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P01137 (TGFB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 196. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length390 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

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. Ref.12 Ref.15 Ref.17

Subcellular location

Secretedextracellular spaceextracellular matrix Ref.17.

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. Ref.13 Ref.17

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.

Post-translational modification

Glycosylated.

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

Camurati-Engelmann disease (CE) [MIM:131300]: 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.23 Ref.24 Ref.26 Ref.27 Ref.28

Sequence similarities

Belongs to the TGF-beta family.

Ontologies

Keywords
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainSignal
   Molecular functionGrowth factor
Mitogen
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP biosynthetic process

Inferred from direct assay PubMed 10513816. Source: BHF-UCL

MAPK cascade

Inferred from mutant phenotype PubMed 21147091. Source: UniProtKB

SMAD protein complex assembly

Inferred from direct assay PubMed 17438144. Source: BHF-UCL

SMAD protein import into nucleus

Inferred from direct assay PubMed 15334054. Source: BHF-UCL

T cell homeostasis

Inferred from electronic annotation. Source: Ensembl

active induction of host immune response by virus

Traceable author statement. Source: Reactome

adaptive immune response based on somatic recombination of immune receptors built from immunoglobulin superfamily domains

Inferred from electronic annotation. Source: Ensembl

aging

Inferred from electronic annotation. Source: Ensembl

blood coagulation

Traceable author statement. Source: Reactome

branch elongation involved in mammary gland duct branching

Inferred from electronic annotation. Source: Ensembl

cell cycle arrest

Inferred from direct assay PubMed 14555988. Source: BHF-UCL

cell growth

Inferred from electronic annotation. Source: InterPro

cell-cell junction organization

Inferred from direct assay PubMed 18505915. Source: BHF-UCL

cellular calcium ion homeostasis

Inferred from electronic annotation. Source: Ensembl

cellular response to dexamethasone stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to organic cyclic compound

Inferred from direct assay PubMed 21147091. Source: UniProtKB

chondrocyte differentiation

Inferred from direct assay PubMed 15040835. Source: UniProtKB

common-partner SMAD protein phosphorylation

Inferred from direct assay PubMed 20573232. Source: UniProtKB

connective tissue replacement involved in inflammatory response wound healing

Traceable author statement PubMed 9639571. Source: BHF-UCL

defense response to fungus, incompatible interaction

Inferred from electronic annotation. Source: Ensembl

digestive tract development

Inferred from electronic annotation. Source: Ensembl

embryo development

Inferred from electronic annotation. Source: Ensembl

endoderm development

Inferred from electronic annotation. Source: Ensembl

epidermal growth factor receptor signaling pathway

Inferred from direct assay PubMed 18625725. Source: BHF-UCL

epithelial to mesenchymal transition

Inferred from electronic annotation. Source: Ensembl

evasion or tolerance of host defenses by virus

Inferred from direct assay PubMed 15334054. Source: BHF-UCL

extracellular matrix assembly

Inferred from direct assay PubMed 19734317. Source: BHF-UCL

extracellular matrix organization

Traceable author statement. Source: Reactome

extrinsic apoptotic signaling pathway

Inferred from direct assay PubMed 15334054. Source: BHF-UCL

face morphogenesis

Inferred from electronic annotation. Source: Ensembl

female pregnancy

Inferred from electronic annotation. Source: Ensembl

frontal suture morphogenesis

Inferred from electronic annotation. Source: Ensembl

germ cell migration

Inferred from electronic annotation. Source: Ensembl

hematopoietic progenitor cell differentiation

Inferred from direct assay PubMed 15451575. Source: UniProtKB

hyaluronan catabolic process

Inferred from direct assay PubMed 17324121. Source: UniProtKB

inflammatory response

Inferred from direct assay PubMed 21147091. Source: UniProtKB

inner ear development

Inferred from electronic annotation. Source: Ensembl

lens fiber cell differentiation

Inferred from electronic annotation. Source: Ensembl

lipopolysaccharide-mediated signaling pathway

Inferred from direct assay PubMed 21147091. Source: UniProtKB

lymph node development

Inferred from sequence or structural similarity. Source: UniProtKB

macrophage derived foam cell differentiation

Inferred by curator PubMed 15219857. Source: BHF-UCL

mammary gland branching involved in thelarche

Inferred from electronic annotation. Source: Ensembl

mitotic cell cycle checkpoint

Inferred from direct assay PubMed 15334054. Source: BHF-UCL

modulation by virus of host morphology or physiology

Traceable author statement. Source: Reactome

mononuclear cell proliferation

Inferred from electronic annotation. Source: Ensembl

myelination

Inferred from electronic annotation. Source: Ensembl

myeloid dendritic cell differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of DNA replication

Inferred from mutant phenotype PubMed 11158066. Source: BHF-UCL

negative regulation of T cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of blood vessel endothelial cell migration

Inferred from direct assay PubMed 18555217. Source: BHF-UCL

negative regulation of cell cycle

Inferred from direct assay PubMed 11502704. Source: HGNC

negative regulation of cell growth

Inferred from direct assay PubMed 15334054. Source: BHF-UCL

negative regulation of cell proliferation

Inferred from direct assay PubMed 15334054. Source: BHF-UCL

negative regulation of cell-cell adhesion

Inferred from direct assay PubMed 18593713. Source: BHF-UCL

negative regulation of epithelial cell proliferation

Inferred from direct assay PubMed 9950587. Source: BHF-UCL

negative regulation of fat cell differentiation

Inferred from direct assay PubMed 15040835. Source: UniProtKB

negative regulation of hyaluronan biosynthetic process

Inferred from direct assay PubMed 17324121. Source: UniProtKB

negative regulation of immune response

Inferred from electronic annotation. Source: Ensembl

negative regulation of macrophage cytokine production

Inferred from direct assay PubMed 20875417. Source: DFLAT

negative regulation of mitotic cell cycle

Inferred from direct assay PubMed 14555988. Source: BHF-UCL

negative regulation of myoblast differentiation

Inferred from direct assay PubMed 9770491. Source: UniProtKB

negative regulation of neuroblast proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of ossification

Inferred from electronic annotation. Source: Ensembl

negative regulation of phagocytosis

Inferred from electronic annotation. Source: Ensembl

negative regulation of protein phosphorylation

Inferred from direct assay PubMed 8053900. Source: BHF-UCL

negative regulation of release of sequestered calcium ion into cytosol

Inferred from electronic annotation. Source: Ensembl

negative regulation of skeletal muscle tissue development

Inferred from direct assay PubMed 9770491. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 18832382. Source: UniProtKB

negative regulation of transforming growth factor beta receptor signaling pathway

Traceable author statement. Source: Reactome

organ regeneration

Inferred from electronic annotation. Source: Ensembl

ossification involved in bone remodeling

Inferred from expression pattern PubMed 17401695. Source: BHF-UCL

pathway-restricted SMAD protein phosphorylation

Inferred from direct assay PubMed 11157754PubMed 17999987PubMed 18453574. Source: BHF-UCL

phosphate-containing compound metabolic process

Inferred from direct assay PubMed 10513816. 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 PubMed 18625725. Source: BHF-UCL

positive regulation of NAD+ ADP-ribosyltransferase activity

Inferred from direct assay PubMed 22073128. Source: BHF-UCL

positive regulation of NF-kappaB transcription factor activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of SMAD protein import into nucleus

Inferred from direct assay PubMed 19366691PubMed 9389648. Source: BHF-UCL

positive regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of blood vessel endothelial cell migration

Inferred from direct assay PubMed 18555217. Source: BHF-UCL

positive regulation of bone mineralization

Inferred from expression pattern PubMed 17401695. Source: BHF-UCL

positive regulation of branching involved in ureteric bud morphogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell cycle arrest

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell division

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of cell migration

Inferred from direct assay PubMed 19736306. Source: BHF-UCL

positive regulation of cell proliferation

Inferred from direct assay PubMed 10513816. Source: BHF-UCL

positive regulation of cellular protein metabolic process

Inferred from direct assay PubMed 15219857. Source: BHF-UCL

positive regulation of chemotaxis

Inferred from direct assay PubMed 18555217. Source: BHF-UCL

positive regulation of collagen biosynthetic process

Inferred from direct assay PubMed 19734317PubMed 22269326. Source: BHF-UCL

positive regulation of epithelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of epithelial to mesenchymal transition

Inferred from direct assay PubMed 17999987PubMed 18505915. Source: BHF-UCL

positive regulation of exit from mitosis

Inferred from electronic annotation. Source: Ensembl

positive regulation of fibroblast migration

Inferred from direct assay PubMed 18555217. Source: BHF-UCL

positive regulation of gene expression

Inferred from direct assay PubMed 18832382. Source: UniProtKB

positive regulation of histone acetylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of histone deacetylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of interleukin-17 production

Inferred from direct assay PubMed 18453574. Source: BHF-UCL

positive regulation of isotype switching to IgA isotypes

Inferred from direct assay PubMed 14988498. Source: MGI

positive regulation of odontogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of pathway-restricted SMAD protein phosphorylation

Inferred from direct assay PubMed 19736306PubMed 9389648. Source: BHF-UCL

positive regulation of peptidyl-serine phosphorylation

Inferred from direct assay PubMed 18625725PubMed 19736306. Source: BHF-UCL

positive regulation of peptidyl-threonine phosphorylation

Inferred from direct assay PubMed 18625725PubMed 19736306. Source: BHF-UCL

positive regulation of phosphatidylinositol 3-kinase activity

Inferred from direct assay PubMed 18625725. Source: BHF-UCL

positive regulation of protein complex assembly

Inferred from direct assay PubMed 19366691. Source: BHF-UCL

positive regulation of protein dephosphorylation

Inferred from direct assay PubMed 14555988. Source: BHF-UCL

positive regulation of protein import into nucleus

Inferred from direct assay PubMed 19366691. Source: BHF-UCL

positive regulation of protein kinase B signaling

Inferred from direct assay PubMed 18625725. Source: BHF-UCL

positive regulation of protein phosphorylation

Inferred from direct assay PubMed 18625725. Source: BHF-UCL

positive regulation of protein secretion

Inferred from direct assay PubMed 18505915. Source: BHF-UCL

positive regulation of smooth muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of superoxide anion generation

Inferred from direct assay PubMed 22073128. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 18832382. Source: UniProtKB

positive regulation of transcription regulatory region DNA binding

Inferred from direct assay PubMed 22073128. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 16816361. Source: UniProtKB

positive regulation vascular endothelial growth factor production

Traceable author statement PubMed 19506300. Source: BHF-UCL

protein export from nucleus

Inferred from direct assay PubMed 18588859PubMed 9770491. Source: UniProtKB

protein import into nucleus, translocation

Inferred from direct assay PubMed 21390327. Source: UniProtKB

protein kinase B signaling

Inferred from mutant phenotype PubMed 21147091. Source: UniProtKB

protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

receptor catabolic process

Inferred from direct assay PubMed 17878231. Source: BHF-UCL

regulation of DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of binding

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of branching involved in mammary gland duct morphogenesis

Inferred from electronic annotation. Source: Ensembl

regulation of cartilage development

Inferred from electronic annotation. Source: Ensembl

regulation of cell migration

Traceable author statement PubMed 19018011. Source: BHF-UCL

regulation of protein import into nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of sodium ion transport

Inferred from electronic annotation. Source: Ensembl

regulation of striated muscle tissue development

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of transforming growth factor beta receptor signaling pathway

Inferred from direct assay PubMed 15334054. Source: BHF-UCL

regulatory T cell differentiation

Inferred from electronic annotation. Source: Ensembl

response to cholesterol

Inferred from direct assay PubMed 17878231. Source: BHF-UCL

response to drug

Inferred from electronic annotation. Source: Ensembl

response to estradiol

Inferred from direct assay PubMed 18039789. Source: BHF-UCL

response to glucose

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to laminar fluid shear stress

Inferred from electronic annotation. Source: Ensembl

response to progesterone

Inferred from direct assay PubMed 18039789. Source: BHF-UCL

response to radiation

Inferred from electronic annotation. Source: Ensembl

response to vitamin D

Inferred from electronic annotation. Source: Ensembl

response to wounding

Inferred from expression pattern PubMed 18040277. Source: BHF-UCL

salivary gland morphogenesis

Inferred from expression pattern PubMed 18080134. Source: BHF-UCL

tolerance induction to self antigen

Inferred from electronic annotation. Source: Ensembl

transforming growth factor beta receptor signaling pathway

Inferred from direct assay PubMed 11157754PubMed 9389648. Source: BHF-UCL

ureteric bud development

Inferred from electronic annotation. Source: Ensembl

viral life cycle

Traceable author statement. Source: Reactome

   Cellular_componentGolgi lumen

Traceable author statement. Source: Reactome

axon

Inferred from electronic annotation. Source: Ensembl

blood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

cell surface

Inferred from mutant phenotype PubMed 19366691. Source: BHF-UCL

cytoplasm

Inferred from direct assay PubMed 18040277. Source: BHF-UCL

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 19734317. Source: BHF-UCL

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 18040277. Source: BHF-UCL

plasma membrane

Traceable author statement. Source: Reactome

platelet alpha granule lumen

Traceable author statement. Source: Reactome

proteinaceous extracellular matrix

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionantigen binding

Inferred from physical interaction Ref.15. Source: UniProt

cytokine activity

Traceable author statement PubMed 24263861. Source: AgBase

enzyme binding

Inferred from physical interaction PubMed 19366691. Source: BHF-UCL

protein binding

Inferred from physical interaction Ref.17PubMed 20505824PubMed 8370410. Source: UniProtKB

type II transforming growth factor beta receptor binding

Inferred from direct assay PubMed 11157754. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Ref.10
Chain30 – 278249Latency-associated peptide
PRO_0000033762
Chain279 – 390112Transforming growth factor beta-1
PRO_0000033763

Regions

Region30 – 7445Straightjacket domain By similarity
Region75 – 271197Arm domain By similarity
Motif244 – 2463Cell attachment site Potential

Amino acid modifications

Glycosylation821N-linked (GlcNAc...) Ref.14 Ref.16
Glycosylation1361N-linked (GlcNAc...) By similarity
Glycosylation1761N-linked (GlcNAc...) By similarity
Disulfide bond33Interchain (with C-1359 or C-1384 in LTBP1); in inactive form By similarity
Disulfide bond223Interchain (with C-225) By similarity
Disulfide bond225Interchain (with C-223) By similarity
Disulfide bond285 ↔ 294
Disulfide bond293 ↔ 356
Disulfide bond322 ↔ 387
Disulfide bond326 ↔ 389
Disulfide bond355Interchain

Natural variations

Natural variant101L → P Associated with higher bone mineral density and lower frequency of vertebral fractures in Japanese post-menopausal women. Ref.2 Ref.22 Ref.25
Corresponds to variant rs1800470 [ dbSNP | Ensembl ].
VAR_016171
Natural variant251R → P. Ref.2
Corresponds to variant rs1800471 [ dbSNP | Ensembl ].
VAR_016172
Natural variant811Y → H in CE; leads to TGF-beta-1 intracellular accumulation. Ref.24 Ref.26
VAR_017607
Natural variant2181R → C in CE; higher levels of active TGF-beta-1 in the culture medium; enhances osteoclast formation in vitro. Ref.23 Ref.24 Ref.26 Ref.27
VAR_017608
Natural variant2181R → H in CE. Ref.23
VAR_017609
Natural variant2221H → D in CE; sporadic case; higher levels of active TGF-beta-1 in the culture medium. Ref.26
VAR_017610
Natural variant2231C → G in CE. Ref.28
VAR_067303
Natural variant2231C → R in CE. Ref.28
VAR_067304
Natural variant2251C → R in CE; higher levels of active TGF-beta-1 in the culture medium. Ref.23 Ref.24 Ref.26
VAR_017611
Natural variant2631T → I.
Corresponds to variant rs1800472 [ dbSNP | Ensembl ].
VAR_016173

Experimental info

Sequence conflict1591R → RR in CAA26580. Ref.2

Secondary structure

....................... 390
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P01137 [UniParc].

Last modified February 1, 1991. Version 2.
Checksum: 75391614250288FE

FASTA39044,341
        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 

« Hide

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS PRO-10 AND PRO-25.
[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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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 [MRNA] 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-82.
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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-82.
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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH ASPN.
[18]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"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] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 279-390.
[20]"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] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 279-390.
[21]"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] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 279-390.
[22]"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] [Europe PMC] [Abstract]
Cited for: VARIANT PRO-10.
[23]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS CE CYS-218; HIS-218 AND ARG-225.
[24]"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] [Europe PMC] [Abstract]
Cited for: VARIANTS CE HIS-81; CYS-218 AND ARG-225.
[25]"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] [Europe PMC] [Abstract]
Cited for: VARIANT PRO-10.
[26]"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] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS CE HIS-81; CYS-218; ASP-222 AND ARG-225.
[27]"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] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT CE CYS-218.
[28]"TGFB1 mutations in four new families with Camurati-Engelmann disease: confirmation of independently arising LAP-domain-specific mutations."
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.
Am. J. Med. Genet. 127A:104-107(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CE GLY-223 AND ARG-223.
+Additional computationally mapped references.

Web resources

Wikipedia

TGF beta-1 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X05839 expand/collapse EMBL AC list , X05840, X05843, X05844, X05849, X05850 Genomic DNA. Translation: CAA29283.1.
X02812 mRNA. Translation: CAA26580.1.
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.
CCDSCCDS33031.1.
PIRWFHU2. A27513.
RefSeqNP_000651.3. NM_000660.5.
UniGeneHs.645227.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KLANMR-A/B279-390[»]
1KLCNMR-A/B279-390[»]
1KLDNMR-A/B279-390[»]
3KFDX-ray3.00A/B/C/D279-390[»]
ProteinModelPortalP01137.
SMRP01137. Positions 30-390.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112898. 32 interactions.
DIPDIP-5934N.
IntActP01137. 18 interactions.
MINTMINT-6806111.
STRING9606.ENSP00000221930.

Chemistry

BindingDBP01137.
ChEMBLCHEMBL1795178.
DrugBankDB00070. Hyaluronidase.

PTM databases

PhosphoSiteP01137.

Polymorphism databases

DMDM135674.

2D gel databases

OGPP01137.

Proteomic databases

MaxQBP01137.
PaxDbP01137.
PRIDEP01137.

Protocols and materials databases

DNASU7040.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000221930; ENSP00000221930; ENSG00000105329.
GeneID7040.
KEGGhsa:7040.
UCSCuc002oqh.2. human.

Organism-specific databases

CTD7040.
GeneCardsGC19M041837.
GeneReviewsTGFB1.
H-InvDBHIX0015152.
HGNCHGNC:11766. TGFB1.
HPACAB000361.
HPA047516.
MIM131300. phenotype.
190180. gene.
neXtProtNX_P01137.
Orphanet1328. Camurati-Engelmann disease.
586. Cystic fibrosis.
PharmGKBPA350.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG279949.
HOGENOMHOG000290198.
HOVERGENHBG074115.
InParanoidP01137.
KOK13375.
PhylomeDBP01137.
TreeFamTF318514.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_118779. Extracellular matrix organization.
REACT_604. Hemostasis.
SignaLinkP01137.

Gene expression databases

ArrayExpressP01137.
BgeeP01137.
CleanExHS_TGFB1.
GenevestigatorP01137.

Family and domain databases

Gene3D2.10.90.10. 1 hit.
InterProIPR029034. Cystine-knot_cytokine.
IPR001839. TGF-b_C.
IPR001111. TGF-b_N.
IPR016319. TGF-beta.
IPR015615. TGF-beta-rel.
IPR003939. TGFb1.
IPR017948. TGFb_CS.
[Graphical view]
PANTHERPTHR11848. PTHR11848. 1 hit.
PfamPF00019. TGF_beta. 1 hit.
PF00688. TGFb_propeptide. 1 hit.
[Graphical view]
PIRSFPIRSF001787. TGF-beta. 1 hit.
PRINTSPR01423. TGFBETA.
PR01424. TGFBETA1.
SMARTSM00204. TGFB. 1 hit.
[Graphical view]
SUPFAMSSF57501. SSF57501. 1 hit.
PROSITEPS00250. TGF_BETA_1. 1 hit.
PS51362. TGF_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTGFB1. human.
EvolutionaryTraceP01137.
GeneWikiTGF_beta_1.
GenomeRNAi7040.
NextBio27507.
PROP01137.
SOURCESearch...

Entry information

Entry nameTGFB1_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 196 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM