Gene Ontology annotation through association of InterPro records with GO terms.
Annotation inferences using phylogenetic trees
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara.
Combined Automated Annotation using Multiple IEA Methods.
Cartilage oligomeric matrix protein is a calcium-binding protein, and a mutation in its type 3 repeats causes conformational changes.
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COMP binds 11-14 calcium ions per subunit
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Each TSP type-3 repeat binds two calcium ions
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Mutations affect COMP conformation
Mutations in cartilage oligomeric matrix protein causing pseudoachondroplasia and multiple epiphyseal dysplasia affect binding of calcium and collagen I, II, and IX.
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Disease mutations affect calcium binding
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COMP binds collagens I, II, and IX
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Collagen binding is zinc-dependent
Matrix-matrix interaction of cartilage oligomeric matrix protein and fibronectin.
Interactions between the cartilage oligomeric matrix protein and matrilins. Implications for matrix assembly and the pathogenesis of chondrodysplasias.
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COMP interacts with MATN1, MATN3, MATN4
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Important for ECM assembly
Cartilage oligomeric matrix protein/thrombospondin 5 supports chondrocyte attachment through interaction with integrins.
Cartilage oligomeric matrix protein is involved in human limb development and in the pathogenesis of osteoarthritis.
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COMP expressed during early limb development
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Found in joint development regions
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Role in osteoarthritis pathogenesis
ADAMTS-12 associates with and degrades cartilage oligomeric matrix protein.
Interaction of cartilage oligomeric matrix protein/thrombospondin 5 with aggrecan.
Cartilage oligomeric matrix protein protects cells against death by elevating members of the IAP family of survival proteins.
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COMP suppresses apoptosis
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Blocks caspase-3 activation
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Induces BIRC2, BIRC3, BIRC5, XIAP
Extracellular matrix retention of thrombospondin 1 is controlled by its conserved C-terminal region.
Inhibition of ADAMTS-7 and ADAMTS-12 degradation of cartilage oligomeric matrix protein by alpha-2-macroglobulin.
Proteomics characterization of extracellular space components in the human aorta.
In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine.
A proteome-scale map of the human interactome network.
Extracellular matrix remodelling in response to venous hypertension: proteomics of human varicose veins.
Lubricin binds cartilage proteins, cartilage oligomeric matrix protein, fibronectin and collagen II at the cartilage surface.
Extensive disruption of protein interactions by genetic variants across the allele frequency spectrum in human populations.
A reference map of the human binary protein interactome.
Author Correction: Mutations in COMP cause familial carpal tunnel syndrome.
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COMP mutations cause CTS2
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Affect pentamerization and secretion
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Induce ER stress in tendon cells
Pseudoachondroplasia and multiple epiphyseal dysplasia due to mutations in the cartilage oligomeric matrix protein gene.
Characterization of human and mouse cartilage oligomeric matrix protein.
COMP binds collagen, fibronectin, aggrecan and matrilins
COMP binds Integrin alpha5beta1, Integrin alphaVbeta3, CD47
Deep research on COMP function
Electronic Gene Ontology annotations created by ARBA machine learning models
The crystal structure of the signature domain of cartilage oligomeric matrix protein: implications for collagen, glycosaminoglycan and integrin binding.
MatrisomeDB 2.0: 2023 updates to the ECM-protein knowledge database.
Mutations in COMP cause familial carpal tunnel syndrome.
COMP acts as a catalyst in collagen fibrillogenesis.
Cartilage oligomeric matrix protein is a natural inhibitor of thrombin.
Cartilage oligomeric matrix protein inhibits vascular smooth muscle calcification by interacting with bone morphogenetic protein-2.
Mild myopathy is associated with COMP but not MATN3 mutations in mouse models of genetic skeletal diseases.
Collagen XII and XIV, new partners of cartilage oligomeric matrix protein in the skin extracellular matrix suprastructure.
Extracellular matrix secretion by cardiac fibroblasts: role of microRNA-29b and microRNA-30c.
Shift of Macrophage Phenotype Due to Cartilage Oligomeric Matrix Protein Deficiency Drives Atherosclerotic Calcification.
Reduced cell proliferation and increased apoptosis are significant pathological mechanisms in a murine model of mild pseudoachondroplasia resulting from a mutation in the C-terminal domain of COMP.
COMP-assisted collagen secretion--a novel intracellular function required for fibrosis.
A mouse model offers novel insights into the myopathy and tendinopathy often associated with pseudoachondroplasia and multiple epiphyseal dysplasia.