TGFB1

TGFB1
Наявні структури
PDB	Пошук ортологів: PDBe RCSB
Список кодів PDB
	1KLA, 1KLC, 1KLD, 3KFD, 4KV5
Ідентифікатори
Символи	TGFB1, CED, DPD1, LAP, TGFB, TGFbeta, transforming growth factor beta 1, IBDIMDE, TGF-beta1
Зовнішні ІД	OMIM: 190180 MGI: 98725 HomoloGene: 540 GeneCards: TGFB1
Пов'язані генетичні захворювання
	Camurati-Engelmann disease
Онтологія гена
Молекулярна функція	• type II transforming growth factor beta receptor binding; • зв'язування з N-кінцем білка; • активність цитокінів; • enzyme binding; • growth factor activity; • GO:0003823, GO:0051635 antigen binding; • type I transforming growth factor beta receptor binding; • гомодимеризація білків; • protein serine/threonine kinase activator activity; • GO:0001948, GO:0016582 зв’язування з білками плазми; • активність гетеродимеризації білків; • type III transforming growth factor beta receptor binding; • transforming growth factor beta receptor binding; • identical protein binding;
Клітинна компонента	• цитоплазма; • extracellular region; • клітинне ядро; • Мікроворсинки; • поверхня клітини; • мікрочастинка крові; • клітинна мембрана; • секреторна гранула; • аксон; • сома; • Golgi lumen; • platelet alpha granule lumen; • GO:0005578 позаклітинний матрикс; • міжклітинний простір;
Біологічний процес	• 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; • відгук на органічну речовину; • mammary gland development; • T cell homeostasis; • пригнічення осифікації; • 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; • розвиток внутрішнього вуха; • myelination; • negative regulation of macrophage cytokine production; • проліферація; • transforming growth factor beta receptor signaling pathway; • face morphogenesis; • негативна регуляція проліферації клітин; • 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; • GO:0051247, GO:0051200 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; • GO:0060469, GO:0009371 позитивна регуляція транскрипції, ДНК-шаблонна; • 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; • позитивна регуляція імпорту білків у ядро; • 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; • Сигнальний шлях Notch; • GO:0033128 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; • жіноча вагітність; • GO:1904579 cellular response to organic cyclic compound; • positive regulation of extracellular matrix assembly; • cellular calcium ion homeostasis; • Загоєння ран; • GO:1901227 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; • GO:0019049, GO:0030683 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; • Епітеліально-мезенхімальний перехід; • phosphate-containing compound metabolic process; • регуляція експресії генів; • 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; • GO:0045996 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; • GO:1904578 response to organic cyclic compound; • positive regulation of protein-containing complex assembly; • protein kinase B signaling; • negative regulation of cell-cell adhesion; • GO:1905617 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; • GO:0010260 старіння людини; • regulation of regulatory T cell differentiation; • дегрануляція тромбоцитів; • 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; • позитивна регуляція апоптозу; • 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; • GO:0003257, GO:0010735, GO:1901228, GO:1900622, GO:1904488 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; • GO:1901313 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; • клітинна відповідь на іонізуюче випромінювання; • васкулогенез; • 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; • розвиток клітин; • GO:0097285 апоптоз; • 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;
	Джерела:Amigo / QuickGO
Шаблон експресії
	; ;
	Більше даних
Ортологи
	7040
	21803
	ENSG00000105329
	ENSMUSG00000002603
	P01137
	P04202
	NM_000660
	NM_011577
	NP_000651
	NP_035707
	Вікідані
Див./Ред. для людей	Див./Ред. для мишей

TGFB1 (англ. Transforming growth factor beta 1) – білок, який кодується однойменним геном, розташованим у людей на короткому плечі 19-ї хромосоми.^[4] Довжина поліпептидного ланцюга білка становить 390 амінокислот, а молекулярна маса — 44 341^[5].

Послідовність амінокислот

10	20	30	40	50
MPPSGLRLLL	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

A: Аланін
C: Цистеїн
D: Аспарагінова кислота
E: Глутамінова кислота
F: Фенілаланін
G: Гліцин
H: Гістидин
I: Ізолейцин
K: Лізин
L: Лейцин
M: Метіонін
N: Аспарагін
P: Пролін
Q: Глутамін
R: Аргінін
S: Серин
T: Треонін
V: Валін
W: Триптофан

Y: Тирозин

Кодований геном білок за функціями належить до факторів росту, мітогенів. Локалізований у позаклітинному матриксі. Також секретований назовні.

Література

Derynck R., Rhee L., Chen E.Y., van Tilburg A. (1987). Intron-exon structure of the human transforming growth factor-beta precursor gene. Nucleic Acids Res. 15: 3188—3189. PMID 3470709 doi:10.1093/nar/15.7.3188
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 14: 2121—2127. 2004. PMID 15489334 doi:10.1101/gr.2596504
Okamoto O., Fujiwara S., Abe M., Sato Y. (1999). Dermatopontin interacts with transforming growth factor beta and enhances its biological activity. Biochem. J. 337: 537—541. PMID 9895299 doi:10.1042/bj3370537
Shur I., Lokiec F., Bleiberg I., Benayahu D. (2001). Differential gene expression of cultured human osteoblasts. J. Cell. Biochem. 83: 547—553. PMID 11746498 doi:10.1002/jcb.1249
Lewandrowski U., Moebius J., Walter U., Sickmann A. (2006). Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach. Mol. Cell. Proteomics. 5: 226—233. PMID 16263699 doi:10.1074/mcp.M500324-MCP200
Suzuki S., Kulkarni A.B. (2010). Extracellular heat shock protein HSP90beta secreted by MG63 osteosarcoma cells inhibits activation of latent TGF-beta1. Biochem. Biophys. Res. Commun. 398: 525—531. PMID 20599762 doi:10.1016/j.bbrc.2010.06.112