Transforming growth factor, beta 1

mammalian protein found in Mus musculus

Protein protein Q14904616

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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 subclass of is recorded as protein^[3].
Transforming growth factor, beta 1's UniProt protein ID is recorded as P04202^[4].
Transforming growth factor, beta 1's part of is recorded as Transforming growth factor beta-1 proprotein^[5].
Transforming growth factor, beta 1's part of is recorded as Cystine-knot cytokine^[6].
Transforming growth factor, beta 1's part of is recorded as Transforming growth factor-beta, C-terminal domain, protein family^[7].
Transforming growth factor, beta 1's part of is recorded as TGF-beta, propeptide family^[8].
Transforming growth factor, beta 1's part of is recorded as Transforming growth factor beta, conserved site, protein family^[9].
Transforming growth factor, beta 1's has part is recorded as Transforming growth factor-beta, C-terminal^[10].
Transforming growth factor, beta 1's has part is recorded as Transforming growth factor beta, conserved site^[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_035707^[13].
Transforming growth factor, beta 1's RefSeq protein ID is recorded as XP_036008776^[14].
Transforming growth factor, beta 1's UNII is recorded as T7D25J14LT^[15].
Transforming growth factor, beta 1's molecular function is recorded as type II transforming growth factor beta receptor binding^[16].
Transforming growth factor, beta 1's molecular function is recorded as type III transforming growth factor beta receptor binding^[17].
Transforming growth factor, beta 1's molecular function is recorded as cytokine activity^[18].
Transforming growth factor, beta 1's molecular function is recorded as enzyme binding^[19].
Transforming growth factor, beta 1's molecular function is recorded as transforming growth factor beta receptor binding^[20].
Transforming growth factor, beta 1's molecular function is recorded as growth factor activity^[21].
Transforming growth factor, beta 1's molecular function is recorded as antigen binding^[22].
Transforming growth factor, beta 1's molecular function is recorded as type I transforming growth factor beta receptor binding^[23].
Transforming growth factor, beta 1's molecular function is recorded as protein serine/threonine kinase activator activity^[24].
Transforming growth factor, beta 1's molecular function is recorded as protein binding^[25].
Transforming growth factor, beta 1's molecular function is recorded as identical protein binding^[26].

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Quick Facts

Instance of protein

Subclass 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, skeletal system development, tolerance induction to self antigen, positive regulation of protein phosphorylation, endoderm development, response to cholesterol, ureteric bud development, positive regulation of MAP kinase activity, regulation of sodium ion transport, response to progesterone, negative regulation of cell cycle, mammary gland development, T cell homeostasis, negative regulation of ossification, negative regulation of hyaluronan biosynthetic process, T cell differentiation, positive regulation of vascular permeability, positive regulation of blood vessel endothelial cell migration, negative regulation of epithelial cell proliferation, regulation of binding, animal organ morphogenesis, inner ear development, 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, regulation of MAPK cascade, SMAD protein signal transduction, epidermal growth factor receptor signaling pathway, negative regulation of blood vessel endothelial cell migration, positive regulation of protein dephosphorylation, extrinsic apoptotic signaling pathway, mitotic cell cycle checkpoint signaling, positive regulation of fibroblast proliferation, negative regulation of cell differentiation, regulation of branching involved in mammary gland duct morphogenesis, negative regulation of gene expression, cell activation, positive regulation of peptidyl-serine phosphorylation, negative regulation of T cell proliferation, response to wounding, CD4-positive, CD25-positive, alpha-beta regulatory T cell lineage commitment, 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, 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, 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, female pregnancy, cellular response to organic cyclic compound, cellular calcium ion homeostasis, negative regulation of transcription by RNA polymerase II, response to glucose, positive regulation of epithelial to mesenchymal transition, mitigation of host defenses by virus, lens fiber cell differentiation, 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, 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, defense response, response to estradiol, response to hypoxia, hyaluronan catabolic process, regulation of CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation, 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 cell migration, positive regulation of regulatory T cell differentiation, cellular response to growth factor stimulus, positive regulation of pathway-restricted SMAD protein phosphorylation, regulation of regulatory T cell differentiation, mammary gland branching involved in thelarche, ageing, response to laminar fluid shear stress, myeloid dendritic cell differentiation, salivary gland morphogenesis, receptor catabolic process, T-helper 17 cell lineage commitment, 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 gene expression, positive regulation of NAD+ ADP-ribosyltransferase activity, 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, positive regulation of cell population proliferation, ossification involved in bone remodeling, positive regulation of superoxide anion generation, digestive tract development, skeletal muscle tissue development, 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, cellular response to insulin-like growth factor stimulus, vasculogenesis, embryonic liver development, cellular response to ionizing radiation, ventricular cardiac muscle tissue morphogenesis, heart valve morphogenesis, regulation of epithelial to mesenchymal transition involved in endocardial cushion formation, neural tube development, positive regulation of cardiac muscle cell differentiation, liver regeneration, cellular response to mechanical stimulus, development of the heart, regulation of SMAD protein signal transduction, neural tube closure, cell migration, negative regulation of production of miRNAs involved in gene silencing by miRNA, response to immobilization stress, BMP signaling pathway, membrane protein intracellular domain proteolysis, positive regulation of transcription, DNA-templated, positive regulation of ERK1 and ERK2 cascade, positive regulation of pri-miRNA transcription by RNA polymerase II, transforming growth factor beta receptor signaling pathway involved in heart development, positive regulation of production of miRNAs involved in gene silencing by miRNA, regulation of signaling receptor activity, response to salt, osteoclast differentiation, morphogenesis of a branching structure, protein phosphorylation, negative regulation of neuroblast proliferation, response to organic substance, animal organ regeneration, positive regulation of exit from mitosis, wound healing, myelination, positive regulation of apoptotic process, positive regulation of epithelial cell proliferation, negative regulation of phagocytosis, negative regulation of immune response, positive regulation of NF-kappaB transcription factor activity, negative regulation of release of sequestered calcium ion into cytosol, cellular response to dexamethasone stimulus, positive regulation of mononuclear cell migration, positive regulation of branching involved in ureteric bud morphogenesis, positive regulation of gene expression, negative regulation of gene expression, negative regulation of biomineral tissue development, positive regulation of protein localization to nucleus, negative regulation of biomineral tissue development, positive regulation of protein localization to nucleus

Cell component cytoplasm, extracellular region, nucleus, microvillus, cell surface, extracellular space, blood microparticle, secretory granule, axon, extracellular matrix, soma, extracellular matrix

Encoded by Tgfb1

Found in taxon house mouse

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

Imported from wholeness_audit_2026-05-02

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

External References (4)

Ensembl protein id ENSMUSP00000002678, ENSMUSP00000130413

Refseq protein id NP_035707, XP_036008776

Unii T7D25J14LT

Uniprot protein id P04202

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 2022-05-25. wikidata.org.
[3] ↑ Transforming growth factor, beta 1 — subclass of (P279): protein. Q905695. Retrieved 2017-01-19. wikidata.org.
[4] ↑ Transforming growth factor, beta 1 — UniProt protein ID (P352): P04202. Q905695. Retrieved 2022-05-25. wikidata.org.
[5] ↑ Transforming growth factor, beta 1 — part of (P361): Transforming growth factor beta-1 proprotein. InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
[6] ↑ Transforming growth factor, beta 1 — part of (P361): Cystine-knot cytokine. InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
[7] ↑ Transforming growth factor, beta 1 — part of (P361): Transforming growth factor-beta, C-terminal domain, protein family. wikidata.org.
[8] ↑ Transforming growth factor, beta 1 — part of (P361): TGF-beta, propeptide family. wikidata.org.
[9] ↑ Transforming growth factor, beta 1 — part of (P361): Transforming growth factor beta, conserved site, protein family. wikidata.org.
[10] ↑ 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.
[11] ↑ 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.
[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_035707. Q20641742. Retrieved 2022-03-20. wikidata.org.
[14] ↑ Transforming growth factor, beta 1 — RefSeq protein ID (P637): XP_036008776. Q20641742. Retrieved 2022-03-20. wikidata.org.
[15] ↑ Transforming growth factor, beta 1 — UNII (P652): T7D25J14LT. wikidata.org.
[16] ↑ Transforming growth factor, beta 1 — molecular function (P680): type II transforming growth factor beta receptor binding. GOA. Retrieved 2018-06-21. ebi.ac.uk. Provenance: wikidata.org.
[17] ↑ Transforming growth factor, beta 1 — molecular function (P680): type III transforming growth factor beta receptor binding. GOA. Retrieved 2018-06-21. ebi.ac.uk. Provenance: wikidata.org.
[18] ↑ Transforming growth factor, beta 1 — molecular function (P680): cytokine activity. GOA. Retrieved 2018-06-21. ebi.ac.uk. Provenance: wikidata.org.
[19] ↑ Transforming growth factor, beta 1 — molecular function (P680): enzyme binding. GOA. Retrieved 2018-06-21. ebi.ac.uk. Provenance: wikidata.org.
[20] ↑ Transforming growth factor, beta 1 — molecular function (P680): transforming growth factor beta receptor binding. Targeted disruption of the mouse transforming growth factor-beta 1 gene results in multifocal inflammatory disease. Retrieved 2018-06-21. ebi.ac.uk. Provenance: wikidata.org.
[21] ↑ Transforming growth factor, beta 1 — molecular function (P680): growth factor activity. GOA. Retrieved 2018-06-21. ebi.ac.uk. Provenance: wikidata.org.
[22] ↑ Transforming growth factor, beta 1 — molecular function (P680): antigen binding. GOA. Retrieved 2018-06-21. ebi.ac.uk. Provenance: wikidata.org.
[23] ↑ Transforming growth factor, beta 1 — molecular function (P680): type I transforming growth factor beta receptor binding. GOA. Retrieved 2018-06-21. ebi.ac.uk. Provenance: wikidata.org.
[24] ↑ Transforming growth factor, beta 1 — molecular function (P680): protein serine/threonine kinase activator activity. Galectin-9-CD44 interaction enhances stability and function of adaptive regulatory T cells. Retrieved 2018-06-21. ebi.ac.uk. Provenance: wikidata.org.
[25] ↑ Transforming growth factor, beta 1 — molecular function (P680): protein binding. GOA. Retrieved 2018-06-21. ebi.ac.uk. Provenance: wikidata.org.
[26] ↑ Transforming growth factor, beta 1 — molecular function (P680): identical protein binding. GOA. Retrieved 2018-06-21. ebi.ac.uk. Provenance: 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

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BibTeX

@misc{4ortxyz_transforming-growth-factor-beta-1-q14904616_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Transforming growth factor, beta 1}}, year = {2026}, url = {https://4ort.xyz/entity/transforming-growth-factor-beta-1-q14904616}, 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-q14904616 (retrieved 2026-05-03)

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