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Transforming growth factor beta-1 (TGF-beta-1) [Cleaved into: Latency-associated peptide (LAP)]

 TGFB1_MOUSE             Reviewed;         390 AA.
P04202;
20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
20-MAR-1987, sequence version 1.
22-NOV-2017, entry version 194.
RecName: Full=Transforming growth factor beta-1;
Short=TGF-beta-1;
Contains:
RecName: Full=Latency-associated peptide;
Short=LAP;
Flags: Precursor;
Name=Tgfb1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3007454;
Derynck R., Jarrett J.A., Chen E.Y., Goeddel D.V.;
"The murine transforming growth factor-beta precursor.";
J. Biol. Chem. 261:4377-4379(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=BALB/cJ;
PubMed=8522200; DOI=10.1016/0378-1119(95)00460-N;
Guron C., Sudarshan C., Raghow R.;
"Molecular organization of the gene encoding murine transforming
growth factor beta 1.";
Gene 165:325-326(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J, and NOD/LT; TISSUE=Spleen;
Poirot L., Benoist C., Mathis D.;
"Transforming growth factor-beta 1 sequence and expression: no
difference between NOD/Lt and C57Bl/6 mouse strains.";
Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
INTERACTION WITH NREP.
PubMed=14985127; DOI=10.1016/j.bbrc.2004.01.171;
Paliwal S., Shi J., Dhru U., Zhou Y., Schuger L.;
"P311 binds to the latency associated protein and downregulates the
expression of TGF-beta1 and TGF-beta2.";
Biochem. Biophys. Res. Commun. 315:1104-1109(2004).
[6]
INTERACTION WITH HTRA3.
PubMed=15206957; DOI=10.1111/j.1440-169X.2004.00743.x;
Tocharus J., Tsuchiya A., Kajikawa M., Ueta Y., Oka C., Kawaichi M.;
"Developmentally regulated expression of mouse HtrA3 and its role as
an inhibitor of TGF-beta signaling.";
Dev. Growth Differ. 46:257-274(2004).
[7]
INTERACTION WITH HTRA1.
PubMed=14973287; DOI=10.1242/dev.00999;
Oka C., Tsujimoto R., Kajikawa M., Koshiba-Takeuchi K., Ina J.,
Yano M., Tsuchiya A., Ueta Y., Soma A., Kanda H., Matsumoto M.,
Kawaichi M.;
"HtrA1 serine protease inhibits signaling mediated by Tgfbeta family
proteins.";
Development 131:1041-1053(2004).
[8]
FUNCTION.
PubMed=18368049; DOI=10.1038/nature06878;
Zhou L., Lopes J.E., Chong M.M., Ivanov I.I., Min R., Victora G.D.,
Shen Y., Du J., Rubtsov Y.P., Rudensky A.Y., Ziegler S.F.,
Littman D.R.;
"TGF-beta-induced Foxp3 inhibits T(H)17 cell differentiation by
antagonizing RORgammat function.";
Nature 453:236-240(2008).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[10]
INTERACTION WITH THSD4.
PubMed=21880733; DOI=10.1074/jbc.M111.243451;
Saito M., Kurokawa M., Oda M., Oshima M., Tsutsui K., Kosaka K.,
Nakao K., Ogawa M., Manabe R., Suda N., Ganjargal G., Hada Y.,
Noguchi T., Teranaka T., Sekiguchi K., Yoneda T., Tsuji T.;
"ADAMTSL6beta protein rescues fibrillin-1 microfibril disorder in a
Marfan syndrome mouse model through the promotion of fibrillin-1
assembly.";
J. Biol. Chem. 286:38602-38613(2011).
[11]
FUNCTION.
PubMed=22781750; DOI=10.1016/j.cellsig.2012.07.003;
Bruce D.L., Macartney T., Yong W., Shou W., Sapkota G.P.;
"Protein phosphatase 5 modulates SMAD3 function in the transforming
growth factor-beta pathway.";
Cell. Signal. 24:1999-2006(2012).
-!- FUNCTION: Multifunctional protein that controls proliferation,
differentiation and other functions in many cell types. Many cells
synthesize TGFB1 and have specific receptors for it. It positively
and negatively regulates many other growth factors. It plays an
important role in bone remodeling as it is a potent stimulator of
osteoblastic bone formation, causing chemotaxis, proliferation and
differentiation in committed osteoblasts (PubMed:22781750).
Stimulates sustained production of collagen through the activation
of CREB3L1 by regulated intramembrane proteolysis (RIP) (By
similarity). Can promote either T-helper 17 cells (Th17) or
regulatory T-cells (Treg) lineage differentiation in a
concentration-dependent manner. At high concentrations, leads to
FOXP3-mediated suppression of RORC and down-regulation of IL-17
expression, favoring Treg cell development. At low concentrations
in concert with IL-6 and IL-21, leads to expression of the IL-17
and IL-23 receptors, favoring differentiation to Th17 cells
(PubMed:18368049). Mediates SMAD2/3 activation by inducing its
phosphorylation and subsequent translocation to the nucleus. Can
induce epithelial-to-mesenchymal transition (EMT) and cell
migration in various cell types (By similarity).
{ECO:0000250|UniProtKB:P01137, ECO:0000269|PubMed:18368049,
ECO:0000269|PubMed:22781750}.
-!- SUBUNIT: Homodimer; disulfide-linked, or heterodimer with TGFB2
(By similarity). Secreted and stored as a biologically inactive
form in the extracellular matrix in a 290 kDa complex (large
latent TGF-beta1 complex) containing the TGFB1 homodimer, the
latency-associated peptide (LAP), and the latent TGFB1 binding
protein-1 (LTBP1). The complex without LTBP1 is known as the'small
latent TGF-beta1 complex'. Dissociation of the TGFB1 from LAP is
required for growth factor activation and biological activity.
Release of the large latent TGF-beta1 complex from the
extracellular matrix is carried out by the matrix
metalloproteinase MMP3 (By similarity). Interacts with CD109 and
DPT. Interacts with ASPN (By similarity). May interact with THSD4;
this interaction may lead to sequestration by FBN1 microfibril
assembly and attenuation of TGFB signaling. Interacts with the
serine proteases, HTRA1 and HTRA3: the interaction with either
inhibits TGFB1-mediated signaling. The HTRA protease activity is
required for this inhibition. Latency-associated peptide interacts
with NREP; the interaction results in a decrease in TGFB1
autoinduction. Interacts (via processed form (LAP)) with HSP90AB1;
inhibits latent TGFB1 activation (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:P01137, ECO:0000269|PubMed:14973287,
ECO:0000269|PubMed:14985127, ECO:0000269|PubMed:15206957,
ECO:0000269|PubMed:21880733}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000250}.
-!- DOMAIN: The 'straitjacket' and 'arm' domains encircle the growth
factor monomers and are fastened together by strong bonding
between Lys-56 and Tyr-103/Tyr-104. Activation of TGF-beta1
requires the binding of integrin alpha-V to an RGD sequence in the
prodomain and exertion of force on this domain, which is held in
the extracellular matrix by latent TGF-beta binding proteins. The
sheer physical force unfastens the straitjacket and releases the
active growth factor dimer (By similarity). {ECO:0000250}.
-!- PTM: Glycosylated. {ECO:0000250}.
-!- PTM: The precursor is cleaved into mature TGF-beta-1 and LAP,
which remains non-covalently linked to mature TGF-beta-1 rendering
it inactive. {ECO:0000250}.
-!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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EMBL; M13177; AAA40423.1; -; mRNA.
EMBL; L42462; AAB00138.1; -; Genomic_DNA.
EMBL; L42456; AAB00138.1; JOINED; Genomic_DNA.
EMBL; L42457; AAB00138.1; JOINED; Genomic_DNA.
EMBL; L42458; AAB00138.1; JOINED; Genomic_DNA.
EMBL; L42459; AAB00138.1; JOINED; Genomic_DNA.
EMBL; L42460; AAB00138.1; JOINED; Genomic_DNA.
EMBL; L42461; AAB00138.1; JOINED; Genomic_DNA.
EMBL; AJ009862; CAA08900.1; -; mRNA.
EMBL; BC013738; AAH13738.1; -; mRNA.
CCDS; CCDS20993.1; -.
PIR; A01396; WFMS2.
RefSeq; NP_035707.1; NM_011577.2.
UniGene; Mm.248380; -.
ProteinModelPortal; P04202; -.
SMR; P04202; -.
BioGrid; 204157; 4.
DIP; DIP-48640N; -.
IntAct; P04202; 1.
STRING; 10090.ENSMUSP00000002678; -.
iPTMnet; P04202; -.
PhosphoSitePlus; P04202; -.
EPD; P04202; -.
PaxDb; P04202; -.
PeptideAtlas; P04202; -.
PRIDE; P04202; -.
Ensembl; ENSMUST00000002678; ENSMUSP00000002678; ENSMUSG00000002603.
GeneID; 21803; -.
KEGG; mmu:21803; -.
UCSC; uc009ftq.1; mouse.
CTD; 7040; -.
MGI; MGI:98725; Tgfb1.
eggNOG; KOG3900; Eukaryota.
eggNOG; ENOG410XT8Z; LUCA.
GeneTree; ENSGT00760000119112; -.
HOGENOM; HOG000290198; -.
HOVERGEN; HBG074115; -.
InParanoid; P04202; -.
KO; K13375; -.
OMA; AENKYSQ; -.
OrthoDB; EOG091G0BMM; -.
PhylomeDB; P04202; -.
TreeFam; TF318514; -.
Reactome; R-MMU-114608; Platelet degranulation.
Reactome; R-MMU-202733; Cell surface interactions at the vascular wall.
Reactome; R-MMU-2129379; Molecules associated with elastic fibres.
Reactome; R-MMU-2173788; Downregulation of TGF-beta receptor signaling.
Reactome; R-MMU-2173789; TGF-beta receptor signaling activates SMADs.
Reactome; R-MMU-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
Reactome; R-MMU-3000170; Syndecan interactions.
Reactome; R-MMU-442533; Transcriptional Regulation of Adipocyte Differentiation in 3T3-L1 Pre-adipocytes.
Reactome; R-MMU-8941855; RUNX3 regulates CDKN1A transcription.
Reactome; R-MMU-8941858; Regulation of RUNX3 expression and activity.
Reactome; R-MMU-8951936; RUNX3 regulates p14-ARF.
PMAP-CutDB; P04202; -.
PRO; PR:P04202; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000002603; -.
CleanEx; MM_TGFB1; -.
ExpressionAtlas; P04202; baseline and differential.
Genevisible; P04202; MM.
GO; GO:0030424; C:axon; IEA:Ensembl.
GO; GO:0072562; C:blood microparticle; ISS:AgBase.
GO; GO:0009986; C:cell surface; ISS:BHF-UCL.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0031012; C:extracellular matrix; ISO:MGI.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005902; C:microvillus; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005578; C:proteinaceous extracellular matrix; IDA:MGI.
GO; GO:0030141; C:secretory granule; IEA:Ensembl.
GO; GO:0003823; F:antigen binding; ISS:AgBase.
GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0047485; F:protein N-terminus binding; IEA:Ensembl.
GO; GO:0043539; F:protein serine/threonine kinase activator activity; IDA:UniProtKB.
GO; GO:0005160; F:transforming growth factor beta receptor binding; IPI:MGI.
GO; GO:0034713; F:type I transforming growth factor beta receptor binding; ISS:AgBase.
GO; GO:0005114; F:type II transforming growth factor beta receptor binding; ISS:UniProtKB.
GO; GO:0034714; F:type III transforming growth factor beta receptor binding; ISS:AgBase.
GO; GO:0002460; P:adaptive immune response based on somatic recombination of immune receptors built from immunoglobulin superfamily domains; IDA:BHF-UCL.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0009887; P:animal organ morphogenesis; TAS:MGI.
GO; GO:0006754; P:ATP biosynthetic process; ISS:UniProtKB.
GO; GO:0030509; P:BMP signaling pathway; IBA:GO_Central.
GO; GO:0060751; P:branch elongation involved in mammary gland duct branching; IMP:MGI.
GO; GO:0002362; P:CD4-positive, CD25-positive, alpha-beta regulatory T cell lineage commitment; TAS:UniProtKB.
GO; GO:0001775; P:cell activation; IDA:MGI.
GO; GO:0007050; P:cell cycle arrest; ISS:UniProtKB.
GO; GO:0016049; P:cell growth; IEA:InterPro.
GO; GO:0016477; P:cell migration; ISS:UniProtKB.
GO; GO:0008283; P:cell proliferation; IDA:MGI.
GO; GO:0045216; P:cell-cell junction organization; ISS:UniProtKB.
GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:MGI.
GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
GO; GO:0071363; P:cellular response to growth factor stimulus; IDA:MGI.
GO; GO:1990314; P:cellular response to insulin-like growth factor stimulus; IEA:Ensembl.
GO; GO:0071479; P:cellular response to ionizing radiation; IEA:Ensembl.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0071407; P:cellular response to organic cyclic compound; ISS:UniProtKB.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IDA:MGI.
GO; GO:0002062; P:chondrocyte differentiation; ISS:UniProtKB.
GO; GO:0007182; P:common-partner SMAD protein phosphorylation; ISS:UniProtKB.
GO; GO:0006952; P:defense response; TAS:MGI.
GO; GO:0009817; P:defense response to fungus, incompatible interaction; IEA:Ensembl.
GO; GO:0048565; P:digestive tract development; IEA:Ensembl.
GO; GO:1990402; P:embryonic liver development; IMP:BHF-UCL.
GO; GO:0007492; P:endoderm development; IDA:MGI.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:UniProtKB.
GO; GO:0019049; P:evasion or tolerance of host defenses by virus; ISS:UniProtKB.
GO; GO:0085029; P:extracellular matrix assembly; IDA:BHF-UCL.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; ISS:BHF-UCL.
GO; GO:0060325; P:face morphogenesis; IEP:UniProtKB.
GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
GO; GO:0060364; P:frontal suture morphogenesis; IEA:Ensembl.
GO; GO:0008354; P:germ cell migration; IDA:MGI.
GO; GO:0007507; P:heart development; IMP:BHF-UCL.
GO; GO:0003179; P:heart valve morphogenesis; IMP:BHF-UCL.
GO; GO:0002244; P:hematopoietic progenitor cell differentiation; ISS:UniProtKB.
GO; GO:0030214; P:hyaluronan catabolic process; ISS:UniProtKB.
GO; GO:0006954; P:inflammatory response; IMP:MGI.
GO; GO:0048839; P:inner ear development; IEA:Ensembl.
GO; GO:0070306; P:lens fiber cell differentiation; IMP:MGI.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
GO; GO:0048535; P:lymph node development; IMP:MGI.
GO; GO:0060744; P:mammary gland branching involved in thelarche; IMP:MGI.
GO; GO:0030879; P:mammary gland development; IDA:MGI.
GO; GO:0000165; P:MAPK cascade; ISS:UniProtKB.
GO; GO:0031293; P:membrane protein intracellular domain proteolysis; ISS:UniProtKB.
GO; GO:0007093; P:mitotic cell cycle checkpoint; ISS:UniProtKB.
GO; GO:0032943; P:mononuclear cell proliferation; IMP:MGI.
GO; GO:0042552; P:myelination; IEA:Ensembl.
GO; GO:0043011; P:myeloid dendritic cell differentiation; IMP:MGI.
GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; ISS:UniProtKB.
GO; GO:0045786; P:negative regulation of cell cycle; ISS:UniProtKB.
GO; GO:0030308; P:negative regulation of cell growth; IDA:BHF-UCL.
GO; GO:0008285; P:negative regulation of cell proliferation; ISS:UniProtKB.
GO; GO:0022408; P:negative regulation of cell-cell adhesion; ISS:UniProtKB.
GO; GO:0008156; P:negative regulation of DNA replication; ISS:UniProtKB.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISS:UniProtKB.
GO; GO:0045599; P:negative regulation of fat cell differentiation; ISS:UniProtKB.
GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
GO; GO:0060965; P:negative regulation of gene silencing by miRNA; ISO:MGI.
GO; GO:1900126; P:negative regulation of hyaluronan biosynthetic process; ISS:UniProtKB.
GO; GO:0032700; P:negative regulation of interleukin-17 production; IDA:UniProtKB.
GO; GO:0010936; P:negative regulation of macrophage cytokine production; ISS:AgBase.
GO; GO:0045930; P:negative regulation of mitotic cell cycle; ISS:UniProtKB.
GO; GO:0045662; P:negative regulation of myoblast differentiation; ISS:UniProtKB.
GO; GO:0007406; P:negative regulation of neuroblast proliferation; IEA:Ensembl.
GO; GO:0030279; P:negative regulation of ossification; IDA:MGI.
GO; GO:0050765; P:negative regulation of phagocytosis; IEA:Ensembl.
GO; GO:1903799; P:negative regulation of production of miRNAs involved in gene silencing by miRNA; ISO:MGI.
GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; ISO:MGI.
GO; GO:0001933; P:negative regulation of protein phosphorylation; ISS:UniProtKB.
GO; GO:0051280; P:negative regulation of release of sequestered calcium ion into cytosol; IEA:Ensembl.
GO; GO:0048642; P:negative regulation of skeletal muscle tissue development; ISS:UniProtKB.
GO; GO:0050868; P:negative regulation of T cell activation; IMP:MGI.
GO; GO:0042130; P:negative regulation of T cell proliferation; IMP:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0001843; P:neural tube closure; IMP:BHF-UCL.
GO; GO:0021915; P:neural tube development; IMP:BHF-UCL.
GO; GO:0007219; P:Notch signaling pathway; IDA:MGI.
GO; GO:0014003; P:oligodendrocyte development; IMP:CACAO.
GO; GO:0043932; P:ossification involved in bone remodeling; ISS:AgBase.
GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; IDA:BHF-UCL.
GO; GO:0006796; P:phosphate-containing compound metabolic process; ISS:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISS:UniProtKB.
GO; GO:0030501; P:positive regulation of bone mineralization; ISS:AgBase.
GO; GO:0090190; P:positive regulation of branching involved in ureteric bud morphogenesis; IEA:Ensembl.
GO; GO:2000727; P:positive regulation of cardiac muscle cell differentiation; ISO:MGI.
GO; GO:0071158; P:positive regulation of cell cycle arrest; IDA:MGI.
GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
GO; GO:0030335; P:positive regulation of cell migration; ISS:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:MGI.
GO; GO:0032270; P:positive regulation of cellular protein metabolic process; ISS:UniProtKB.
GO; GO:0050921; P:positive regulation of chemotaxis; ISS:UniProtKB.
GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IDA:BHF-UCL.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Ensembl.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IDA:MGI.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
GO; GO:0031536; P:positive regulation of exit from mitosis; IEA:Ensembl.
GO; GO:0010763; P:positive regulation of fibroblast migration; IMP:MGI.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IDA:MGI.
GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
GO; GO:0035066; P:positive regulation of histone acetylation; IDA:MGI.
GO; GO:0031065; P:positive regulation of histone deacetylation; IDA:MGI.
GO; GO:0032740; P:positive regulation of interleukin-17 production; IDA:BHF-UCL.
GO; GO:0048298; P:positive regulation of isotype switching to IgA isotypes; ISS:AgBase.
GO; GO:0043406; P:positive regulation of MAP kinase activity; ISS:UniProtKB.
GO; GO:0071677; P:positive regulation of mononuclear cell migration; IEA:Ensembl.
GO; GO:1901666; P:positive regulation of NAD+ ADP-ribosyltransferase activity; ISS:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
GO; GO:0042482; P:positive regulation of odontogenesis; IDA:MGI.
GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; ISS:UniProtKB.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISS:UniProtKB.
GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; ISS:UniProtKB.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; ISS:UniProtKB.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription from RNA polymerase II promoter; ISO:MGI.
GO; GO:1903800; P:positive regulation of production of miRNAs involved in gene silencing by miRNA; ISO:MGI.
GO; GO:0031334; P:positive regulation of protein complex assembly; ISS:UniProtKB.
GO; GO:0035307; P:positive regulation of protein dephosphorylation; ISS:UniProtKB.
GO; GO:0042307; P:positive regulation of protein import into nucleus; ISS:AgBase.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISS:UniProtKB.
GO; GO:1900182; P:positive regulation of protein localization to nucleus; IGI:MGI.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS:UniProtKB.
GO; GO:0050714; P:positive regulation of protein secretion; ISS:UniProtKB.
GO; GO:1903911; P:positive regulation of receptor clustering; IDA:UniProtKB.
GO; GO:0045591; P:positive regulation of regulatory T cell differentiation; IMP:UniProtKB.
GO; GO:0060391; P:positive regulation of SMAD protein import into nucleus; ISS:AgBase.
GO; GO:0051152; P:positive regulation of smooth muscle cell differentiation; ISO:MGI.
GO; GO:0032930; P:positive regulation of superoxide anion generation; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; ISS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0043117; P:positive regulation of vascular permeability; ISO:MGI.
GO; GO:0006611; P:protein export from nucleus; ISS:UniProtKB.
GO; GO:0000060; P:protein import into nucleus, translocation; ISS:UniProtKB.
GO; GO:0043491; P:protein kinase B signaling; ISS:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:0032801; P:receptor catabolic process; ISS:UniProtKB.
GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; IGI:MGI.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0051098; P:regulation of binding; IDA:MGI.
GO; GO:0060762; P:regulation of branching involved in mammary gland duct morphogenesis; IGI:MGI.
GO; GO:0061035; P:regulation of cartilage development; IDA:MGI.
GO; GO:0032829; P:regulation of CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation; TAS:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; IDA:MGI.
GO; GO:0051101; P:regulation of DNA binding; IDA:MGI.
GO; GO:0010468; P:regulation of gene expression; IDA:MGI.
GO; GO:0032667; P:regulation of interleukin-23 production; IDA:UniProtKB.
GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
GO; GO:0042306; P:regulation of protein import into nucleus; IDA:MGI.
GO; GO:0045589; P:regulation of regulatory T cell differentiation; IGI:MGI.
GO; GO:0060390; P:regulation of SMAD protein import into nucleus; ISS:UniProtKB.
GO; GO:0002028; P:regulation of sodium ion transport; IDA:MGI.
GO; GO:0016202; P:regulation of striated muscle tissue development; IDA:MGI.
GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
GO; GO:0045066; P:regulatory T cell differentiation; IDA:MGI.
GO; GO:0070723; P:response to cholesterol; ISS:UniProtKB.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; ISS:UniProtKB.
GO; GO:0009749; P:response to glucose; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0035902; P:response to immobilization stress; IEA:Ensembl.
GO; GO:0034616; P:response to laminar fluid shear stress; IEA:Ensembl.
GO; GO:0032570; P:response to progesterone; ISS:UniProtKB.
GO; GO:0033280; P:response to vitamin D; IEA:Ensembl.
GO; GO:0009611; P:response to wounding; ISS:AgBase.
GO; GO:0007435; P:salivary gland morphogenesis; ISS:AgBase.
GO; GO:0007519; P:skeletal muscle tissue development; TAS:MGI.
GO; GO:0001501; P:skeletal system development; TAS:MGI.
GO; GO:0007183; P:SMAD protein complex assembly; ISS:UniProtKB.
GO; GO:0007184; P:SMAD protein import into nucleus; ISS:UniProtKB.
GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
GO; GO:0042110; P:T cell activation; IDA:MGI.
GO; GO:0030217; P:T cell differentiation; IMP:MGI.
GO; GO:0043029; P:T cell homeostasis; IMP:MGI.
GO; GO:0072540; P:T-helper 17 cell lineage commitment; TAS:UniProtKB.
GO; GO:0002513; P:tolerance induction to self antigen; IMP:MGI.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:MGI.
GO; GO:1905313; P:transforming growth factor beta receptor signaling pathway involved in heart development; IMP:BHF-UCL.
GO; GO:0001657; P:ureteric bud development; IEP:UniProtKB.
GO; GO:0001570; P:vasculogenesis; IMP:BHF-UCL.
GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IMP:BHF-UCL.
GO; GO:0042060; P:wound healing; IEA:Ensembl.
Gene3D; 2.10.90.10; -; 1.
InterPro; IPR029034; Cystine-knot_cytokine.
InterPro; IPR001839; TGF-b_C.
InterPro; IPR001111; TGF-b_propeptide.
InterPro; IPR016319; TGF-beta.
InterPro; IPR015615; TGF-beta-rel.
InterPro; IPR003939; TGFb1.
InterPro; IPR017948; TGFb_CS.
PANTHER; PTHR11848; PTHR11848; 1.
Pfam; PF00019; TGF_beta; 1.
Pfam; PF00688; TGFb_propeptide; 1.
PIRSF; PIRSF001787; TGF-beta; 1.
PRINTS; PR01423; TGFBETA.
PRINTS; PR01424; TGFBETA1.
SMART; SM00204; TGFB; 1.
SUPFAM; SSF57501; SSF57501; 1.
PROSITE; PS00250; TGF_BETA_1; 1.
PROSITE; PS51362; TGF_BETA_2; 1.
1: Evidence at protein level;
Cleavage on pair of basic residues; Complete proteome; Disulfide bond;
Extracellular matrix; Glycoprotein; Growth factor; Mitogen;
Reference proteome; Secreted; Signal.
SIGNAL 1 29 {ECO:0000250}.
CHAIN 30 278 Latency-associated peptide.
/FTId=PRO_0000033766.
CHAIN 279 390 Transforming growth factor beta-1.
/FTId=PRO_0000033767.
REGION 30 74 Straightjacket domain. {ECO:0000250}.
REGION 75 271 Arm domain. {ECO:0000250}.
MOTIF 244 246 Cell attachment site. {ECO:0000255}.
CARBOHYD 82 82 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
CARBOHYD 136 136 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
CARBOHYD 176 176 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
DISULFID 33 33 Interchain (with C-1350 or C-1375 in
LTBP1); in inactive form. {ECO:0000250}.
DISULFID 223 223 Interchain (with C-225). {ECO:0000250}.
DISULFID 225 225 Interchain (with C-223). {ECO:0000250}.
DISULFID 285 294 {ECO:0000250}.
DISULFID 293 356 {ECO:0000250}.
DISULFID 322 387 {ECO:0000250}.
DISULFID 326 389 {ECO:0000250}.
DISULFID 355 355 Interchain. {ECO:0000250}.
SEQUENCE 390 AA; 44310 MW; 4381A51B711D689E CRC64;
MPPSGLRLLP LLLPLPWLLV LTPGRPAAGL STCKTIDMEL VKRKRIEAIR GQILSKLRLA
SPPSQGEVPP GPLPEAVLAL YNSTRDRVAG ESADPEPEPE ADYYAKEVTR VLMVDRNNAI
YEKTKDISHS IYMFFNTSDI REAVPEPPLL SRAELRLQRL KSSVEQHVEL YQKYSNNSWR
YLGNRLLTPT DTPEWLSFDV TGVVRQWLNQ GDGIQGFRFS AHCSCDSKDN KLHVEINGIS
PKRRGDLGTI HDMNRPFLLL MATPLERAQH LHSSRHRRAL DTNYCFSSTE KNCCVRQLYI
DFRKDLGWKW IHEPKGYHAN FCLGPCPYIW SLDTQYSKVL ALYNQHNPGA SASPCCVPQA
LEPLPIVYYV GRKPKVEQLS NMIVRSCKCS


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