RHEA:18673
| Enzymes help_outline | 9,726 proteins (UniProtKB) |
| Enzyme class help_outline |
Reaction participants Show >> << Hide
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Namehelp_outline
[receptor-protein]-L-serine
Identifier
RHEA-COMP:11022
Reactive part
help_outline
- Name help_outline L-serine residue Identifier CHEBI:29999 Charge 0 Formula C3H5NO2 SMILEShelp_outline C([C@H](CO)N*)(=O)* 2D coordinates Mol file for the small molecule Search links Involved in 58 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline ATP Identifier CHEBI:30616 (Beilstein: 3581767) help_outline Charge -4 Formula C10H12N5O13P3 InChIKeyhelp_outline ZKHQWZAMYRWXGA-KQYNXXCUSA-J SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,038 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
[receptor-protein]-O-phospho-L-serine
Identifier
RHEA-COMP:11023
Reactive part
help_outline
- Name help_outline O-phospho-L-serine residue Identifier CHEBI:83421 Charge -2 Formula C3H4NO5P SMILEShelp_outline [O-]P([O-])(=O)OC[C@H](N-*)C(-*)=O 2D coordinates Mol file for the small molecule Search links Involved in 22 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline ADP Identifier CHEBI:456216 (Beilstein: 3783669) help_outline Charge -3 Formula C10H12N5O10P2 InChIKeyhelp_outline XTWYTFMLZFPYCI-KQYNXXCUSA-K SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 704 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge +1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 7,773 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Links to other resources
| RHEA:18673 | RHEA:18674 | RHEA:18675 | RHEA:18676 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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| EC numbers help_outline | ||||
| MetaCyc help_outline |
Citations
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Controlling TGF-beta signaling.
Massague J., Chen Y.G.
Genes Dev 14:627-644(2000) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Mechanism of activation of the TGF-beta receptor.
Wrana J.L., Attisano L., Wieser R., Ventura F., Massague J.
Transforming growth factor-beta (TGF-beta) signals by contacting two distantly related transmembrane serine/threonine kinases called receptors I and II. The role of these molecules in signalling has now been determined. TGF-beta binds directly to receptor II, which is a constitutively active kinas ... >> More
Transforming growth factor-beta (TGF-beta) signals by contacting two distantly related transmembrane serine/threonine kinases called receptors I and II. The role of these molecules in signalling has now been determined. TGF-beta binds directly to receptor II, which is a constitutively active kinase. Bound TGF-beta is then recognized by receptor I which is recruited into the complex and becomes phosphorylated by receptor II. Phosphorylation allows receptor I to propagate the signal to downstream substrates. This provides a mechanism by which a cytokine can generate the first step of a signalling cascade. << Less
Nature 370:341-347(1994) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Characterization of functional domains within Smad4/DPC4.
de Caestecker M.P., Hemmati P., Larisch-Bloch S., Ajmera R., Roberts A.B., Lechleider R.J.
Smad proteins are a family of highly conserved, intracellular proteins that signal cellular responses downstream of transforming growth factor-beta (TGF-beta) family serine/threonine kinase receptors. One of these molecules, Smad4, originally identified as the candidate tumor suppressor gene dpc-4 ... >> More
Smad proteins are a family of highly conserved, intracellular proteins that signal cellular responses downstream of transforming growth factor-beta (TGF-beta) family serine/threonine kinase receptors. One of these molecules, Smad4, originally identified as the candidate tumor suppressor gene dpc-4, reconstitutes TGF-beta- and activin-dependent transcriptional responses in Smad4 null cell lines and interacts in a ligand-dependent manner with other Smad family members in both TGF-beta, activin, and bone morphogenetic protein-2/-4 pathways. Here, we used an assay based on the restoration of ligand-dependent transcriptional responses in a Smad4 null cell line to characterize functional domain structures within Smad4. We showed that restoration of TGF-beta-induced transcriptional responses by Smad4 was inhibited by co-transfection with a kinase dead TGF-beta type II receptor and that constitutive activation was blocked with TGF-beta neutralizing antibodies, confirming the essential role of Smad4 in TGF-beta signaling. Using a series of Smad4 mutation, deletion, and Smad1/Smad4 chimera constructs we identified a 47-amino acid deletion within the middle-linker region of Smad4 that is essential for the mediation of signaling responses. In addition, we showed that the NH2-terminal domain of Smad4 augments ligand-dependent activation associated with the middle-linker region, indicating that there is a distinct ligand-response domain within the N terminus of this molecule. << Less
J Biol Chem 272:13690-13696(1997) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.