 Q9GKR4 O09064 O14510 Q92940 (UniProt | EBI)

Last sequence update: 2004-07-05
Last annotation update: 2024-03-27

Sequence description from provider

RecName: Full=Mothers against decapentaplegic homolog 3; Short=MAD homolog 3; Short=Mad3; Short=Mothers against DPP homolog 3; Short=mMad3;AltName: Full=SMAD family member 3; Short=SMAD 3; Short=Smad3;

Provider

SWISS-PROT

Sequence

Polypeptide 425 aa

Source

Organism mouse

See UniProt | EBI for source

Annotated genes and markers

Follow the symbol links to get more information on the GO terms, expression assays, orthologs, phenotypic alleles, and other information for the genes or markers below.

Type	Symbol	Name	GO Terms	Expression Assays	Orthologs	Phenotypic Alleles
Gene	Smad3	SMAD family member 3	243	147	4	18

Sequence references in MGI

J:57220 Kano K, et al., Cloning and studies of the mouse cDNA encoding Smad3. J Vet Med Sci. 1999 Mar;61(3):213-9
J:59673 Ashcroft GS, et al., Mice lacking Smad3 show accelerated wound healing and an impaired local inflammatory response [see comments]. Nat Cell Biol. 1999 Sep;1(5):260-6
J:60559 Shoji H, et al., Identification and characterization of a PDZ protein that interacts with activin type II receptors. J Biol Chem. 2000 Feb 25;275(8):5485-92
J:65990 Miura S, et al., Hgs (Hrs), a FYVE domain protein, is involved in smad signaling through cooperation with SARA. Mol Cell Biol. 2000 Dec;20(24):9346-55
J:79484 Jiao K, et al., Identification of mZnf8, a Mouse Kruppel-Like Transcriptional Repressor, as a Novel Nuclear Interaction Partner of Smad1. Mol Cell Biol. 2002 Nov;22(21):7633-44
J:92664 Lin HK, et al., Cytoplasmic PML function in TGF-beta signalling. Nature. 2004 Sep 9;431(7005):205-11
J:99680 The FANTOM Consortium and RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group), The Transcriptional Landscape of the Mammalian Genome. Science. 2005;309(5740):1559-1563
J:106894 Collart C, et al., Smicl is a novel Smad interacting protein and cleavage and polyadenylation specificity factor associated protein. Genes Cells. 2005 Sep;10(9):897-906
J:111518 Borton AJ, et al., 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. 2001 Oct;16(10):1754-64
J:122005 Mavrakis KJ, et al., Arkadia Enhances Nodal/TGF-beta Signaling by Coupling Phospho-Smad2/3 Activity and Turnover. PLoS Biol. 2007 Mar 6;5(3):e67
J:122807 Warner DR, et al., PRDM16/MEL1: a novel Smad binding protein expressed in murine embryonic orofacial tissue. Biochim Biophys Acta. 2007 Jun;1773(6):814-20
J:140377 Esguerra CV, et al., Ttrap is an essential modulator of Smad3-dependent Nodal signaling during zebrafish gastrulation and left-right axis determination. Development. 2007 Dec;134(24):4381-93
J:148556 Blount AL, et al., FoxL2 and Smad3 coordinately regulate follistatin gene transcription. J Biol Chem. 2009 Mar 20;284(12):7631-45
J:169049 Varelas X, et al., The Crumbs complex couples cell density sensing to Hippo-dependent control of the TGF-beta-SMAD pathway. Dev Cell. 2010 Dec 14;19(6):831-44
J:175198 Ashcroft GS, et al., Role of Smad3 in the hormonal modulation of in vivo wound healing responses. Wound Repair Regen. 2003 Nov-Dec;11(6):468-73
J:175326 Kawakatsu M, et al., Loss of Smad3 gives rise to poor soft callus formation and accelerates early fracture healing. Exp Mol Pathol. 2011 Feb;90(1):107-15