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

 TGFB1_HUMAN             Reviewed;         390 AA.
P01137; A8K792; Q9UCG4;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-FEB-1991, sequence version 2.
30-AUG-2017, entry version 229.
RecName: Full=Transforming growth factor beta-1;
Short=TGF-beta-1;
Contains:
RecName: Full=Latency-associated peptide;
Short=LAP;
Flags: Precursor;
Name=TGFB1; Synonyms=TGFB;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3470709; DOI=10.1093/nar/15.7.3188;
Derynck R., Rhee L., Chen E.Y., van Tilburg A.;
"Intron-exon structure of the human transforming growth factor-beta
precursor gene.";
Nucleic Acids Res. 15:3188-3189(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS PRO-10 AND PRO-25.
PubMed=3861940; DOI=10.1038/316701a0;
Derynck R., Jarrett J.A., Chen E.Y., Eaton D.H., Bell J.R.,
Assoian R.K., Roberts A.B., Sporn M.B., Goeddel D.V.;
"Human transforming growth factor-beta complementary DNA sequence and
expression in normal and transformed cells.";
Nature 316:701-705(1985).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Duodenum, and Eye;
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).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 279-390.
TISSUE=Carcinoma;
Urushizaki Y., Niitsu Y., Terui T., Koshida Y., Mahara K., Kohgo Y.,
Urushizaki I., Takahashi Y., Ito H.;
"Cloning and expression of the gene for human transforming growth
factor-beta in Escherichia coli.";
Tumor Res. 22:41-55(1987).
[8]
PROTEIN SEQUENCE OF 279-329.
TISSUE=Urinary bladder carcinoma;
PubMed=8471846; DOI=10.1006/prep.1993.1019;
Bourdrel L., Lin C.-H., Lauren S.L., Elmore R.H., Sugarman B.J.,
Hu S., Westcott K.R.;
"Recombinant human transforming growth factor-beta 1: expression by
Chinese hamster ovary cells, isolation, and characterization.";
Protein Expr. Purif. 4:130-140(1993).
[9]
PROTEIN SEQUENCE OF 279-301.
PubMed=2982829;
Massague J., Like B.;
"Cellular receptors for type beta transforming growth factor. Ligand
binding and affinity labeling in human and rodent cell lines.";
J. Biol. Chem. 260:2636-2645(1985).
[10]
PROTEIN SEQUENCE OF 30-42 AND 279-290, AND CHARACTERIZATION.
PubMed=3162913;
Miyazono K., Hellman U., Wernstedt C., Heldin C.H.;
"Latent high molecular weight complex of transforming growth factor
beta 1. Purification from human platelets and structural
characterization.";
J. Biol. Chem. 263:6407-6415(1988).
[11]
REVIEW.
PubMed=9150447; DOI=10.1038/ki.1997.188;
Munger J.S., Harpel J.G., Gleizes P.E., Mazzieri R., Nunes I.,
Rifkin D.B.;
"Latent transforming growth factor-beta: structural features and
mechanisms of activation.";
Kidney Int. 51:1376-1382(1997).
[12]
INTERACTION WITH DPT.
PubMed=9895299; DOI=10.1042/bj3370537;
Okamoto O., Fujiwara S., Abe M., Sato Y.;
"Dermatopontin interacts with transforming growth factor beta and
enhances its biological activity.";
Biochem. J. 337:537-541(1999).
[13]
TISSUE SPECIFICITY.
PubMed=11746498; DOI=10.1002/jcb.1249;
Shur I., Lokiec F., Bleiberg I., Benayahu D.;
"Differential gene expression of cultured human osteoblasts.";
J. Cell. Biochem. 83:547-553(2001).
[14]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-82.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[15]
INTERACTION WITH CD109.
PubMed=16754747; DOI=10.1096/fj.05-5229fje;
Finnson K.W., Tam B.Y.Y., Liu K., Marcoux A., Lepage P., Roy S.,
Bizet A.A., Philip A.;
"Identification of CD109 as part of the TGF-beta receptor system in
human keratinocytes.";
FASEB J. 20:1525-1527(2006).
[16]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-82.
TISSUE=Platelet;
PubMed=16263699; DOI=10.1074/mcp.M500324-MCP200;
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
"Elucidation of N-glycosylation sites on human platelet proteins: a
glycoproteomic approach.";
Mol. Cell. Proteomics 5:226-233(2006).
[17]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH ASPN.
PubMed=17827158; DOI=10.1074/jbc.M700522200;
Nakajima M., Kizawa H., Saitoh M., Kou I., Miyazono K., Ikegawa S.;
"Mechanisms for asporin function and regulation in articular
cartilage.";
J. Biol. Chem. 282:32185-32192(2007).
[18]
INTERACTION WITH HSP90AB1.
PubMed=20599762; DOI=10.1016/j.bbrc.2010.06.112;
Suzuki S., Kulkarni A.B.;
"Extracellular heat shock protein HSP90beta secreted by MG63
osteosarcoma cells inhibits activation of latent TGF-beta1.";
Biochem. Biophys. Res. Commun. 398:525-531(2010).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
FUNCTION.
PubMed=25310401; DOI=10.1371/journal.pone.0108528;
Chen Q., Lee C.E., Denard B., Ye J.;
"Sustained induction of collagen synthesis by TGF-beta requires
regulated intramembrane proteolysis of CREB3L1.";
PLoS ONE 9:E108528-E108528(2014).
[21]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[22]
FUNCTION.
PubMed=25893292; DOI=10.1038/onc.2015.100;
Hwangbo C., Tae N., Lee S., Kim O., Park O.K., Kim J., Kwon S.H.,
Lee J.H.;
"Syntenin regulates TGF-beta1-induced Smad activation and the
epithelial-to-mesenchymal transition by inhibiting caveolin-mediated
TGF-beta type I receptor internalization.";
Oncogene 35:389-401(2016).
[23]
STRUCTURE BY NMR OF 279-390.
PubMed=8424942; DOI=10.1021/bi00055a021;
Archer S.J., Bax A., Roberts A.B., Sporn M.B., Ogawa Y., Piez K.A.,
Weatherbee J.A., Tsang M.L.-S., Lucas R., Zheng B.-L., Wenker J.,
Torchia D.A.;
"Transforming growth factor beta 1: NMR signal assignments of the
recombinant protein expressed and isotopically enriched using Chinese
hamster ovary cells.";
Biochemistry 32:1152-1163(1993).
[24]
STRUCTURE BY NMR OF 279-390.
PubMed=8424943; DOI=10.1021/bi00055a022;
Archer S.J., Bax A., Roberts A.B., Sporn M.B., Ogawa Y., Piez K.A.,
Weatherbee J.A., Tsang M.L.-S., Lucas R., Zheng B.-L., Wenker J.,
Torchia D.A.;
"Transforming growth factor beta 1: secondary structure as determined
by heteronuclear magnetic resonance spectroscopy.";
Biochemistry 32:1164-1171(1993).
[25]
STRUCTURE BY NMR OF 279-390.
PubMed=8679613; DOI=10.1021/bi9604946;
Hinck A.P., Archer S.J., Qian S.W., Roberts A.B., Sporn M.B.,
Weatherbee J.A., Tsang M.L.-S., Lucas R., Zheng B.-L., Wenker J.,
Torchia D.A.;
"Transforming growth factor beta 1: three-dimensional structure in
solution and comparison with the X-ray structure of transforming
growth factor beta 2.";
Biochemistry 35:8517-8534(1996).
[26]
VARIANT PRO-10.
PubMed=9783545; DOI=10.1359/jbmr.1998.13.10.1569;
Yamada Y., Miyauchi A., Goto J., Takagi Y., Okuizumi H., Kanematsu M.,
Hase M., Takai H., Harada A., Ikeda K.;
"Association of a polymorphism of the transforming growth factor-beta1
gene with genetic susceptibility to osteoporosis in postmenopausal
Japanese women.";
J. Bone Miner. Res. 13:1569-1576(1998).
[27]
VARIANTS CAEND CYS-218; HIS-218 AND ARG-225.
PubMed=10973241; DOI=10.1038/79128;
Kinoshita A., Saito T., Tomita H., Makita Y., Yoshida K., Ghadami M.,
Yamada K., Kondo S., Ikegawa S., Nishimura G., Fukushima Y.,
Nakagomi T., Saito H., Sugimoto T., Kamegaya M., Hisa K., Murray J.C.,
Taniguchi N., Niikawa N., Yoshiura K.;
"Domain-specific mutations in TGFB1 result in Camurati-Engelmann
disease.";
Nat. Genet. 26:19-20(2000).
[28]
VARIANTS CAEND HIS-81; CYS-218 AND ARG-225.
PubMed=11062463; DOI=10.1038/81563;
Janssens K., Gershoni-Baruch R., Guanabens N., Migone N., Ralston S.,
Bonduelle M., Lissens W., Van Maldergem L., Vanhoenacker F.,
Verbruggen L., Van Hul W.;
"Mutations in the gene encoding the latency-associated peptide of TGF-
beta 1 cause Camurati-Engelmann disease.";
Nat. Genet. 26:273-275(2000).
[29]
VARIANT PRO-10.
PubMed=12202987; DOI=10.1007/s100380200069;
Watanabe Y., Kinoshita A., Yamada T., Ohta T., Kishino T.,
Matsumoto N., Ishikawa M., Niikawa N., Yoshiura K.;
"A catalog of 106 single-nucleotide polymorphisms (SNPs) and 11 other
types of variations in genes for transforming growth factor-beta1
(TGF-beta1) and its signaling pathway.";
J. Hum. Genet. 47:478-483(2002).
[30]
CHARACTERIZATION OF VARIANTS CAEND HIS-81; CYS-218; ASP-222 AND
ARG-225.
PubMed=12493741; DOI=10.1074/jbc.M208857200;
Janssens K., ten Dijke P., Ralston S.H., Bergmann C., Van Hul W.;
"Transforming growth factor-beta-1 mutations in Camurati-Engelmann
disease lead to increased signaling by altering either activation or
secretion of the mutant protein.";
J. Biol. Chem. 278:7718-7724(2003).
[31]
CHARACTERIZATION OF VARIANT CAEND CYS-218.
PubMed=12843182; DOI=10.1210/jc.2002-020564;
McGowan N.W., MacPherson H., Janssens K., Van Hul W., Frith J.C.,
Fraser W.D., Ralston S.H., Helfrich M.H.;
"A mutation affecting the latency-associated peptide of TGFbeta1 in
Camurati-Engelmann disease enhances osteoclast formation in vitro.";
J. Clin. Endocrinol. Metab. 88:3321-3326(2003).
[32]
VARIANTS CAEND GLY-223 AND ARG-223.
PubMed=15103729; DOI=10.1002/ajmg.a.20671;
Kinoshita A., Fukumaki Y., Shirahama S., Miyahara A., Nishimura G.,
Haga N., Namba A., Ueda H., Hayashi H., Ikegawa S., Seidel J.,
Niikawa N., Yoshiura K.;
"TGFB1 mutations in four new families with Camurati-Engelmann disease:
confirmation of independently arising LAP-domain-specific mutations.";
Am. J. Med. Genet. 127A:104-107(2004).
-!- 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 (By similarity).
Stimulates sustained production of collagen through the activation
of CREB3L1 by regulated intramembrane proteolysis (RIP)
(PubMed:25310401). 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.
Mediates SMAD2/3 activation by inducing its phosphorylation and
subsequent translocation to the nucleus (PubMed:25893292). Can
induce epithelial-to-mesenchymal transition (EMT) and cell
migration in various cell types (PubMed:25893292).
{ECO:0000250|UniProtKB:P04202, ECO:0000269|PubMed:25310401,
ECO:0000269|PubMed:25893292}.
-!- 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). 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 (By similarity). Latency-associated
peptide interacts with NREP; the interaction results in a decrease
in TGFB1 autoinduction (By similarity). Interacts with CD109, DPT
and ASPN. Interacts (via processed form (LAP)) with HSP90AB1;
inhibits latent TGFB1 activation (PubMed:20599762). {ECO:0000250,
ECO:0000269|PubMed:16754747, ECO:0000269|PubMed:17827158,
ECO:0000269|PubMed:20599762, ECO:0000269|PubMed:9895299}.
-!- INTERACTION:
P05067:APP; NbExp=3; IntAct=EBI-779636, EBI-77613;
Q14689:DIP2A; NbExp=2; IntAct=EBI-779636, EBI-2564275;
P17813:ENG; NbExp=2; IntAct=EBI-779636, EBI-2834630;
Q12841:FSTL1; NbExp=2; IntAct=EBI-779636, EBI-2349801;
P50222:MEOX2; NbExp=3; IntAct=EBI-779636, EBI-748397;
P36897:TGFBR1; NbExp=2; IntAct=EBI-779636, EBI-1027557;
P37173:TGFBR2; NbExp=6; IntAct=EBI-779636, EBI-296151;
Q03167:TGFBR3; NbExp=2; IntAct=EBI-779636, EBI-2852679;
Q90998:TGFBR3 (xeno); NbExp=2; IntAct=EBI-779636, EBI-6620843;
P07996:THBS1; NbExp=2; IntAct=EBI-779636, EBI-2530274;
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000269|PubMed:17827158}.
-!- TISSUE SPECIFICITY: Highly expressed in bone. Abundantly expressed
in articular cartilage and chondrocytes and is increased in
osteoarthritis (OA). Colocalizes with ASPN in chondrocytes within
OA lesions of articular cartilage. {ECO:0000269|PubMed:11746498,
ECO:0000269|PubMed:17827158}.
-!- INDUCTION: Activated in vitro at pH below 3.5 and over 12.5.
-!- 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:0000269|PubMed:16263699,
ECO:0000269|PubMed:16335952}.
-!- 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.
-!- POLYMORPHISM: In post-menopausal Japanese women, the frequency of
Leu-10 is higher in subjects with osteoporosis than in controls.
{ECO:0000269|PubMed:9783545}.
-!- DISEASE: Camurati-Engelmann disease (CAEND) [MIM:131300]: An
autosomal dominant disorder characterized by hyperostosis and
sclerosis of the diaphyses of long bones. The disease typically
presents in early childhood with pain, muscular weakness and
waddling gait, and in some cases other features such as
exophthalmos, facial paralysis, hearing difficulties and loss of
vision. {ECO:0000269|PubMed:10973241, ECO:0000269|PubMed:11062463,
ECO:0000269|PubMed:12493741, ECO:0000269|PubMed:12843182,
ECO:0000269|PubMed:15103729}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=TGF beta-1 entry;
URL="https://en.wikipedia.org/wiki/TGF_beta_1";
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EMBL; X05839; CAA29283.1; -; Genomic_DNA.
EMBL; X05840; CAA29283.1; JOINED; Genomic_DNA.
EMBL; X05843; CAA29283.1; JOINED; Genomic_DNA.
EMBL; X05844; CAA29283.1; JOINED; Genomic_DNA.
EMBL; X05849; CAA29283.1; JOINED; Genomic_DNA.
EMBL; X05850; CAA29283.1; JOINED; Genomic_DNA.
EMBL; X02812; CAA26580.1; -; mRNA.
EMBL; BT007245; AAP35909.1; -; mRNA.
EMBL; AK291907; BAF84596.1; -; mRNA.
EMBL; CH471126; EAW57032.1; -; Genomic_DNA.
EMBL; BC001180; AAH01180.1; -; mRNA.
EMBL; BC000125; AAH00125.1; -; mRNA.
EMBL; BC022242; AAH22242.1; -; mRNA.
EMBL; M38449; AAA36735.1; -; mRNA.
CCDS; CCDS33031.1; -.
PIR; A27513; WFHU2.
RefSeq; NP_000651.3; NM_000660.6.
UniGene; Hs.645227; -.
PDB; 1KLA; NMR; -; A/B=279-390.
PDB; 1KLC; NMR; -; A/B=279-390.
PDB; 1KLD; NMR; -; A/B=279-390.
PDB; 3KFD; X-ray; 3.00 A; A/B/C/D=279-390.
PDB; 4KV5; X-ray; 3.00 A; A/B/C/D=279-390.
PDB; 5FFO; X-ray; 3.49 A; C/D/G/H=34-390.
PDBsum; 1KLA; -.
PDBsum; 1KLC; -.
PDBsum; 1KLD; -.
PDBsum; 3KFD; -.
PDBsum; 4KV5; -.
PDBsum; 5FFO; -.
ProteinModelPortal; P01137; -.
SMR; P01137; -.
BioGrid; 112898; 69.
DIP; DIP-5934N; -.
IntAct; P01137; 76.
MINT; MINT-6806111; -.
STRING; 9606.ENSP00000221930; -.
BindingDB; P01137; -.
ChEMBL; CHEMBL1795178; -.
DrugBank; DB00070; Hyaluronidase.
DrugBank; DB06205; Hyaluronidase (Human Recombinant).
iPTMnet; P01137; -.
PhosphoSitePlus; P01137; -.
BioMuta; TGFB1; -.
DMDM; 135674; -.
OGP; P01137; -.
EPD; P01137; -.
MaxQB; P01137; -.
PaxDb; P01137; -.
PeptideAtlas; P01137; -.
PRIDE; P01137; -.
DNASU; 7040; -.
Ensembl; ENST00000221930; ENSP00000221930; ENSG00000105329.
GeneID; 7040; -.
KEGG; hsa:7040; -.
UCSC; uc002oqh.4; human.
CTD; 7040; -.
DisGeNET; 7040; -.
GeneCards; TGFB1; -.
GeneReviews; TGFB1; -.
H-InvDB; HIX0015152; -.
HGNC; HGNC:11766; TGFB1.
HPA; CAB000361; -.
HPA; CAB073543; -.
MalaCards; TGFB1; -.
MIM; 131300; phenotype.
MIM; 190180; gene.
neXtProt; NX_P01137; -.
Orphanet; 1328; Camurati-Engelmann disease.
Orphanet; 586; Cystic fibrosis.
PharmGKB; PA350; -.
eggNOG; KOG3900; Eukaryota.
eggNOG; ENOG410XT8Z; LUCA.
HOGENOM; HOG000290198; -.
HOVERGEN; HBG074115; -.
InParanoid; P01137; -.
KO; K13375; -.
OrthoDB; EOG091G0BMM; -.
PhylomeDB; P01137; -.
TreeFam; TF318514; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-168277; Influenza Virus Induced Apoptosis.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
Reactome; R-HSA-2129379; Molecules associated with elastic fibres.
Reactome; R-HSA-2173788; Downregulation of TGF-beta receptor signaling.
Reactome; R-HSA-2173789; TGF-beta receptor signaling activates SMADs.
Reactome; R-HSA-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
Reactome; R-HSA-3000170; Syndecan interactions.
Reactome; R-HSA-3000178; ECM proteoglycans.
Reactome; R-HSA-3304356; SMAD2/3 Phosphorylation Motif Mutants in Cancer.
Reactome; R-HSA-3315487; SMAD2/3 MH2 Domain Mutants in Cancer.
Reactome; R-HSA-3642279; TGFBR2 MSI Frameshift Mutants in Cancer.
Reactome; R-HSA-3645790; TGFBR2 Kinase Domain Mutants in Cancer.
Reactome; R-HSA-3656532; TGFBR1 KD Mutants in Cancer.
Reactome; R-HSA-3656535; TGFBR1 LBD Mutants in Cancer.
Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
Reactome; R-HSA-5689603; UCH proteinases.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
Reactome; R-HSA-8941855; RUNX3 regulates CDKN1A transcription.
Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
Reactome; R-HSA-8951936; RUNX3 regulates p14-ARF.
SignaLink; P01137; -.
SIGNOR; P01137; -.
ChiTaRS; TGFB1; human.
EvolutionaryTrace; P01137; -.
GeneWiki; TGF_beta_1; -.
GenomeRNAi; 7040; -.
PRO; PR:P01137; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000105329; -.
CleanEx; HS_TGFB1; -.
ExpressionAtlas; P01137; baseline and differential.
Genevisible; P01137; HS.
GO; GO:0030424; C:axon; IEA:Ensembl.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0009986; C:cell surface; IMP:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0031012; C:extracellular matrix; IDA:BHF-UCL.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
GO; GO:0005578; C:proteinaceous extracellular matrix; ISS:UniProtKB.
GO; GO:0003823; F:antigen binding; IPI:UniProtKB.
GO; GO:0005125; F:cytokine activity; TAS:AgBase.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0001948; F:glycoprotein binding; IPI:UniProtKB.
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; IEA:Ensembl.
GO; GO:0005160; F:transforming growth factor beta receptor binding; TAS:Reactome.
GO; GO:0034713; F:type I transforming growth factor beta receptor binding; IMP:AgBase.
GO; GO:0005114; F:type II transforming growth factor beta receptor binding; IDA:BHF-UCL.
GO; GO:0034714; F:type III transforming growth factor beta receptor binding; IMP:AgBase.
GO; GO:0046732; P:active induction of host immune response by virus; TAS:Reactome.
GO; GO:0002460; P:adaptive immune response based on somatic recombination of immune receptors built from immunoglobulin superfamily domains; IEA:Ensembl.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0006754; P:ATP biosynthetic process; IDA:BHF-UCL.
GO; GO:0030509; P:BMP signaling pathway; IBA:GO_Central.
GO; GO:0060751; P:branch elongation involved in mammary gland duct branching; IEA:Ensembl.
GO; GO:0007050; P:cell cycle arrest; IDA:BHF-UCL.
GO; GO:0048468; P:cell development; IBA:GO_Central.
GO; GO:0016049; P:cell growth; IEA:InterPro.
GO; GO:0016477; P:cell migration; IDA:UniProtKB.
GO; GO:0045216; P:cell-cell junction organization; IDA:BHF-UCL.
GO; GO:0006874; P:cellular calcium ion homeostasis; IEA:Ensembl.
GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
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; IDA:UniProtKB.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IDA:BHF-UCL.
GO; GO:0002062; P:chondrocyte differentiation; IDA:UniProtKB.
GO; GO:0007182; P:common-partner SMAD protein phosphorylation; IDA:UniProtKB.
GO; GO:0002248; P:connective tissue replacement involved in inflammatory response wound healing; TAS:BHF-UCL.
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; ISS:BHF-UCL.
GO; GO:0007492; P:endoderm development; IEA:Ensembl.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0001837; P:epithelial to mesenchymal transition; IDA:UniProtKB.
GO; GO:0019049; P:evasion or tolerance of host defenses by virus; IDA:BHF-UCL.
GO; GO:0085029; P:extracellular matrix assembly; IDA:BHF-UCL.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IDA:BHF-UCL.
GO; GO:0060325; P:face morphogenesis; IEA:Ensembl.
GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
GO; GO:0060364; P:frontal suture morphogenesis; IEA:Ensembl.
GO; GO:0008354; P:germ cell migration; IEA:Ensembl.
GO; GO:0007507; P:heart development; ISS:BHF-UCL.
GO; GO:0003179; P:heart valve morphogenesis; ISS:BHF-UCL.
GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IDA:UniProtKB.
GO; GO:0030214; P:hyaluronan catabolic process; IDA:UniProtKB.
GO; GO:0006954; P:inflammatory response; IDA:UniProtKB.
GO; GO:0048839; P:inner ear development; IEA:Ensembl.
GO; GO:0070306; P:lens fiber cell differentiation; IEA:Ensembl.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
GO; GO:0048535; P:lymph node development; ISS:UniProtKB.
GO; GO:0010742; P:macrophage derived foam cell differentiation; IC:BHF-UCL.
GO; GO:0060744; P:mammary gland branching involved in thelarche; IEA:Ensembl.
GO; GO:0000165; P:MAPK cascade; IMP:UniProtKB.
GO; GO:0031293; P:membrane protein intracellular domain proteolysis; IDA:UniProtKB.
GO; GO:0007093; P:mitotic cell cycle checkpoint; IDA:BHF-UCL.
GO; GO:0032943; P:mononuclear cell proliferation; IEA:Ensembl.
GO; GO:0042552; P:myelination; IEA:Ensembl.
GO; GO:0043011; P:myeloid dendritic cell differentiation; IEA:Ensembl.
GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; IDA:BHF-UCL.
GO; GO:0045786; P:negative regulation of cell cycle; IDA:HGNC.
GO; GO:0045596; P:negative regulation of cell differentiation; IEP:CACAO.
GO; GO:0030308; P:negative regulation of cell growth; IDA:BHF-UCL.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:BHF-UCL.
GO; GO:0022408; P:negative regulation of cell-cell adhesion; IDA:BHF-UCL.
GO; GO:0008156; P:negative regulation of DNA replication; IMP:BHF-UCL.
GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IDA:BHF-UCL.
GO; GO:0010716; P:negative regulation of extracellular matrix disassembly; IC:BHF-UCL.
GO; GO:0045599; P:negative regulation of fat cell differentiation; IDA:UniProtKB.
GO; GO:0010629; P:negative regulation of gene expression; IDA:BHF-UCL.
GO; GO:0060965; P:negative regulation of gene silencing by miRNA; IGI:BHF-UCL.
GO; GO:1900126; P:negative regulation of hyaluronan biosynthetic process; IDA:UniProtKB.
GO; GO:0032700; P:negative regulation of interleukin-17 production; IEA:Ensembl.
GO; GO:0010936; P:negative regulation of macrophage cytokine production; IDA:DFLAT.
GO; GO:0045930; P:negative regulation of mitotic cell cycle; IDA:BHF-UCL.
GO; GO:0045662; P:negative regulation of myoblast differentiation; IDA:UniProtKB.
GO; GO:0007406; P:negative regulation of neuroblast proliferation; IEA:Ensembl.
GO; GO:0030279; P:negative regulation of ossification; IEA:Ensembl.
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; IGI:BHF-UCL.
GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; IDA:UniProtKB.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IDA:BHF-UCL.
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; IDA:UniProtKB.
GO; GO:0042130; P:negative regulation of T cell proliferation; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; TAS:Reactome.
GO; GO:0001843; P:neural tube closure; ISS:BHF-UCL.
GO; GO:0021915; P:neural tube development; ISS:BHF-UCL.
GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
GO; GO:0014003; P:oligodendrocyte development; IEA:Ensembl.
GO; GO:0043932; P:ossification involved in bone remodeling; IEP:BHF-UCL.
GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; IDA:UniProtKB.
GO; GO:0006796; P:phosphate-containing compound metabolic process; IDA:BHF-UCL.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IDA:BHF-UCL.
GO; GO:0030501; P:positive regulation of bone mineralization; IEP:BHF-UCL.
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; IDA:BHF-UCL.
GO; GO:0071158; P:positive regulation of cell cycle arrest; IEA:Ensembl.
GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
GO; GO:0030335; P:positive regulation of cell migration; IDA:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:BHF-UCL.
GO; GO:0032270; P:positive regulation of cellular protein metabolic process; IDA:BHF-UCL.
GO; GO:0050921; P:positive regulation of chemotaxis; IDA:BHF-UCL.
GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IDA:UniProtKB.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Ensembl.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IDA:BHF-UCL.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
GO; GO:0031536; P:positive regulation of exit from mitosis; IEA:Ensembl.
GO; GO:1901203; P:positive regulation of extracellular matrix assembly; IC:BHF-UCL.
GO; GO:0010763; P:positive regulation of fibroblast migration; IDA:BHF-UCL.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
GO; GO:0035066; P:positive regulation of histone acetylation; IEA:Ensembl.
GO; GO:0031065; P:positive regulation of histone deacetylation; IEA:Ensembl.
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; IDA:MGI.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:BHF-UCL.
GO; GO:0071677; P:positive regulation of mononuclear cell migration; IEA:Ensembl.
GO; GO:1901666; P:positive regulation of NAD+ ADP-ribosyltransferase activity; IDA:BHF-UCL.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
GO; GO:0042482; P:positive regulation of odontogenesis; IEA:Ensembl.
GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IDA:BHF-UCL.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IDA:BHF-UCL.
GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; IDA:BHF-UCL.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IDA:BHF-UCL.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:1903800; P:positive regulation of production of miRNAs involved in gene silencing by miRNA; IDA:BHF-UCL.
GO; GO:0031334; P:positive regulation of protein complex assembly; IDA:BHF-UCL.
GO; GO:0035307; P:positive regulation of protein dephosphorylation; IDA:BHF-UCL.
GO; GO:0042307; P:positive regulation of protein import into nucleus; IDA:BHF-UCL.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:BHF-UCL.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:BHF-UCL.
GO; GO:0050714; P:positive regulation of protein secretion; IDA:BHF-UCL.
GO; GO:1903911; P:positive regulation of receptor clustering; IEA:Ensembl.
GO; GO:0045591; P:positive regulation of regulatory T cell differentiation; IEA:Ensembl.
GO; GO:0060391; P:positive regulation of SMAD protein import into nucleus; IDA:BHF-UCL.
GO; GO:0051152; P:positive regulation of smooth muscle cell differentiation; IEA:Ensembl.
GO; GO:0032930; P:positive regulation of superoxide anion generation; IDA:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; IDA:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; TAS:BHF-UCL.
GO; GO:0043117; P:positive regulation of vascular permeability; IDA:UniProtKB.
GO; GO:0006611; P:protein export from nucleus; IDA:UniProtKB.
GO; GO:0000060; P:protein import into nucleus, translocation; IDA:UniProtKB.
GO; GO:0043491; P:protein kinase B signaling; IMP:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
GO; GO:0032801; P:receptor catabolic process; IDA:BHF-UCL.
GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; IEA:Ensembl.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0051098; P:regulation of binding; ISS:UniProtKB.
GO; GO:0060312; P:regulation of blood vessel remodeling; NAS:BHF-UCL.
GO; GO:0060762; P:regulation of branching involved in mammary gland duct morphogenesis; IEA:Ensembl.
GO; GO:0061035; P:regulation of cartilage development; IEA:Ensembl.
GO; GO:0030334; P:regulation of cell migration; TAS:BHF-UCL.
GO; GO:0051101; P:regulation of DNA binding; ISS:UniProtKB.
GO; GO:0032667; P:regulation of interleukin-23 production; IEA:Ensembl.
GO; GO:0042306; P:regulation of protein import into nucleus; ISS:UniProtKB.
GO; GO:0060390; P:regulation of SMAD protein import into nucleus; IDA:UniProtKB.
GO; GO:0002028; P:regulation of sodium ion transport; IEA:Ensembl.
GO; GO:0016202; P:regulation of striated muscle tissue development; ISS:UniProtKB.
GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0045066; P:regulatory T cell differentiation; IEA:Ensembl.
GO; GO:0070723; P:response to cholesterol; IDA:BHF-UCL.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IDA:BHF-UCL.
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; IDA:BHF-UCL.
GO; GO:0033280; P:response to vitamin D; IEA:Ensembl.
GO; GO:0009611; P:response to wounding; IEP:BHF-UCL.
GO; GO:0007435; P:salivary gland morphogenesis; IEP:BHF-UCL.
GO; GO:0007183; P:SMAD protein complex assembly; IDA:BHF-UCL.
GO; GO:0007184; P:SMAD protein import into nucleus; IDA:BHF-UCL.
GO; GO:0060395; P:SMAD protein signal transduction; IBA:GO_Central.
GO; GO:0043029; P:T cell homeostasis; IEA:Ensembl.
GO; GO:0002513; P:tolerance induction to self antigen; IEA:Ensembl.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:BHF-UCL.
GO; GO:1905313; P:transforming growth factor beta receptor signaling pathway involved in heart development; ISS:BHF-UCL.
GO; GO:0001657; P:ureteric bud development; IEA:Ensembl.
GO; GO:0001570; P:vasculogenesis; ISS:BHF-UCL.
GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; ISS:BHF-UCL.
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;
3D-structure; Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
Extracellular matrix; Glycoprotein; Growth factor; Mitogen;
Polymorphism; Reference proteome; Secreted; Signal.
SIGNAL 1 29 {ECO:0000269|PubMed:3162913}.
CHAIN 30 278 Latency-associated peptide.
/FTId=PRO_0000033762.
CHAIN 279 390 Transforming growth factor beta-1.
/FTId=PRO_0000033763.
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:0000269|PubMed:16263699,
ECO:0000269|PubMed:16335952}.
CARBOHYD 136 136 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
CARBOHYD 176 176 N-linked (GlcNAc...) asparagine.
{ECO:0000250}.
DISULFID 33 33 Interchain (with C-1359 or C-1384 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
DISULFID 293 356
DISULFID 322 387
DISULFID 326 389
DISULFID 355 355 Interchain.
VARIANT 10 10 L -> P (associated with higher bone
mineral density and lower frequency of
vertebral fractures in Japanese post-
menopausal women; dbSNP:rs1800470).
{ECO:0000269|PubMed:12202987,
ECO:0000269|PubMed:3861940,
ECO:0000269|PubMed:9783545}.
/FTId=VAR_016171.
VARIANT 25 25 R -> P (in dbSNP:rs1800471).
{ECO:0000269|PubMed:3861940}.
/FTId=VAR_016172.
VARIANT 81 81 Y -> H (in CAEND; leads to TGF-beta-1
intracellular accumulation).
{ECO:0000269|PubMed:11062463,
ECO:0000269|PubMed:12493741}.
/FTId=VAR_017607.
VARIANT 218 218 R -> C (in CAEND; higher levels of active
TGF-beta-1 in the culture medium;
enhances osteoclast formation in vitro).
{ECO:0000269|PubMed:10973241,
ECO:0000269|PubMed:11062463,
ECO:0000269|PubMed:12493741,
ECO:0000269|PubMed:12843182}.
/FTId=VAR_017608.
VARIANT 218 218 R -> H (in CAEND).
{ECO:0000269|PubMed:10973241}.
/FTId=VAR_017609.
VARIANT 222 222 H -> D (in CAEND; sporadic case; higher
levels of active TGF-beta-1 in the
culture medium).
{ECO:0000269|PubMed:12493741}.
/FTId=VAR_017610.
VARIANT 223 223 C -> G (in CAEND).
{ECO:0000269|PubMed:15103729}.
/FTId=VAR_067303.
VARIANT 223 223 C -> R (in CAEND).
{ECO:0000269|PubMed:15103729}.
/FTId=VAR_067304.
VARIANT 225 225 C -> R (in CAEND; higher levels of active
TGF-beta-1 in the culture medium).
{ECO:0000269|PubMed:10973241,
ECO:0000269|PubMed:11062463,
ECO:0000269|PubMed:12493741}.
/FTId=VAR_017611.
VARIANT 263 263 T -> I (in dbSNP:rs1800472).
/FTId=VAR_016173.
CONFLICT 159 159 R -> RR (in Ref. 2; CAA26580).
{ECO:0000305}.
HELIX 38 56 {ECO:0000244|PDB:5FFO}.
STRAND 70 72 {ECO:0000244|PDB:5FFO}.
HELIX 75 84 {ECO:0000244|PDB:5FFO}.
STRAND 106 112 {ECO:0000244|PDB:5FFO}.
TURN 118 123 {ECO:0000244|PDB:5FFO}.
STRAND 131 136 {ECO:0000244|PDB:5FFO}.
HELIX 137 143 {ECO:0000244|PDB:5FFO}.
STRAND 144 146 {ECO:0000244|PDB:5FFO}.
TURN 147 149 {ECO:0000244|PDB:5FFO}.
STRAND 150 156 {ECO:0000244|PDB:5FFO}.
STRAND 167 174 {ECO:0000244|PDB:5FFO}.
TURN 175 177 {ECO:0000244|PDB:5FFO}.
STRAND 178 186 {ECO:0000244|PDB:5FFO}.
STRAND 197 199 {ECO:0000244|PDB:5FFO}.
HELIX 201 209 {ECO:0000244|PDB:5FFO}.
STRAND 213 221 {ECO:0000244|PDB:5FFO}.
STRAND 242 244 {ECO:0000244|PDB:5FFO}.
TURN 245 247 {ECO:0000244|PDB:5FFO}.
STRAND 257 262 {ECO:0000244|PDB:5FFO}.
HELIX 265 268 {ECO:0000244|PDB:5FFO}.
HELIX 282 285 {ECO:0000244|PDB:3KFD}.
STRAND 291 296 {ECO:0000244|PDB:3KFD}.
STRAND 299 301 {ECO:0000244|PDB:3KFD}.
HELIX 302 306 {ECO:0000244|PDB:3KFD}.
STRAND 311 313 {ECO:0000244|PDB:3KFD}.
STRAND 315 318 {ECO:0000244|PDB:3KFD}.
STRAND 321 324 {ECO:0000244|PDB:3KFD}.
STRAND 330 332 {ECO:0000244|PDB:3KFD}.
HELIX 335 346 {ECO:0000244|PDB:3KFD}.
STRAND 347 349 {ECO:0000244|PDB:3KFD}.
STRAND 350 353 {ECO:0000244|PDB:5FFO}.
STRAND 356 370 {ECO:0000244|PDB:3KFD}.
STRAND 373 389 {ECO:0000244|PDB:3KFD}.
SEQUENCE 390 AA; 44341 MW; 75391614250288FE CRC64;
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


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