TGF beta 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 (i.e., TGFB2).

TGFB2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1TFG, 2TGI, 4KXZ
Identifiers
Aliases	TGFB2, TGF-beta2, transforming growth factor beta 2, G-TSF
External IDs	OMIM: 190220; MGI: 98726; HomoloGene: 2432; GeneCards: TGFB2; OMA:TGFB2 - orthologs
Gene location (Human) Chr. Chromosome 1 (human) Band 1q41 Start 218,345,336 bp End 218,444,619 bp
Gene location (Mouse) Chr. Chromosome 1 (mouse) Band 1 H5|1 89.95 cM Start 186,354,989 bp End 186,438,186 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Achilles tendon cartilage tissue germinal epithelium tendon of biceps brachii sperm minor salivary glands ventricular zone tibia islet of Langerhans smooth muscle tissue Top expressed in epithelium of lens decidua ciliary body iris external carotid artery secondary oocyte internal carotid artery Epithelium of choroid plexus semi-lunar valve submandibular gland More reference expression data BioGPS More reference expression data
Gene ontology Molecular function type II transforming growth factor beta receptor binding signaling receptor binding type III transforming growth factor beta receptor binding cytokine activity transforming growth factor beta receptor binding growth factor activity protein homodimerization activity amyloid-beta binding protein binding protein heterodimerization activity Cellular component extracellular region extracellular matrix platelet alpha granule lumen extracellular space axon soma collagen-containing extracellular matrix Biological process eye development regulation of transforming growth factor beta2 production response to progesterone cell death cardioblast differentiation positive regulation of integrin biosynthetic process protein phosphorylation positive regulation of heart contraction positive regulation of neuron apoptotic process angiogenesis negative regulation of epithelial cell proliferation uterine wall breakdown negative regulation of alkaline phosphatase activity negative regulation of macrophage cytokine production positive regulation of cell adhesion mediated by integrin cell population proliferation transforming growth factor beta receptor signaling pathway negative regulation of cell population proliferation positive regulation of stress-activated MAPK cascade cell-cell junction organization extrinsic apoptotic signaling pathway collagen fibril organization positive regulation of epithelial cell migration neutrophil chemotaxis positive regulation of cell growth response to wounding negative regulation of cell growth positive regulation of cardioblast differentiation glial cell migration wound healing positive regulation of ossification cardiac muscle cell proliferation positive regulation of epithelial to mesenchymal transition odontogenesis positive regulation of timing of catagen positive regulation of immune response regulation of complement-dependent cytotoxicity positive regulation of protein secretion epithelial to mesenchymal transition embryonic digestive tract development response to hypoxia cell-cell signaling positive regulation of pathway-restricted SMAD protein phosphorylation heart morphogenesis platelet degranulation salivary gland morphogenesis generation of neurons negative regulation of immune response cell morphogenesis positive regulation of cell population proliferation positive regulation of phosphatidylinositol 3-kinase signaling cell migration activation of protein kinase activity positive regulation of cell division cardiac epithelial to mesenchymal transition BMP signaling pathway cell development skeletal system development kidney development neural tube closure hair follicle development outflow tract septum morphogenesis membranous septum morphogenesis heart valve morphogenesis atrioventricular valve morphogenesis pulmonary valve morphogenesis endocardial cushion morphogenesis cardiac right ventricle morphogenesis ventricular trabecula myocardium morphogenesis endocardial cushion fusion atrial septum primum morphogenesis neural retina development heart development male gonad development hemopoiesis embryonic limb morphogenesis hair follicle morphogenesis ascending aorta morphogenesis dopamine biosynthetic process positive regulation of cell cycle negative regulation of Ras protein signal transduction somatic stem cell division neuron development inner ear development uterus development pathway-restricted SMAD protein phosphorylation ventricular septum morphogenesis atrial septum morphogenesis pharyngeal arch artery morphogenesis regulation of apoptotic process involved in outflow tract morphogenesis substantia propria of cornea development cranial skeletal system development negative regulation of epithelial to mesenchymal transition involved in endocardial cushion formation positive regulation of epithelial to mesenchymal transition involved in endocardial cushion formation regulation of signaling receptor activity negative regulation of gene expression negative regulation of angiogenesis positive regulation of Notch signaling pathway SMAD protein signal transduction positive regulation of pri-miRNA transcription by RNA polymerase II embryo development ending in birth or egg hatching regulation of timing of catagen secondary palate development regulation of cell population proliferation regulation of apoptotic process regulation of MAPK cascade Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 7042 21808 Ensembl ENSG00000092969 ENSMUSG00000039239 UniProt P61812 P27090 RefSeq (mRNA) NM_003238 NM_001135599 NM_009367 NM_001329107 RefSeq (protein) NP_001129071 NP_003229 NP_001316036 NP_033393 Location (UCSC) Chr 1: 218.35 – 218.44 Mb Chr 1: 186.35 – 186.44 Mb PubMed search
Wikidata
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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. S2CID 21461718.
• 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. Bibcode:1992Sci...257..369D. 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. Bibcode:1992Natur.358..430S. doi:10.1038/358430a0. PMID 1641027. S2CID 4239431.
• 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. doi:10.1002/j.1460-2075.1987.tb02700.x. 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. doi:10.1016/S0021-9258(18)45325-2. 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) (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. S2CID 85850306.
• 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. S2CID 21284888.