Signaling by Activin (Homo sapiens)

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4, 22, 27, 314, 15, 33, 354, 11, 28, 31, 356, 9, 17, 23, 391, 3, 7, 24, 25, 3616, 20, 21, 26, 308, 14, 32, 345, 10, 18, 37, 38, 402, 12, 19, 29, 34cytosolnucleoplasmACVR2A ACVR2B p-S465,S467-SMAD2 INHBA INHBB INHBA p-4S,T188,T206-ACVR1B ADPATPFOXH1 p-S423,S425-SMAD3 DRAP1 p-T175,S177,S179,S181,T194-ACVR1C SMAD4p-S423,S425-SMAD3 ADPSMAD4 ATPActivinA,AB,B:ACVR2A,B:p-ACVR1BINHBB SMAD2 Activin A,AB,B:FSTFOXH1 INHBB p-2S-SMAD2/3:SMAD4INHBB ACVR2B INHBA FOXH1INHBA ACVR2B SMAD2,3:SMAD4:FOXH1:Activin Response ElementINHBA ACVR1B ACVR1CACVR2B ACVR2A FOXH1:DRAP1Activin AB,BSMAD4 SMAD3 SMAD2/3ACVR1C ActivinAB,B:ACVR2A,B:p-ACVR1Cp-4S,T188,T206-ACVR1B p-S465,S467-SMAD2 Activin Response Element INHBB ACVR2A,BINHBB INHBB p-2S-SMAD2/3:SMAD4Activin:ACVR2A,B:p-ACVR1B,CACVR2A Activin A,AB,B:FSTL3ACVR2B p-2S-SMAD2/3SMAD4 FSTL3 INHBA FST ADPp-S465,S467-SMAD2 p-T175,S177,S179,S181,T194-ACVR1C ACVR2A FSTL3p-S465,S467-SMAD2 INHBA INHBA Activin ResponseElementACVR1BFSTINHBB p-S423,S425-SMAD3 ActivinA,AB,B:ACVR2A,B:ACVR1BACVR2A INHBB ActivinAB,B:ACVR2A,B:ACVR1CActivin A,AB,BACVR2B INHBA ATPACVR2A p-S423,S425-SMAD3 21212, 12, 19, 29, 3411, 33, 351314, 32, 34134, 11, 31, 33, 3521


Description

Activin was initially discovered as an activator of follicle stimulating hormone in the pituitary gland. It has since been shown to be an important participant in the differentiation of embryonic cells into mesodermal and endodermal layers. Activin binds the Activin receptor and triggers downstream events: phosphorylation of SMAD2 and SMAD3 followed by activation of gene expression (reviewed in Attisano et al. 1996, Willis et al. 1996, Chen et al. 2006, Hinck 2012). Activins are dimers comprising activin A (INHBA:INHBA), activin AB (INHBA:INHBB), and activin B (INHBB:INHBB). Activin first binds the type II receptor (ACVR2A, ACVR2B) and this complex then interacts with the type I receptor (ACVR1B, ACVR1C) (Attisano et al. 1996). The type II receptor phosphorylates the type I receptor and then the phosphorylated type I receptor phosphorylates SMAD2 and SMAD3. Dimers of phosphorylated SMAD2/3 bind SMAD4 and the resulting ternary complex enters the nucleus and activates target genes. View original pathway at:Reactome.

Comments

Reactome-Converter 
Pathway is converted from Reactome ID: 1502540
Reactome-version 
Reactome version: 66
Reactome Author 
Reactome Author: May, Bruce

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Ontology Terms

 

Bibliography

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  2. Schneyer AL, Rzucidlo DA, Sluss PM, Crowley WF.; ''Characterization of unique binding kinetics of follistatin and activin or inhibin in serum.''; PubMed Europe PMC
  3. Wu JW, Hu M, Chai J, Seoane J, Huse M, Li C, Rigotti DJ, Kyin S, Muir TW, Fairman R, Massagué J, Shi Y.; ''Crystal structure of a phosphorylated Smad2. Recognition of phosphoserine by the MH2 domain and insights on Smad function in TGF-beta signaling.''; PubMed Europe PMC
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  5. Hill CS.; ''Nucleocytoplasmic shuttling of Smad proteins.''; PubMed Europe PMC
  6. Zhou Y, Scolavino S, Funderburk SF, Ficociello LF, Zhang X, Klibanski A.; ''Receptor internalization-independent activation of Smad2 in activin signaling.''; PubMed Europe PMC
  7. Kawabata M, Inoue H, Hanyu A, Imamura T, Miyazono K.; ''Smad proteins exist as monomers in vivo and undergo homo- and hetero-oligomerization upon activation by serine/threonine kinase receptors.''; PubMed Europe PMC
  8. Tortoriello DV, Sidis Y, Holtzman DA, Holmes WE, Schneyer AL.; ''Human follistatin-related protein: a structural homologue of follistatin with nuclear localization.''; PubMed Europe PMC
  9. Wang Q, Huang Z, Xue H, Jin C, Ju XL, Han JD, Chen YG.; ''MicroRNA miR-24 inhibits erythropoiesis by targeting activin type I receptor ALK4.''; PubMed Europe PMC
  10. Dai F, Duan X, Liang YY, Lin X, Feng XH.; ''Coupling of dephosphorylation and nuclear export of Smads in TGF-beta signaling.''; PubMed Europe PMC
  11. Harrison CA, Gray PC, Fischer WH, Donaldson C, Choe S, Vale W.; ''An activin mutant with disrupted ALK4 binding blocks signaling via type II receptors.''; PubMed Europe PMC
  12. Schneyer AL, O'Neil DA, Crowley WF.; ''Activin-binding proteins in human serum and follicular fluid.''; PubMed Europe PMC
  13. Saito S, Sidis Y, Mukherjee A, Xia Y, Schneyer A.; ''Differential biosynthesis and intracellular transport of follistatin isoforms and follistatin-like-3.''; PubMed Europe PMC
  14. Sidis Y, Tortoriello DV, Holmes WE, Pan Y, Keutmann HT, Schneyer AL.; ''Follistatin-related protein and follistatin differentially neutralize endogenous vs. exogenous activin.''; PubMed Europe PMC
  15. Cárcamo J, Weis FM, Ventura F, Wieser R, Wrana JL, Attisano L, Massagué J.; ''Type I receptors specify growth-inhibitory and transcriptional responses to transforming growth factor beta and activin.''; PubMed Europe PMC
  16. Yanagisawa K, Uchida K, Nagatake M, Masuda A, Sugiyama M, Saito T, Yamaki K, Takahashi T, Osada H.; ''Heterogeneities in the biological and biochemical functions of Smad2 and Smad4 mutants naturally occurring in human lung cancers.''; PubMed Europe PMC
  17. Burdette JE, Jeruss JS, Kurley SJ, Lee EJ, Woodruff TK.; ''Activin A mediates growth inhibition and cell cycle arrest through Smads in human breast cancer cells.''; PubMed Europe PMC
  18. Xiao Z, Latek R, Lodish HF.; ''An extended bipartite nuclear localization signal in Smad4 is required for its nuclear import and transcriptional activity.''; PubMed Europe PMC
  19. Thompson TB, Lerch TF, Cook RW, Woodruff TK, Jardetzky TS.; ''The structure of the follistatin:activin complex reveals antagonism of both type I and type II receptor binding.''; PubMed Europe PMC
  20. Chen X, Rubock MJ, Whitman M.; ''A transcriptional partner for MAD proteins in TGF-beta signalling.''; PubMed Europe PMC
  21. Zhou S, Zawel L, Lengauer C, Kinzler KW, Vogelstein B.; ''Characterization of human FAST-1, a TGF beta and activin signal transducer.''; PubMed Europe PMC
  22. Hinck AP.; ''Structural studies of the TGF-βs and their receptors - insights into evolution of the TGF-β superfamily.''; PubMed Europe PMC
  23. Coutts SM, Childs AJ, Fulton N, Collins C, Bayne RA, McNeilly AS, Anderson RA.; ''Activin signals via SMAD2/3 between germ and somatic cells in the human fetal ovary and regulates kit ligand expression.''; PubMed Europe PMC
  24. Chen YG, Wang Z, Ma J, Zhang L, Lu Z.; ''Endofin, a FYVE domain protein, interacts with Smad4 and facilitates transforming growth factor-beta signaling.''; PubMed Europe PMC
  25. Nakao A, Imamura T, Souchelnytskyi S, Kawabata M, Ishisaki A, Oeda E, Tamaki K, Hanai J, Heldin CH, Miyazono K, ten Dijke P.; ''TGF-beta receptor-mediated signalling through Smad2, Smad3 and Smad4.''; PubMed Europe PMC
  26. Chen X, Weisberg E, Fridmacher V, Watanabe M, Naco G, Whitman M.; ''Smad4 and FAST-1 in the assembly of activin-responsive factor.''; PubMed Europe PMC
  27. Chen YG, Wang Q, Lin SL, Chang CD, Chuang J, Ying SY.; ''Activin signaling and its role in regulation of cell proliferation, apoptosis, and carcinogenesis.''; PubMed Europe PMC
  28. Willis SA, Mathews LS.; ''Regulation of activin type I receptor function by phosphorylation of residues outside the GS domain.''; PubMed Europe PMC
  29. Krummen LA, Woodruff TK, DeGuzman G, Cox ET, Baly DL, Mann E, Garg S, Wong WL, Cossum P, Mather JP.; ''Identification and characterization of binding proteins for inhibin and activin in human serum and follicular fluids.''; PubMed Europe PMC
  30. Yeo CY, Chen X, Whitman M.; ''The role of FAST-1 and Smads in transcriptional regulation by activin during early Xenopus embryogenesis.''; PubMed Europe PMC
  31. Willis SA, Zimmerman CM, Li LI, Mathews LS.; ''Formation and activation by phosphorylation of activin receptor complexes.''; PubMed Europe PMC
  32. Stamler R, Keutmann HT, Sidis Y, Kattamuri C, Schneyer A, Thompson TB.; ''The structure of FSTL3.activin A complex. Differential binding of N-terminal domains influences follistatin-type antagonist specificity.''; PubMed Europe PMC
  33. Lebrun JJ, Vale WW.; ''Activin and inhibin have antagonistic effects on ligand-dependent heteromerization of the type I and type II activin receptors and human erythroid differentiation.''; PubMed Europe PMC
  34. Schneyer A, Schoen A, Quigg A, Sidis Y.; ''Differential binding and neutralization of activins A and B by follistatin and follistatin like-3 (FSTL-3/FSRP/FLRG).''; PubMed Europe PMC
  35. Zhou Y, Sun H, Danila DC, Johnson SR, Sigai DP, Zhang X, Klibanski A.; ''Truncated activin type I receptor Alk4 isoforms are dominant negative receptors inhibiting activin signaling.''; PubMed Europe PMC
  36. Qin BY, Chacko BM, Lam SS, de Caestecker MP, Correia JJ, Lin K.; ''Structural basis of Smad1 activation by receptor kinase phosphorylation.''; PubMed Europe PMC
  37. Xu L, Chen YG, Massagué J.; ''The nuclear import function of Smad2 is masked by SARA and unmasked by TGFbeta-dependent phosphorylation.''; PubMed Europe PMC
  38. Kurisaki A, Kose S, Yoneda Y, Heldin CH, Moustakas A.; ''Transforming growth factor-beta induces nuclear import of Smad3 in an importin-beta1 and Ran-dependent manner.''; PubMed Europe PMC
  39. Watanabe R, Shen ZP, Tsuda K, Yamada Y.; ''Insulin gene is a target in activin receptor-like kinase 7 signaling pathway in pancreatic beta-cells.''; PubMed Europe PMC
  40. Schmierer B, Hill CS.; ''Kinetic analysis of Smad nucleocytoplasmic shuttling reveals a mechanism for transforming growth factor beta-dependent nuclear accumulation of Smads.''; PubMed Europe PMC

History

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CompareRevisionActionTimeUserComment
101384view11:27, 1 November 2018ReactomeTeamreactome version 66
100922view21:02, 31 October 2018ReactomeTeamreactome version 65
100462view19:37, 31 October 2018ReactomeTeamreactome version 64
100008view16:21, 31 October 2018ReactomeTeamreactome version 63
99561view14:54, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
94007view13:51, 16 August 2017ReactomeTeamreactome version 61
93622view11:29, 9 August 2017ReactomeTeamreactome version 61
87118view18:36, 18 July 2016EgonwOntology Term : 'signaling pathway' added !
86732view09:25, 11 July 2016ReactomeTeamreactome version 56
83227view10:26, 18 November 2015ReactomeTeamVersion54
81622view13:10, 21 August 2015ReactomeTeamVersion53
77082view08:38, 17 July 2014ReactomeTeamFixed remaining interactions
76787view12:15, 16 July 2014ReactomeTeamFixed remaining interactions
76110view10:17, 11 June 2014ReactomeTeamRe-fixing comment source
75822view11:37, 10 June 2014ReactomeTeamReactome 48 Update
75172view14:12, 8 May 2014AnweshaFixing comment source for displaying WikiPathways description
74819view08:55, 30 April 2014ReactomeTeamNew pathway

External references

DataNodes

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NameTypeDatabase referenceComment
ACVR1B ProteinP36896 (Uniprot-TrEMBL)
ACVR1BProteinP36896 (Uniprot-TrEMBL)
ACVR1C ProteinQ8NER5 (Uniprot-TrEMBL)
ACVR1CProteinQ8NER5 (Uniprot-TrEMBL)
ACVR2A ProteinP27037 (Uniprot-TrEMBL)
ACVR2A,BComplexR-HSA-1181136 (Reactome)
ACVR2B ProteinQ13705 (Uniprot-TrEMBL)
ADPMetaboliteCHEBI:16761 (ChEBI)
ATPMetaboliteCHEBI:15422 (ChEBI)
Activin A,AB,B:ACVR2A,B:ACVR1BComplexR-HSA-1549493 (Reactome)
Activin A,AB,B:ACVR2A,B:p-ACVR1BComplexR-HSA-1549500 (Reactome)
Activin AB,B:ACVR2A,B:ACVR1CComplexR-HSA-2470469 (Reactome)
Activin AB,B:ACVR2A,B:p-ACVR1CComplexR-HSA-2470475 (Reactome)
Activin A,AB,B:FSTL3ComplexR-HSA-2473219 (Reactome)
Activin A,AB,B:FSTComplexR-HSA-2473196 (Reactome)
Activin A,AB,BComplexR-HSA-2470494 (Reactome)
Activin AB,BComplexR-HSA-2470478 (Reactome)
Activin Response ElementR-ALL-1225892 (Reactome) The inferred consensus sequence of the activin response element is TGT(G/T)(G/T)ATT (Zhou et al. 1998).
Activin Response Element R-ALL-1225892 (Reactome) The inferred consensus sequence of the activin response element is TGT(G/T)(G/T)ATT (Zhou et al. 1998).
Activin:ACVR2A,B:p-ACVR1B,CComplexR-HSA-2470484 (Reactome)
DRAP1 ProteinQ14919 (Uniprot-TrEMBL)
FOXH1 ProteinO75593 (Uniprot-TrEMBL)
FOXH1:DRAP1ComplexR-HSA-1226031 (Reactome)
FOXH1ProteinO75593 (Uniprot-TrEMBL)
FST ProteinP19883 (Uniprot-TrEMBL)
FSTL3 ProteinO95633 (Uniprot-TrEMBL)
FSTL3ProteinO95633 (Uniprot-TrEMBL)
FSTProteinP19883 (Uniprot-TrEMBL)
INHBA ProteinP08476 (Uniprot-TrEMBL)
INHBB ProteinP09529 (Uniprot-TrEMBL)
SMAD2 ProteinQ15796 (Uniprot-TrEMBL)
SMAD2,3:SMAD4:FOXH1:Activin Response ElementComplexR-HSA-1225870 (Reactome)
SMAD2/3ComplexR-HSA-171172 (Reactome)
SMAD3 ProteinP84022 (Uniprot-TrEMBL)
SMAD4 ProteinQ13485 (Uniprot-TrEMBL)
SMAD4ProteinQ13485 (Uniprot-TrEMBL)
p-2S-SMAD2/3:SMAD4ComplexR-HSA-171175 (Reactome)
p-2S-SMAD2/3:SMAD4ComplexR-HSA-173511 (Reactome)
p-2S-SMAD2/3ComplexR-HSA-171182 (Reactome)
p-4S,T188,T206-ACVR1B ProteinP36896 (Uniprot-TrEMBL)
p-S423,S425-SMAD3 ProteinP84022 (Uniprot-TrEMBL)
p-S465,S467-SMAD2 ProteinQ15796 (Uniprot-TrEMBL)
p-T175,S177,S179,S181,T194-ACVR1C ProteinQ8NER5 (Uniprot-TrEMBL)

Annotated Interactions

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SourceTargetTypeDatabase referenceComment
ACVR1BR-HSA-1181153 (Reactome)
ACVR1CR-HSA-2470483 (Reactome)
ACVR2A,BR-HSA-1181153 (Reactome)
ACVR2A,BR-HSA-2470483 (Reactome)
ADPArrowR-HSA-1181149 (Reactome)
ADPArrowR-HSA-1549526 (Reactome)
ADPArrowR-HSA-2470508 (Reactome)
ATPR-HSA-1181149 (Reactome)
ATPR-HSA-1549526 (Reactome)
ATPR-HSA-2470508 (Reactome)
Activin A,AB,B:ACVR2A,B:ACVR1BArrowR-HSA-1181153 (Reactome)
Activin A,AB,B:ACVR2A,B:ACVR1BR-HSA-1181149 (Reactome)
Activin A,AB,B:ACVR2A,B:ACVR1Bmim-catalysisR-HSA-1181149 (Reactome)
Activin A,AB,B:ACVR2A,B:p-ACVR1BArrowR-HSA-1181149 (Reactome)
Activin AB,B:ACVR2A,B:ACVR1CArrowR-HSA-2470483 (Reactome)
Activin AB,B:ACVR2A,B:ACVR1CR-HSA-2470508 (Reactome)
Activin AB,B:ACVR2A,B:ACVR1Cmim-catalysisR-HSA-2470508 (Reactome)
Activin AB,B:ACVR2A,B:p-ACVR1CArrowR-HSA-2470508 (Reactome)
Activin A,AB,B:FSTArrowR-HSA-2473184 (Reactome)
Activin A,AB,B:FSTL3ArrowR-HSA-2473186 (Reactome)
Activin A,AB,BR-HSA-1181153 (Reactome)
Activin A,AB,BR-HSA-2473184 (Reactome)
Activin A,AB,BR-HSA-2473186 (Reactome)
Activin AB,BR-HSA-2470483 (Reactome)
Activin Response ElementR-HSA-1225919 (Reactome)
Activin:ACVR2A,B:p-ACVR1B,Cmim-catalysisR-HSA-1549526 (Reactome)
FOXH1:DRAP1TBarR-HSA-1225919 (Reactome)
FOXH1R-HSA-1225919 (Reactome)
FSTL3R-HSA-2473186 (Reactome)
FSTR-HSA-2473184 (Reactome)
R-HSA-1181149 (Reactome) Upon binding Activin A (INHBA:INHBA), Activin AB (INHBA:INHBB), or Activin B (INHBB:INHBB), the type II component of the activin receptor (ACVR2A or ACVR2B) phosphorylates the type I component ACVR1B (ALK4) at multiple serine and threonine residues within the GS domain (Attisano et al. 1996, Willis et al. 1996, Willis and Mathews 1997, Zhou et al. 2000).
R-HSA-1181153 (Reactome) Activin binds the Activin receptor composed of a type II receptor (ACVR2A/B) and a type I receptor, in this case ACVR1B (ALK4) (Attisano et al. 1996, Zhou et al. 2000). Activin appears to interact initially with the type II receptor component (Attisano et al. 1996). It is unclear if the type II and type I receptors are associated before binding Activin. Any of Activin A (INHBA:INHBA), Activin AB (INHBA:INHBB), and Activin B (INHBB:INHBB) can bind and signal via an activin receptor containing the ACVR1B (ALK4) type I receptor.
R-HSA-1225919 (Reactome) SMAD2 and SMAD3 do not bind DNA efficiently. They must interact with DNA-binding proteins to activate transcription. FOXH1 interacts with phospho-SMAD2 and phospho-SMAD3 complexed with CO-SMAD (SMAD4) at promoters containing the Activin Response Element (Zhou et al. 1998, Yanagisawa et al. 2000, inferred from Xenopus in Chen et al. 1996, Chen et al. 1997, Yeo et al. 1999). Follicle-stimulating hormone beta subunit (FSHB) and the Lim1 homeobox gene (LXH1) are examples of genes regulated by Activin.
R-HSA-1549526 (Reactome) Activin receptors containing the type II receptors ACVR2A/B (ActRIIA, ActRIIB) and the type I receptors ACVR1B/C (ALK4, ALK7) signal through SMAD2 and SMAD3. The phosphorylated type I receptor (ACVR1B/C) phosphorylates SMAD2 or SMAD3. Homodimers or heterodimers of SMAD2 and SMAD3 bind the co-Smad SMAD4 and the ternary complex (SMAD2/3:SMAD2/3:SMAD4) enters the nucleus and activates expression of target genes.
R-HSA-170847 (Reactome) The phosphorylated C-terminal tail of R-SMAD induces a conformational change in the MH2 domain (Qin et al. 2001, Chacko et al. 2004), which now acquires high affinity towards Co-SMAD i.e. SMAD4 (common mediator of signal transduction in TGF-beta/BMP signaling). The R-SMAD:Co-SMAD complex (Nakao et al. 1997) most likely is a trimer of two R-SMADs with one Co-SMAD (Kawabata et al. 1998). It is important to note that the Co-SMAD itself cannot be phosphorylated as it lacks the C-terminal serine motif.

ZFYVE16 (endofin) promotes SMAD heterotrimer formation. ZFYVE16 can bind TGFBR1 and facilitate SMAD2 phosphorylation, and it can also bind SMAD4, but the exact mechanism of ZFYVE16 (endofin) action in the context of TGF-beta receptor signaling is not known (Chen et al. 2007).
R-HSA-173488 (Reactome) The phosphorylated R-SMAD:CO-SMAD complex rapidly translocates to the nucleus (Xu et al. 2000, Kurisaki et al. 2001, Xiao et al. 2003) where it binds directly to DNA and interacts with a plethora of transcription co-factors. Regulation of target gene expression can be either positive or negative. A classic example of a target gene of the pathway are the genes encoding for I-SMADs. Thus, TGF-beta/SMAD signaling induces the expression of the negative regulators of the pathway (negative feedback loop).
R-HSA-2470483 (Reactome) As inferred from mouse, Activin binds the Activin receptor composed of a type II receptor (ACVR2A/B) and a type I receptor, in this case ACVR1C (ALK7). It is unclear if the type II receptor and the type I receptor are associated before binding Activin, Activin AB (INHBA:INHBB) and Activin B (INHBB:INHBB), but not Activin A (INHBA:INHBA) can bind and signal via an activin receptor containing the ACVR1C (ALK7) type I receptor.
R-HSA-2470508 (Reactome) As inferred from mouse, upon binding Activin AB (INHBA:INHBB) or Activin B (INHBB:INHBB), the type II component of the activin receptor (ACVR2A or ACVR2B) phosphorylates the type I component ACVR1C (ALK7) at multiple serine and threonine residues within the GS domain.
R-HSA-2473184 (Reactome) Two molecules of Follistatin (FST) bind an Activin dimer in serum or follicular fluid (Schneyer et al. 1992, Krummen et al. 1993, Schneyer et al. 1994, Thompson et al. 2005). FST has been experimentally shown to bind Activin A and Activin B (Schneyer et al. 2003). Binding of FST to Activin AB is inferred.
R-HSA-2473186 (Reactome) Two molecules of FSTL3 bind an Activin dimer (Sidis et al. 2002, Stamler et al. 2008). FSTL3 has been experimentally shown to bind Activin A and Activin B (Schneyer et al. 2003). Binding of FSTL3 to Activin AB is inferred. A portion of FSTL3 is also located in the nucleus (Tortoriello et al. 2001), however FSTL3:Activin complexes have not been demonstrated in the nucleus.
SMAD2,3:SMAD4:FOXH1:Activin Response ElementArrowR-HSA-1225919 (Reactome)
SMAD2/3R-HSA-1549526 (Reactome)
SMAD4R-HSA-170847 (Reactome)
p-2S-SMAD2/3:SMAD4ArrowR-HSA-170847 (Reactome)
p-2S-SMAD2/3:SMAD4ArrowR-HSA-173488 (Reactome)
p-2S-SMAD2/3:SMAD4R-HSA-1225919 (Reactome)
p-2S-SMAD2/3:SMAD4R-HSA-173488 (Reactome)
p-2S-SMAD2/3ArrowR-HSA-1549526 (Reactome)
p-2S-SMAD2/3R-HSA-170847 (Reactome)
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