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

 TGFB1_MOUSE             Reviewed;         390 AA.
P04202;
20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
20-MAR-1987, sequence version 1.
22-APR-2020, entry version 216.
RecName: Full=Transforming growth factor beta-1 proprotein;
Contains:
RecName: Full=Latency-associated peptide {ECO:0000250|UniProtKB:P01137};
Short=LAP;
Contains:
RecName: Full=Transforming growth factor beta-1 {ECO:0000250|UniProtKB:P01137};
Short=TGF-beta-1;
Flags: Precursor;
Name=Tgfb1 {ECO:0000312|MGI:MGI:98725};
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]
FUNCTION, AND INTERACTION WITH ITGAV AND ITGB6.
PubMed=10025398; DOI=10.1016/s0092-8674(00)80545-0;
Munger J.S., Huang X., Kawakatsu H., Griffiths M.J., Dalton S.L., Wu J.,
Pittet J.F., Kaminski N., Garat C., Matthay M.A., Rifkin D.B., Sheppard D.;
"The integrin alpha v beta 6 binds and activates latent TGF beta 1: a
mechanism for regulating pulmonary inflammation and fibrosis.";
Cell 96:319-328(1999).
[6]
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).
[7]
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).
[8]
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).
[9]
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).
[10]
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).
[11]
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).
[12]
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).
[13]
FUNCTION, AND INTERACTION WITH NRROS.
PubMed=29909984; DOI=10.1016/j.cell.2018.05.027;
Qin Y., Garrison B.S., Ma W., Wang R., Jiang A., Li J., Mistry M.,
Bronson R.T., Santoro D., Franco C., Robinton D.A., Stevens B., Rossi D.J.,
Lu C., Springer T.A.;
"A milieu molecule for TGF-beta required for microglia function in the
nervous system.";
Cell 174:156-171(2018).
-!- FUNCTION: Transforming growth factor beta-1 proprotein: Precursor of
the Latency-associated peptide (LAP) and Transforming growth factor
beta-1 (TGF-beta-1) chains, which constitute the regulatory and active
subunit of TGF-beta-1, respectively. {ECO:0000250|UniProtKB:P01137}.
-!- FUNCTION: [Latency-associated peptide]: Required to maintain the
Transforming growth factor beta-1 (TGF-beta-1) chain in a latent state
during storage in extracellular matrix (PubMed:29909984). Associates
non-covalently with TGF-beta-1 and regulates its activation via
interaction with 'milieu molecules', such as LTBP1, LRRC32/GARP and
LRRC33/NRROS, that control activation of TGF-beta-1 (PubMed:29909984).
Interaction with LRRC33/NRROS regulates activation of TGF-beta-1 in
macrophages and microglia (PubMed:29909984). Interaction with
LRRC32/GARP controls activation of TGF-beta-1 on the surface of
activated regulatory T-cells (Tregs) (By similarity). Interaction with
integrins (ITGAV:ITGB6 or ITGAV:ITGB8) results in distortion of the
Latency-associated peptide chain and subsequent release of the active
TGF-beta-1 (PubMed:10025398). {ECO:0000250|UniProtKB:P01137,
ECO:0000269|PubMed:10025398, ECO:0000269|PubMed:29909984}.
-!- FUNCTION: Transforming growth factor beta-1: Multifunctional protein
that regulates the growth and differentiation of various cell types and
is involved in various processes, such as normal development, immune
function, microglia function and responses to neurodegeneration
(PubMed:22781750, PubMed:29909984). Activation into mature form follows
different steps: following cleavage of the proprotein in the Golgi
apparatus, Latency-associated peptide (LAP) and Transforming growth
factor beta-1 (TGF-beta-1) chains remain non-covalently linked
rendering TGF-beta-1 inactive during storage in extracellular matrix
(By similarity). At the same time, LAP chain interacts with 'milieu
molecules', such as LTBP1, LRRC32/GARP and LRRC33/NRROS that control
activation of TGF-beta-1 and maintain it in a latent state during
storage in extracellular milieus (PubMed:29909984). TGF-beta-1 is
released from LAP by integrins (ITGAV:ITGB6 or ITGAV:ITGB8): integrin-
binding to LAP stabilizes an alternative conformation of the LAP bowtie
tail and results in distortion of the LAP chain and subsequent release
of the active TGF-beta-1 (PubMed:10025398) (By similarity). Once
activated following release of LAP, TGF-beta-1 acts by binding to TGF-
beta receptors (TGFBR1 and TGFBR2), which transduce signal (By
similarity). While expressed by many cells types, TGF-beta-1 only has a
very localized range of action within cell environment thanks to fine
regulation of its activation by Latency-associated peptide chain (LAP)
and 'milieu molecules' (PubMed:29909984). Plays an important role in
bone remodeling: acts as a potent stimulator of osteoblastic bone
formation, causing chemotaxis, proliferation and differentiation in
committed osteoblasts (PubMed:22781750). Can promote either T-helper 17
cells (Th17) or regulatory T-cells (Treg) lineage differentiation in a
concentration-dependent manner (PubMed:18368049). At high
concentrations, leads to FOXP3-mediated suppression of RORC and down-
regulation of IL-17 expression, favoring Treg cell development
(PubMed:18368049). 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). Stimulates sustained
production of collagen through the activation of CREB3L1 by regulated
intramembrane proteolysis (RIP) (By similarity). 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:10025398,
ECO:0000269|PubMed:18368049, ECO:0000269|PubMed:22781750,
ECO:0000269|PubMed:29909984}.
-!- SUBUNIT: Homodimer; disulfide-linked (By similarity). 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 (PubMed:14973287, PubMed:15206957). May
interact with THSD4; this interaction may lead to sequestration by FBN1
microfibril assembly and attenuation of TGFB signaling
(PubMed:21880733). Interacts with CD109, DPT and ASPN. Latency-
associated peptide: Homodimer; disulfide-linked (By similarity).
Latency-associated peptide: Interacts with Transforming growth factor
beta-1 (TGF-beta-1) chain; interaction is non-covalent and maintains
(TGF-beta-1) in a latent state; each Latency-associated peptide (LAP)
monomer interacts with TGF-beta-1 in the other monomer (By similarity).
Latency-associated peptide: Interacts with LTBP1; leading to regulate
activation of TGF-beta-1 (By similarity). Latency-associated peptide:
Interacts with LRRC32/GARP; leading to regulate activation of TGF-beta-
1 on the surface of activated regulatory T-cells (Tregs) (By
similarity). Latency-associated peptide: Interacts with LRRC33/NRROS;
leading to regulate activation of TGF-beta-1 in macrophages and
microglia (PubMed:29909984). Latency-associated peptide: Interacts (via
cell attachment site) with integrins ITGAV and ITGB6 (ITGAV:ITGB6),
leading to release of the active TGF-beta-1 (PubMed:10025398). Latency-
associated peptide: Interacts with NREP; the interaction results in a
decrease in TGFB1 autoinduction (PubMed:14985127). Latency-associated
peptide: Interacts with HSP90AB1; inhibits latent TGFB1 activation.
Transforming growth factor beta-1: Homodimer; disulfide-linked.
Transforming growth factor beta-1: Interacts with TGF-beta receptors
(TGFBR1 and TGFBR2), leading to signal transduction (By similarity).
{ECO:0000250|UniProtKB:P01137, ECO:0000269|PubMed:10025398,
ECO:0000269|PubMed:14973287, ECO:0000269|PubMed:14985127,
ECO:0000269|PubMed:15206957, ECO:0000269|PubMed:21880733,
ECO:0000269|PubMed:29909984}.
-!- SUBCELLULAR LOCATION: [Latency-associated peptide]: Secreted,
extracellular space, extracellular matrix
{ECO:0000250|UniProtKB:P01137}.
-!- SUBCELLULAR LOCATION: [Transforming growth factor beta-1]: Secreted
{ECO:0000250|UniProtKB:P01137}.
-!- DOMAIN: [Latency-associated peptide]: The 'straitjacket' and 'arm'
domains encircle the Transforming growth factor beta-1 (TGF-beta-1)
monomers and are fastened together by strong bonding between Lys-56 and
Tyr-103/Tyr-104. {ECO:0000250|UniProtKB:P07200}.
-!- DOMAIN: [Latency-associated peptide]: The cell attachment site motif
mediates binding to integrins (ITGAV:ITGB6 or ITGAV:ITGB8). The motif
locates to a long loop in the arm domain called the bowtie tail.
Integrin-binding stabilizes an alternative conformation of the bowtie
tail. Activation by integrin requires force application by the actin
cytoskeleton, which is resisted by the 'milieu molecules' (such as
LTBP1, LRRC32/GARP and/or LRRC33/NRROS), resulting in distortion of the
prodomain and release of the active TGF-beta-1.
{ECO:0000250|UniProtKB:P01137}.
-!- PTM: Transforming growth factor beta-1 proprotein: The precursor
proprotein is cleaved in the Golgi apparatus by FURIN to form
Transforming growth factor beta-1 (TGF-beta-1) and Latency-associated
peptide (LAP) chains, which remain non-covalently linked, rendering
TGF-beta-1 inactive. {ECO:0000250|UniProtKB:P01137}.
-!- PTM: [Latency-associated peptide]: N-glycosylated. Deglycosylation
leads to activation of Transforming growth factor beta-1 (TGF-beta-1);
mechanisms triggering deglycosylation-driven activation of TGF-beta-1
are however unclear. {ECO:0000250|UniProtKB:P01137}.
-!- 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.
SMR; P04202; -.
BioGrid; 204157; 4.
ComplexPortal; CPX-821; TGF-beta-1 complex.
ComplexPortal; CPX-823; TGF-beta-1-TGFR complex.
DIP; DIP-48640N; -.
IntAct; P04202; 1.
STRING; 10090.ENSMUSP00000002678; -.
iPTMnet; P04202; -.
PhosphoSitePlus; P04202; -.
CPTAC; non-CPTAC-3952; -.
EPD; P04202; -.
PaxDb; P04202; -.
PeptideAtlas; P04202; -.
PRIDE; P04202; -.
Antibodypedia; 4372; 1770 antibodies.
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; ENSGT00940000160457; -.
HOGENOM; CLU_039840_0_0_1; -.
InParanoid; P04202; -.
KO; K13375; -.
OMA; FSAHCSC; -.
OrthoDB; 643840at2759; -.
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-8941855; RUNX3 regulates CDKN1A transcription.
Reactome; R-MMU-8941858; Regulation of RUNX3 expression and activity.
Reactome; R-MMU-8951936; RUNX3 regulates p14-ARF.
PRO; PR:P04202; -.
Proteomes; UP000000589; Chromosome 7.
RNAct; P04202; protein.
Bgee; ENSMUSG00000002603; Expressed in bone marrow and 222 other tissues.
ExpressionAtlas; P04202; baseline and differential.
Genevisible; P04202; MM.
GO; GO:0030424; C:axon; ISO:MGI.
GO; GO:0072562; C:blood microparticle; ISS:AgBase.
GO; GO:0005623; C:cell; IEA:GOC.
GO; GO:0009986; C:cell surface; ISS:BHF-UCL.
GO; GO:0062023; C:collagen-containing extracellular matrix; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:MGI.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0043025; C:neuronal cell body; ISO:MGI.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0030141; C:secretory granule; ISO:MGI.
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:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
GO; GO:0043539; F:protein serine/threonine kinase activator activity; IDA:UniProtKB.
GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
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:0031100; P:animal organ regeneration; ISO:MGI.
GO; GO:0003180; P:aortic valve morphogenesis; IMP:BHF-UCL.
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:0016477; P:cell migration; ISS:UniProtKB.
GO; GO:0008283; P:cell population 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; ISO:MGI.
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:0061448; P:connective tissue development; IGI:MGI.
GO; GO:0006952; P:defense response; TAS:MGI.
GO; GO:0009817; P:defense response to fungus, incompatible interaction; ISO:MGI.
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: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:0001763; P:morphogenesis of a branching structure; ISO:MGI.
GO; GO:0046716; P:muscle cell cellular homeostasis; IGI:MGI.
GO; GO:0042552; P:myelination; ISO:MGI.
GO; GO:0043011; P:myeloid dendritic cell differentiation; IMP:MGI.
GO; GO:0070168; P:negative regulation of biomineral tissue development; IMP:BHF-UCL.
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 population proliferation; ISS:UniProtKB.
GO; GO:0022408; P:negative regulation of cell-cell adhesion; ISS:UniProtKB.
GO; GO:0045918; P:negative regulation of cytolysis; ISO:MGI.
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; IMP:BHF-UCL.
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:0050777; P:negative regulation of immune response; ISO:MGI.
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; ISO:MGI.
GO; GO:0030279; P:negative regulation of ossification; IDA:MGI.
GO; GO:0050765; P:negative regulation of phagocytosis; ISO:MGI.
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; ISO:MGI.
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 by RNA polymerase II; 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:0030316; P:osteoclast differentiation; IDA:MGI.
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; ISO:MGI.
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; ISO:MGI.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:MGI.
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 population 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; ISO:MGI.
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; ISO:MGI.
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:0014008; P:positive regulation of microglia differentiation; IMP:UniProtKB.
GO; GO:0071677; P:positive regulation of mononuclear cell migration; ISO:MGI.
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; ISO:MGI.
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 by RNA polymerase II; ISO:MGI.
GO; GO:1903800; P:positive regulation of production of miRNAs involved in gene silencing by miRNA; ISO:MGI.
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:0031334; P:positive regulation of protein-containing complex assembly; 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 signal transduction; 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 by RNA polymerase II; 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: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: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 population 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: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 signal transduction; 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: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:0010033; P:response to organic substance; ISO:MGI.
GO; GO:0032570; P:response to progesterone; ISS:UniProtKB.
GO; GO:1902074; P:response to salt; IEA:Ensembl.
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: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; ISO:MGI.
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; Disulfide bond; Extracellular matrix;
Glycoprotein; Growth factor; Mitogen; Reference proteome; Secreted; Signal.
SIGNAL 1..29
/evidence="ECO:0000250|UniProtKB:P01137"
CHAIN 30..278
/note="Latency-associated peptide"
/evidence="ECO:0000250|UniProtKB:P01137"
/id="PRO_0000033766"
CHAIN 279..390
/note="Transforming growth factor beta-1"
/evidence="ECO:0000250|UniProtKB:P01137"
/id="PRO_0000033767"
REGION 30..74
/note="Straightjacket domain"
/evidence="ECO:0000250|UniProtKB:P07200"
REGION 75..271
/note="Arm domain"
/evidence="ECO:0000250|UniProtKB:P07200"
REGION 226..252
/note="Bowtie tail"
/evidence="ECO:0000250|UniProtKB:P01137"
MOTIF 244..246
/note="Cell attachment site"
/evidence="ECO:0000255"
SITE 278..279
/note="Cleavage; by FURIN"
/evidence="ECO:0000250|UniProtKB:P01137"
CARBOHYD 82
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 136
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
CARBOHYD 176
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
DISULFID 33
/note="Interchain (with C-1359 or C-1384 in LTBP1); in
inactive form"
/evidence="ECO:0000250|UniProtKB:P07200"
DISULFID 223
/note="Interchain (with C-225)"
/evidence="ECO:0000250|UniProtKB:P01137"
DISULFID 225
/note="Interchain (with C-223)"
/evidence="ECO:0000250|UniProtKB:P01137"
DISULFID 285..294
/evidence="ECO:0000250|UniProtKB:P01137"
DISULFID 293..356
/evidence="ECO:0000250|UniProtKB:P01137"
DISULFID 322..387
/evidence="ECO:0000250|UniProtKB:P01137"
DISULFID 326..389
/evidence="ECO:0000250|UniProtKB:P01137"
DISULFID 355
/note="Interchain"
/evidence="ECO:0000250|UniProtKB:P01137"
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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Related Genes :
[TGFB1 TGFB] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[Tgfb1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[Tgfb1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFB2] Transforming growth factor beta-2 proprotein (Cetermin) (Glioblastoma-derived T-cell suppressor factor) (G-TSF) [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-2 (TGF-beta-2)]
[TGFB3] Transforming growth factor beta-3 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-3 (TGF-beta-3)]
[TGFB2] Transforming growth factor beta-2 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-2 (TGF-beta-2)]
[TGFB1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[TGFBR1 ALK5 SKR4] TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (Activin A receptor type II-like protein kinase of 53kD) (Activin receptor-like kinase 5) (ALK-5) (ALK5) (Serine/threonine-protein kinase receptor R4) (SKR4) (TGF-beta type I receptor) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I)
[Tgfbr1] TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (Serine/threonine-protein kinase receptor R4) (SKR4) (TGF-beta type I receptor) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I)
[TGFBR1] TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (TGF-beta type I receptor) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I)
[TGFBR1] TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (TGF-beta type I receptor) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I)
[Tgfbr3] Transforming growth factor beta receptor type 3 (TGF-beta receptor type 3) (TGFR-3) (Betaglycan) (Transforming growth factor beta receptor III) (TGF-beta receptor type III)
[Tgfbr1] TGF-beta receptor type-1 (TGFR-1) (EC 2.7.11.30) (ESK2) (Transforming growth factor-beta receptor type I) (TGF-beta receptor type I) (TbetaR-I)
[MAP3K7 TAK1] Mitogen-activated protein kinase kinase kinase 7 (EC 2.7.11.25) (Transforming growth factor-beta-activated kinase 1) (TGF-beta-activated kinase 1)
[Lefty1 Ebaf Lefty Stra3 Tgfb4] Left-right determination factor 1 (Protein lefty-1) (Lefty protein) (Stimulated by retinoic acid gene 3 protein) (Transforming growth factor beta-4) (TGF-beta-4)
[TGFBR2] TGF-beta receptor type-2 (TGFR-2) (EC 2.7.11.30) (TGF-beta type II receptor) (Transforming growth factor-beta receptor type II) (TGF-beta receptor type II) (TbetaR-II)
[Map3k7 Tak1] Mitogen-activated protein kinase kinase kinase 7 (EC 2.7.11.25) (Transforming growth factor-beta-activated kinase 1) (TGF-beta-activated kinase 1)
[LEFTY2 EBAF LEFTA LEFTYA TGFB4 PSEC0024] Left-right determination factor 2 (Endometrial bleeding-associated factor) (Left-right determination factor A) (Protein lefty-2) (Protein lefty-A) (Transforming growth factor beta-4) (TGF-beta-4)
[Nrros Lrrc33] Transforming growth factor beta activator LRRC33 (Leucine-rich repeat-containing protein 33) (Negative regulator of reactive oxygen species)
[LTBP4] Latent-transforming growth factor beta-binding protein 4 (LTBP-4)
[tgfb1] Transforming growth factor beta-1 proprotein (TGF-beta-5) [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]
[tgfb1] Transforming growth factor beta-1 proprotein [Cleaved into: Latency-associated peptide (LAP); Transforming growth factor beta-1 (TGF-beta-1)]

Bibliography :