| Transforming growth factor, beta 2
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| PDB rendering based on 1tfg.
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| Available structures: 1tfg, 2tgi
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| Identifiers
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| Symbol(s)
| TGFB2; MGC116892; TGF-beta2
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| External IDs
| OMIM: 190220 MGI: 98726 Homologene: 2432
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| Gene Ontology
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| Molecular Function:
| • beta-amyloid binding
• cytokine activity
• transforming growth factor beta receptor binding
• growth factor activity
• protein homodimerization activity
• protein heterodimerization activity
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| Cellular Component:
| • extracellular region
• axon
• cell soma
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| Biological Process:
| • cell morphogenesis
• angiogenesis
• eye development
• mesoderm formation
• cell-cell signaling
• heart development
• cell death
• cell proliferation
• positive regulation of cell proliferation
• negative regulation of cell proliferation
• embryonic development
• cardioblast differentiation
• cell growth
• hemopoiesis
• positive regulation of cell growth
• neutrophil chemotaxis
• hair follicle morphogenesis
• wound healing
• dopamine biosynthetic process
• catagen
• positive regulation of neuron apoptosis
• negative regulation of keratinocyte differentiation
• positive regulation of progression through cell cycle
• positive regulation of heart contraction
• somatic stem cell division
• neuron development
• generation of neurons
• negative regulation of immune response
• positive regulation of immune response
• positive regulation of catagen
• positive regulation of cardioblast differentiation
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| RNA expression pattern
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Additional recommended knowledge
More reference expression data
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| Orthologs
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| Human
| Mouse
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| Entrez
| 7042
| 21808
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| Ensembl
| ENSG00000092969
| ENSMUSG00000039239
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| Uniprot
| P61812
| Q3TWH5
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| Refseq
| NM_003238 (mRNA)
NP_003229 (protein)
| NM_009367 (mRNA)
NP_033393 (protein)
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| Location
| Chr 1: 216.59 - 216.68 Mb
| Chr 1: 188.32 - 188.41 Mb
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| Pubmed search
| [1]
| [2]
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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). This is an extracellular glycosilated 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. 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. PMID 11716069.
- Bissell DM (2002). "Chronic liver injury, TGF-beta, and cancer.". Exp. Mol. Med. 33 (4): 179-90. 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/JCI200320530. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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. 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:<153::AID-JCP16>3.0.CO;2-K 10.1002/(SICI)1097-4652(199910)181:1<153::AID-JCP16>3.0.CO;2-K. PMID 10457363.
| Cell signaling: TGF beta signaling pathway |
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| 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 A and B/Inhibin A and B, Anti-müllerian hormone, Nodal) |
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| TGF beta receptors | TGFBR1: Activin type 1 receptors (ACVR1, ACVR1B, ACVR1C) - ACVRL1 - BMPR1 (BMPR1A - BMPR1B)
TGFBR2: Activin type 2 receptors (ACVR2A, ACVR2B) - AMHR2 - BMPR2
TGFBR3: betaglycan |
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| Transducers/SMAD | R-SMAD (SMAD1, SMAD2, SMAD3, SMAD5, SMAD9) - I-SMAD (SMAD6, SMAD7) - SMAD4 |
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| Ligand Inhibitors | Cerberus - Chordin - DAN - Decorin - Follistatin - Gremlin - Lefty - LTBP1 - Noggin - THBS1 |
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| Coreceptors | BAMBI - Cripto |
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| Other | SARA |
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