Gene Ontology annotation through association of InterPro records with GO terms.
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity.
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt.
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara.
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods.
Isolation and characterization of a high molecular weight glycoprotein from human blood platelets.
Signals leading to apoptosis-dependent inhibition of neovascularization by thrombospondin-1.
Histidine-rich glycoprotein inhibits the antiangiogenic effect of thrombospondin-1.
Thrombospondin 1 is an autocrine negative regulator of human dendritic cell activation.
Insulin-like growth factor binding protein-5 (IGFBP-5) interacts with thrombospondin-1 to induce negative regulatory effects on IGF-I actions.
A functional SNP in CILP, encoding cartilage intermediate layer protein, is associated with susceptibility to lumbar disc disease.
Thrombospondin-1 inhibits endothelial cell responses to nitric oxide in a cGMP-dependent manner.
Human colostrum: identification of minor proteins in the aqueous phase by proteomics.
Apoptotic cell thrombospondin-1 and heparin-binding domain lead to dendritic-cell phagocytic and tolerizing states.
Interaction of alpha9beta1 integrin with thrombospondin-1 promotes angiogenesis.
Thrombospondin-1 inhibits nitric oxide signaling via CD36 by inhibiting myristic acid uptake.
Novel antiangiogenic pathway of thrombospondin-1 mediated by suppression of the cell cycle.
Syndecan-4 contributes to endothelial tubulogenesis through interactions with two motifs inside the pro-angiogenic N-terminal domain of thrombospondin-1.
Fibroblast growth factor-2 binding to the thrombospondin-1 type III repeats, a novel antiangiogenic domain.
TSG-6 binds via its CUB_C domain to the cell-binding domain of fibronectin and increases fibronectin matrix assembly.
Cell type-specific post-transcriptional regulation of production of the potent antiangiogenic and proatherogenic protein thrombospondin-1 by high glucose.
Extracellular matrix retention of thrombospondin 1 is controlled by its conserved C-terminal region.
Differential involvement of TGF-beta1 in mediating the motogenic effects of TSP-1 on endothelial cells, fibroblasts and oral tumour cells.
Thrombospondin 1 binding to calreticulin-LRP1 signals resistance to anoikis.
Thrombospondin-1 and transforming growth factor beta are pro-inflammatory molecules in rheumatoid arthritis.
Calumenin but not reticulocalbin forms a Ca2+-dependent complex with thrombospondin-1. A potential role in haemostasis and thrombosis.
Thrombospondin-1-induced apoptosis of brain microvascular endothelial cells can be mediated by TNF-R1.
Thrombospondin 1 promotes tumor macrophage recruitment and enhances tumor cell cytotoxicity of differentiated U937 cells.
Phosphatidylserine-positive erythrocytes bind to immobilized and soluble thrombospondin-1 via its heparin-binding domain.
Differential interactions of thrombospondin-1, -2, and -4 with CD47 and effects on cGMP signaling and ischemic injury responses.
Large-scale proteomics and phosphoproteomics of urinary exosomes.
Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT).
The first draft of the endostatin interaction network.
Induction of thrombospondin-1 partially mediates the anti-angiogenic activity of dexrazoxane.
Proteomics characterization of extracellular space components in the human aorta.
Protein profile of exosomes from trabecular meshwork cells.
Proteomics analysis of cardiac extracellular matrix remodeling in a porcine model of ischemia/reperfusion injury.
Endogenous thrombospondin-1 regulates leukocyte recruitment and activation and accelerates death from systemic candidiasis.
In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine.
Comparative proteomic analysis of supportive and unsupportive extracellular matrix substrates for human embryonic stem cell maintenance.
Thrombospondin-1 modulates VEGF signaling via CD36 by recruiting SHP-1 to VEGFR2 complex in microvascular endothelial cells.
SILAC-based proteomics of human primary endothelial cell morphogenesis unveils tumor angiogenic markers.
Extended interaction network of procollagen C-proteinase enhancer-1 in the extracellular matrix.
MicroRNA miR-27b rescues bone marrow-derived angiogenic cell function and accelerates wound healing in type 2 diabetes mellitus.
Isolation of the thrombospondin membrane receptor.
Thrombospondin-1 activation of signal-regulatory protein-α stimulates reactive oxygen species production and promotes renal ischemia reperfusion injury.
Interleukin-18 may lead to benign prostatic hyperplasia via thrombospondin-1 production in prostatic smooth muscle cells.
An integrin receptor on normal and thrombasthenic platelets that binds thrombospondin.
miR-487b promotes human umbilical vein endothelial cell proliferation, migration, invasion and tube formation through regulating THBS1.
Angiogenic microRNAs Linked to Incidence and Progression of Diabetic Retinopathy in Type 1 Diabetes.
Extracellular Fibrinogen-binding Protein (Efb) from Staphylococcus aureus Inhibits the Formation of Platelet-Leukocyte Complexes.
Extracellular matrix remodelling in response to venous hypertension: proteomics of human varicose veins.
Bone morphogenetic protein 4 regulates microRNAs miR-494 and miR-126-5p in control of endothelial cell function in angiogenesis.
Comprehensive proteomic characterization of stem cell-derived extracellular matrices.
Proteomic characterization of human multiple myeloma bone marrow extracellular matrix.
Interaction of thrombospondin with resting and stimulated human platelets.
Complex formation of human thrombospondin with osteonectin.
Incorporation of thrombospondin into fibrin clots.
Cultured human fibroblasts synthesize and secrete thrombospondin and incorporate it into extracellular matrix.
Complex formation of platelet thrombospondin with plasminogen. Modulation of activation by tissue activator.
Thrombospondin interactions with fibronectin and fibrinogen. Mutual inhibition in binding.
Interactions of thrombospondin with extracellular matrix proteins: selective binding to type V collagen.
Ca2+-mediated association of glycoprotein G (thrombinsensitive protein, thrombospondin) with human platelets.
Characterization of the antiplasmin activity of human thrombospondin-1 in solution.
Thrombospondin 3 is a developmentally regulated heparin binding protein.
Integrin-associated protein is a receptor for the C-terminal domain of thrombospondin.
THBS1 (Thrombospondin-1) binds Integrin alpha3beta1, alpha4beta1
Interaction of integrin alphaIIb beta 3 with THBS1 (Thrombospondin-1)
PDGF binds to extracellular matrix proteins
Exocytosis of platelet alpha granule contents
B3GALTL transfers glucose to O-fucosyl-proteins
POFUT2 transfers fucose to TSR domain-containing proteins
Defective B3GALTL does not transfer glucose to O-fucosyl-proteins
THBS1 gene transcription is stimulated by the complex containing RUNX1, PRMT1 and GATA1 and inhibited by the complex of RUNX1, SIN3A and PRMT6
Deep research on THBS1 function
Falcon (Edison) deep research on THBS1 function
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THBS1/TSP-1 is a secreted matricellular (ECM-associated) glycoprotein in the Group A thrombospondin subfamily that forms trimers in the extracellular space; the CTD contains a CD47-binding site and the TSRs (type I repeats) are necessary for binding latent TGF-β and CD36, while the NTD and EGF-like domains participate in integrin interactions.
"a secreted matricellular (ECM-associated) glycoprotein in the Group A thrombospondin subfamily that forms trimers in the extracellular space"
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THBS1 is repeatedly described as a major activator of latent TGF-β1 in vivo, positioning it upstream of profibrotic and immunoregulatory Smad signaling and ECM remodeling.
"Multiple 2023–2024 sources characterize THBS1/TSP‑1 as a major mediator/activator of latent TGF‑β. This function positions THBS1 upstream of profibrotic and immunoregulatory programs (e.g., Smad signaling and downstream ECM remodeling)."
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THBS1 binds CD47 via its C-terminal domain and triggers signaling that suppresses nitric oxide (NO) pathway effects, antagonising NO/cGMP-dependent vasodilation.
"THBS1 binds CD47 (via CTD) and triggers signaling that suppresses nitric oxide (NO) pathway effects."
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THBS1-CD47 signaling antagonises NO/cGMP-dependent signaling, with consequences for vascular smooth muscle relaxation/vasodilation and ischaemic survival.
"THBS1–CD47 signaling **antagonizes NO/cGMP-dependent signaling**, with consequences for vascular smooth muscle relaxation/vasodilation and ischemic survival."
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THBS1 binds CD36 via its TSRs and contributes to platelet and vascular effects; CD36 also mediates THBS1's anti-angiogenic signaling.
"THBS1 binds CD36 (via TSRs) and contributes to platelet and vascular effects; CD36 is also part of anti-angiogenic signaling."
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THBS1 binds multiple integrins through its NTD and EGF-like domains, contributing to endothelial migration and vascular remodelling.
"THBS1 binds multiple integrins; 2024 synthesis places integrin binding across NTD and EGF-like domains and highlights integrin involvement in endothelial migration/vascular remodeling."
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THBS1 is a major component of platelet α-granules, rapidly released at injury sites and supporting platelet activation, vasoconstriction, and thrombus formation (via CD36 and NO pathway suppression).
"THBS1 is described as a major component of platelet α‑granules and is rapidly released at injury sites, supporting platelet activation, vasoconstriction, and thrombus formation"
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In intestinal mucosal wound repair, epithelial THBS1 promotes restitution through CD47- and TGF-β1-dependent signaling, with effects on SMAD2/3 phosphorylation and RhoA/Rac1 cytoskeletal dynamics (Wilson et al. 2024 JCI Insight).
"a tissue-protective role for epithelial THBS1 in intestinal mucosal wound repair, mechanistically coupled to CD47 and TGF-β1 signaling and to cytoskeletal pathway interrogation (RhoA/Rac1; SMAD2/3)"
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In prostate cancer models, THBS1 is a TGF-β-induced secreted ECM protein that interacts with integrin αV (ITGAV) and TGF-β receptor I (TβRI) at the leading edge to mediate migration, invasion, and metastasis (Mu et al. 2024 Oncogene).
"THBS1 mediates migration/invasion by **interacting with integrin αV (ITGAV) and TGF‑β receptor I (TβRI)**; deletion of THBS1 or TβRI prevented migration and invasion in experimental systems."
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Kaur & Roberts (2023) highlight that, despite viable Thbs1 knockout mice, human population genetics indicate THBS1 is loss-intolerant, consistent with an essential stress-response role in surviving environmental challenges between birth and reproduction.
"human population genetics indicate THBS1 is **loss-intolerant**, and propose that THBS1's essentiality in humans may reflect the need to survive **environmental stresses** encountered between birth and reproduction"