Cartilage oligomeric matrix protein

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactorⁱ

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• BMP binding Source: RGDInferred from sequence orthologyⁱ
  • "Cartilage oligomeric matrix protein inhibits vascular smooth muscle calcification by interacting with bone morphogenetic protein-2."
    Du Y., Wang Y., Wang L., Liu B., Tian Q., Liu C.J., Zhang T., Xu Q., Zhu Y., Ake O., Qi Y., Tang C., Kong W., Wang X.
    Circ. Res. 108:917-928(2011) [PubMed] [Europe PMC] [Abstract]
• calcium ion binding Source: RGDInferred from sequence orthologyⁱ
  • "Cartilage oligomeric matrix protein is a calcium-binding protein, and a mutation in its type 3 repeats causes conformational changes."
    Chen H., Deere M., Hecht J.T., Lawler J.
    J. Biol. Chem. 275:26538-26544(2000) [PubMed] [Europe PMC] [Abstract]
  • "Mutations in cartilage oligomeric matrix protein causing pseudoachondroplasia and multiple epiphyseal dysplasia affect binding of calcium and collagen I, II, and IX."
    Thur J., Rosenberg K., Nitsche D.P., Pihlajamaa T., Ala-Kokko L., Heinegaard D., Paulsson M., Maurer P.
    J. Biol. Chem. 276:6083-6092(2001) [PubMed] [Europe PMC] [Abstract]
• collagen binding Source: RGDInferred from sequence orthologyⁱ
  • "Mutations in cartilage oligomeric matrix protein causing pseudoachondroplasia and multiple epiphyseal dysplasia affect binding of calcium and collagen I, II, and IX."
    Thur J., Rosenberg K., Nitsche D.P., Pihlajamaa T., Ala-Kokko L., Heinegaard D., Paulsson M., Maurer P.
    J. Biol. Chem. 276:6083-6092(2001) [PubMed] [Europe PMC] [Abstract]
• extracellular matrix structural constituent Source: RGD <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • "Matrix-matrix interaction of cartilage oligomeric matrix protein and fibronectin."
    Di Cesare P.E., Chen F.S., Moergelin M., Carlson C.S., Leslie M.P., Perris R., Fang C.
    Matrix Biol. 21:461-470(2002) [PubMed] [Europe PMC] [Abstract]
• fibronectin binding Source: RGDInferred from direct assayⁱ
  • "Matrix-matrix interaction of cartilage oligomeric matrix protein and fibronectin."
    Di Cesare P.E., Chen F.S., Moergelin M., Carlson C.S., Leslie M.P., Perris R., Fang C.
    Matrix Biol. 21:461-470(2002) [PubMed] [Europe PMC] [Abstract]
• heparan sulfate proteoglycan binding Source: RGDInferred from sequence orthologyⁱ
  • "Interaction of cartilage oligomeric matrix protein/thrombospondin 5 with aggrecan."
    Chen F.-H., Herndon M.E., Patel N., Hecht J.T., Tuan R.S., Lawler J.
    J. Biol. Chem. 282:24591-24598(2007) [PubMed] [Europe PMC] [Abstract]
• heparin binding Source: RGDInferred from sequence orthologyⁱ
  • "Interaction of cartilage oligomeric matrix protein/thrombospondin 5 with aggrecan."
    Chen F.-H., Herndon M.E., Patel N., Hecht J.T., Tuan R.S., Lawler J.
    J. Biol. Chem. 282:24591-24598(2007) [PubMed] [Europe PMC] [Abstract]
• integrin binding Source: RGDInferred from sequence orthologyⁱ
  • "Shift of Macrophage Phenotype Due to Cartilage Oligomeric Matrix Protein Deficiency Drives Atherosclerotic Calcification."
    Fu Y., Gao C., Liang Y., Wang M., Huang Y., Ma W., Li T., Jia Y., Yu F., Zhu W., Cui Q., Li Y., Xu Q., Wang X., Kong W.
    Circ. Res. 119:261-276(2016) [PubMed] [Europe PMC] [Abstract]
• protease binding Source: RGDInferred from sequence orthologyⁱ
  • "ADAMTS-12 associates with and degrades cartilage oligomeric matrix protein."
    Liu C.-J., Kong W., Xu K., Luan Y., Ilalov K., Sehgal B., Yu S., Howell R.D., Di Cesare P.E.
    J. Biol. Chem. 281:15800-15808(2006) [PubMed] [Europe PMC] [Abstract]
  • "Inhibition of ADAMTS-7 and ADAMTS-12 degradation of cartilage oligomeric matrix protein by alpha-2-macroglobulin."
    Luan Y., Kong L., Howell D.R., Ilalov K., Fajardo M., Bai X.-H., Di Cesare P.E., Goldring M.B., Abramson S.B., Liu C.-J.
    Osteoarthritis Cartilage 16:1413-1420(2008) [PubMed] [Europe PMC] [Abstract]
• proteoglycan binding Source: RGDInferred from sequence orthologyⁱ
  • "Lubricin binds cartilage proteins, cartilage oligomeric matrix protein, fibronectin and collagen II at the cartilage surface."
    Flowers S.A., Zieba A., Ornros J., Jin C., Rolfson O., Bjorkman L.I., Eisler T., Kalamajski S., Kamali-Moghaddam M., Karlsson N.G.
    Sci Rep 7:13149-13149(2017) [PubMed] [Europe PMC] [Abstract]
• vitamin D binding Source: RGD <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "Storage function of cartilage oligomeric matrix protein: the crystal structure of the coiled-coil domain in complex with vitamin D(3)."
    Ozbek S., Engel J., Stetefeld J.
    EMBO J. 21:5960-5968(2002) [PubMed] [Europe PMC] [Abstract]

GO - Biological processⁱ

• animal organ senescence Source: RGDInferred from sequence orthologyⁱ
  • "Cartilage oligomeric matrix protein prevents vascular aging and vascular smooth muscle cells senescence."
    Wang M., Fu Y., Gao C., Jia Y., Huang Y., Liu L., Wang X., Wang W., Kong W.
    Biochem. Biophys. Res. Commun. 478:1006-1013(2016) [PubMed] [Europe PMC] [Abstract]
• apoptotic process Source: RGDInferred from sequence orthologyⁱ
  • "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."
    Pirog-Garcia K.A., Meadows R.S., Knowles L., Heinegard D., Thornton D.J., Kadler K.E., Boot-Handford R.P., Briggs M.D.
    Hum. Mol. Genet. 16:2072-2088(2007) [PubMed] [Europe PMC] [Abstract]
• artery morphogenesis Source: RGDInferred from sequence orthologyⁱ
  • "Shift of Macrophage Phenotype Due to Cartilage Oligomeric Matrix Protein Deficiency Drives Atherosclerotic Calcification."
    Fu Y., Gao C., Liang Y., Wang M., Huang Y., Ma W., Li T., Jia Y., Yu F., Zhu W., Cui Q., Li Y., Xu Q., Wang X., Kong W.
    Circ. Res. 119:261-276(2016) [PubMed] [Europe PMC] [Abstract]
• blood coagulation Source: RGDInferred from sequence orthologyⁱ
  • "Cartilage oligomeric matrix protein is a natural inhibitor of thrombin."
    Liang Y., Fu Y., Qi R., Wang M., Yang N., He L., Yu F., Zhang J., Yun C.H., Wang X., Liu J., Kong W.
    Blood 126:905-914(2015) [PubMed] [Europe PMC] [Abstract]
• BMP signaling pathway Source: RGDInferred from sequence orthologyⁱ
  • "Cartilage oligomeric matrix protein inhibits vascular smooth muscle calcification by interacting with bone morphogenetic protein-2."
    Du Y., Wang Y., Wang L., Liu B., Tian Q., Liu C.J., Zhang T., Xu Q., Zhu Y., Ake O., Qi Y., Tang C., Kong W., Wang X.
    Circ. Res. 108:917-928(2011) [PubMed] [Europe PMC] [Abstract]
• bone growth Source: RGDInferred from sequence orthologyⁱ
  • "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."
    Pirog-Garcia K.A., Meadows R.S., Knowles L., Heinegard D., Thornton D.J., Kadler K.E., Boot-Handford R.P., Briggs M.D.
    Hum. Mol. Genet. 16:2072-2088(2007) [PubMed] [Europe PMC] [Abstract]
• bone mineralization Source: RGDInferred from sequence orthologyⁱ
  • "Shift of Macrophage Phenotype Due to Cartilage Oligomeric Matrix Protein Deficiency Drives Atherosclerotic Calcification."
    Fu Y., Gao C., Liang Y., Wang M., Huang Y., Ma W., Li T., Jia Y., Yu F., Zhu W., Cui Q., Li Y., Xu Q., Wang X., Kong W.
    Circ. Res. 119:261-276(2016) [PubMed] [Europe PMC] [Abstract]
• bone morphogenesis Source: RGDInferred from sequence orthologyⁱ
  • "Ablation of collagen IX and COMP disrupts epiphyseal cartilage architecture."
    Blumbach K., Niehoff A., Paulsson M., Zaucke F.
    Matrix Biol. 27:306-318(2008) [PubMed] [Europe PMC] [Abstract]
• cartilage development Source: RGDInferred from sequence orthologyⁱ
  • "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."
    Pirog-Garcia K.A., Meadows R.S., Knowles L., Heinegard D., Thornton D.J., Kadler K.E., Boot-Handford R.P., Briggs M.D.
    Hum. Mol. Genet. 16:2072-2088(2007) [PubMed] [Europe PMC] [Abstract]
  • "Ablation of collagen IX and COMP disrupts epiphyseal cartilage architecture."
    Blumbach K., Niehoff A., Paulsson M., Zaucke F.
    Matrix Biol. 27:306-318(2008) [PubMed] [Europe PMC] [Abstract]
  • "Analysis of the cartilage proteome from three different mouse models of genetic skeletal diseases reveals common and discrete disease signatures."
    Bell P.A., Wagener R., Zaucke F., Koch M., Selley J., Warwood S., Knight D., Boot-Handford R.P., Thornton D.J., Briggs M.D.
    Biol Open 2:802-811(2013) [PubMed] [Europe PMC] [Abstract]
• chondrocyte development Source: RGDInferred from sequence orthologyⁱ
  • "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."
    Pirog-Garcia K.A., Meadows R.S., Knowles L., Heinegard D., Thornton D.J., Kadler K.E., Boot-Handford R.P., Briggs M.D.
    Hum. Mol. Genet. 16:2072-2088(2007) [PubMed] [Europe PMC] [Abstract]
  • "A novel form of chondrocyte stress is triggered by a COMP mutation causing pseudoachondroplasia."
    Suleman F., Gualeni B., Gregson H.J., Leighton M.P., Pirog K.A., Edwards S., Holden P., Boot-Handford R.P., Briggs M.D.
    Hum. Mutat. 33:218-231(2012) [PubMed] [Europe PMC] [Abstract]
• chondrocyte proliferation Source: RGDInferred from sequence orthologyⁱ
  • "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."
    Pirog-Garcia K.A., Meadows R.S., Knowles L., Heinegard D., Thornton D.J., Kadler K.E., Boot-Handford R.P., Briggs M.D.
    Hum. Mol. Genet. 16:2072-2088(2007) [PubMed] [Europe PMC] [Abstract]
  • "Ablation of collagen IX and COMP disrupts epiphyseal cartilage architecture."
    Blumbach K., Niehoff A., Paulsson M., Zaucke F.
    Matrix Biol. 27:306-318(2008) [PubMed] [Europe PMC] [Abstract]
  • "A novel form of chondrocyte stress is triggered by a COMP mutation causing pseudoachondroplasia."
    Suleman F., Gualeni B., Gregson H.J., Leighton M.P., Pirog K.A., Edwards S., Holden P., Boot-Handford R.P., Briggs M.D.
    Hum. Mutat. 33:218-231(2012) [PubMed] [Europe PMC] [Abstract]
• collagen fibril organization Source: RGDInferred from sequence orthologyⁱ
  • "A mouse model offers novel insights into the myopathy and tendinopathy often associated with pseudoachondroplasia and multiple epiphyseal dysplasia."
    Pirog K.A., Jaka O., Katakura Y., Meadows R.S., Kadler K.E., Boot-Handford R.P., Briggs M.D.
    Hum. Mol. Genet. 19:52-64(2010) [PubMed] [Europe PMC] [Abstract]
  • "Mild myopathy is associated with COMP but not MATN3 mutations in mouse models of genetic skeletal diseases."
    Pirog K.A., Katakura Y., Mironov A., Briggs M.D.
    PLoS ONE 8:e82412-e82412(2013) [PubMed] [Europe PMC] [Abstract]
  • "COMP-assisted collagen secretion--a novel intracellular function required for fibrosis."
    Schulz J.N., Nuchel J., Niehoff A., Bloch W., Schonborn K., Hayashi S., Kamper M., Brinckmann J., Plomann M., Paulsson M., Krieg T., Zaucke F., Eckes B.
    J. Cell. Sci. 129:706-716(2016) [PubMed] [Europe PMC] [Abstract]
• endochondral bone growth Source: RGDInferred from sequence orthologyⁱ
  • "Interaction between cartilage oligomeric matrix protein and extracellular matrix protein 1 mediates endochondral bone growth."
    Kong L., Tian Q., Guo F., Mucignat M.T., Perris R., Sercu S., Merregaert J., Di Cesare P.E., Liu C.J.
    Matrix Biol. 29:276-286(2010) [PubMed] [Europe PMC] [Abstract]
• growth plate cartilage development Source: RGDInferred from sequence orthologyⁱ
  • "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."
    Pirog-Garcia K.A., Meadows R.S., Knowles L., Heinegard D., Thornton D.J., Kadler K.E., Boot-Handford R.P., Briggs M.D.
    Hum. Mol. Genet. 16:2072-2088(2007) [PubMed] [Europe PMC] [Abstract]
  • "Ablation of collagen IX and COMP disrupts epiphyseal cartilage architecture."
    Blumbach K., Niehoff A., Paulsson M., Zaucke F.
    Matrix Biol. 27:306-318(2008) [PubMed] [Europe PMC] [Abstract]
  • "Skeletal abnormalities in mice lacking extracellular matrix proteins, thrombospondin-1, thrombospondin-3, thrombospondin-5, and type IX collagen."
    Posey K.L., Hankenson K., Veerisetty A.C., Bornstein P., Lawler J., Hecht J.T.
    Am. J. Pathol. 172:1664-1674(2008) [PubMed] [Europe PMC] [Abstract]
• limb development Source: RGDInferred from sequence orthologyⁱ
  • "Cartilage oligomeric matrix protein is involved in human limb development and in the pathogenesis of osteoarthritis."
    Koelling S., Clauditz T.S., Kaste M., Miosge N.
    Arthritis Res. Ther. 8:R56-R56(2006) [PubMed] [Europe PMC] [Abstract]
  • "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."
    Pirog-Garcia K.A., Meadows R.S., Knowles L., Heinegard D., Thornton D.J., Kadler K.E., Boot-Handford R.P., Briggs M.D.
    Hum. Mol. Genet. 16:2072-2088(2007) [PubMed] [Europe PMC] [Abstract]
  • "A novel form of chondrocyte stress is triggered by a COMP mutation causing pseudoachondroplasia."
    Suleman F., Gualeni B., Gregson H.J., Leighton M.P., Pirog K.A., Edwards S., Holden P., Boot-Handford R.P., Briggs M.D.
    Hum. Mutat. 33:218-231(2012) [PubMed] [Europe PMC] [Abstract]
• multicellular organism aging Source: RGDInferred from sequence orthologyⁱ
  • "Cartilage oligomeric matrix protein prevents vascular aging and vascular smooth muscle cells senescence."
    Wang M., Fu Y., Gao C., Jia Y., Huang Y., Liu L., Wang X., Wang W., Kong W.
    Biochem. Biophys. Res. Commun. 478:1006-1013(2016) [PubMed] [Europe PMC] [Abstract]
• multicellular organism growth Source: RGDInferred from sequence orthologyⁱ
  • "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."
    Pirog-Garcia K.A., Meadows R.S., Knowles L., Heinegard D., Thornton D.J., Kadler K.E., Boot-Handford R.P., Briggs M.D.
    Hum. Mol. Genet. 16:2072-2088(2007) [PubMed] [Europe PMC] [Abstract]
  • "A novel form of chondrocyte stress is triggered by a COMP mutation causing pseudoachondroplasia."
    Suleman F., Gualeni B., Gregson H.J., Leighton M.P., Pirog K.A., Edwards S., Holden P., Boot-Handford R.P., Briggs M.D.
    Hum. Mutat. 33:218-231(2012) [PubMed] [Europe PMC] [Abstract]
• muscle fiber development Source: RGDInferred from sequence orthologyⁱ
  • "A mouse model offers novel insights into the myopathy and tendinopathy often associated with pseudoachondroplasia and multiple epiphyseal dysplasia."
    Pirog K.A., Jaka O., Katakura Y., Meadows R.S., Kadler K.E., Boot-Handford R.P., Briggs M.D.
    Hum. Mol. Genet. 19:52-64(2010) [PubMed] [Europe PMC] [Abstract]
  • "Mild myopathy is associated with COMP but not MATN3 mutations in mouse models of genetic skeletal diseases."
    Pirog K.A., Katakura Y., Mironov A., Briggs M.D.
    PLoS ONE 8:e82412-e82412(2013) [PubMed] [Europe PMC] [Abstract]
• musculoskeletal movement Source: RGDInferred from sequence orthologyⁱ
  • "A mouse model offers novel insights into the myopathy and tendinopathy often associated with pseudoachondroplasia and multiple epiphyseal dysplasia."
    Pirog K.A., Jaka O., Katakura Y., Meadows R.S., Kadler K.E., Boot-Handford R.P., Briggs M.D.
    Hum. Mol. Genet. 19:52-64(2010) [PubMed] [Europe PMC] [Abstract]
• negative regulation of apoptotic process Source: RGDInferred from sequence orthologyⁱ
  • "Cartilage oligomeric matrix protein protects cells against death by elevating members of the IAP family of survival proteins."
    Gagarina V., Carlberg A.L., Pereira-Mouries L., Hall D.J.
    J. Biol. Chem. 283:648-659(2008) [PubMed] [Europe PMC] [Abstract]
• negative regulation of hemostasis Source: RGDInferred from sequence orthologyⁱ
  • "Cartilage oligomeric matrix protein is a natural inhibitor of thrombin."
    Liang Y., Fu Y., Qi R., Wang M., Yang N., He L., Yu F., Zhang J., Yun C.H., Wang X., Liu J., Kong W.
    Blood 126:905-914(2015) [PubMed] [Europe PMC] [Abstract]
• neuromuscular process Source: RGDInferred from sequence orthologyⁱ
  • "Mild myopathy is associated with COMP but not MATN3 mutations in mouse models of genetic skeletal diseases."
    Pirog K.A., Katakura Y., Mironov A., Briggs M.D.
    PLoS ONE 8:e82412-e82412(2013) [PubMed] [Europe PMC] [Abstract]
• ossification Source: RGDInferred from sequence orthologyⁱ
  • "Cartilage oligomeric matrix protein inhibits vascular smooth muscle calcification by interacting with bone morphogenetic protein-2."
    Du Y., Wang Y., Wang L., Liu B., Tian Q., Liu C.J., Zhang T., Xu Q., Zhu Y., Ake O., Qi Y., Tang C., Kong W., Wang X.
    Circ. Res. 108:917-928(2011) [PubMed] [Europe PMC] [Abstract]
  • "Shift of Macrophage Phenotype Due to Cartilage Oligomeric Matrix Protein Deficiency Drives Atherosclerotic Calcification."
    Fu Y., Gao C., Liang Y., Wang M., Huang Y., Ma W., Li T., Jia Y., Yu F., Zhu W., Cui Q., Li Y., Xu Q., Wang X., Kong W.
    Circ. Res. 119:261-276(2016) [PubMed] [Europe PMC] [Abstract]
• platelet aggregation Source: RGDInferred from sequence orthologyⁱ
  • "Cartilage oligomeric matrix protein is a natural inhibitor of thrombin."
    Liang Y., Fu Y., Qi R., Wang M., Yang N., He L., Yu F., Zhang J., Yun C.H., Wang X., Liu J., Kong W.
    Blood 126:905-914(2015) [PubMed] [Europe PMC] [Abstract]
• positive regulation of chondrocyte proliferation Source: RGDInferred from sequence orthologyⁱ
  • "Cartilage oligomeric matrix protein associates with granulin-epithelin precursor (GEP) and potentiates GEP-stimulated chondrocyte proliferation."
    Xu K., Zhang Y., Ilalov K., Carlson C.S., Feng J.Q., Di Cesare P.E., Liu C.J.
    J. Biol. Chem. 282:11347-11355(2007) [PubMed] [Europe PMC] [Abstract]
• protein processing Source: RGDInferred from sequence orthologyⁱ
  • "Cartilage oligomeric matrix protein is a natural inhibitor of thrombin."
    Liang Y., Fu Y., Qi R., Wang M., Yang N., He L., Yu F., Zhang J., Yun C.H., Wang X., Liu J., Kong W.
    Blood 126:905-914(2015) [PubMed] [Europe PMC] [Abstract]
• protein secretion Source: RGDInferred from sequence orthologyⁱ
  • "COMP-assisted collagen secretion--a novel intracellular function required for fibrosis."
    Schulz J.N., Nuchel J., Niehoff A., Bloch W., Schonborn K., Hayashi S., Kamper M., Brinckmann J., Plomann M., Paulsson M., Krieg T., Zaucke F., Eckes B.
    J. Cell. Sci. 129:706-716(2016) [PubMed] [Europe PMC] [Abstract]
• regulation of bone mineralization Source: RGDInferred from sequence orthologyⁱ
  • "Cartilage oligomeric matrix protein inhibits vascular smooth muscle calcification by interacting with bone morphogenetic protein-2."
    Du Y., Wang Y., Wang L., Liu B., Tian Q., Liu C.J., Zhang T., Xu Q., Zhu Y., Ake O., Qi Y., Tang C., Kong W., Wang X.
    Circ. Res. 108:917-928(2011) [PubMed] [Europe PMC] [Abstract]
• regulation of gene expression Source: RGDInferred from sequence orthologyⁱ
  • "A novel form of chondrocyte stress is triggered by a COMP mutation causing pseudoachondroplasia."
    Suleman F., Gualeni B., Gregson H.J., Leighton M.P., Pirog K.A., Edwards S., Holden P., Boot-Handford R.P., Briggs M.D.
    Hum. Mutat. 33:218-231(2012) [PubMed] [Europe PMC] [Abstract]
  • "Cartilage oligomeric matrix protein prevents vascular aging and vascular smooth muscle cells senescence."
    Wang M., Fu Y., Gao C., Jia Y., Huang Y., Liu L., Wang X., Wang W., Kong W.
    Biochem. Biophys. Res. Commun. 478:1006-1013(2016) [PubMed] [Europe PMC] [Abstract]
• response to unfolded protein Source: RGDInferred from sequence orthologyⁱ
  • "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."
    Pirog-Garcia K.A., Meadows R.S., Knowles L., Heinegard D., Thornton D.J., Kadler K.E., Boot-Handford R.P., Briggs M.D.
    Hum. Mol. Genet. 16:2072-2088(2007) [PubMed] [Europe PMC] [Abstract]
• skeletal system development Source: RGDInferred from sequence orthologyⁱ
  • "Ablation of collagen IX and COMP disrupts epiphyseal cartilage architecture."
    Blumbach K., Niehoff A., Paulsson M., Zaucke F.
    Matrix Biol. 27:306-318(2008) [PubMed] [Europe PMC] [Abstract]
• skin development Source: RGDInferred from sequence orthologyⁱ
  • "COMP-assisted collagen secretion--a novel intracellular function required for fibrosis."
    Schulz J.N., Nuchel J., Niehoff A., Bloch W., Schonborn K., Hayashi S., Kamper M., Brinckmann J., Plomann M., Paulsson M., Krieg T., Zaucke F., Eckes B.
    J. Cell. Sci. 129:706-716(2016) [PubMed] [Europe PMC] [Abstract]
• tendon development Source: RGDInferred from sequence orthologyⁱ
  • "A mouse model offers novel insights into the myopathy and tendinopathy often associated with pseudoachondroplasia and multiple epiphyseal dysplasia."
    Pirog K.A., Jaka O., Katakura Y., Meadows R.S., Kadler K.E., Boot-Handford R.P., Briggs M.D.
    Hum. Mol. Genet. 19:52-64(2010) [PubMed] [Europe PMC] [Abstract]
  • "Mild myopathy is associated with COMP but not MATN3 mutations in mouse models of genetic skeletal diseases."
    Pirog K.A., Katakura Y., Mironov A., Briggs M.D.
    PLoS ONE 8:e82412-e82412(2013) [PubMed] [Europe PMC] [Abstract]
• vascular smooth muscle cell development Source: RGDInferred from sequence orthologyⁱ
  • "Cartilage oligomeric matrix protein inhibits vascular smooth muscle calcification by interacting with bone morphogenetic protein-2."
    Du Y., Wang Y., Wang L., Liu B., Tian Q., Liu C.J., Zhang T., Xu Q., Zhu Y., Ake O., Qi Y., Tang C., Kong W., Wang X.
    Circ. Res. 108:917-928(2011) [PubMed] [Europe PMC] [Abstract]
• vascular smooth muscle contraction Source: RGDInferred from sequence orthologyⁱ
  • "Cartilage oligomeric matrix protein prevents vascular aging and vascular smooth muscle cells senescence."
    Wang M., Fu Y., Gao C., Jia Y., Huang Y., Liu L., Wang X., Wang W., Kong W.
    Biochem. Biophys. Res. Commun. 478:1006-1013(2016) [PubMed] [Europe PMC] [Abstract]

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

Keywords - Cellular componentⁱ

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

Keywords - PTMⁱ

Proteomic databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityⁱ

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

GO - Molecular functionⁱ

• BMP binding Source: RGDInferred from sequence orthologyⁱ
  • "Cartilage oligomeric matrix protein inhibits vascular smooth muscle calcification by interacting with bone morphogenetic protein-2."
    Du Y., Wang Y., Wang L., Liu B., Tian Q., Liu C.J., Zhang T., Xu Q., Zhu Y., Ake O., Qi Y., Tang C., Kong W., Wang X.
    Circ. Res. 108:917-928(2011) [PubMed] [Europe PMC] [Abstract]
• fibronectin binding Source: RGDInferred from direct assayⁱ
  • "Matrix-matrix interaction of cartilage oligomeric matrix protein and fibronectin."
    Di Cesare P.E., Chen F.S., Moergelin M., Carlson C.S., Leslie M.P., Perris R., Fang C.
    Matrix Biol. 21:461-470(2002) [PubMed] [Europe PMC] [Abstract]
• heparan sulfate proteoglycan binding Source: RGDInferred from sequence orthologyⁱ
  • "Interaction of cartilage oligomeric matrix protein/thrombospondin 5 with aggrecan."
    Chen F.-H., Herndon M.E., Patel N., Hecht J.T., Tuan R.S., Lawler J.
    J. Biol. Chem. 282:24591-24598(2007) [PubMed] [Europe PMC] [Abstract]
• integrin binding Source: RGDInferred from sequence orthologyⁱ
  • "Shift of Macrophage Phenotype Due to Cartilage Oligomeric Matrix Protein Deficiency Drives Atherosclerotic Calcification."
    Fu Y., Gao C., Liang Y., Wang M., Huang Y., Ma W., Li T., Jia Y., Yu F., Zhu W., Cui Q., Li Y., Xu Q., Wang X., Kong W.
    Circ. Res. 119:261-276(2016) [PubMed] [Europe PMC] [Abstract]
• protease binding Source: RGDInferred from sequence orthologyⁱ
  • "ADAMTS-12 associates with and degrades cartilage oligomeric matrix protein."
    Liu C.-J., Kong W., Xu K., Luan Y., Ilalov K., Sehgal B., Yu S., Howell R.D., Di Cesare P.E.
    J. Biol. Chem. 281:15800-15808(2006) [PubMed] [Europe PMC] [Abstract]
  • "Inhibition of ADAMTS-7 and ADAMTS-12 degradation of cartilage oligomeric matrix protein by alpha-2-macroglobulin."
    Luan Y., Kong L., Howell D.R., Ilalov K., Fajardo M., Bai X.-H., Di Cesare P.E., Goldring M.B., Abramson S.B., Liu C.-J.
    Osteoarthritis Cartilage 16:1413-1420(2008) [PubMed] [Europe PMC] [Abstract]
• proteoglycan binding Source: RGDInferred from sequence orthologyⁱ
  • "Lubricin binds cartilage proteins, cartilage oligomeric matrix protein, fibronectin and collagen II at the cartilage surface."
    Flowers S.A., Zieba A., Ornros J., Jin C., Rolfson O., Bjorkman L.I., Eisler T., Kalamajski S., Kamali-Moghaddam M., Karlsson N.G.
    Sci Rep 7:13149-13149(2017) [PubMed] [Europe PMC] [Abstract]

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Domains and Repeats

Region

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domainⁱ

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)ⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

        10         20         30         40         50
MSPTACVLVL ALAALRATGQ GQIPLGGDLA PQMLRELQET NAALQDVREL 
        60         70         80         90        100
LRHRVKEITF LKNTVMECDA CGMQPARTPG LSVRPVALCA PGSCFPGVVC 
       110        120        130        140        150
TETATGARCG PCPPGYTGNG SHCTDVNECN AHPCFPRVRC INTSPGFHCE 
       160        170        180        190        200
ACPPGFSGPT HEGVGLTFAK TNKQVCTDIN ECETGQHNCV PNSVCVNTRG 
       210        220        230        240        250
SFQCGPCQPG FVGDQRSGCQ RRGQHFCPDG SPSPCHEKAD CILERDGSRS 
       260        270        280        290        300
CVCAVGWAGN GLLCGRDTDL DGFPDEKLRC SERQCRKDNC VTVPNSGQED 
       310        320        330        340        350
VDRDRIGDAC DPDADGDGVP NEQDNCPLVR NPDQRNSDKD KWGDACDNCR 
       360        370        380        390        400
SQKNDDQKDT DRDGQGDACD DDIDGDRIRN VADNCPRVPN FDQSDSDGDG 
       410        420        430        440        450
VGDACDNCPQ KDNPDQRDVD HDFVGDACDS DQDQDGDGHQ DSRDNCPTVP 
       460        470        480        490        500
NSAQQDSDHD GKGDACDDDD DNDGVPDSRD NCRLVPNPGQ EDNDRDGVGD 
       510        520        530        540        550
ACQGDFDADK VIDKIDVCPE NAEVTLTDFR AFQTVVLDPE GDAQIDPNWV 
       560        570        580        590        600
VLNQGMEIVQ TMNSDPGLAV GYTAFNGVDF EGTFHVNTAT DDDYAGFIFG 
       610        620        630        640        650
YQDSSSFYVV MWKQMEQTYW QANPFRAVAE PGIQLKAVKS STGPGEQLRN 
       660        670        680        690        700
ALWHTGDTAS QVRLLWKDPR NVGWKDKTSY RWFLQHRPQV GYIRVRFYEG 
       710        720        730        740        750
PELVADSNVV LDTAMRGGRL GVFCFSQENI IWANLRYRCN DTIPEDYERH 

RLRRA                                                  

Sequence databases

Genome annotation databases

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

1. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
2. SIMILARITY comments
   Index of protein domains and families