TGF beta 2

Protein-coding gene in the species Homo sapiens
TGFB2
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1TFG, 2TGI, 4KXZ

Identifiers
AliasesTGFB2, TGF-beta2, transforming growth factor beta 2, G-TSF
External IDsOMIM: 190220 MGI: 98726 HomoloGene: 2432 GeneCards: TGFB2
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for TGFB2
Genomic location for TGFB2
Band1q41Start218,345,336 bp[1]
End218,444,619 bp[1]
Gene location (Mouse)
Chromosome 1 (mouse)
Chr.Chromosome 1 (mouse)[2]
Chromosome 1 (mouse)
Genomic location for TGFB2
Genomic location for TGFB2
Band1 H5|1 89.95 cMStart186,354,989 bp[2]
End186,438,186 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • Achilles tendon

  • germinal epithelium

  • sperm

  • minor salivary glands

  • tibia

  • islet of Langerhans

  • smooth muscle tissue

  • right coronary artery

  • canal of the cervix

  • hair follicle
Top expressed in
  • ciliary body

  • iris

  • external carotid artery

  • secondary oocyte

  • internal carotid artery

  • semi-lunar valve

  • submandibular gland

  • atrioventricular canal

  • pineal gland

  • ascending aorta
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
  • 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
  • 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
SpeciesHumanMouse
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 MbChr 1: 186.35 – 186.44 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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 (i.e., TGFB2).

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.
  • v
  • t
  • e
  • 1tfg: AN UNUSUAL FEATURE REVEALED BY THE CRYSTAL STRUCTURE AT 2.2 ANGSTROMS RESOLUTION OF HUMAN TRANSFORMING GROWTH FACTOR-BETA2
    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
    2tgi: CRYSTAL STRUCTURE OF TRANSFORMING GROWTH FACTOR-BETA2: AN UNUSUAL FOLD FOR THE SUPERFAMILY
  • v
  • t
  • e
TGF beta superfamily of ligands
Ligand of ACVR or TGFBR
Ligand of BMPR
TGF beta receptors
(Activin, BMP, family)
TGFBR1:
TGFBR2:
TGFBR3:
Transducers/SMAD
Ligand inhibitors
Coreceptors
Other
  • v
  • t
  • e
TGFβ receptor superfamily modulators
Type I
ALK1 (ACVRL1)
  • Kinase inhibitors: K-02288
  • ML-347 (LDN-193719, VU0469381)
  • Other inhibitors: Disitertide
ALK2 (ACVR1A)
  • Kinase inhibitors: DMH-1
  • DMH-2
  • Dorsomorphin (BML-275)
  • K-02288
  • ML-347 (LDN-193719, VU0469381)
ALK3 (BMPR1A)
  • Kinase inhibitors: DMH-2
  • Dorsomorphin (BML-275)
  • K-02288
ALK4 (ACVR1B)
  • Kinase inhibitors: A 83-01
  • SB-431542
  • SB-505124
ALK5 (TGFβR1)
ALK6 (BMPR1B)
  • Kinase inhibitors: DMH-2
  • Dorsomorphin (BML-275)
  • K-02288
ALK7 (ACVR1C)
  • Antagonists: Lefty (1, 2)
  • Kinase inhibitors: A 83-01
  • SB-431542
  • SB-505124
Type II
TGFβR2
  • Kinase inhibitors: DMH-2
  • LY-364947
BMPR2
ACVR2A (ACVR2)
ACVR2B
  • Decoy receptors: Ramatercept
AMHR2 (AMHR)
Type III
TGFβR3 (β-glycan)
Unsorted
  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000092969 – Ensembl, May 2017
  2. ^ a b c 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.