transforming growth factor beta 1

mammalian protein found in Homo sapiens

Protein protein Q2062543

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transforming growth factor beta 1

Summary

transforming growth factor beta 1 is a protein^[1].

Key Facts

transforming growth factor beta 1's instance of is recorded as protein^[2].
transforming growth factor beta 1's UniProt protein ID is recorded as P01137^[3].
transforming growth factor beta 1's part of is recorded as Transforming growth factor beta-1 proprotein^[4].
transforming growth factor beta 1's part of is recorded as Cystine-knot cytokine^[5].
transforming growth factor beta 1's part of is recorded as Transforming growth factor-beta, C-terminal domain, protein family^[6].
transforming growth factor beta 1's part of is recorded as TGF-beta, propeptide family^[7].
transforming growth factor beta 1's part of is recorded as Transforming growth factor beta, conserved site, protein family^[8].
transforming growth factor beta 1's MeSH descriptor ID is recorded as D053773^[9].
transforming growth factor beta 1's has part is recorded as Transforming growth factor beta, conserved site^[10].
transforming growth factor beta 1's has part is recorded as Transforming growth factor-beta, C-terminal^[11].
transforming growth factor beta 1's has part is recorded as TGF-beta, propeptide^[12].
transforming growth factor beta 1's RefSeq protein ID is recorded as NP_000651^[13].
transforming growth factor beta 1's RefSeq protein ID is recorded as XP_011525544^[14].
transforming growth factor beta 1's PDB structure ID is recorded as 1KLA^[15].
transforming growth factor beta 1's PDB structure ID is recorded as 1KLC^[16].
transforming growth factor beta 1's PDB structure ID is recorded as 1KLD^[17].
transforming growth factor beta 1's PDB structure ID is recorded as 3KFD^[18].
transforming growth factor beta 1's PDB structure ID is recorded as 4KV5^[19].
transforming growth factor beta 1's Freebase ID is recorded as /m/02p9q5b^[20].
transforming growth factor beta 1's MeSH tree code is recorded as D12.644.276.374.687.100^[21].
transforming growth factor beta 1's MeSH tree code is recorded as D12.644.276.954.775.100^[22].
transforming growth factor beta 1's MeSH tree code is recorded as D12.776.467.374.687.100^[23].
transforming growth factor beta 1's MeSH tree code is recorded as D12.776.467.942.775.100^[24].
transforming growth factor beta 1's MeSH tree code is recorded as D23.529.374.687.100^[25].
transforming growth factor beta 1's MeSH tree code is recorded as D23.529.942.775.100^[26].

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Quick Facts

Instance of protein

Part of Transforming growth factor beta-1 proprotein, Cystine-knot cytokine, Transforming growth factor-beta, C-terminal domain, protein family, TGF-beta, propeptide family, Transforming growth factor beta, conserved site, protein family

Properties

Biological process positive regulation of histone deacetylation, positive regulation of transcription regulatory region DNA binding, ureteric bud development, tolerance induction to self antigen, positive regulation of protein phosphorylation, endoderm development, response to cholesterol, positive regulation of MAP kinase activity, regulation of sodium ion transport, response to progesterone, negative regulation of cell cycle, response to organic substance, mammary gland development, T cell homeostasis, negative regulation of ossification, negative regulation of hyaluronan biosynthetic process, protein phosphorylation, T cell differentiation, positive regulation of vascular permeability, animal organ regeneration, positive regulation of blood vessel endothelial cell migration, negative regulation of epithelial cell proliferation, regulation of binding, inner ear development, myelination, negative regulation of macrophage cytokine production, cell population proliferation, transforming growth factor beta receptor signaling pathway, face morphogenesis, negative regulation of cell population proliferation, positive regulation of receptor clustering, regulation of apoptotic process, positive regulation of collagen biosynthetic process, cellular response to transforming growth factor beta stimulus, pathway-restricted SMAD protein phosphorylation, regulation of DNA binding, regulation of actin cytoskeleton reorganization, negative regulation of fat cell differentiation, positive regulation of protein metabolic process, cell-cell junction organization, negative regulation of myoblast differentiation, positive regulation of protein kinase B signaling, common-partner SMAD protein phosphorylation, positive regulation of branching involved in ureteric bud morphogenesis, SMAD protein signal transduction, epidermal growth factor receptor signaling pathway, macrophage derived foam cell differentiation, negative regulation of blood vessel endothelial cell migration, positive regulation of protein dephosphorylation, extrinsic apoptotic signaling pathway, negative regulation of extracellular matrix disassembly, mitotic cell cycle checkpoint signaling, positive regulation of fibroblast proliferation, negative regulation of cell differentiation, regulation of branching involved in mammary gland duct morphogenesis, positive regulation of exit from mitosis, negative regulation of transforming growth factor beta receptor signaling pathway, negative regulation of gene expression, morphogenesis of a branching structure, regulation of SMAD protein signal transduction, positive regulation of peptidyl-serine phosphorylation, cell activation, negative regulation of neuroblast proliferation, positive regulation of transcription, DNA-templated, cell growth, negative regulation of T cell proliferation, response to wounding, negative regulation of cell growth, positive regulation of chemotaxis, protein export from nucleus, regulation of protein import into nucleus, positive regulation of peptidyl-tyrosine phosphorylation, positive regulation of protein import into nucleus, positive regulation of cardiac muscle cell differentiation, oligodendrocyte development, positive regulation of interleukin-17 production, inflammatory response, negative regulation of interleukin-17 production, lymph node development, T cell activation, Notch signaling pathway, negative regulation of protein phosphorylation, regulation of blood vessel remodeling, SMAD protein complex assembly, regulation of striated muscle tissue development, response to vitamin D, chondrocyte differentiation, regulatory T cell differentiation, regulation of cartilage development, branch elongation involved in mammary gland duct branching, positive regulation of bone mineralization, positive regulation of epithelial cell proliferation, female pregnancy, cellular response to organic cyclic compound, positive regulation of extracellular matrix assembly, cellular calcium ion homeostasis, wound healing, negative regulation of transcription by RNA polymerase II, response to glucose, positive regulation of epithelial to mesenchymal transition, cellular response to dexamethasone stimulus, negative regulation of production of miRNAs involved in gene silencing by miRNA, mitigation of host defenses by virus, lens fiber cell differentiation, positive regulation of NF-kappaB transcription factor activity, extracellular matrix assembly, ATP biosynthetic process, hematopoietic progenitor cell differentiation, regulation of interleukin-23 production, positive regulation of protein secretion, frontal suture morphogenesis, epithelial to mesenchymal transition, phosphate-containing compound metabolic process, regulation of gene expression, adaptive immune response based on somatic recombination of immune receptors built from immunoglobulin superfamily domains, negative regulation of release of sequestered calcium ion into cytosol, response to radiation, mononuclear cell proliferation, negative regulation of transcription, DNA-templated, negative regulation of T cell activation, positive regulation of odontogenesis, lipopolysaccharide-mediated signaling pathway, positive regulation of protein localization to nucleus, response to estradiol, regulation of cell migration, response to hypoxia, hyaluronan catabolic process, negative regulation of phagocytosis, response to organic cyclic compound, positive regulation of protein-containing complex assembly, protein kinase B signaling, negative regulation of cell-cell adhesion, negative regulation of gene silencing by miRNA, positive regulation of regulatory T cell differentiation, cellular response to growth factor stimulus, positive regulation of pathway-restricted SMAD protein phosphorylation, mammary gland branching involved in thelarche, response to laminar fluid shear stress, ageing, regulation of regulatory T cell differentiation, platelet degranulation, negative regulation of DNA replication, myeloid dendritic cell differentiation, salivary gland morphogenesis, receptor catabolic process, MAPK cascade, positive regulation of histone acetylation, regulation of transforming growth factor beta receptor signaling pathway, positive regulation of phosphatidylinositol 3-kinase activity, negative regulation of protein localization to plasma membrane, positive regulation of NAD+ ADP-ribosyltransferase activity, negative regulation of immune response, regulation of cell population proliferation, negative regulation of skeletal muscle tissue development, positive regulation of peptidyl-threonine phosphorylation, positive regulation of smooth muscle cell differentiation, positive regulation of isotype switching to IgA isotypes, connective tissue replacement involved in inflammatory response wound healing, ossification involved in bone remodeling, positive regulation of apoptotic process, positive regulation of vascular endothelial growth factor production, positive regulation of superoxide anion generation, digestive tract development, cell migration, positive regulation of fibroblast migration, positive regulation of cell division, germ cell migration, positive regulation of transcription by RNA polymerase II, negative regulation of mitotic cell cycle, positive regulation of SMAD protein signal transduction, positive regulation of pri-miRNA transcription by RNA polymerase II, positive regulation of gene expression, positive regulation of cell population proliferation, liver regeneration, regulation of epithelial to mesenchymal transition involved in endocardial cushion formation, positive regulation of mononuclear cell migration, cellular response to insulin-like growth factor stimulus, positive regulation of cell migration, response to immobilization stress, cellular response to mechanical stimulus, cellular response to ionizing radiation, vasculogenesis, neural tube closure, heart valve morphogenesis, development of the heart, neural tube development, membrane protein intracellular domain proteolysis, leukocyte migration, ventricular cardiac muscle tissue morphogenesis, positive regulation of ERK1 and ERK2 cascade, transforming growth factor beta receptor signaling pathway involved in heart development, embryonic liver development, BMP signaling pathway, cell development, apoptotic process, regulation of pri-miRNA transcription by RNA polymerase II, positive regulation of production of miRNAs involved in gene silencing by miRNA, regulation of signaling receptor activity

Cell component cytoplasm, extracellular region, nucleus, microvillus, cell surface, blood microparticle, plasma membrane, secretory granule, axon, soma, Golgi lumen, platelet alpha granule lumen, extracellular matrix, extracellular space

Encoded by TGFB1

Found in taxon Homo sapiens

Has part(s) Transforming growth factor beta, conserved site, Transforming growth factor-beta, C-terminal, TGF-beta, propeptide

Imported from wholeness_audit_2026-05-02

Molecular function type II transforming growth factor beta receptor binding, protein N-terminus binding, cytokine activity, enzyme binding, growth factor activity, antigen binding, type I transforming growth factor beta receptor binding, protein homodimerization activity, protein serine/threonine kinase activator activity, protein binding, protein heterodimerization activity, type III transforming growth factor beta receptor binding, transforming growth factor beta receptor binding, identical protein binding

External References (8)

Ensembl protein id ENSP00000221930, ENSP00000472767

Freebase id /m/02p9q5b

Mesh descriptor id D053773

Mesh tree code D12.644.276.374.687.100, D12.644.276.954.775.100, D12.776.467.374.687.100, D12.776.467.942.775.100, D23.529.374.687.100, D23.529.942.775.100

Pdb structure id 1KLA, 1KLC, 1KLD, 3KFD, 4KV5

Refseq protein id NP_000651, XP_011525544

Umls cui C0169144

Uniprot protein id P01137

References

Programmatic citations — every numbered marker resolves to a verifiable graph row below.

Direct Wikidata claims

[2] ↑ transforming growth factor beta 1 — instance of (P31): protein. Q905695. Retrieved 2019-11-13. wikidata.org.
[3] ↑ transforming growth factor beta 1 — UniProt protein ID (P352): P01137. Q905695. Retrieved 2019-11-13. wikidata.org.
[4] ↑ transforming growth factor beta 1 — part of (P361): Transforming growth factor beta-1 proprotein. InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
[5] ↑ transforming growth factor beta 1 — part of (P361): Cystine-knot cytokine. InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
[6] ↑ transforming growth factor beta 1 — part of (P361): Transforming growth factor-beta, C-terminal domain, protein family. wikidata.org.
[7] ↑ transforming growth factor beta 1 — part of (P361): TGF-beta, propeptide family. wikidata.org.
[8] ↑ transforming growth factor beta 1 — part of (P361): Transforming growth factor beta, conserved site, protein family. wikidata.org.
[9] ↑ transforming growth factor beta 1 — MeSH descriptor ID (P486): D053773. wikidata.org.
[10] ↑ transforming growth factor beta 1 — has part(s) (P527): Transforming growth factor beta, conserved site. InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
[11] ↑ transforming growth factor beta 1 — has part(s) (P527): Transforming growth factor-beta, C-terminal. InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
[12] ↑ transforming growth factor beta 1 — has part(s) (P527): TGF-beta, propeptide. InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
[13] ↑ transforming growth factor beta 1 — RefSeq protein ID (P637): NP_000651. Q20641742. Retrieved 2020-05-30. wikidata.org.
[14] ↑ transforming growth factor beta 1 — RefSeq protein ID (P637): XP_011525544. Q20641742. Retrieved 2020-05-30. wikidata.org.
[15] ↑ transforming growth factor beta 1 — PDB structure ID (P638): 1KLA. Q905695. Retrieved 2016-08-09. wikidata.org.
[16] ↑ transforming growth factor beta 1 — PDB structure ID (P638): 1KLC. Q905695. Retrieved 2016-08-09. wikidata.org.
[17] ↑ transforming growth factor beta 1 — PDB structure ID (P638): 1KLD. Q905695. Retrieved 2016-08-09. wikidata.org.
[18] ↑ transforming growth factor beta 1 — PDB structure ID (P638): 3KFD. Q905695. Retrieved 2016-08-09. wikidata.org.
[19] ↑ transforming growth factor beta 1 — PDB structure ID (P638): 4KV5. Q905695. Retrieved 2016-08-09. wikidata.org.
[20] ↑ transforming growth factor beta 1 — Freebase ID (P646): /m/02p9q5b. Freebase Data Dumps. wikidata.org.
[21] ↑ transforming growth factor beta 1 — MeSH tree code (P672): D12.644.276.374.687.100. wikidata.org.
[22] ↑ transforming growth factor beta 1 — MeSH tree code (P672): D12.644.276.954.775.100. wikidata.org.
[23] ↑ transforming growth factor beta 1 — MeSH tree code (P672): D12.776.467.374.687.100. wikidata.org.
[24] ↑ transforming growth factor beta 1 — MeSH tree code (P672): D12.776.467.942.775.100. wikidata.org.
[25] ↑ transforming growth factor beta 1 — MeSH tree code (P672): D23.529.374.687.100. wikidata.org.
[26] ↑ transforming growth factor beta 1 — MeSH tree code (P672): D23.529.942.775.100. wikidata.org.

Class ancestry

[1] ↑ transforming growth factor beta 1 is an instance of protein (Q8054) [P31, primary]. Wikidata. wikidata.org.

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APA

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MLA

“transforming growth factor beta 1.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/transforming-growth-factor-beta-1-q2062543.

BibTeX

@misc{4ortxyz_transforming-growth-factor-beta-1-q2062543_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{transforming growth factor beta 1}}, year = {2026}, url = {https://4ort.xyz/entity/transforming-growth-factor-beta-1-q2062543}, note = {Accessed: 2026-05-03}}

LLM prompt

According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): transforming growth factor beta 1 — https://4ort.xyz/entity/transforming-growth-factor-beta-1-q2062543 (retrieved 2026-05-03)

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