TGF beta 2

TGFB2
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1TFG, 2TGI, 4KXZ
Identifiers
Aliases	TGFB2, LDS4, TGF-beta2, transforming growth factor beta 2, G-TSF
External IDs	OMIM: 190220 MGI: 98726 HomoloGene: 2432 GeneCards: TGFB2
Gene location (Human)
Chr.	Chromosome 1 (human)[1]
End	218,444,619 bp[1]
Gene location (Mouse)
Chr.	Chromosome 1 (mouse)[2]
End	186,705,989 bp[2]
RNA expression pattern
	; ; ; ;
	More reference expression data
Gene ontology
Molecular function	• type II transforming growth factor beta receptor binding; • 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; • GO:0001948 protein binding; • protein heterodimerization activity;
Cellular component	• extracellular region; • extracellular matrix; • platelet alpha granule lumen; • extracellular; • axon; • neuronal cell body; • 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; • cellular proliferation; • transforming growth factor beta receptor signaling pathway; • negative regulation of cell 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–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 cycle arrest; • cell morphogenesis; • positive regulation of cell proliferation; • positive regulation of phosphatidylinositol 3-kinase signaling; • cell migration; • activation of protein kinase activity; • positive regulation of cell division; • response to drug; • 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; • haematopoiesis; • 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 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 from RNA polymerase II promoter; • embryo development ending in birth or egg hatching; • regulation of timing of catagen; • secondary palate development; • regulation of cell proliferation; • regulation of apoptotic process; • regulation of MAPK cascade;
	Sources:Amigo / QuickGO
Orthologs
	7042
	21808
	ENSG00000092969
	ENSMUSG00000039239
	P61812
	P27090
	NM_003238; NM_001135599
	NM_009367; NM_001329107
	NP_001129071; NP_003229
	NP_001316036; NP_033393
	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. 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. 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. 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) (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.

GRCh38: Ensembl release 89: ENSG00000092969 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000039239 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

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[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000092969 - Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000039239 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

TGF beta 2

Further reading