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Protein Page:
TGFB1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
TGFB1 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. Homodimer; disulfide-linked, or heterodimer with TGFB2. 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. 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. Interacts with CD109, DPT and ASPN. Activated in vitro at pH below 3.5 and over 12.5. 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. Belongs to the TGF-beta family. Note: This description may include information from UniProtKB.
Protein type: Secreted; Secreted, signal peptide; Motility/polarity/chemotaxis
Cellular Component: proteinaceous extracellular matrix; extracellular space; microvillus; cell surface; cell soma; axon; Golgi lumen; cytoplasm; plasma membrane; extracellular region; nucleus
Molecular Function: protein binding; enzyme binding; protein homodimerization activity; growth factor activity; protein heterodimerization activity; punt binding; cytokine activity; protein N-terminus binding; glycoprotein binding; antigen binding
Biological Process: extracellular matrix organization and biogenesis; positive regulation of apoptosis; positive regulation of transcription, DNA-dependent; SMAD protein nuclear translocation; female pregnancy; positive regulation of protein amino acid dephosphorylation; activation of NF-kappaB transcription factor; regulation of protein import into nucleus; positive regulation of MAP kinase activity; connective tissue replacement during inflammatory response; regulation of transforming growth factor beta receptor signaling pathway; negative regulation of ossification; cell cycle arrest; inner ear development; positive regulation of isotype switching to IgA isotypes; regulatory T cell differentiation; positive regulation of interleukin-17 production; response to drug; positive regulation of chemotaxis; positive regulation of smooth muscle cell differentiation; active induction of host immune response by virus; positive regulation of blood vessel endothelial cell migration; negative regulation of immune response; regulation of sodium ion transport; negative regulation of fat cell differentiation; negative regulation of blood vessel endothelial cell migration; lymph node development; positive regulation of protein secretion; positive regulation of cell division; positive regulation of transcription from RNA polymerase II promoter; response to progesterone stimulus; endoderm development; myelination; positive regulation of odontogenesis; negative regulation of phagocytosis; evasion of host defenses by virus; positive regulation of cellular protein metabolic process; myeloid dendritic cell differentiation; negative regulation of transcription from RNA polymerase II promoter; phosphate metabolic process; negative regulation of cell proliferation; negative regulation of T cell proliferation; regulation of DNA binding; ureteric bud development; negative regulation of release of sequestered calcium ion into cytosol; salivary gland morphogenesis; positive regulation of cell proliferation; protein kinase B signaling cascade; protein export from nucleus; inflammatory response; positive regulation of exit from mitosis; aging; epidermal growth factor receptor signaling pathway; mitotic cell cycle checkpoint; common-partner SMAD protein phosphorylation; positive regulation of phosphoinositide 3-kinase activity; positive regulation of bone mineralization; positive regulation of peptidyl-serine phosphorylation; SMAD protein complex assembly; positive regulation of protein kinase B signaling cascade; embryonic development; positive regulation of protein complex assembly; positive regulation of protein import into nucleus; response to hypoxia; epithelial to mesenchymal transition; negative regulation of cell-cell adhesion; negative regulation of cell growth; negative regulation of transforming growth factor beta receptor signaling pathway; negative regulation of skeletal muscle development; mononuclear cell proliferation; protein amino acid phosphorylation; regulation of cell migration; hyaluronan catabolic process; response to vitamin D; negative regulation of neuroblast proliferation; receptor catabolic process; transforming growth factor beta receptor signaling pathway; positive regulation of superoxide release; germ cell migration; response to glucose stimulus; chondrocyte differentiation; negative regulation of mitotic cell cycle; T cell homeostasis; defense response to fungus, incompatible interaction; cell growth; tolerance induction to self antigen; regulation of striated muscle development; platelet activation; organ regeneration; negative regulation of DNA replication; virus-host interaction; hemopoietic progenitor cell differentiation; negative regulation of transcription, DNA-dependent; positive regulation of epithelial cell proliferation; positive regulation of collagen biosynthetic process; viral infectious cycle; response to estradiol stimulus; negative regulation of cell cycle; response to radiation; positive regulation of histone deacetylation; platelet degranulation; negative regulation of protein amino acid phosphorylation; lipopolysaccharide-mediated signaling pathway; response to wounding; adaptive immune response based on somatic recombination of immune receptors built from immunoglobulin superfamily domains; negative regulation of epithelial cell proliferation; intercellular junction assembly and maintenance; regulation of binding; MAPKKK cascade; cellular calcium ion homeostasis; gut development; protein import into nucleus, translocation; ATP biosynthetic process; positive regulation of histone acetylation; positive regulation of protein amino acid phosphorylation; blood coagulation; negative regulation of myoblast differentiation; positive regulation of cell migration
Reference #:  P01137 (UniProtKB)
Alt. Names/Synonyms: CED; DPD1; LAP; Latency-associated peptide; TGF-beta 1 protein; TGF-beta-1; TGFB; TGFB1; TGFbeta; Transforming growth factor beta-1; transforming growth factor, beta 1
Gene Symbols: TGFB1
Molecular weight: 44,341 Da
Basal Isoelectric point: 8.83  Predict pI for various phosphorylation states
CST Pathways:  Regulation of P38 MAPKs  |  Wnt/ß-Catenin Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

TGFB1

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 K106-ub PEADYYAkEVTRVLM
0 1 K163-ub RLLRLKLkVEQHVEL
0 2 K291-ub YCFSSTEkNCCVRQL
0 1 Y317-p WIHEPKGyHANFCLG
  mouse

 
K106 PEADYYAKEVTRVLM
S163 RLQRLKSSVEQHVEL
K291 YCFSSTEKNCCVRQL
Y317 WIHEPKGYHANFCLG
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