LTBP1
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
TGFB1
Gene Ontology Biological Process
- ATP biosynthetic process [IDA]
- MAPK cascade [IMP]
- SMAD protein complex assembly [IDA]
- SMAD protein import into nucleus [IDA]
- SMAD protein signal transduction [IBA]
- active induction of host immune response by virus [TAS]
- blood coagulation [TAS]
- cell cycle arrest [IDA]
- cell-cell junction organization [IDA]
- cellular response to organic cyclic compound [IDA]
- cellular response to transforming growth factor beta stimulus [IDA]
- chondrocyte differentiation [IDA]
- common-partner SMAD protein phosphorylation [IDA]
- connective tissue replacement involved in inflammatory response wound healing [TAS]
- epidermal growth factor receptor signaling pathway [IDA]
- evasion or tolerance of host defenses by virus [IDA]
- extracellular matrix assembly [IDA]
- extracellular matrix organization [TAS]
- extrinsic apoptotic signaling pathway [IDA]
- hematopoietic progenitor cell differentiation [IDA]
- hyaluronan catabolic process [IDA]
- inflammatory response [IDA]
- lipopolysaccharide-mediated signaling pathway [IDA]
- lymph node development [ISS]
- macrophage derived foam cell differentiation [IC]
- mitotic cell cycle checkpoint [IDA]
- modulation by virus of host morphology or physiology [TAS]
- negative regulation of DNA replication [IMP]
- negative regulation of blood vessel endothelial cell migration [IDA]
- negative regulation of cell cycle [IDA]
- negative regulation of cell growth [IDA]
- negative regulation of cell proliferation [IDA]
- negative regulation of cell-cell adhesion [IDA]
- negative regulation of epithelial cell proliferation [IDA, IMP]
- negative regulation of extracellular matrix disassembly [IC]
- negative regulation of fat cell differentiation [IDA]
- negative regulation of gene expression [IDA]
- negative regulation of hyaluronan biosynthetic process [IDA]
- negative regulation of macrophage cytokine production [IDA]
- negative regulation of mitotic cell cycle [IDA]
- negative regulation of myoblast differentiation [IDA]
- negative regulation of protein phosphorylation [IDA]
- negative regulation of skeletal muscle tissue development [IDA]
- negative regulation of transcription, DNA-templated [IDA]
- negative regulation of transforming growth factor beta receptor signaling pathway [TAS]
- ossification involved in bone remodeling [IEP]
- pathway-restricted SMAD protein phosphorylation [IDA]
- phosphate-containing compound metabolic process [IDA]
- platelet activation [TAS]
- platelet degranulation [TAS]
- positive regulation of MAP kinase activity [IDA]
- positive regulation of NAD+ ADP-ribosyltransferase activity [IDA]
- positive regulation of SMAD protein import into nucleus [IDA]
- positive regulation of blood vessel endothelial cell migration [IDA]
- positive regulation of bone mineralization [IEP]
- positive regulation of cell migration [IDA]
- positive regulation of cell proliferation [IDA]
- positive regulation of cellular protein metabolic process [IDA]
- positive regulation of chemotaxis [IDA]
- positive regulation of collagen biosynthetic process [IDA, IMP]
- positive regulation of epithelial to mesenchymal transition [IDA, NAS]
- positive regulation of extracellular matrix assembly [IC]
- positive regulation of fibroblast migration [IDA]
- positive regulation of gene expression [IDA]
- positive regulation of interleukin-17 production [IDA]
- positive regulation of isotype switching to IgA isotypes [IDA]
- positive regulation of pathway-restricted SMAD protein phosphorylation [IDA]
- positive regulation of peptidyl-serine phosphorylation [IDA]
- positive regulation of peptidyl-threonine phosphorylation [IDA]
- positive regulation of phosphatidylinositol 3-kinase activity [IDA]
- positive regulation of protein complex assembly [IDA]
- positive regulation of protein dephosphorylation [IDA]
- positive regulation of protein import into nucleus [IDA]
- positive regulation of protein kinase B signaling [IDA]
- positive regulation of protein phosphorylation [IDA]
- positive regulation of protein secretion [IDA]
- positive regulation of superoxide anion generation [IDA]
- positive regulation of transcription from RNA polymerase II promoter [IDA]
- positive regulation of transcription regulatory region DNA binding [IDA]
- positive regulation of transcription, DNA-templated [IDA, ISS]
- positive regulation vascular endothelial growth factor production [TAS]
- protein export from nucleus [IDA]
- protein import into nucleus, translocation [IDA]
- protein kinase B signaling [IMP]
- protein phosphorylation [ISS]
- receptor catabolic process [IDA]
- regulation of DNA binding [ISS]
- regulation of apoptotic process [IBA]
- regulation of binding [ISS]
- regulation of blood vessel remodeling [IC]
- regulation of cell migration [TAS]
- regulation of miRNA metabolic process [IDA]
- regulation of protein import into nucleus [ISS]
- regulation of striated muscle tissue development [ISS]
- regulation of transforming growth factor beta receptor signaling pathway [IDA]
- response to cholesterol [IDA]
- response to estradiol [IDA]
- response to progesterone [IDA]
- response to wounding [IEP]
- salivary gland morphogenesis [IEP]
- transforming growth factor beta receptor signaling pathway [IDA, TAS]
- viral life cycle [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Reconstituted Complex
An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator.
Publication
Specific sequence motif of 8-Cys repeats of TGF-beta binding proteins, LTBPs, creates a hydrophobic interaction surface for binding of small latent TGF-beta.
Transforming growth factor (TGF)-betas are secreted in large latent complexes consisting of TGF-beta, its N-terminal latency-associated peptide (LAP) propeptide, and latent TGF-beta binding protein (LTBP). LTBPs are required for secretion and subsequent deposition of TGF-beta into the extracellular matrix. TGF-beta1 associates with the 3(rd) 8-Cys repeat of LTBP-1 by LAP. All LTBPs, as well as fibrillins, contain multiple 8-Cys repeats. ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| LTBP1 TGFB1 | Affinity Capture-Western Affinity Capture-Western An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins. | Low | - | BioGRID | - |
Curated By
- BioGRID