P01137 (TGFB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transforming growth factor beta-1
Short name=TGF-beta-1

Cleaved into the following chain:

1. Latency-associated peptide
   Short name=LAP

Gene names

Name:	TGFB1
Synonyms:	TGFB

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	390 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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.
Subunit structure	The inactive form consists of a TGFB1 homodimer non-covalently linked to a latency-associated peptide (LAP) homodimer. The inactive complex can contain a latent TGFB1-binding protein. The active form is a homodimer of mature TGFB1; disulfide-linked. Heterodimers of TGFB1/TGFB2 have been found in bone. Interacts with CD109 and DPT. Interacts with ASPN. Ref.12 Ref.15 Ref.17
Subcellular location	Secreted › extracellular space › extracellular matrix Ref.17.
Tissue specificity	Highly expressed in bone. Abundantly expressed in articular cartilage and chondrocytes and is increased in osteoarthritis (OA). Co-localizes with ASPN in chondrocytes within OA lesions of articular cartilage. Ref.13 Ref.17
Induction	Activated in vitro at pH below 3.5 and over 12.5.
Post-translational modification	Glycosylated. Ref.14 Ref.16 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.
Involvement in disease	Defects in TGFB1 are the cause of Camurati-Engelmann disease (CE) [MIM:131300]; also known as progressive diaphyseal dysplasia 1 (DPD1). CE is 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. Ref.22 Ref.23 Ref.25 Ref.26
Sequence similarities	Belongs to the TGF-beta family.

Ontologies

Keywords
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Polymorphism
Disease	Disease mutation
Domain	Signal
Molecular function	Growth factor Mitogen
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	ATP biosynthetic process Inferred from direct assay. Source: BHF-UCL SMAD protein complex assembly Inferred from direct assay. Source: BHF-UCL SMAD protein import into nucleus Inferred from direct assay. Source: BHF-UCL active induction of host immune response by virus Traceable author statement. Source: Reactome cell cycle arrest Inferred from direct assay. Source: BHF-UCL cell growth Inferred from electronic annotation. Source: InterPro cell-cell junction organization Inferred from direct assay. Source: BHF-UCL chondrocyte differentiation Inferred from direct assay. Source: UniProtKB connective tissue replacement involved in inflammatory response wound healing Traceable author statement. Source: BHF-UCL epidermal growth factor receptor signaling pathway Inferred from direct assay. Source: BHF-UCL evasion of host defenses by virus Inferred from direct assay. Source: BHF-UCL hemopoietic progenitor cell differentiation Inferred from direct assay. Source: UniProtKB induction of apoptosis Inferred from direct assay. Source: BHF-UCL lymph node development Inferred from sequence or structural similarity. Source: UniProtKB macrophage derived foam cell differentiation Inferred by curator. Source: BHF-UCL mitotic cell cycle G1/S transition checkpoint Inferred from direct assay. Source: BHF-UCL negative regulation of DNA replication Inferred from mutant phenotype. Source: BHF-UCL negative regulation of blood vessel endothelial cell migration Inferred from direct assay. Source: BHF-UCL negative regulation of cell growth Inferred from direct assay. Source: BHF-UCL negative regulation of cell-cell adhesion Inferred from direct assay. Source: BHF-UCL negative regulation of epithelial cell proliferation Inferred from mutant phenotype. Source: BHF-UCL negative regulation of fat cell differentiation Inferred from direct assay. Source: UniProtKB negative regulation of macrophage cytokine production Inferred from direct assay. Source: DFLAT negative regulation of mitotic cell cycle Inferred from direct assay. Source: BHF-UCL negative regulation of myoblast differentiation Inferred from direct assay. Source: UniProtKB negative regulation of protein phosphorylation Inferred from direct assay. Source: BHF-UCL negative regulation of skeletal muscle tissue development Inferred from direct assay. Source: UniProtKB ossification involved in bone remodeling Inferred from expression pattern. Source: BHF-UCL pathway-restricted SMAD protein phosphorylation Inferred from direct assay. Source: BHF-UCL platelet activation Traceable author statement. Source: Reactome platelet degranulation Traceable author statement. Source: Reactome positive regulation of MAP kinase activity Inferred from direct assay. Source: BHF-UCL positive regulation of SMAD protein import into nucleus Inferred from direct assay. Source: BHF-UCL positive regulation of blood vessel endothelial cell migration Inferred from direct assay. Source: BHF-UCL positive regulation of bone mineralization Inferred from expression pattern. Source: BHF-UCL positive regulation of cell division Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of chemotaxis Inferred from direct assay. Source: BHF-UCL positive regulation of collagen biosynthetic process Inferred from direct assay. Source: BHF-UCL positive regulation of epithelial to mesenchymal transition Inferred from direct assay. Source: BHF-UCL positive regulation of fibroblast migration Inferred from direct assay. Source: BHF-UCL positive regulation of interleukin-17 production Inferred from direct assay. Source: BHF-UCL positive regulation of isotype switching to IgA isotypes Inferred from direct assay. Source: MGI positive regulation of pathway-restricted SMAD protein phosphorylation Inferred from direct assay. Source: BHF-UCL positive regulation of peptidyl-serine phosphorylation Inferred from direct assay. Source: BHF-UCL positive regulation of peptidyl-threonine phosphorylation Inferred from direct assay. Source: BHF-UCL positive regulation of phosphatidylinositol 3-kinase activity Inferred from direct assay. Source: BHF-UCL positive regulation of protein dephosphorylation Inferred from direct assay. Source: BHF-UCL positive regulation of protein kinase B signaling cascade Inferred from direct assay. Source: BHF-UCL positive regulation of protein secretion Inferred from direct assay. Source: BHF-UCL positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay. Source: UniProtKB protein export from nucleus Inferred from direct assay. Source: UniProtKB protein import into nucleus, translocation Inferred from direct assay. Source: UniProtKB receptor catabolic process Inferred from direct assay. Source: BHF-UCL regulation of DNA binding Inferred from sequence or structural similarity. Source: UniProtKB regulation of transforming growth factor beta receptor signaling pathway Inferred from direct assay. Source: BHF-UCL response to cholesterol Inferred from direct assay. Source: BHF-UCL response to estradiol stimulus Inferred from direct assay. Source: BHF-UCL response to progesterone stimulus Inferred from direct assay. Source: BHF-UCL salivary gland morphogenesis Inferred from expression pattern. Source: BHF-UCL transforming growth factor beta receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB viral infectious cycle Traceable author statement. Source: Reactome
Cellular component	Golgi lumen Traceable author statement. Source: Reactome extracellular space Inferred from direct assay. Source: BHF-UCL nucleus Inferred from direct assay. Source: BHF-UCL platelet alpha granule lumen Traceable author statement. Source: Reactome proteinaceous extracellular matrix Inferred from sequence or structural similarity. Source: UniProtKB
Molecular function	growth factor activity Inferred from electronic annotation. Source: UniProtKB-KW type II transforming growth factor beta receptor binding Inferred from direct assay. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
APP	P05067	2	EBI-779636,EBI-77613
ENG	P17813	2	EBI-779636,EBI-2834630
TGFBR1	P36897	2	EBI-779636,EBI-1027557
TGFBR2	P37173	2	EBI-779636,EBI-296151
TGFBR3	Q03167	2	EBI-779636,EBI-2852679

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 29

29

Ref.10

Chain

30 – 278

249

Latency-associated peptide

PRO_0000033762

Chain

279 – 390

112

Transforming growth factor beta-1

PRO_0000033763

Regions

Motif

244 – 246

3

Cell attachment site Potential

Amino acid modifications

Glycosylation

82

1

N-linked (GlcNAc...) Ref.14 Ref.16

Glycosylation

136

1

N-linked (GlcNAc...) By similarity

Glycosylation

176

1

N-linked (GlcNAc...) By similarity

Disulfide bond

285 ↔ 294

Disulfide bond

293 ↔ 356

Disulfide bond

322 ↔ 387

Disulfide bond

326 ↔ 389

Disulfide bond

355

Interchain

Natural variations

Natural variant

10

1

L → P Associated with higher bone mineral density and lower frequency of vertebral fractures in Japanese post-menopausal women. Ref.2 Ref.21 Ref.24
Corresponds to variant rs1800470 [ dbSNP | Ensembl ].

VAR_016171

Natural variant

25

1

R → P.
Corresponds to variant rs1800471 [ dbSNP | Ensembl ].

VAR_016172

Natural variant

81

1

Y → H in CE; leads to TGF-beta-1 intracellular accumulation. Ref.23 Ref.25

VAR_017607

Natural variant

218

1

R → C in CE; higher levels of active TGF-beta-1 in the culture medium; enhances osteoclast formation in vitro. Ref.22 Ref.23 Ref.25 Ref.26

VAR_017608

Natural variant

218

1

R → H in CE. Ref.22

VAR_017609

Natural variant

222

1

H → D in CE; sporadic case; higher levels of active TGF-beta-1 in the culture medium. Ref.25

VAR_017610

Natural variant

225

1

C → R in CE; higher levels of active TGF-beta-1 in the culture medium. Ref.22 Ref.23 Ref.25

VAR_017611

Natural variant

263

1

T → I.
Corresponds to variant rs1800472 [ dbSNP | Ensembl ].

VAR_016173

Experimental info

Sequence conflict

159

1

R → RR in CAA26580. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

390

Helix Strand Turn

Details...

Turn

282 – 287

6

Beta strand

294 – 296

3

Turn

302 – 304

3

Beta strand

313 – 315

3

Beta strand

321 – 324

4

Beta strand

328 – 330

3

Helix

335 – 346

12

Beta strand

358 – 370

13

Beta strand

373 – 387

15

Sequences

	Sequence		Length	Mass (Da)
	P01137 [UniParc]. Last modified February 1, 1991. Version 2. Checksum: 75391614250288FE	FASTA	390	44,341
	10 20 30 40 50 60 MPPSGLRLLL LLLPLLWLLV LTPGRPAAGL STCKTIDMEL VKRKRIEAIR GQILSKLRLA 70 80 90 100 110 120 SPPSQGEVPP GPLPEAVLAL YNSTRDRVAG ESAEPEPEPE ADYYAKEVTR VLMVETHNEI 130 140 150 160 170 180 YDKFKQSTHS IYMFFNTSEL REAVPEPVLL SRAELRLLRL KLKVEQHVEL YQKYSNNSWR 190 200 210 220 230 240 YLSNRLLAPS DSPEWLSFDV TGVVRQWLSR GGEIEGFRLS AHCSCDSRDN TLQVDINGFT 250 260 270 280 290 300 TGRRGDLATI HGMNRPFLLL MATPLERAQH LQSSRHRRAL DTNYCFSSTE KNCCVRQLYI 310 320 330 340 350 360 DFRKDLGWKW IHEPKGYHAN FCLGPCPYIW SLDTQYSKVL ALYNQHNPGA SAAPCCVPQA 370 380 390 LEPLPIVYYV GRKPKVEQLS NMIVRSCKCS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Intron-exon structure of the human transforming growth factor-beta precursor gene." Derynck R., Rhee L., Chen E.Y., van Tilburg A. Nucleic Acids Res. 15:3188-3189(1987) [PubMed: 3470709] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Human transforming growth factor-beta complementary DNA sequence and expression in normal and transformed cells." 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. Nature 316:701-705(1985) [PubMed: 3861940] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT PRO-10.
[3]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." 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. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Duodenum and Eye.
[7]	"Cloning and expression of the gene for human transforming growth factor-beta in Escherichia coli." Urushizaki Y., Niitsu Y., Terui T., Koshida Y., Mahara K., Kohgo Y., Urushizaki I., Takahashi Y., Ito H. Tumor Res. 22:41-55(1987) Cited for: NUCLEOTIDE SEQUENCE OF 279-390. Tissue: Carcinoma.
[8]	"Recombinant human transforming growth factor-beta 1: expression by Chinese hamster ovary cells, isolation, and characterization." Bourdrel L., Lin C.-H., Lauren S.L., Elmore R.H., Sugarman B.J., Hu S., Westcott K.R. Protein Expr. Purif. 4:130-140(1993) [PubMed: 8471846] [Abstract] Cited for: PROTEIN SEQUENCE OF 279-329. Tissue: Urinary bladder carcinoma.
[9]	"Cellular receptors for type beta transforming growth factor. Ligand binding and affinity labeling in human and rodent cell lines." Massague J., Like B. J. Biol. Chem. 260:2636-2645(1985) [PubMed: 2982829] [Abstract] Cited for: PROTEIN SEQUENCE OF 279-301.
[10]	"Latent high molecular weight complex of transforming growth factor beta 1. Purification from human platelets and structural characterization." Miyazono K., Hellman U., Wernstedt C., Heldin C.H. J. Biol. Chem. 263:6407-6415(1988) [PubMed: 3162913] [Abstract] Cited for: PROTEIN SEQUENCE OF 30-42 AND 279-290, CHARACTERIZATION.
[11]	"Latent transforming growth factor-beta: structural features and mechanisms of activation." Munger J.S., Harpel J.G., Gleizes P.E., Mazzieri R., Nunes I., Rifkin D.B. Kidney Int. 51:1376-1382(1997) [PubMed: 9150447] [Abstract] Cited for: REVIEW.
[12]	"Dermatopontin interacts with transforming growth factor beta and enhances its biological activity." Okamoto O., Fujiwara S., Abe M., Sato Y. Biochem. J. 337:537-541(1999) [PubMed: 9895299] [Abstract] Cited for: INTERACTION WITH DPT.
[13]	"Differential gene expression of cultured human osteoblasts." Shur I., Lokiec F., Bleiberg I., Benayahu D. J. Cell. Biochem. 83:547-553(2001) [PubMed: 11746498] [Abstract] Cited for: TISSUE SPECIFICITY.
[14]	"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry." Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D. J. Proteome Res. 4:2070-2080(2005) [PubMed: 16335952] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-82, MASS SPECTROMETRY. Tissue: Plasma.
[15]	"Identification of CD109 as part of the TGF-beta receptor system in human keratinocytes." Finnson K.W., Tam B.Y.Y., Liu K., Marcoux A., Lepage P., Roy S., Bizet A.A., Philip A. FASEB J. 20:1525-1527(2006) [PubMed: 16754747] [Abstract] Cited for: INTERACTION WITH CD109.
[16]	"Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach." Lewandrowski U., Moebius J., Walter U., Sickmann A. Mol. Cell. Proteomics 5:226-233(2006) [PubMed: 16263699] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-82, MASS SPECTROMETRY. Tissue: Platelet.
[17]	"Mechanisms for asporin function and regulation in articular cartilage." Nakajima M., Kizawa H., Saitoh M., Kou I., Miyazono K., Ikegawa S. J. Biol. Chem. 282:32185-32192(2007) [PubMed: 17827158] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH ASPN.
[18]	"Transforming growth factor beta 1: NMR signal assignments of the recombinant protein expressed and isotopically enriched using Chinese hamster ovary cells." 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. Biochemistry 32:1152-1163(1993) [PubMed: 8424942] [Abstract] Cited for: STRUCTURE BY NMR OF 279-390.
[19]	"Transforming growth factor beta 1: secondary structure as determined by heteronuclear magnetic resonance spectroscopy." 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. Biochemistry 32:1164-1171(1993) [PubMed: 8424943] [Abstract] Cited for: STRUCTURE BY NMR OF 279-390.
[20]	"Transforming growth factor beta 1: three-dimensional structure in solution and comparison with the X-ray structure of transforming growth factor beta 2." 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. Biochemistry 35:8517-8534(1996) [PubMed: 8679613] [Abstract] Cited for: STRUCTURE BY NMR OF 279-390.
[21]	"Association of a polymorphism of the transforming growth factor-beta1 gene with genetic susceptibility to osteoporosis in postmenopausal Japanese women." Yamada Y., Miyauchi A., Goto J., Takagi Y., Okuizumi H., Kanematsu M., Hase M., Takai H., Harada A., Ikeda K. J. Bone Miner. Res. 13:1569-1576(1998) [PubMed: 9783545] [Abstract] Cited for: VARIANT PRO-10.
[22]	"Domain-specific mutations in TGFB1 result in Camurati-Engelmann disease." 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. Nat. Genet. 26:19-20(2000) [PubMed: 10973241] [Abstract] Cited for: VARIANTS CE CYS-218; HIS-218 AND ARG-225.
[23]	"Mutations in the gene encoding the latency-associated peptide of TGF-beta 1 cause Camurati-Engelmann disease." 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. Nat. Genet. 26:273-275(2000) [PubMed: 11062463] [Abstract] Cited for: VARIANTS CE HIS-81; CYS-218 AND ARG-225.
[24]	"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." Watanabe Y., Kinoshita A., Yamada T., Ohta T., Kishino T., Matsumoto N., Ishikawa M., Niikawa N., Yoshiura K. J. Hum. Genet. 47:478-483(2002) [PubMed: 12202987] [Abstract] Cited for: VARIANT PRO-10.
[25]	"Transforming growth factor-beta-1 mutations in Camurati-Engelmann disease lead to increased signaling by altering either activation or secretion of the mutant protein." Janssens K., ten Dijke P., Ralston S.H., Bergmann C., Van Hul W. J. Biol. Chem. 278:7718-7724(2003) [PubMed: 12493741] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS CE HIS-81; CYS-218; ASP-222 AND ARG-225.
[26]	"A mutation affecting the latency-associated peptide of TGFbeta1 in Camurati-Engelmann disease enhances osteoclast formation in vitro." McGowan N.W., MacPherson H., Janssens K., Van Hul W., Frith J.C., Fraser W.D., Ralston S.H., Helfrich M.H. J. Clin. Endocrinol. Metab. 88:3321-3326(2003) [PubMed: 12843182] [Abstract] Cited for: CHARACTERIZATION OF VARIANT CE CYS-218.
+	Additional computationally mapped references.

Web resources

GeneReviews

Wikipedia

TGF beta-1 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X05839 , X05840, X05843, X05844, X05849, X05850 Genomic DNA. Translation: CAA29283.1.
X02812 mRNA. Translation: CAA26580.1. Sequence problems.
BT007245 mRNA. Translation: AAP35909.1.
AK291907 mRNA. Translation: BAF84596.1.
CH471126 Genomic DNA. Translation: EAW57032.1.
BC001180 mRNA. Translation: AAH01180.1.
BC000125 mRNA. Translation: AAH00125.1.
BC022242 mRNA. Translation: AAH22242.1.
M38449 mRNA. Translation: AAA36735.1.

IPI

IPI00000075.

PIR

WFHU2. A27513.

RefSeq

NP_000651.3. NM_000660.4.

UniGene

Hs.645227.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KLA	NMR	-	A/B	279-390	[»]
1KLC	NMR	-	A/B	279-390	[»]
1KLD	NMR	-	A/B	279-390	[»]
3KFD	X-ray	3.00	A/B/C/D	279-390	[»]

ProteinModelPortal

P01137.

SMR

P01137. Positions 30-390.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5934N.

IntAct

P01137. 8 interactions.

STRING

P01137.

Polymorphism databases

DMDM

135674.

2D gel databases

OGP

P01137.

Proteomic databases

PRIDE

P01137.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000221930; ENSP00000221930; ENSG00000105329.

GeneID

7040.

KEGG

hsa:7040.

Organism-specific databases

CTD

7040.

GeneCards

GC19M041837.

H-InvDB

HIX0015152.

HGNC

HGNC:11766. TGFB1.

HPA

CAB000361.

MIM

131300. phenotype.
190180. gene.

neXtProt

NX_P01137.

Orphanet

1328. Camurati-Engelmann disease.
98963. Corneal dystrophy, Avellino type.

PharmGKB

PA350.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG16068.

HOGENOM

HBG444250.

HOVERGEN

HBG074115.

InParanoid

P01137.

OrthoDB

EOG4NKBVP.

Enzyme and pathway databases

Pathway_Interaction_DB

glypican_1pathway. Glypican 1 network.
il12_stat4pathway. IL12 signaling mediated by STAT4.
il27pathway. IL27-mediated signaling events.
rxr_vdr_pathway. RXR and RAR hetrodimerization with other nuclear receptor.
syndecan_2_pathway. Syndecan-2-mediated signaling events.
tgfbrpathway. TGF-beta receptor signaling.

Reactome

REACT_111102. Signal Transduction.
REACT_604. Hemostasis.
REACT_6167. Influenza Infection.

Gene expression databases

ArrayExpress

P01137.

Bgee

P01137.

CleanEx

HS_TGFB1.

Genevestigator

P01137.

GermOnline

ENSG00000105329. Homo sapiens.

Family and domain databases

InterPro

IPR001839. TGF-b_C.
IPR001111. TGF-b_N.
IPR016319. TGF-beta.
IPR015615. TGF-beta-rel.
IPR003939. TGFb1.
IPR017948. TGFb_CS.
[Graphical view]

KO

K13375.

PANTHER

PTHR11848. TGFbeta. 1 hit.

Pfam

PF00019. TGF_beta. 1 hit.
PF00688. TGFb_propeptide. 1 hit.
[Graphical view]

PIRSF

PIRSF001787. TGF-beta. 1 hit.

PRINTS

PR01423. TGFBETA.
PR01424. TGFBETA1.

SMART

SM00204. TGFB. 1 hit.
[Graphical view]

PROSITE

PS00250. TGF_BETA_1. 1 hit.
PS51362. TGF_BETA_2. 1 hit.
[Graphical view]

ProtoNet

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Other

DrugBank

DB00070. Hyaluronidase.

NextBio

27507.

SOURCE

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Entry information

Entry name

TGFB1_HUMAN

Accession

Primary (citable) accession number: P01137
Secondary accession number(s): A8K792, Q9UCG4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	February 1, 1991
Last modified:	January 25, 2012
This is version 167 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.