TGF beta 2

Transforming growth factor, beta 2
PDB rendering based on 1tfg.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 1TFG​, 2TGI​, 4KXZ​
Identifiers
Symbols	TGFB2 ; LDS4; 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 • cytokine activity • transforming growth factor beta receptor binding • protein binding • growth factor activity • type III transforming growth factor beta receptor binding • protein homodimerization activity • protein heterodimerization activity Cellular component • extracellular region • extracellular space • endosome • axon • extracellular matrix • platelet alpha granule lumen • neuronal cell body Biological process • cell morphogenesis • cartilage condensation • angiogenesis • eye development • response to hypoxia • epithelial to mesenchymal transition • hair follicle development • blood vessel remodeling • platelet degranulation • heart morphogenesis • heart valve morphogenesis • protein phosphorylation • cell cycle arrest • transforming growth factor beta receptor signaling pathway • SMAD protein import into nucleus • cell-cell signaling • axon guidance • 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 gene expression • positive regulation of epithelial cell migration • negative regulation of alkaline phosphatase activity • positive regulation of epithelial to mesenchymal transition • positive regulation of pathway-restricted SMAD protein phosphorylation • negative regulation of macrophage cytokine production • positive regulation of phosphatidylinositol 3-kinase signaling • cell growth • cell migration • signal transduction by protein phosphorylation • hemopoiesis • platelet activation • extracellular matrix organization • collagen fibril organization • positive regulation of cell growth • negative regulation of cell growth • neutrophil chemotaxis • hair follicle morphogenesis • activation of protein kinase activity • response to progesterone • 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 • response to drug • catagen • uterine wall breakdown • positive regulation of neuron apoptotic process • 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 • cell development • embryonic digestive tract development • neuron fate commitment • neuron development • generation of neurons • 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 • face morphogenesis • pathway-restricted SMAD protein phosphorylation • SMAD protein signal transduction • negative regulation of cartilage development • positive regulation of activation-induced cell death of T cells • extrinsic apoptotic signaling pathway • regulation of extracellular matrix organization • regulation of complement-dependent cytotoxicity • positive regulation of extrinsic apoptotic signaling pathway in absence of ligand 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_001135599	NM_009367
RefSeq (protein)	NP_001129071	NP_033393
Location (UCSC)	Chr 1: 218.35 – 218.44 Mb	Chr 1: 186.62 – 186.71 Mb
PubMed search

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.

Further reading

• Clark DA, Coker R (1998). "Transforming growth factor-beta (TGF-beta).". Int. J. Biochem. Cell Biol. 30 (3): 293–8. doi:10.1016/S1357-2725(97)00128-3. PMID 9611771.
• 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. 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.