TGF beta 1

TGFB1

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1KLA, 1KLC, 1KLD, 3KFD, 4KV5

Identifiers

Aliases

TGFB1, CED, DPD1, LAP, TGFB, TGFbeta, transforming growth factor beta 1

External IDs

OMIM: 190180 MGI: 98725 HomoloGene: 540 GeneCards: TGFB1

Gene location (Human)

Chr.	Chromosome 19 (human)^[1]

Band	No data available	Start	41,301,587 bp^[1]
Band	No data available	End	41,353,911 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 7 (mouse)^[2]

Band	No data available	Start	25,687,002 bp^[2]
Band	No data available	End	25,705,077 bp^[2]

RNA expression pattern

More reference expression data

Gene ontology
Molecular function	• type II transforming growth factor beta receptor binding • protein N-terminus binding • cytokine activity • enzyme binding • growth factor activity • antigen binding • type I transforming growth factor beta receptor binding • protein homodimerization activity • protein serine/threonine kinase activator activity • protein binding • protein heterodimerization activity • type III transforming growth factor beta receptor binding • transforming growth factor beta receptor binding
Cellular component	• cytoplasm • extracellular region • nucleus • microvillus • cell surface • blood microparticle • proteinaceous extracellular matrix • plasma membrane • secretory granule • axon • neuronal cell body • Golgi lumen • platelet alpha granule lumen • extracellular matrix • extracellular space
Biological process	• positive regulation of histone deacetylation • positive regulation of transcription regulatory region DNA binding • ureteric bud development • tolerance induction to self antigen • positive regulation of protein phosphorylation • endoderm development • response to cholesterol • positive regulation of MAP kinase activity • regulation of sodium ion transport • response to progesterone • negative regulation of cell cycle • response to organic substance • mammary gland development • T cell homeostasis • negative regulation of ossification • negative regulation of hyaluronan biosynthetic process • protein phosphorylation • T cell differentiation • positive regulation of vascular permeability • animal organ regeneration • positive regulation of blood vessel endothelial cell migration • negative regulation of epithelial cell proliferation • regulation of binding • inner ear development • myelination • negative regulation of macrophage cytokine production • cell proliferation • transforming growth factor beta receptor signaling pathway • face morphogenesis • negative regulation of cell proliferation • positive regulation of receptor clustering • regulation of apoptotic process • defense response to fungus, incompatible interaction • positive regulation of collagen biosynthetic process • cellular response to transforming growth factor beta stimulus • pathway-restricted SMAD protein phosphorylation • regulation of DNA binding • regulation of actin cytoskeleton reorganization • negative regulation of fat cell differentiation • positive regulation of cellular protein metabolic process • cell-cell junction organization • negative regulation of myoblast differentiation • positive regulation of protein kinase B signaling • active induction of host immune response by virus • common-partner SMAD protein phosphorylation • positive regulation of branching involved in ureteric bud morphogenesis • SMAD protein signal transduction • epidermal growth factor receptor signaling pathway • macrophage derived foam cell differentiation • negative regulation of blood vessel endothelial cell migration • positive regulation of protein dephosphorylation • extrinsic apoptotic signaling pathway • SMAD protein import into nucleus • negative regulation of extracellular matrix disassembly • mitotic cell cycle checkpoint • positive regulation of fibroblast proliferation • negative regulation of cell differentiation • regulation of branching involved in mammary gland duct morphogenesis • positive regulation of exit from mitosis • negative regulation of transforming growth factor beta receptor signaling pathway • negative regulation of gene expression • morphogenesis of a branching structure • regulation of SMAD protein import into nucleus • positive regulation of peptidyl-serine phosphorylation • cell activation • negative regulation of neuroblast proliferation • positive regulation of transcription, DNA-templated • cell growth • negative regulation of T cell proliferation • response to wounding • negative regulation of cell growth • positive regulation of chemotaxis • protein export from nucleus • regulation of protein import into nucleus • positive regulation of peptidyl-tyrosine phosphorylation • positive regulation of protein import into nucleus • positive regulation of cardiac muscle cell differentiation • oligodendrocyte development • positive regulation of interleukin-17 production • inflammatory response • negative regulation of interleukin-17 production • lymph node development • T cell activation • Notch signaling pathway • negative regulation of protein phosphorylation • regulation of blood vessel remodeling • SMAD protein complex assembly • regulation of striated muscle tissue development • response to vitamin D • chondrocyte differentiation • regulatory T cell differentiation • regulation of cartilage development • branch elongation involved in mammary gland duct branching • positive regulation of bone mineralization • positive regulation of epithelial cell proliferation • female pregnancy • cellular response to organic cyclic compound • positive regulation of extracellular matrix assembly • cellular calcium ion homeostasis • wound healing • negative regulation of transcription from RNA polymerase II promoter • response to glucose • positive regulation of epithelial to mesenchymal transition • cellular response to dexamethasone stimulus • negative regulation of production of miRNAs involved in gene silencing by miRNA • evasion or tolerance of host defenses by virus • lens fiber cell differentiation • positive regulation of NF-kappaB transcription factor activity • extracellular matrix assembly • ATP biosynthetic process • hematopoietic progenitor cell differentiation • regulation of interleukin-23 production • positive regulation of protein secretion • frontal suture morphogenesis • epithelial to mesenchymal transition • phosphate-containing compound metabolic process • regulation of gene expression • adaptive immune response based on somatic recombination of immune receptors built from immunoglobulin superfamily domains • negative regulation of release of sequestered calcium ion into cytosol • response to radiation • mononuclear cell proliferation • negative regulation of transcription, DNA-templated • negative regulation of T cell activation • positive regulation of odontogenesis • lipopolysaccharide-mediated signaling pathway • positive regulation of protein localization to nucleus • response to estradiol • regulation of cell migration • response to hypoxia • hyaluronan catabolic process • negative regulation of phagocytosis • response to organic cyclic compound • positive regulation of protein complex assembly • protein kinase B signaling • negative regulation of cell-cell adhesion • negative regulation of gene silencing by miRNA • positive regulation of regulatory T cell differentiation • cellular response to growth factor stimulus • positive regulation of pathway-restricted SMAD protein phosphorylation • protein import into nucleus, translocation • mammary gland branching involved in thelarche • response to laminar fluid shear stress • aging • regulation of regulatory T cell differentiation • platelet degranulation • negative regulation of DNA replication • myeloid dendritic cell differentiation • salivary gland morphogenesis • receptor catabolic process • MAPK cascade • positive regulation of histone acetylation • regulation of transforming growth factor beta receptor signaling pathway • positive regulation of phosphatidylinositol 3-kinase activity • negative regulation of protein localization to plasma membrane • positive regulation of NAD+ ADP-ribosyltransferase activity • negative regulation of immune response • regulation of cell proliferation • negative regulation of skeletal muscle tissue development • positive regulation of peptidyl-threonine phosphorylation • positive regulation of smooth muscle cell differentiation • cell cycle arrest • positive regulation of isotype switching to IgA isotypes • connective tissue replacement involved in inflammatory response wound healing • ossification involved in bone remodeling • positive regulation of apoptotic process • positive regulation of vascular endothelial growth factor production • positive regulation of superoxide anion generation • digestive tract development • cell migration • positive regulation of fibroblast migration • positive regulation of cell division • response to drug • germ cell migration • positive regulation of transcription from RNA polymerase II promoter • negative regulation of mitotic cell cycle • positive regulation of SMAD protein import into nucleus • positive regulation of cell cycle arrest • positive regulation of pri-miRNA transcription from RNA polymerase II promoter • positive regulation of gene expression • positive regulation of cell proliferation • liver regeneration • regulation of epithelial to mesenchymal transition involved in endocardial cushion formation • positive regulation of mononuclear cell migration • cellular response to insulin-like growth factor stimulus • positive regulation of cell migration • response to immobilization stress • cellular response to mechanical stimulus • cellular response to ionizing radiation • vasculogenesis • neural tube closure • heart valve morphogenesis • heart development • neural tube development • membrane protein intracellular domain proteolysis • leukocyte migration • ventricular cardiac muscle tissue morphogenesis • positive regulation of ERK1 and ERK2 cascade • transforming growth factor beta receptor signaling pathway involved in heart development • embryonic liver development • BMP signaling pathway • cell development • apoptotic process • regulation of pri-miRNA transcription from RNA polymerase II promoter • positive regulation of production of miRNAs involved in gene silencing by miRNA
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


7040


21803

Ensembl


ENSG00000105329


ENSMUSG00000002603

UniProt


P01137


P04202

RefSeq (mRNA)


NM_000660


NM_011577

RefSeq (protein)


NP_000651


NP_035707

Location (UCSC)

Chr 19: 41.3 – 41.35 Mb

Chr 7: 25.69 – 25.71 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Transforming growth factor beta 1 or TGF-β1 is a polypeptide member of the transforming growth factor beta superfamily of cytokines. It is a secreted protein that performs many cellular functions, including the control of cell growth, cell proliferation, cell differentiation and apoptosis. In humans, TGF-β1 is encoded by the TGFB1 gene.^[5]^[6]

Function

TGF-β is a multifunctional set of peptides that controls proliferation, differentiation, and other functions in many cell types. TGF-β acts synergistically with TGFA in inducing transformation. It also acts as a negative autocrine growth factor. Dysregulation of TGF-β activation and signaling may result in apoptosis. Many cells synthesize TGF-β and almost all of them have specific receptors for this peptide. TGF-β1, TGF-β2, and TGF-β3 all function through the same receptor signaling systems.^[7]

TGF-β1 was first identified in human platelets as a protein with a molecular mass of 25 kilodaltons with a potential role in wound healing.^[8] It was later characterized as a large protein precursor (containing 390 amino acids) that was proteolytically processed to produce a mature peptide of 112 amino acids.^[9]

TGF-β1 plays an important role in controlling the immune system, and shows different activities on different types of cell, or cells at different developmental stages. Most immune cells (or leukocytes) secrete TGF-β1.^[10]

T cells

Some T cells (e.g. regulatory T cells) release TGF-β1 to inhibit the actions of other T cells. Interleukin 1- and interleukin 2-dependent proliferation of activated T cells,^[11]^[12] and the activation of quiescent helper T cells and cytotoxic T cells is prevented by the activity of TGF-β1.^[13]^[14] Similarly, TGF-β1 can inhibit the secretion and activity of many other cytokines including interferon-γ, tumor necrosis factor-alpha (TNF-α) and various interleukins. It can also decrease the expression levels of cytokine receptors, such as the IL-2 receptor to down-regulate the activity of immune cells. However, TGF-β1 can also increase the expression of certain cytokines in T cells and promote their proliferation, particularly if the cells are immature.^[10]

B cells

TGF-β1 has similar effects on B cells that also vary according to the differentiation state of the cell. It inhibits proliferation and stimulates apoptosis of B cells,^[15] and plays a role in controlling the expression of antibody, transferrin and MHC class II proteins on immature and mature B cells.^[10]^[15]

Myeloid cells

The effects of TGF-β1 on macrophages and monocytes is predominantly suppressive; this cytokine can inhibit the proliferation of these cells and prevent their production of reactive oxygen (e.g. superoxide (O₂⁻)) and nitrogen (e.g. nitric oxide (NO)) intermediates. However, as with other cell types, TGF-β1 can also have the opposite effect on cells of myeloid origin. For example, TGF-β1 acts as a chemoattractant, directing an immune response to some pathogens; macrophages and monocytes respond to low levels of TGF-β1 in a chemotactic manner. Furthermore, the expression of monocytic cytokines (including interleukin-1(IL-1)-alpha, IL-1-beta, and TNF-α),^[14] and phagocytic killing by macrophages can be increased by the action of TGF-β1.^[10]

Interactions

TGF beta 1 has been shown to interact with:

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000105329 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000002603 - Ensembl, May 2017
↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ Ghadami M, Makita Y, Yoshida K, Nishimura G, Fukushima Y, Wakui K, Ikegawa S, Yamada K, Kondo S, Niikawa N, Tomita Ha (January 2000). "Genetic mapping of the Camurati-Engelmann disease locus to chromosome 19q13.1-q13.3". Am. J. Hum. Genet. 66 (1): 143–7. PMC 1288319 . PMID 10631145. doi:10.1086/302728.
↑ Vaughn SP, Broussard S, Hall CR, Scott A, Blanton SH, Milunsky JM, Hecht JT (May 2000). "Confirmation of the mapping of the Camurati-Englemann locus to 19q13. 2 and refinement to a 3.2-cM region". Genomics. 66 (1): 119–21. PMID 10843814. doi:10.1006/geno.2000.6192.
↑ "Entrez Gene: TGFB1 transforming growth factor, beta 1".
↑ Assoian RK, Komoriya A, Meyers CA, Miller DM, Sporn MB (1983). "Transforming growth factor-beta in human platelets. Identification of a major storage site, purification, and characterization". J. Biol. Chem. 258 (11): 7155–60. PMID 6602130.
↑ Derynck R, Jarrett JA, Chen EY, Eaton DH, Bell JR, Assoian RK, Roberts AB, Sporn MB, Goeddel DV (1985). "Human transforming growth factor-beta complementary DNA sequence and expression in normal and transformed cells". Nature. 316 (6030): 701–5. PMID 3861940. doi:10.1038/316701a0.
1 2 3 4 Letterio JJ, Roberts AB (1998). "Regulation of immune responses by TGF-beta". Annu. Rev. Immunol. 16: 137–61. PMID 9597127. doi:10.1146/annurev.immunol.16.1.137.
↑ Wahl SM, Hunt DA, Wong HL, Dougherty S, McCartney-Francis N, Wahl LM, Ellingsworth L, Schmidt JA, Hall G, Roberts AB (1988). "Transforming growth factor-beta is a potent immunosuppressive agent that inhibits IL-1-dependent lymphocyte proliferation". J. Immunol. 140 (9): 3026–32. PMID 3129508.
↑ Tiemessen MM, Kunzmann S, Schmidt-Weber CB, Garssen J, Bruijnzeel-Koomen CA, Knol EF, van Hoffen E (2003). "Transforming growth factor-beta inhibits human antigen-specific CD4+ T cell proliferation without modulating the cytokine response". Int. Immunol. 15 (12): 1495–504. PMID 14645158. doi:10.1093/intimm/dxg147.
↑ Gilbert KM, Thoman M, Bauche K, Pham T, Weigle WO (1997). "Transforming growth factor-beta 1 induces antigen-specific unresponsiveness in naive T cells". Immunol. Invest. 26 (4): 459–72. PMID 9246566. doi:10.3109/08820139709022702.
1 2 Wahl SM, Wen J, Moutsopoulos N (2006). "TGF-beta: a mobile purveyor of immune privilege". Immunol. Rev. 213: 213–27. PMID 16972906. doi:10.1111/j.1600-065X.2006.00437.x.
1 2 Lebman DA, Edmiston JS (1999). "The role of TGF-beta in growth, differentiation, and maturation of B lymphocytes". Microbes Infect. 1 (15): 1297–304. PMID 10611758. doi:10.1016/S1286-4579(99)00254-3.
↑ Hildebrand A, Romarís M, Rasmussen LM, Heinegård D, Twardzik DR, Border WA, Ruoslahti E (September 1994). "Interaction of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor beta". Biochem. J. 302 (2): 527–34. PMC 1137259 . PMID 8093006. doi:10.1042/bj3020527.
↑ Schönherr E, Broszat M, Brandan E, Bruckner P, Kresse H (July 1998). "Decorin core protein fragment Leu155-Val260 interacts with TGF-beta but does not compete for decorin binding to type I collagen". Arch. Biochem. Biophys. 355 (2): 241–8. PMID 9675033. doi:10.1006/abbi.1998.0720.
↑ Takeuchi Y, Kodama Y, Matsumoto T (Dec 1994). "Bone matrix decorin binds transforming growth factor-beta and enhances its bioactivity". J. Biol. Chem. 269 (51): 32634–8. PMID 7798269.
↑ Choy L, Derynck R (November 1998). "The type II transforming growth factor (TGF)-beta receptor-interacting protein TRIP-1 acts as a modulator of the TGF-beta response". J. Biol. Chem. 273 (47): 31455–62. PMID 9813058. doi:10.1074/jbc.273.47.31455.
↑ Saharinen J, Keski-Oja J (August 2000). "Specific sequence motif of 8-Cys repeats of TGF-beta binding proteins, LTBPs, creates a hydrophobic interaction surface for binding of small latent TGF-beta". Mol. Biol. Cell. 11 (8): 2691–704. PMC 14949 . PMID 10930463. doi:10.1091/mbc.11.8.2691.
↑ Ebner R, Chen RH, Lawler S, Zioncheck T, Derynck R (November 1993). "Determination of type I receptor specificity by the type II receptors for TGF-beta or activin". Science. 262 (5135): 900–2. PMID 8235612. doi:10.1126/science.8235612.
↑ Oh SP, Seki T, Goss KA, Imamura T, Yi Y, Donahoe PK, Li L, Miyazono K, ten Dijke P, Kim S, Li E (March 2000). "Activin receptor-like kinase 1 modulates transforming growth factor-beta 1 signaling in the regulation of angiogenesis". Proc. Natl. Acad. Sci. U.S.A. 97 (6): 2626–31. PMC 15979 . PMID 10716993. doi:10.1073/pnas.97.6.2626.
↑ McGonigle S, Beall MJ, Feeney EL, Pearce EJ (February 2001). "Conserved role for 14-3-3epsilon downstream of type I TGFbeta receptors". FEBS Lett. 490 (1-2): 65–9. PMID 11172812. doi:10.1016/s0014-5793(01)02133-0.

Border WA, Noble NA (1994). "Transforming growth factor beta in tissue fibrosis". N. Engl. J. Med. 331 (19): 1286–92. PMID 7935686. doi:10.1056/NEJM199411103311907.
Munger JS, Harpel JG, Gleizes PE, Mazzieri R, Nunes I, Rifkin DB (1997). "Latent transforming growth factor-beta: structural features and mechanisms of activation". Kidney Int. 51 (5): 1376–82. PMID 9150447. doi:10.1038/ki.1997.188.
Iozzo RV (1999). "The biology of the small leucine-rich proteoglycans. Functional network of interactive proteins". J. Biol. Chem. 274 (27): 18843–6. PMID 10383378. doi:10.1074/jbc.274.27.18843.
Reinhold D, Wrenger S, Kähne T, Ansorge S (1999). "HIV-1 Tat: immunosuppression via TGF-beta1 induction". Immunol. Today. 20 (8): 384–5. PMID 10431160. doi:10.1016/S0167-5699(99)01497-8.
Yamada Y (2001). "Association of polymorphisms of the transforming growth factor-beta1 gene with genetic susceptibility to osteoporosis". Pharmacogenetics. 11 (9): 765–71. PMID 11740340. doi:10.1097/00008571-200112000-00004.
Chen W, Wahl SM (2002). "TGF-beta: receptors, signaling pathways and autoimmunity". Curr. Dir. Autoimmun. Current Directions in Autoimmunity. 5: 62–91. ISBN 3-8055-7308-1. PMID 11826761. doi:10.1159/000060548.
Marone M, Bonanno G, Rutella S, Leone G, Scambia G, Pierelli L (2002). "Survival and cell cycle control in early hematopoiesis: role of bcl-2, and the cyclin dependent kinase inhibitors P27 and P21". Leuk. Lymphoma. 43 (1): 51–7. PMID 11908736. doi:10.1080/10428190210195.
Schnaper HW, Hayashida T, Hubchak SC, Poncelet AC (2003). "TGF-beta signal transduction and mesangial cell fibrogenesis". Am. J. Physiol. Renal Physiol. 284 (2): F243–52. PMID 12529270. doi:10.1152/ajprenal.00300.2002.
Kalluri R, Neilson EG (2003). "Epithelial-mesenchymal transition and its implications for fibrosis". J. Clin. Invest. 112 (12): 1776–84. PMC 297008 . PMID 14679171. doi:10.1172/JCI20530.
Grainger DJ (2004). "Transforming growth factor beta and atherosclerosis: so far, so good for the protective cytokine hypothesis". Arterioscler. Thromb. Vasc. Biol. 24 (3): 399–404. PMID 14699019. doi:10.1161/01.ATV.0000114567.76772.33.
Attisano L, Labbé E (2004). "TGFbeta and Wnt pathway cross-talk". Cancer Metastasis Rev. 23 (1-2): 53–61. PMID 15000149. doi:10.1023/A:1025811012690.
McGowan TA, Zhu Y, Sharma K (2004). "Transforming growth factor-beta: a clinical target for the treatment of diabetic nephropathy". Curr. Diab. Rep. 4 (6): 447–54. PMID 15539010. doi:10.1007/s11892-004-0055-z.
Sheppard D (2005). "Integrin-mediated activation of latent transforming growth factor beta". Cancer Metastasis Rev. 24 (3): 395–402. PMID 16258727. doi:10.1007/s10555-005-5131-6.
Gressner AM, Weiskirchen R (2006). "Modern pathogenetic concepts of liver fibrosis suggest stellate cells and TGF-beta as major players and therapeutic targets". J. Cell. Mol. Med. 10 (1): 76–99. PMID 16563223. doi:10.1111/j.1582-4934.2006.tb00292.x.
Seoane J (2006). "Escaping from the TGFbeta anti-proliferative control". Carcinogenesis. 27 (11): 2148–56. PMID 16698802. doi:10.1093/carcin/bgl068.
Lee CG, Kang HR, Homer RJ, Chupp G, Elias JA (2006). "Transgenic modeling of transforming growth factor-beta(1): role of apoptosis in fibrosis and alveolar remodeling". Proc Am Thorac Soc. 3 (5): 418–23. PMC 2658706 . PMID 16799085. doi:10.1513/pats.200602-017AW.
Wahl SM (2007). "Transforming growth factor-beta: innately bipolar". Curr. Opin. Immunol. 19 (1): 55–62. PMID 17137775. doi:10.1016/j.coi.2006.11.008.
Redondo S, Santos-Gallego CG, Tejerina T (2007). "TGF-beta1: a novel target for cardiovascular pharmacology". Cytokine Growth Factor Rev. 18 (3-4): 279–86. PMID 17485238. doi:10.1016/j.cytogfr.2007.04.005.

PDB gallery

1kla: SOLUTION STRUCTURE OF TGF-B1, NMR, MODELS 1-17 OF 33 STRUCTURES

1klc: SOLUTION STRUCTURE OF TGF-B1, NMR, MINIMIZED AVERAGE STRUCTURE

1kld: SOLUTION STRUCTURE OF TGF-B1, NMR, MODELS 18-33 OF 33 STRUCTURES

Cell signaling: TGFβ signaling pathway

TGF beta superfamily of ligands

TGF beta family	TGF-β1 TGF-β2 TGF-β3
Bone morphogenetic proteins	BMP2 BMP3 BMP4 BMP5 BMP6 BMP7 BMP8a BMP8b BMP10 BMP15
Growth differentiation factors	GDF1 GDF2 GDF3 GDF5 GDF6 GDF7 Myostatin/GDF8 GDF9 GDF10 GDF11 GDF15
Other	Activin and inhibin Anti-müllerian hormone Nodal

TGF beta receptors
(Activin, BMP)

TGFBR1:	Activin type 1 receptors ACVR1 ACVR1B ACVR1C ACVRL1 BMPR1 BMPR1A BMPR1B
TGFBR2:	Activin type 2 receptors ACVR2A ACVR2B AMHR2 BMPR2
TGFBR3:	betaglycan

Transducers/SMAD

Ligand inhibitors

Coreceptors

BAMBI
Cripto

Other

SARA

Growth factors

Fibroblast

FGF receptor ligands:	FGF1/FGF2/FGF5 FGF3/FGF4/FGF6
KGF	FGF7/FGF10/FGF22 FGF8/FGF17/FGF18 FGF9/FGF16/FGF20
FGF homologous factors:	FGF11 FGF12 FGF13 FGF14
hormone-like:	FGF19 FGF21 FGF23

EGF-like domain

TGFβ pathway

TGFβ
- TGFβ1
- TGFβ2
- TGFβ3

Insulin-like

IGF1
IGF2

Platelet-derived

Vascular endothelial

Other

TGFβ receptor superfamily modulators

Type I

ALK1 (ACVRL1)	Agonists: Activin (A, B, AB) Avotermin BMP (10) Cetermin GDF (2 (BMP9)) TGFβ (1, 2, 3) Antibodies: Ascrinvacumab Kinase inhibitors: K-02288 ML-347 (LDN-193719, VU0469381) Decoy receptors: Dalantercept Other inhibitors: Disitertide
ALK2 (ACVR1A)	Agonists: Activin (A, B, AB) AMH (MIS) Avotermin BMP (5, 6, 7, 8A, 8B) Eptotermin alfa TGFβ (1, 2, 3) Kinase inhibitors: DMH-1 DMH-2 Dorsomorphin (BML-275) K-02288 ML-347 (LDN-193719, VU0469381)
ALK3 (BMPR1A)	Agonists: AMH (MIS) BMP (2, 4, 5, 6, 7, 8A, 8B) Dibotermin alfa Eptotermin alfa Kinase inhibitors: DMH-2 Dorsomorphin (BML-275) K-02288
ALK4 (ACVR1B)	Agonists: Activin (A, B, AB) GDF (1, 3, 11 (BMP11)) Myostatin (GDF8) Nodal Antagonists: Inhibin (A, B) Lefty (1, 2) Kinase inhibitors: A 83-01 SB-431542 SB-505124
ALK5 (TGFβR1)	Agonists: Avotermin GDF (10 (BMP3B), 11 (BMP11)) TGFβ (1, 2, 3) Antibodies: Fresolimumab Lerdelimumab Metelimumab Kinase inhibitors: A 83-01 D-4476 GW-788388 LY-364947 LY-2109761 Galunisertib (LY-2157299) R-268712 RepSox (E-616452, SJN-2511) SB-431542 SB-505124 SB-525334 SD-208
ALK6 (BMPR1B)	Agonists: BMP (2, 4, 5, 6, 7, 8A, 8B, 15 (GDF9B)) Dibotermin alfa Eptotermin alfa GDF (5 (BMP14), 6 (BMP13), 7 (BMP12), 9, 15) Radotermin Kinase inhibitors: DMH-2 Dorsomorphin (BML-275) K-02288
ALK7 (ACVR1C)	Agonists: GDF (1, 3, 11 (BMP11)) Nodal Antagonists: Lefty (1, 2) Kinase inhibitors: A 83-01 SB-431542 SB-505124

Type II

TGFβR2	Agonists: Avotermin GDF (10 (BMP3B)) TGFβ (1, 2, 3) Antibodies: Fresolimumab Lerdelimumab Metelimumab Kinase inhibitors: DMH-2 LY-364947
BMPR2	Agonists: BMP (2, 4, 6, 7, 10) Dibotermin alfa Eptotermin alfa GDF (2 (BMP9), 5 (BMP14), 6 (BMP13), 7 (BMP12)) Radotermin Antagonists: Inhibin (A, B)
ACVR2A (ACVR2)	Agonists: Activin (A, B, AB) BMP (2, 4, 5, 6, 7, 8A, 8B, 15 (GDF9B)) Dibotermin alfa Eptotermin alfa GDF (1, 3, 5 (BMP14), 6 (BMP13), 7 (BMP12), 9, 11 (BMP11), 15) Myostatin (GDF8) Nodal Radotermin Antagonists: Inhibin (A, B) Lefty (1, 2) Decoy receptors: Sotatercept
ACVR2B	Agonists: Activin (A, B, AB) BMP (2, 4, 6, 7) Dibotermin alfa Eptotermin alfa GDF (1, 3, 5 (BMP14), 6 (BMP13), 7 (BMP12)) Myostatin (GDF8) Nodal Osteogenin (BMP3, BMP3A) Radotermin Antagonists: Inhibin (A, B) Lefty (1, 2) Decoy receptors: Ramatercept
AMHR2 (AMHR)	Agonists: AMH (MIS)

Type III

TGFβR3 (β-glycan)	Ligands: Avotermin Inhibin (A, B) TGFβ (1, 2, 3)

Unsorted

Endogenous antagonists/inhibitors: BAMBI
Cerberus (CER1)
Chordin
DAN (PARN)
Decorin
Follistatin
Gremlin (Drm)
LTBP1
Noggin
TGIF
Thrombospondin 1 (THBS1)
Tomoregulin 1

Antibodies: Stamulumab (against myostatin)
TRC105 (against endoglin)

Others: Endoglin

See also: Receptor/signaling modulators; Signaling peptide/protein receptor modulators; Growth factor receptor modulators; Cytokine receptor modulators

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