TGF beta 2

TGFB2

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
1TFG, 2TGI, 4KXZ

Identifiers

Aliases

TGFB2, LDS4, TGF-beta2, transforming growth factor beta 2

External IDs

OMIM: 190220 MGI: 98726 HomoloGene: 2432 GeneCards: TGFB2

Genetically Related Diseases

chronic obstructive pulmonary disease^[1]

Gene ontology
Molecular function	• type II transforming growth factor beta receptor binding • receptor binding • type III transforming growth factor beta receptor binding • cytokine activity • signal transducer, downstream of receptor, with serine/threonine kinase activity • transforming growth factor beta receptor binding • growth factor activity • protein homodimerization activity • beta-amyloid binding • protein binding • protein heterodimerization activity
Cellular component	• endosome • extracellular region • extracellular fluid • extracellular matrix • axon • neuronal cell body • platelet alpha granule lumen
Biological process	• eye development • hemopoiesis • regulation of transforming growth factor beta2 production • embryo development • response to progesterone • cell death • cardioblast differentiation • positive regulation of integrin biosynthetic process • protein phosphorylation • positive regulation of heart contraction • positive regulation of extrinsic apoptotic signaling pathway in absence of ligand • blood vessel remodeling • positive regulation of neuron apoptotic process • blood vessel development • angiogenesis • negative regulation of epithelial cell proliferation • uterine wall breakdown • negative regulation of alkaline phosphatase activity • hair follicle morphogenesis • negative regulation of macrophage cytokine production • positive regulation of cell adhesion mediated by integrin • positive regulation of activation-induced cell death of T cells • cell proliferation • transforming growth factor beta receptor signaling pathway • face morphogenesis • negative regulation of cell proliferation • positive regulation of stress-activated MAPK cascade • regulation of apoptotic process • pathway-restricted SMAD protein phosphorylation • cell-cell junction organization • SMAD protein signal transduction • extrinsic apoptotic signaling pathway • SMAD protein import into nucleus • collagen fibril organization • positive regulation of epithelial cell migration • neuron development • negative regulation of gene expression • neutrophil chemotaxis • growth • cell growth • heart development • positive regulation of cell growth • positive regulation of cell cycle • response to wounding • negative regulation of cell growth • positive regulation of cardioblast differentiation • glial cell migration • hair follicle development • regulation of actin cytoskeleton organization • negative regulation of cartilage development • dopamine biosynthetic process • wound healing • positive regulation of ossification • cardiac muscle cell proliferation • positive regulation of epithelial to mesenchymal transition • odontogenesis • positive regulation of catagen • positive regulation of immune response • regulation of complement-dependent cytotoxicity • positive regulation of protein secretion • epithelial to mesenchymal transition • catagen • embryonic digestive tract development • cartilage condensation • positive regulation of protein localization to nucleus • response to hypoxia • cell-cell signaling • positive regulation of pathway-restricted SMAD protein phosphorylation • somatic stem cell division • heart morphogenesis • platelet degranulation • positive regulation of GTP binding • salivary gland morphogenesis • generation of neurons • axon guidance • positive regulation of extracellular matrix disassembly • positive regulation of gene expression • negative regulation of immune response • cell cycle arrest • cell morphogenesis • positive regulation of cell proliferation • regulation of extracellular matrix organization • positive regulation of phosphatidylinositol 3-kinase signaling • neuron fate commitment • cell migration • activation of protein kinase activity • positive regulation of cell division • response to drug • cardiac epithelial to mesenchymal transition • outflow tract septum morphogenesis • signal transduction by protein phosphorylation • palate development • embryonic limb morphogenesis • positive regulation of epithelial to mesenchymal transition involved in endocardial cushion formation • neural tube closure • atrial septum primum morphogenesis • ventricular septum morphogenesis • atrioventricular valve morphogenesis • kidney development • pulmonary valve morphogenesis • inner ear development • uterus development • neural retina development • negative regulation of epithelial to mesenchymal transition involved in endocardial cushion formation • endocardial cushion morphogenesis • endocardial cushion fusion • extracellular matrix organization • pharyngeal arch artery morphogenesis • cranial skeletal system development • atrial septum morphogenesis • negative regulation of Ras protein signal transduction • ascending aorta morphogenesis • cardiac right ventricle morphogenesis • heart valve morphogenesis • membranous septum morphogenesis • substantia propria of cornea development • ventricular trabecula myocardium morphogenesis • male gonad development • regulation of apoptotic process involved in outflow tract morphogenesis • skeletal system development
Sources:Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

Entrez


7042


21808

Ensembl


ENSG00000092969


ENSMUSG00000039239

UniProt


P61812


P27090

RefSeq (mRNA)


NM_003238 NM_001135599


NM_009367

RefSeq (protein)


NP_001129071.1 NP_003229.1


NP_033393.2

Location (UCSC)

Chr 1: 218.35 – 218.44 Mb

Chr 1: 186.62 – 186.71 Mb

PubMed search

^[2]

^[3]

Wikidata

View/Edit Human

View/Edit Mouse

Transforming growth factor-beta 2 (TGF-β2) is a secreted protein known as a cytokine that performs many cellular functions and has a vital role during embryonic development (alternative names: Glioblastoma-derived T-cell suppressor factor, G-TSF, BSC-1 cell growth inhibitor, Polyergin, Cetermin). It is an extracellular glycosylated protein. It is known to suppress the effects of interleukin dependent T-cell tumors. There are two named isoforms of this protein, created by alternative splicing of the same gene.

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Wick W, Platten M, Weller M (2002). "Glioma cell invasion: regulation of metalloproteinase activity by TGF-beta.". J. Neurooncol. 53 (2): 177–85. doi:10.1023/A:1012209518843. PMID 11716069.
Bissell DM (2002). "Chronic liver injury, TGF-beta, and cancer.". Experimental & Molecular Medicine. 33 (4): 179–90. doi:10.1038/emm.2001.31. PMID 11795478.
Kalluri R, Neilson EG (2004). "Epithelial-mesenchymal transition and its implications for fibrosis.". J. Clin. Invest. 112 (12): 1776–84. doi:10.1172/JCI20530. PMC 297008. PMID 14679171.
Daopin S, Piez KA, Ogawa Y, Davies DR (1992). "Crystal structure of transforming growth factor-beta 2: an unusual fold for the superfamily.". Science. 257 (5068): 369–73. doi:10.1126/science.1631557. PMID 1631557.
Schlunegger MP, Grütter MG (1992). "An unusual feature revealed by the crystal structure at 2.2 A resolution of human transforming growth factor-beta 2.". Nature. 358 (6385): 430–4. doi:10.1038/358430a0. PMID 1641027.
Noma T, Glick AB, Geiser AG, et al. (1992). "Molecular cloning and structure of the human transforming growth factor-beta 2 gene promoter.". Growth Factors. 4 (4): 247–55. doi:10.3109/08977199109043910. PMID 1764261.
Bodmer S, Podlisny MB, Selkoe DJ, et al. (1990). "Transforming growth factor-beta bound to soluble derivatives of the beta amyloid precursor protein of Alzheimer's disease.". Biochem. Biophys. Res. Commun. 171 (2): 890–7. doi:10.1016/0006-291X(90)91229-L. PMID 2119582.
Webb NR, Madisen L, Rose TM, Purchio AF (1989). "Structural and sequence analysis of TGF-beta 2 cDNA clones predicts two different precursor proteins produced by alternative mRNA splicing.". DNA. 7 (7): 493–7. doi:10.1089/dna.1.1988.7.493. PMID 2850146.
Madisen L, Webb NR, Rose TM, et al. (1988). "Transforming growth factor-beta 2: cDNA cloning and sequence analysis.". DNA. 7 (1): 1–8. doi:10.1089/dna.1988.7.1. PMID 3162414.
Barton DE, Foellmer BE, Du J, et al. (1989). "Chromosomal mapping of genes for transforming growth factors beta 2 and beta 3 in man and mouse: dispersion of TGF-beta gene family.". Oncogene Res. 3 (4): 323–31. PMID 3226728.
de Martin R, Haendler B, Hofer-Warbinek R, et al. (1988). "Complementary DNA for human glioblastoma-derived T cell suppressor factor, a novel member of the transforming growth factor-beta gene family.". EMBO J. 6 (12): 3673–7. PMC 553836. PMID 3322813.
Marquardt H, Lioubin MN, Ikeda T (1987). "Complete amino acid sequence of human transforming growth factor type beta 2.". J. Biol. Chem. 262 (25): 12127–31. PMID 3476488.
Philip A, Bostedt L, Stigbrand T, O'Connor-McCourt MD (1994). "Binding of transforming growth factor-beta (TGF-beta) to pregnancy zone protein (PZP). Comparison to the TGF-beta-alpha 2-macroglobulin interaction.". Eur. J. Biochem. 221 (2): 687–93. doi:10.1111/j.1432-1033.1994.tb18781.x. PMID 7513640.
Lin HY, Moustakas A, Knaus P, et al. (1995). "The soluble exoplasmic domain of the type II transforming growth factor (TGF)-beta receptor. A heterogeneously glycosylated protein with high affinity and selectivity for TGF-beta ligands.". J. Biol. Chem. 270 (6): 2747–54. doi:10.1074/jbc.270.6.2747. PMID 7852346.
Hildebrand A, Romarís M, Rasmussen LM, et al. (1994). "Interaction of the small interstitial proteoglycans biglycan, decorin and fibromodulin with transforming growth factor beta.". Biochem. J. 302. ( Pt 2): 527–34. doi:10.1042/bj3020527. PMC 1137259. PMID 8093006.
López-Casillas F, Payne HM, Andres JL, Massagué J (1994). "Betaglycan can act as a dual modulator of TGF-beta access to signaling receptors: mapping of ligand binding and GAG attachment sites.". J. Cell Biol. 124 (4): 557–68. doi:10.1083/jcb.124.4.557. PMC 2119924. PMID 8106553.
Fromigué O, Marie PJ, Lomri A (1998). "Bone morphogenetic protein-2 and transforming growth factor-beta2 interact to modulate human bone marrow stromal cell proliferation and differentiation.". J. Cell. Biochem. 68 (4): 411–26. doi:10.1002/(SICI)1097-4644(19980315)68:4<411::AID-JCB2>3.0.CO;2-T. PMID 9493905.
Mori T, Kawara S, Shinozaki M, et al. (1999). "Role and interaction of connective tissue growth factor with transforming growth factor-beta in persistent fibrosis: A mouse fibrosis model.". J. Cell. Physiol. 181 (1): 153–9. doi:10.1002/(SICI)1097-4652(199910)181:1<153::AID-JCP16>3.0.CO;2-K. PMID 10457363.

PDB gallery

1tfg: AN UNUSUAL FEATURE REVEALED BY THE CRYSTAL STRUCTURE AT 2.2 ANGSTROMS RESOLUTION OF HUMAN TRANSFORMING GROWTH FACTOR-BETA2

2tgi: CRYSTAL STRUCTURE OF TRANSFORMING GROWTH FACTOR-BETA2: AN UNUSUAL FOLD FOR THE SUPERFAMILY

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: Growth factor receptor modulators
Cytokine receptor modulators
Peptide receptor modulators

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TGF beta 2

Further reading