TGF beta 2

Transforming growth factor, beta 2

PDB rendering based on 1tfg.

Available structures
PDB	1TFG, 2TGI

Identifiers

Symbols

TGFB2; MGC116892; TGF-beta2

External IDs

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

Gene Ontology
Molecular function	• beta-amyloid binding • receptor signaling protein serine/threonine kinase activity • receptor binding • type II transforming growth factor beta receptor binding • type II transforming growth factor beta receptor binding • cytokine activity • transforming growth factor beta receptor binding • protein binding • protein binding • growth factor activity • protein homodimerization activity • protein heterodimerization activity
Cellular component	• extracellular region • extracellular region • extracellular space • axon • extracellular matrix • platelet alpha granule lumen • neuronal cell body
Biological process	• cell morphogenesis • angiogenesis • eye development • response to hypoxia • epithelial to mesenchymal transition • epithelial to mesenchymal transition • hair follicle development • hair follicle development • platelet degranulation • heart morphogenesis • protein phosphorylation • cell cycle arrest • transforming growth factor beta receptor signaling pathway • SMAD protein import into nucleus • cell-cell signaling • salivary gland morphogenesis • heart development • blood coagulation • cell death • cell proliferation • positive regulation of cell proliferation • negative regulation of cell proliferation • glial cell migration • response to wounding • embryo development • cardioblast differentiation • positive regulation of epithelial cell migration • negative regulation of alkaline phosphatase activity • positive regulation of epithelial to mesenchymal transition • negative regulation of macrophage cytokine production • positive regulation of phosphatidylinositol 3-kinase cascade • cell migration • menstrual cycle phase • hemopoiesis • platelet activation • collagen fibril organization • positive regulation of cell growth • negative regulation of cell growth • neutrophil chemotaxis • neutrophil chemotaxis • hair follicle morphogenesis • activation of protein kinase activity • response to progesterone stimulus • positive regulation of stress-activated MAPK cascade • regulation of transforming growth factor-beta2 production • positive regulation of cell adhesion mediated by integrin • wound healing • dopamine biosynthetic process • odontogenesis • catagen • positive regulation of apoptosis • positive regulation of neuron apoptosis • cell-cell junction organization • positive regulation of integrin biosynthetic process • positive regulation of ossification • positive regulation of cell cycle • positive regulation of heart contraction • somatic stem cell division • embryonic digestive tract development • neuron development • generation of neurons • negative regulation of epithelial cell proliferation • negative regulation of epithelial cell proliferation • positive regulation of protein secretion • negative regulation of immune response • positive regulation of immune response • positive regulation of cell division • positive regulation of catagen • positive regulation of cardioblast differentiation • cardiac muscle cell proliferation • cardiac epithelial to mesenchymal transition • pathway-restricted SMAD protein phosphorylation
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 1:
218.52 – 218.62 Mb

Chr 1:
188.45 – 188.53 Mb

PubMed search

[1]

[2]

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.". Exp. Mol. Med. 33 (4): 179–90. PMID 11795478.
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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. 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=553836.
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. PMC 1137259. PMID 8093006. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1137259.
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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: TGF beta 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	R-SMAD (SMAD1, SMAD2, SMAD3, SMAD5, SMAD9) · I-SMAD (SMAD6, SMAD7) · SMAD4

Ligand inhibitors	Cerberus · Chordin · DAN · Decorin · Follistatin · Gremlin · Lefty · LTBP1 · Noggin · THBS1

Coreceptors	BAMBI · Cripto

Other	SARA

B trdu: iter (nrpl/grfl/cytl/horl), csrc (lgic, enzr, gprc, igsr, intg, nrpr/grfr/cytr), itra (adap, gbpr, mapk), calc, lipd; path (hedp, wntp, tgfp+mapp, notp, jakp, fsap, hipp, tlrp)

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	TGF-α · EGF · HB-EGF

TGFβ pathway	TGF-β (TGF-β1, TGF-β2, TGF-β3)

Insulin-like	IGF-1 · IGF-2

Platelet-derived	PDGFA · PDGFB · PDGFC · PDGFD

Vascular endothelial	VEGF-A · VEGF-B · VEGF-C · VEGF-D · PGF

Other	Nerve · Hepatocyte

B trdu: iter (nrpl/grfl/cytl/horl), csrc (lgic, enzr, gprc, igsr, intg, nrpr/grfr/cytr), itra (adap, gbpr, mapk), calc, lipd; path (hedp, wntp, tgfp+mapp, notp, jakp, fsap, hipp, tlrp)

TGF beta 2

Further reading