TGFB1 | ENSG00000105329 | NCBI 7040

Details for: TGFB1

Gene ID: 7040

Symbol: TGFB1

Ensembl ID: ENSG00000105329

Description: transforming growth factor beta 1

Associated with

Adipogenesis
(R-HSA-9843745)
Cell surface interactions at the vascular wall
(R-HSA-202733)
Cytokine signaling in immune system
(R-HSA-1280215)
Deubiquitination
(R-HSA-5688426)
Developmental biology
(R-HSA-1266738)
Disease
(R-HSA-1643685)
Diseases of signal transduction by growth factor receptors and second messengers
(R-HSA-5663202)
Downregulation of tgf-beta receptor signaling
(R-HSA-2173788)
Ecm proteoglycans
(R-HSA-3000178)
Elastic fibre formation
(R-HSA-1566948)
Extracellular matrix organization
(R-HSA-1474244)
Gene expression (transcription)
(R-HSA-74160)
Generic transcription pathway
(R-HSA-212436)
Hemostasis
(R-HSA-109582)
Immune system
(R-HSA-168256)
Infectious disease
(R-HSA-5663205)
Influenza infection
(R-HSA-168255)
Influenza virus induced apoptosis
(R-HSA-168277)
Interleukin-4 and interleukin-13 signaling
(R-HSA-6785807)
Loss of function of smad2/3 in cancer
(R-HSA-3304349)
Loss of function of tgfbr1 in cancer
(R-HSA-3656534)
Loss of function of tgfbr2 in cancer
(R-HSA-3642278)
Metabolism of proteins
(R-HSA-392499)
Molecules associated with elastic fibres
(R-HSA-2129379)
Non-integrin membrane-ecm interactions
(R-HSA-3000171)
Platelet activation, signaling and aggregation
(R-HSA-76002)
Platelet degranulation
(R-HSA-114608)
Post-translational protein modification
(R-HSA-597592)
Regulation of runx3 expression and activity
(R-HSA-8941858)
Response to elevated platelet cytosolic ca2+
(R-HSA-76005)
Rna polymerase ii transcription
(R-HSA-73857)
Runx3 regulates cdkn1a transcription
(R-HSA-8941855)
Runx3 regulates p14-arf
(R-HSA-8951936)
Signaling by interleukins
(R-HSA-449147)
Signaling by tgf-beta receptor complex
(R-HSA-170834)
Signaling by tgf-beta receptor complex in cancer
(R-HSA-3304351)
Signaling by tgfb family members
(R-HSA-9006936)
Signaling by tgfbr3
(R-HSA-9839373)
Signal transduction
(R-HSA-162582)
Smad2/3 phosphorylation motif mutants in cancer
(R-HSA-3304356)
Syndecan interactions
(R-HSA-3000170)
Tgf-beta receptor signaling activates smads
(R-HSA-2173789)
Tgf-beta receptor signaling in emt (epithelial to mesenchymal transition)
(R-HSA-2173791)
Tgfbr1 kd mutants in cancer
(R-HSA-3656532)
Tgfbr1 lbd mutants in cancer
(R-HSA-3656535)
Tgfbr2 kinase domain mutants in cancer
(R-HSA-3645790)
Tgfbr2 msi frameshift mutants in cancer
(R-HSA-3642279)
Tgfbr3 regulates tgf-beta signaling
(R-HSA-9839389)
Transcriptional regulation by runx3
(R-HSA-8878159)
Transcriptional regulation of white adipocyte differentiation
(R-HSA-381340)
Uch proteinases
(R-HSA-5689603)
Viral infection pathways
(R-HSA-9824446)
Adaptive immune response based on somatic recombination of immune receptors built from immunoglobulin superfamily domains
(GO:0002460)
Aortic valve morphogenesis
(GO:0003180)
Apoptotic process
(GO:0006915)
Atp biosynthetic process
(GO:0006754)
Cell morphogenesis
(GO:0000902)
Chondrocyte differentiation
(GO:0002062)
Columnar/cuboidal epithelial cell maturation
(GO:0002069)
Connective tissue replacement involved in inflammatory response wound healing
(GO:0002248)
Cytokine activity
(GO:0005125)
Deubiquitinase activator activity
(GO:0035800)
Enzyme binding
(GO:0019899)
Epithelial to mesenchymal transition
(GO:0001837)
Growth factor activity
(GO:0008083)
Heart valve morphogenesis
(GO:0003179)
Hematopoietic progenitor cell differentiation
(GO:0002244)
Identical protein binding
(GO:0042802)
Intracellular calcium ion homeostasis
(GO:0006874)
Negative regulation of natural killer cell mediated cytotoxicity directed against tumor cell target
(GO:0002859)
Negative regulation of protein phosphorylation
(GO:0001933)
Negative regulation of transcription by rna polymerase ii
(GO:0000122)
Neural tube closure
(GO:0001843)
Phosphate-containing compound metabolic process
(GO:0006796)
Protein-containing complex binding
(GO:0044877)
Protein binding
(GO:0005515)
Protein export from nucleus
(GO:0006611)
Protein phosphorylation
(GO:0006468)
Protein serine/threonine kinase activator activity
(GO:0043539)
Regulation of sodium ion transport
(GO:0002028)
Sprouting angiogenesis
(GO:0002040)
Tolerance induction to self antigen
(GO:0002513)
Transforming growth factor beta receptor signaling pathway
(GO:0007179)
Type iii transforming growth factor beta receptor binding
(GO:0034714)
Type ii transforming growth factor beta receptor binding
(GO:0005114)
Type i transforming growth factor beta receptor binding
(GO:0034713)
Ureteric bud development
(GO:0001657)
Vasculogenesis
(GO:0001570)

Cells (max top 100)

(Cell Significance Index and respective Thresholds are uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

Cell Name: polychromatophilic erythroblast (CL0000550)
Fold Change: 224.0506
Cell Significance Index: -34.8500
Cell Name: hematopoietic oligopotent progenitor cell (CL0002032)
Fold Change: 120.9178
Cell Significance Index: -30.6700
Cell Name: mucosal type mast cell (CL0000485)
Fold Change: 87.6046
Cell Significance Index: -35.5900
Cell Name: smooth muscle fiber of ileum (CL1000278)
Fold Change: 80.6358
Cell Significance Index: -38.0700
Cell Name: peripheral blood mononuclear cell (CL2000001)
Fold Change: 76.6935
Cell Significance Index: -39.4500
Cell Name: ileal goblet cell (CL1000326)
Fold Change: 56.8983
Cell Significance Index: -38.1800
Cell Name: ciliated cell of the bronchus (CL0002332)
Fold Change: 39.2776
Cell Significance Index: -37.5000
Cell Name: orthochromatic erythroblast (CL0000552)
Fold Change: 28.4195
Cell Significance Index: -35.0400
Cell Name: epidermal Langerhans cell (CL0002457)
Fold Change: 11.4457
Cell Significance Index: -25.0500
Cell Name: CD8-positive, alpha-beta regulatory T cell (CL0000795)
Fold Change: 10.0734
Cell Significance Index: -30.9400
Cell Name: CD8-alpha-beta-positive, alpha-beta intraepithelial T cell (CL0000796)
Fold Change: 9.7579
Cell Significance Index: -26.1400
Cell Name: stromal cell of bone marrow (CL0010001)
Fold Change: 9.0318
Cell Significance Index: -35.6400
Cell Name: epithelial cell of pancreas (CL0000083)
Fold Change: 6.5797
Cell Significance Index: 108.4300
Cell Name: hepatic pit cell (CL2000054)
Fold Change: 6.3049
Cell Significance Index: 16.8900
Cell Name: CD14-positive, CD16-negative classical monocyte (CL0002057)
Fold Change: 4.0654
Cell Significance Index: 75.1400
Cell Name: extravillous trophoblast (CL0008036)
Fold Change: 2.1156
Cell Significance Index: 13.1500
Cell Name: CD4-positive, alpha-beta memory T cell, CD45RO-positive (CL0001204)
Fold Change: 1.9490
Cell Significance Index: 57.2400
Cell Name: lung endothelial cell (CL1001567)
Fold Change: 1.6796
Cell Significance Index: 87.4900
Cell Name: early pro-B cell (CL0002046)
Fold Change: 1.5418
Cell Significance Index: 99.4700
Cell Name: odontoblast (CL0000060)
Fold Change: 1.1765
Cell Significance Index: 150.8200
Cell Name: neoplastic cell (CL0001063)
Fold Change: 0.9737
Cell Significance Index: 193.2300
Cell Name: enteroendocrine cell of colon (CL0009042)
Fold Change: 0.8602
Cell Significance Index: 163.7100
Cell Name: colon goblet cell (CL0009039)
Fold Change: 0.5632
Cell Significance Index: 55.7200
Cell Name: tuft cell of colon (CL0009041)
Fold Change: 0.5473
Cell Significance Index: 494.1700
Cell Name: basal cell of urothelium (CL1000486)
Fold Change: 0.3994
Cell Significance Index: 49.1200
Cell Name: stromal cell of ovary (CL0002132)
Fold Change: 0.3831
Cell Significance Index: 52.6100
Cell Name: intermediate cell of urothelium (CL4030055)
Fold Change: 0.3226
Cell Significance Index: 58.1600
Cell Name: tonsil germinal center B cell (CL2000006)
Fold Change: 0.3175
Cell Significance Index: 37.4400
Cell Name: secondary lens fiber (CL0002225)
Fold Change: 0.3175
Cell Significance Index: 431.6600
Cell Name: neutrophil progenitor cell (CL0000834)
Fold Change: 0.2980
Cell Significance Index: 7.9700
Cell Name: cell in vitro (CL0001034)
Fold Change: 0.2559
Cell Significance Index: 139.7600
Cell Name: epithelial cell of small intestine (CL0002254)
Fold Change: 0.2389
Cell Significance Index: 38.8500
Cell Name: lens epithelial cell (CL0002224)
Fold Change: 0.2377
Cell Significance Index: 365.9100
Cell Name: bladder urothelial cell (CL1001428)
Fold Change: 0.1956
Cell Significance Index: 10.1600
Cell Name: hair follicular keratinocyte (CL2000092)
Fold Change: 0.1347
Cell Significance Index: 59.5700
Cell Name: GABAergic interneuron (CL0011005)
Fold Change: 0.1203
Cell Significance Index: 83.2100
Cell Name: endothelial cell of placenta (CL0009092)
Fold Change: 0.1051
Cell Significance Index: 0.6400
Cell Name: anterior lens cell (CL0002223)
Fold Change: 0.0756
Cell Significance Index: 139.4900
Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
Fold Change: 0.0608
Cell Significance Index: 12.2000
Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
Fold Change: 0.0400
Cell Significance Index: 14.3500
Cell Name: pigmented epithelial cell (CL0000529)
Fold Change: 0.0394
Cell Significance Index: 74.1200
Cell Name: intestinal crypt stem cell of colon (CL0009043)
Fold Change: 0.0310
Cell Significance Index: 3.3700
Cell Name: enteroendocrine cell of small intestine (CL0009006)
Fold Change: 0.0080
Cell Significance Index: 0.2000
Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
Fold Change: -0.0232
Cell Significance Index: -14.7400
Cell Name: small intestine goblet cell (CL1000495)
Fold Change: -0.0313
Cell Significance Index: -1.1000
Cell Name: pulmonary alveolar epithelial cell (CL0000322)
Fold Change: -0.0374
Cell Significance Index: -28.3100
Cell Name: pancreatic A cell (CL0000171)
Fold Change: -0.0476
Cell Significance Index: -35.2900
Cell Name: ciliary muscle cell (CL1000443)
Fold Change: -0.0504
Cell Significance Index: -22.8600
Cell Name: placental villous trophoblast (CL2000060)
Fold Change: -0.0524
Cell Significance Index: -1.4000
Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
Fold Change: -0.0530
Cell Significance Index: -38.8400
Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
Fold Change: -0.0534
Cell Significance Index: -3.9800
Cell Name: enterocyte of epithelium of small intestine (CL1000334)
Fold Change: -0.0548
Cell Significance Index: -1.5800
Cell Name: pigmented ciliary epithelial cell (CL0002303)
Fold Change: -0.0609
Cell Significance Index: -8.8500
Cell Name: pancreatic PP cell (CL0002275)
Fold Change: -0.0633
Cell Significance Index: -39.5200
Cell Name: type B pancreatic cell (CL0000169)
Fold Change: -0.0636
Cell Significance Index: -35.9000
Cell Name: basal cell of prostate epithelium (CL0002341)
Fold Change: -0.0691
Cell Significance Index: -1.8800
Cell Name: abnormal cell (CL0001061)
Fold Change: -0.0754
Cell Significance Index: -7.7000
Cell Name: cardiac muscle myoblast (CL0000513)
Fold Change: -0.0947
Cell Significance Index: -7.2700
Cell Name: dopaminergic neuron (CL0000700)
Fold Change: -0.1053
Cell Significance Index: -30.2900
Cell Name: enterocyte of epithelium of large intestine (CL0002071)
Fold Change: -0.1113
Cell Significance Index: -5.0500
Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
Fold Change: -0.1367
Cell Significance Index: -3.8200
Cell Name: pancreatic acinar cell (CL0002064)
Fold Change: -0.1413
Cell Significance Index: -24.1200
Cell Name: pancreatic D cell (CL0000173)
Fold Change: -0.1881
Cell Significance Index: -39.6100
Cell Name: microfold cell of epithelium of small intestine (CL1000353)
Fold Change: -0.2060
Cell Significance Index: -14.2500
Cell Name: epithelial cell of stomach (CL0002178)
Fold Change: -0.2087
Cell Significance Index: -24.3200
Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
Fold Change: -0.2138
Cell Significance Index: -10.0500
Cell Name: lactocyte (CL0002325)
Fold Change: -0.2293
Cell Significance Index: -29.6300
Cell Name: pro-T cell (CL0000827)
Fold Change: -0.2914
Cell Significance Index: -7.4500
Cell Name: pancreatic ductal cell (CL0002079)
Fold Change: -0.2936
Cell Significance Index: -33.6400
Cell Name: intestinal tuft cell (CL0019032)
Fold Change: -0.2983
Cell Significance Index: -18.2900
Cell Name: preadipocyte (CL0002334)
Fold Change: -0.3013
Cell Significance Index: -5.8800
Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
Fold Change: -0.3048
Cell Significance Index: -31.7400
Cell Name: paneth cell of epithelium of small intestine (CL1000343)
Fold Change: -0.3217
Cell Significance Index: -6.9700
Cell Name: fibroblast of mammary gland (CL0002555)
Fold Change: -0.3429
Cell Significance Index: -9.8300
Cell Name: sebum secreting cell (CL0000317)
Fold Change: -0.3688
Cell Significance Index: -26.0800
Cell Name: transit amplifying cell of colon (CL0009011)
Fold Change: -0.3881
Cell Significance Index: -12.4300
Cell Name: gut absorptive cell (CL0000677)
Fold Change: -0.4040
Cell Significance Index: -24.2600
Cell Name: conjunctival epithelial cell (CL1000432)
Fold Change: -0.4148
Cell Significance Index: -5.6600
Cell Name: retinal progenitor cell (CL0002672)
Fold Change: -0.4788
Cell Significance Index: -26.8700
Cell Name: forebrain neuroblast (CL1000042)
Fold Change: -0.4922
Cell Significance Index: -30.2500
Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
Fold Change: -0.4936
Cell Significance Index: -39.0900
Cell Name: cerebellar granule cell (CL0001031)
Fold Change: -0.4954
Cell Significance Index: -8.4900
Cell Name: indirect pathway medium spiny neuron (CL4023029)
Fold Change: -0.5270
Cell Significance Index: -23.3100
Cell Name: transit amplifying cell of small intestine (CL0009012)
Fold Change: -0.5375
Cell Significance Index: -11.1500
Cell Name: hippocampal granule cell (CL0001033)
Fold Change: -0.5666
Cell Significance Index: -38.1000
Cell Name: direct pathway medium spiny neuron (CL4023026)
Fold Change: -0.6058
Cell Significance Index: -22.9400
Cell Name: eye photoreceptor cell (CL0000287)
Fold Change: -0.6121
Cell Significance Index: -38.5800
Cell Name: glycinergic neuron (CL1001509)
Fold Change: -0.6965
Cell Significance Index: -36.5700
Cell Name: vascular lymphangioblast (CL0005022)
Fold Change: -0.7082
Cell Significance Index: -12.5200
Cell Name: acinar cell of salivary gland (CL0002623)
Fold Change: -0.7318
Cell Significance Index: -34.1200
Cell Name: CD4-positive, alpha-beta thymocyte (CL0000810)
Fold Change: -0.7355
Cell Significance Index: -12.6800
Cell Name: eukaryotic cell (CL0000255)
Fold Change: -0.7795
Cell Significance Index: -33.9000
Cell Name: fallopian tube secretory epithelial cell (CL4030006)
Fold Change: -0.8018
Cell Significance Index: -12.4100
Cell Name: mesenchymal cell (CL0008019)
Fold Change: -0.8204
Cell Significance Index: -13.7300
Cell Name: skeletal muscle fiber (CL0008002)
Fold Change: -0.8298
Cell Significance Index: -21.3300
Cell Name: L5 extratelencephalic projecting glutamatergic cortical neuron (CL4023041)
Fold Change: -0.8841
Cell Significance Index: -30.9700
Cell Name: lens fiber cell (CL0011004)
Fold Change: -0.8979
Cell Significance Index: -28.4000
Cell Name: stratified epithelial cell (CL0000079)
Fold Change: -0.9297
Cell Significance Index: -34.1300
Cell Name: type I muscle cell (CL0002211)
Fold Change: -0.9672
Cell Significance Index: -23.6000
Cell Name: L6b glutamatergic cortical neuron (CL4023038)
Fold Change: -1.0049
Cell Significance Index: -32.9000

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

**Key Characteristics** TGFB1 is a 24-kDa protein that is secreted as a proprotein and cleaved into the mature 25-kDa form. It is a member of the TGF-β superfamily, which consists of five TGF-β isoforms (TGF-β1, TGF-β2, TGF-β3, TGF-β4, and TGF-β5) and several accessory proteins. TGFB1 is unique in its ability to regulate cell growth, differentiation, and apoptosis through the activation of Smad proteins, which are transcription factors involved in the regulation of gene expression. **Pathways and Functions** TGFB1 is involved in various cellular processes, including: 1. **Immune responses**: TGFB1 regulates the expression of genes involved in immune responses, including the production of cytokines and chemokines. 2. **Cell growth and differentiation**: TGFB1 regulates cell growth, differentiation, and survival by modulating the expression of genes involved in these processes. 3. **Apoptosis**: TGFB1 can induce apoptosis in certain cell types, including cancer cells. 4. **Fibrosis**: TGFB1 is involved in the regulation of fibrosis, a condition characterized by the excessive deposition of extracellular matrix proteins. 5. **Angiogenesis**: TGFB1 regulates angiogenesis, the formation of new blood vessels from pre-existing vessels. **Clinical Significance** The dysregulation of TGFB1 has been implicated in various diseases, including: 1. **Cancer**: TGFB1 is often downregulated in cancer cells, leading to uncontrolled cell growth and tumor progression. 2. **Cardiovascular diseases**: TGFB1 is involved in the regulation of vascular smooth muscle cell growth and differentiation, and its dysregulation can contribute to cardiovascular diseases, including atherosclerosis and cardiac fibrosis. 3. **Autoimmune disorders**: TGFB1 is involved in the regulation of immune responses, and its dysregulation can contribute to autoimmune disorders, including rheumatoid arthritis and lupus. 4. **Neurological disorders**: TGFB1 is involved in the regulation of neuroinflammation and neurodegenerative diseases, including Alzheimer's disease and multiple sclerosis. In conclusion, TGFB1 is a multifunctional cytokine that plays a crucial role in various cellular processes, including cell growth, differentiation, apoptosis, and immune responses. The dysregulation of TGFB1 has been implicated in various diseases, including cancer, cardiovascular diseases, autoimmune disorders, and neurological disorders. Further research is needed to fully understand the mechanisms of TGFB1 and its role in human disease.

Disclaimer: This summary is generated by an AI language model and may contain inaccuracies or hallucinations. However, it is cross-referenced with curated gene expression data from major biological sources. Please verify the information before use.

Transforming growth factor beta-1 proprotein

Genular Protein ID: 1038819429

Symbol: TGFB1_HUMAN

Name: Transforming growth factor beta-1 proprotein

UniProtKB Accession Codes:

P01137 A8K792 Q9UCG4

Database IDs:

Citations:

PubMed ID: 3470709

Title: Intron-exon structure of the human transforming growth factor-beta precursor gene.

PubMed ID: 3470709

DOI: 10.1093/nar/15.7.3188

PubMed ID: 3861940

Title: Human transforming growth factor-beta complementary DNA sequence and expression in normal and transformed cells.

PubMed ID: 3861940

DOI: 10.1038/316701a0

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 8471846

Title: Recombinant human transforming growth factor-beta 1: expression by Chinese hamster ovary cells, isolation, and characterization.

PubMed ID: 8471846

DOI: 10.1006/prep.1993.1019

PubMed ID: 2982829

Title: Cellular receptors for type beta transforming growth factor. Ligand binding and affinity labeling in human and rodent cell lines.

PubMed ID: 2982829

DOI: 10.1016/s0021-9258(18)89408-x

PubMed ID: 3162913

Title: Latent high molecular weight complex of transforming growth factor beta 1. Purification from human platelets and structural characterization.

PubMed ID: 3162913

DOI: 10.1016/s0021-9258(18)68800-3

PubMed ID: 7737999

Title: Processing of transforming growth factor beta 1 precursor by human furin convertase.

PubMed ID: 7737999

DOI: 10.1074/jbc.270.18.10618

PubMed ID: 2493139

Title: Role for carbohydrate structures in TGF-beta 1 latency.

PubMed ID: 2493139

DOI: 10.1038/338158a0

PubMed ID: 2022183

Title: A role of the latent TGF-beta 1-binding protein in the assembly and secretion of TGF-beta 1.

PubMed ID: 2022183

DOI: 10.1002/j.1460-2075.1991.tb08049.x

PubMed ID: 8617200

Title: Association of the small latent transforming growth factor-beta with an eight cysteine repeat of its binding protein LTBP-1.

PubMed ID: 8617200

DOI: 10.1002/j.1460-2075.1996.tb00355.x

PubMed ID: 8939931

Title: Identification and characterization of an eight-cysteine repeat of the latent transforming growth factor-beta binding protein-1 that mediates bonding to the latent transforming growth factor-beta1.

PubMed ID: 8939931

DOI: 10.1074/jbc.271.47.29891

PubMed ID: 9150447

Title: Latent transforming growth factor-beta: structural features and mechanisms of activation.

PubMed ID: 9150447

DOI: 10.1038/ki.1997.188

PubMed ID: 9895299

Title: Dermatopontin interacts with transforming growth factor beta and enhances its biological activity.

PubMed ID: 9895299

DOI: 10.1042/bj3370537

PubMed ID: 11746498

Title: Differential gene expression of cultured human osteoblasts.

PubMed ID: 11746498

DOI: 10.1002/jcb.1249

PubMed ID: 16335952

Title: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.

PubMed ID: 16335952

DOI: 10.1021/pr0502065

PubMed ID: 16754747

Title: Identification of CD109 as part of the TGF-beta receptor system in human keratinocytes.

PubMed ID: 16754747

DOI: 10.1096/fj.05-5229fje

PubMed ID: 16263699

Title: Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach.

PubMed ID: 16263699

DOI: 10.1074/mcp.m500324-mcp200

PubMed ID: 17827158

Title: Mechanisms for asporin function and regulation in articular cartilage.

PubMed ID: 17827158

DOI: 10.1074/jbc.m700522200

PubMed ID: 19750484

Title: Membrane protein GARP is a receptor for latent TGF-beta on the surface of activated human Treg.

PubMed ID: 19750484

DOI: 10.1002/eji.200939684

PubMed ID: 22278742

Title: GARP regulates the bioavailability and activation of TGFbeta.

PubMed ID: 22278742

DOI: 10.1091/mbc.e11-12-1018

PubMed ID: 19651619

Title: GARP (LRRC32) is essential for the surface expression of latent TGF-beta on platelets and activated FOXP3+ regulatory T cells.

PubMed ID: 19651619

DOI: 10.1073/pnas.0901944106

PubMed ID: 20599762

Title: Extracellular heat shock protein HSP90beta secreted by MG63 osteosarcoma cells inhibits activation of latent TGF-beta1.

PubMed ID: 20599762

DOI: 10.1016/j.bbrc.2010.06.112

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 25310401

Title: Sustained induction of collagen synthesis by TGF-beta requires regulated intramembrane proteolysis of CREB3L1.

PubMed ID: 25310401

DOI: 10.1371/journal.pone.0108528

PubMed ID: 25944712

Title: N-terminome analysis of the human mitochondrial proteome.

PubMed ID: 25944712

DOI: 10.1002/pmic.201400617

PubMed ID: 27339457

Title: Functional consequence of fibulin-4 missense mutations associated with vascular and skeletal abnormalities and cutis laxa.

PubMed ID: 27339457

DOI: 10.1016/j.matbio.2016.06.003

PubMed ID: 25893292

Title: Syntenin regulates TGF-beta1-induced Smad activation and the epithelial-to-mesenchymal transition by inhibiting caveolin-mediated TGF-beta type I receptor internalization.

PubMed ID: 25893292

DOI: 10.1038/onc.2015.100

PubMed ID: 27389696

Title: PSG9 Stimulates Increase in FoxP3+ Regulatory T-Cells through the TGF-beta1 Pathway.

PubMed ID: 27389696

DOI: 10.1371/journal.pone.0158050

PubMed ID: 27252363

Title: Regulation of the bioavailability of TGF-beta and TGF-beta-related proteins.

PubMed ID: 27252363

DOI: 10.1101/cshperspect.a021907

PubMed ID: 29909984

Title: A milieu molecule for TGF-beta required for microglia function in the nervous system.

PubMed ID: 29909984

DOI: 10.1016/j.cell.2018.05.027

PubMed ID: 29483653

Title: Human TGF-beta1 deficiency causes severe inflammatory bowel disease and encephalopathy.

PubMed ID: 29483653

DOI: 10.1038/s41588-018-0063-6

PubMed ID: 30696809

Title: TTC3 contributes to TGF-beta1-induced epithelial-mesenchymal transition and myofibroblast differentiation, potentially through SMURF2 ubiquitylation and degradation.

PubMed ID: 30696809

DOI: 10.1038/s41419-019-1308-8

PubMed ID: 8424942

Title: Transforming growth factor beta 1: NMR signal assignments of the recombinant protein expressed and isotopically enriched using Chinese hamster ovary cells.

PubMed ID: 8424942

DOI: 10.1021/bi00055a021

PubMed ID: 8424943

Title: Transforming growth factor beta 1: secondary structure as determined by heteronuclear magnetic resonance spectroscopy.

PubMed ID: 8424943

DOI: 10.1021/bi00055a022

PubMed ID: 8679613

Title: Transforming growth factor beta 1: three-dimensional structure in solution and comparison with the X-ray structure of transforming growth factor beta 2.

PubMed ID: 8679613

DOI: 10.1021/bi9604946

PubMed ID: 20207738

Title: Ternary complex of transforming growth factor-beta1 reveals isoform-specific ligand recognition and receptor recruitment in the superfamily.

PubMed ID: 20207738

DOI: 10.1074/jbc.m109.079921

PubMed ID: 25209176

Title: Structures of a pan-specific antagonist antibody complexed to different isoforms of TGFbeta reveal structural plasticity of antibody-antigen interactions.

PubMed ID: 25209176

DOI: 10.1002/pro.2548

PubMed ID: 28117447

Title: Force interacts with macromolecular structure in activation of TGF-beta.

PubMed ID: 28117447

DOI: 10.1038/nature21035

PubMed ID: 29109152

Title: Prodomain-growth factor swapping in the structure of pro-TGF-beta1.

PubMed ID: 29109152

DOI: 10.1074/jbc.m117.809657

PubMed ID: 9783545

Title: Association of a polymorphism of the transforming growth factor-beta1 gene with genetic susceptibility to osteoporosis in postmenopausal Japanese women.

PubMed ID: 9783545

DOI: 10.1359/jbmr.1998.13.10.1569

PubMed ID: 10973241

Title: Domain-specific mutations in TGFB1 result in Camurati-Engelmann disease.

PubMed ID: 10973241

DOI: 10.1038/79128

PubMed ID: 11062463

Title: Mutations in the gene encoding the latency-associated peptide of TGF-beta 1 cause Camurati-Engelmann disease.

PubMed ID: 11062463

DOI: 10.1038/81563

PubMed ID: 12202987

Title: A catalog of 106 single-nucleotide polymorphisms (SNPs) and 11 other types of variations in genes for transforming growth factor-beta1 (TGF-beta1) and its signaling pathway.

PubMed ID: 12202987

DOI: 10.1007/s100380200069

PubMed ID: 12493741

Title: Transforming growth factor-beta-1 mutations in Camurati-Engelmann disease lead to increased signaling by altering either activation or secretion of the mutant protein.

PubMed ID: 12493741

DOI: 10.1074/jbc.m208857200

PubMed ID: 12843182

Title: A mutation affecting the latency-associated peptide of TGFbeta1 in Camurati-Engelmann disease enhances osteoclast formation in vitro.

PubMed ID: 12843182

DOI: 10.1210/jc.2002-020564

PubMed ID: 15103729

Title: TGFB1 mutations in four new families with Camurati-Engelmann disease: confirmation of independently arising LAP-domain-specific mutations.

PubMed ID: 15103729

DOI: 10.1002/ajmg.a.20671

Sequence Information:

Length: 390
Mass: 44325
Checksum: 71785979662FC4BE
Sequence:

MPPSGLRLLP LLLPLLWLLV LTPGRPAAGL STCKTIDMEL VKRKRIEAIR GQILSKLRLA 
SPPSQGEVPP GPLPEAVLAL YNSTRDRVAG ESAEPEPEPE ADYYAKEVTR VLMVETHNEI 
YDKFKQSTHS IYMFFNTSEL REAVPEPVLL SRAELRLLRL KLKVEQHVEL YQKYSNNSWR 
YLSNRLLAPS DSPEWLSFDV TGVVRQWLSR GGEIEGFRLS AHCSCDSRDN TLQVDINGFT 
TGRRGDLATI HGMNRPFLLL MATPLERAQH LQSSRHRRAL DTNYCFSSTE KNCCVRQLYI 
DFRKDLGWKW IHEPKGYHAN FCLGPCPYIW SLDTQYSKVL ALYNQHNPGA SAAPCCVPQA 
LEPLPIVYYV GRKPKVEQLS NMIVRSCKCS

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: TGFB1

Associated with

Cells (max top 100)

Other Information

Intron-exon structure of the human transforming growth factor-beta precursor gene. PubMed ID: 3470709

Human transforming growth factor-beta complementary DNA sequence and expression in normal and transformed cells. PubMed ID: 3861940

Complete sequencing and characterization of 21,243 full-length human cDNAs. PubMed ID: 14702039

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Recombinant human transforming growth factor-beta 1: expression by Chinese hamster ovary cells, isolation, and characterization. PubMed ID: 8471846

Cellular receptors for type beta transforming growth factor. Ligand binding and affinity labeling in human and rodent cell lines. PubMed ID: 2982829

Latent high molecular weight complex of transforming growth factor beta 1. Purification from human platelets and structural characterization. PubMed ID: 3162913

Processing of transforming growth factor beta 1 precursor by human furin convertase. PubMed ID: 7737999

Role for carbohydrate structures in TGF-beta 1 latency. PubMed ID: 2493139

A role of the latent TGF-beta 1-binding protein in the assembly and secretion of TGF-beta 1. PubMed ID: 2022183

Association of the small latent transforming growth factor-beta with an eight cysteine repeat of its binding protein LTBP-1. PubMed ID: 8617200

Identification and characterization of an eight-cysteine repeat of the latent transforming growth factor-beta binding protein-1 that mediates bonding to the latent transforming growth factor-beta1. PubMed ID: 8939931

Latent transforming growth factor-beta: structural features and mechanisms of activation. PubMed ID: 9150447

Dermatopontin interacts with transforming growth factor beta and enhances its biological activity. PubMed ID: 9895299

Differential gene expression of cultured human osteoblasts. PubMed ID: 11746498

Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. PubMed ID: 16335952

Identification of CD109 as part of the TGF-beta receptor system in human keratinocytes. PubMed ID: 16754747

Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach. PubMed ID: 16263699

Mechanisms for asporin function and regulation in articular cartilage. PubMed ID: 17827158

Membrane protein GARP is a receptor for latent TGF-beta on the surface of activated human Treg. PubMed ID: 19750484

GARP regulates the bioavailability and activation of TGFbeta. PubMed ID: 22278742

GARP (LRRC32) is essential for the surface expression of latent TGF-beta on platelets and activated FOXP3+ regulatory T cells. PubMed ID: 19651619

Extracellular heat shock protein HSP90beta secreted by MG63 osteosarcoma cells inhibits activation of latent TGF-beta1. PubMed ID: 20599762

Initial characterization of the human central proteome. PubMed ID: 21269460

Sustained induction of collagen synthesis by TGF-beta requires regulated intramembrane proteolysis of CREB3L1. PubMed ID: 25310401

N-terminome analysis of the human mitochondrial proteome. PubMed ID: 25944712

Functional consequence of fibulin-4 missense mutations associated with vascular and skeletal abnormalities and cutis laxa. PubMed ID: 27339457

Syntenin regulates TGF-beta1-induced Smad activation and the epithelial-to-mesenchymal transition by inhibiting caveolin-mediated TGF-beta type I receptor internalization. PubMed ID: 25893292

PSG9 Stimulates Increase in FoxP3+ Regulatory T-Cells through the TGF-beta1 Pathway. PubMed ID: 27389696

Regulation of the bioavailability of TGF-beta and TGF-beta-related proteins. PubMed ID: 27252363

A milieu molecule for TGF-beta required for microglia function in the nervous system. PubMed ID: 29909984

Human TGF-beta1 deficiency causes severe inflammatory bowel disease and encephalopathy. PubMed ID: 29483653

TTC3 contributes to TGF-beta1-induced epithelial-mesenchymal transition and myofibroblast differentiation, potentially through SMURF2 ubiquitylation and degradation. PubMed ID: 30696809

Transforming growth factor beta 1: NMR signal assignments of the recombinant protein expressed and isotopically enriched using Chinese hamster ovary cells. PubMed ID: 8424942

Transforming growth factor beta 1: secondary structure as determined by heteronuclear magnetic resonance spectroscopy. PubMed ID: 8424943

Transforming growth factor beta 1: three-dimensional structure in solution and comparison with the X-ray structure of transforming growth factor beta 2. PubMed ID: 8679613

Ternary complex of transforming growth factor-beta1 reveals isoform-specific ligand recognition and receptor recruitment in the superfamily. PubMed ID: 20207738

Structures of a pan-specific antagonist antibody complexed to different isoforms of TGFbeta reveal structural plasticity of antibody-antigen interactions. PubMed ID: 25209176

Force interacts with macromolecular structure in activation of TGF-beta. PubMed ID: 28117447

Prodomain-growth factor swapping in the structure of pro-TGF-beta1. PubMed ID: 29109152

Association of a polymorphism of the transforming growth factor-beta1 gene with genetic susceptibility to osteoporosis in postmenopausal Japanese women. PubMed ID: 9783545

Domain-specific mutations in TGFB1 result in Camurati-Engelmann disease. PubMed ID: 10973241

Mutations in the gene encoding the latency-associated peptide of TGF-beta 1 cause Camurati-Engelmann disease. PubMed ID: 11062463

A catalog of 106 single-nucleotide polymorphisms (SNPs) and 11 other types of variations in genes for transforming growth factor-beta1 (TGF-beta1) and its signaling pathway. PubMed ID: 12202987

Transforming growth factor-beta-1 mutations in Camurati-Engelmann disease lead to increased signaling by altering either activation or secretion of the mutant protein. PubMed ID: 12493741

A mutation affecting the latency-associated peptide of TGFbeta1 in Camurati-Engelmann disease enhances osteoclast formation in vitro. PubMed ID: 12843182

TGFB1 mutations in four new families with Camurati-Engelmann disease: confirmation of independently arising LAP-domain-specific mutations. PubMed ID: 15103729