We will be switching to the new UniProt website soon. Please explore and share your feedback.
Take me to the new website.
UniProtKB - P49747 (COMP_HUMAN)
(max 400 entries)
Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the 'basket' to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>
Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)
>sp|P49747|COMP_HUMAN Cartilage oligomeric matrix protein OS=Homo sapiens OX=9606 GN=COMP PE=1 SV=2 MVPDTACVLLLTLAALGASGQGQSPLGSDLGPQMLRELQETNAALQDVRELLRQQVREIT FLKNTVMECDACGMQQSVRTGLPSVRPLLHCAPGFCFPGVACIQTESGARCGPCPAGFTG NGSHCTDVNECNAHPCFPRVRCINTSPGFRCEACPPGYSGPTHQGVGLAFAKANKQVCTD INECETGQHNCVPNSVCINTRGSFQCGPCQPGFVGDQASGCQRRAQRFCPDGSPSECHEH ADCVLERDGSRSCVCAVGWAGNGILCGRDTDLDGFPDEKLRCPERQCRKDNCVTVPNSGQ EDVDRDGIGDACDPDADGDGVPNEKDNCPLVRNPDQRNTDEDKWGDACDNCRSQKNDDQK DTDQDGRGDACDDDIDGDRIRNQADNCPRVPNSDQKDSDGDGIGDACDNCPQKSNPDQAD VDHDFVGDACDSDQDQDGDGHQDSRDNCPTVPNSAQEDSDHDGQGDACDDDDDNDGVPDS RDNCRLVPNPGQEDADRDGVGDVCQDDFDADKVVDKIDVCPENAEVTLTDFRAFQTVVLD PEGDAQIDPNWVVLNQGREIVQTMNSDPGLAVGYTAFNGVDFEGTFHVNTVTDDDYAGFI FGYQDSSSFYVVMWKQMEQTYWQANPFRAVAEPGIQLKAVKSSTGPGEQLRNALWHTGDT ESQVRLLWKDPRNVGWKDKKSYRWFLQHRPQVGYIRVRFYEGPELVADSNVVLDTTMRGG RLGVFCFSQENIIWANLRYRCNDTIPEDYETHQLRQACommunity curation ()Add a publicationFeedback
Protein
Cartilage oligomeric matrix protein
Gene
COMP
Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<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
Plays a role in the structural integrity of cartilage via its interaction with other extracellular matrix proteins such as the collagens and fibronectin. Can mediate the interaction of chondrocytes with the cartilage extracellular matrix through interaction with cell surface integrin receptors (PubMed:16542502, PubMed:16051604).
Could play a role in the pathogenesis of osteoarthritis (PubMed:16542502).
Potent suppressor of apoptosis in both primary chondrocytes and transformed cells. Suppresses apoptosis by blocking the activation of caspase-3 and by inducing the IAP family of survival proteins (BIRC3, BIRC2, BIRC5 and XIAP) (PubMed:17993464).
Essential for maintaining a vascular smooth muscle cells (VSMCs) contractile/differentiated phenotype under physiological and pathological stimuli. Maintains this phenotype of VSMCs by interacting with ITGA7 (By similarity).
By similarity<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
3 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.12"Cartilage oligomeric matrix protein/thrombospondin 5 supports chondrocyte attachment through interaction with integrins."
Chen F.-H., Thomas A.O., Hecht J.T., Goldring M.B., Lawler J.
J. Biol. Chem. 280:32655-32661(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH ITGB3 AND ITGA5. - Ref.13"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]Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. - Ref.16"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]Cited for: FUNCTION, DOMAINS.
<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
Ca2+
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
Manual assertion based on experiment ini
- Ref.8"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]Cited for: PROTEIN SEQUENCE OF 80-89, SUBUNIT, CALCIUM-BINDING, CHARACTERIZATION OF VARIANT PSACH ASP-469 DEL. - Ref.9"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]Cited for: PROTEIN SEQUENCE, CALCIUM-BINDING, INTERACTION WITH COLLAGEN I; COLLAGEN II AND COLLAGEN IX, CHARACTERIZATION OF VARIANT PSACH ASP-469 DEL, CHARACTERIZATION OF VARIANT EDM1 TYR-361. - Ref.18"The crystal structure of the signature domain of cartilage oligomeric matrix protein: implications for collagen, glycosaminoglycan and integrin binding."
Tan K., Duquette M., Joachimiak A., Lawler J.
FASEB J. 23:2490-2501(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 225-757 IN COMPLEX WITH CALCIUM IONS, DISULFIDE BONDS, GLYCOSYLATION AT ASN-742.
Manual assertion based on experiment ini
- Ref.18"The crystal structure of the signature domain of cartilage oligomeric matrix protein: implications for collagen, glycosaminoglycan and integrin binding."
Tan K., Duquette M., Joachimiak A., Lawler J.
FASEB J. 23:2490-2501(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 225-757 IN COMPLEX WITH CALCIUM IONS, DISULFIDE BONDS, GLYCOSYLATION AT ASN-742.
<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: Ensembl
- calcium ion binding Source: UniProtKB
<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-go-evidence-codes#ida">GO evidence code guide</a></p>
Inferred from direct assayi
- Ref.8"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]Cited for: PROTEIN SEQUENCE OF 80-89, SUBUNIT, CALCIUM-BINDING, CHARACTERIZATION OF VARIANT PSACH ASP-469 DEL. - Ref.9"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]Cited for: PROTEIN SEQUENCE, CALCIUM-BINDING, INTERACTION WITH COLLAGEN I; COLLAGEN II AND COLLAGEN IX, CHARACTERIZATION OF VARIANT PSACH ASP-469 DEL, CHARACTERIZATION OF VARIANT EDM1 TYR-361.
- collagen binding Source: UniProtKBInferred from direct assayi
- Ref.9"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]Cited for: PROTEIN SEQUENCE, CALCIUM-BINDING, INTERACTION WITH COLLAGEN I; COLLAGEN II AND COLLAGEN IX, CHARACTERIZATION OF VARIANT PSACH ASP-469 DEL, CHARACTERIZATION OF VARIANT EDM1 TYR-361.
- extracellular matrix structural constituent Source: ProtInc
<p>Traceable Author Statement</p>
<p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p>
Traceable author statementi
- Ref.1"Characterization of human and mouse cartilage oligomeric matrix protein."
Newton G., Weremowicz S., Morton C.C., Copeland N.G., Gilbert D.J., Jenkins N.A., Lawler J.
Genomics 24:435-439(1994) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ASP-50; TRP-51; GLY-109; GLY-224 AND PRO-285.
- heparan sulfate proteoglycan binding Source: UniProtKBInferred from direct assayi
- Ref.15"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]Cited for: INTERACTION WITH ACAN; HEPARIN; HEPARAN SULFATE AND CHONDROITIN SULFATE.
- heparin binding Source: UniProtKBInferred from direct assayi
- Ref.15"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]Cited for: INTERACTION WITH ACAN; HEPARIN; HEPARAN SULFATE AND CHONDROITIN SULFATE.
- integrin binding Source: Ensembl
- protease binding Source: BHF-UCL
<p>Inferred from Physical Interaction</p>
<p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p>
Inferred from physical interactioni
- "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: MGIInferred from direct assayi
- "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]
GO - Biological processi
- animal organ morphogenesis Source: ProtIncTraceable author statementi
- Ref.1"Characterization of human and mouse cartilage oligomeric matrix protein."
Newton G., Weremowicz S., Morton C.C., Copeland N.G., Gilbert D.J., Jenkins N.A., Lawler J.
Genomics 24:435-439(1994) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ASP-50; TRP-51; GLY-109; GLY-224 AND PRO-285.
- animal organ senescence Source: Ensembl
- apoptotic process Source: UniProtKB-KW
- artery morphogenesis Source: Ensembl
- BMP signaling pathway Source: Ensembl
- bone mineralization Source: Ensembl
- cartilage homeostasis Source: UniProtKBInferred from direct assayi
- Ref.31"Author Correction: Mutations in COMP cause familial carpal tunnel syndrome."
Li C., Wang N., Schaeffer A.A., Liu X., Zhao Z., Elliott G., Garrett L., Choi N.T., Wang Y., Wang Y., Wang C., Wang J., Chan D., Su P., Cui S., Yang Y., Gao B.
Nat. Commun. 11:3931-3931(2020) [PubMed] [Europe PMC] [Abstract]Cited for: ERRATUM OF PUBMED:32747625.
- chondrocyte development Source: Ensembl
- chondrocyte proliferation Source: Ensembl
- collagen fibril organization Source: Ensembl
- growth plate cartilage development Source: Ensembl
- limb development Source: UniProtKBInferred from direct assayi
- Ref.13"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]Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
- multicellular organism aging Source: Ensembl
- multicellular organism growth Source: Ensembl
- musculoskeletal movement Source: Ensembl
- negative regulation of apoptotic process Source: UniProtKBInferred from direct assayi
- Ref.16"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]Cited for: FUNCTION, DOMAINS.
- negative regulation of hemostasis Source: Ensembl
- platelet aggregation Source: Ensembl
- positive regulation of chondrocyte proliferation Source: Ensembl
- protein homooligomerization Source: UniProtKBInferred from direct assayi
- Ref.31"Author Correction: Mutations in COMP cause familial carpal tunnel syndrome."
Li C., Wang N., Schaeffer A.A., Liu X., Zhao Z., Elliott G., Garrett L., Choi N.T., Wang Y., Wang Y., Wang C., Wang J., Chan D., Su P., Cui S., Yang Y., Gao B.
Nat. Commun. 11:3931-3931(2020) [PubMed] [Europe PMC] [Abstract]Cited for: ERRATUM OF PUBMED:32747625.
- protein processing Source: Ensembl
- protein secretion Source: Ensembl
- regulation of bone mineralization Source: Ensembl
- regulation of gene expression Source: Ensembl
- response to unfolded protein Source: Ensembl
- skeletal system development Source: ProtIncTraceable author statementi
- Ref.7"Pseudoachondroplasia and multiple epiphyseal dysplasia due to mutations in the cartilage oligomeric matrix protein gene."
Briggs M.D., Hoffman S.M.G., King L.M., Olsen A.S., Mohrenweiser H., Leroy J.G., Mortier G.R., Rimoin D.L., Lachman R.S., Gaines E.S., Cekleniak J.A., Knowlton R.G., Cohn D.H.
Nat. Genet. 10:330-336(1995) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 326-344, VARIANT EDM1 TYR-342, VARIANT PSACH ARG-328.
- skin development Source: Ensembl
- tendon development Source: Ensembl
- vascular associated smooth muscle cell development Source: Ensembl
- vascular associated smooth muscle contraction Source: Ensembl
<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
| Molecular function | Heparin-binding |
| Biological process | Apoptosis, Cell adhesion |
| Ligand | Calcium |
Enzyme and pathway databases
Pathway Commons web resource for biological pathway data More...PathwayCommonsi | P49747 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-216083, Integrin cell surface interactions R-HSA-3000178, ECM proteoglycans |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | P49747 |
<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
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Cartilage oligomeric matrix proteinCuratedShort name: COMP Alternative name(s): Thrombospondin-5 Short name: TSP5 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Human Gene Nomenclature Database More...HGNCi | HGNC:2227, COMP |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 600310, gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P49747 |
Eukaryotic Pathogen, Vector and Host Database Resources More...VEuPathDBi | HostDB:ENSG00000105664 |
<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
Extracellular region or secreted
- extracellular matrix 1 Publication
Manual assertion based on experiment ini
- Ref.30"Mutations in COMP cause familial carpal tunnel syndrome."
Li C., Wang N., Schaeffer A.A., Liu X., Zhao Z., Elliott G., Garrett L., Choi N.T., Wang Y., Wang Y., Wang C., Wang J., Chan D., Su P., Cui S., Yang Y., Gao B.
Nat. Commun. 11:3642-3642(2020) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS CTS2 GLU-66 AND TRP-718, CHARACTERIZATION OF VARIANTS CTS2 GLU-66 AND TRP-718, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
- extracellular matrix 1 Publication
Extracellular region or secreted
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
- "In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine."
Principe S., Jones E.E., Kim Y., Sinha A., Nyalwidhe J.O., Brooks J., Semmes O.J., Troyer D.A., Lance R.S., Kislinger T., Drake R.R.
Proteomics 13:1667-1671(2013) [PubMed] [Europe PMC] [Abstract]
- extracellular region Source: UniProtKBInferred from direct assayi
- Ref.31"Author Correction: Mutations in COMP cause familial carpal tunnel syndrome."
Li C., Wang N., Schaeffer A.A., Liu X., Zhao Z., Elliott G., Garrett L., Choi N.T., Wang Y., Wang Y., Wang C., Wang J., Chan D., Su P., Cui S., Yang Y., Gao B.
Nat. Commun. 11:3931-3931(2020) [PubMed] [Europe PMC] [Abstract]Cited for: ERRATUM OF PUBMED:32747625.
- extracellular space Source: BHF-UCLInferred from high throughput direct assayi
- "Proteomics characterization of extracellular space components in the human aorta."
Didangelos A., Yin X., Mandal K., Baumert M., Jahangiri M., Mayr M.
Mol. Cell. Proteomics 9:2048-2062(2010) [PubMed] [Europe PMC] [Abstract]
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
Other locations
- collagen-containing extracellular matrix Source: GO_Central
<p>Inferred from Biological aspect of Ancestor</p>
<p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iba">GO evidence code guide</a></p>
Inferred from biological aspect of ancestori
- "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
Brief Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
- extracellular matrix Source: ProtIncTraceable author statementi
- Ref.1"Characterization of human and mouse cartilage oligomeric matrix protein."
Newton G., Weremowicz S., Morton C.C., Copeland N.G., Gilbert D.J., Jenkins N.A., Lawler J.
Genomics 24:435-439(1994) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ASP-50; TRP-51; GLY-109; GLY-224 AND PRO-285.
- protein-containing complex Source: Ensembl
- collagen-containing extracellular matrix Source: GO_Central
<p>Inferred from Biological aspect of Ancestor</p>
<p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p>
<p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iba">GO evidence code guide</a></p>
Inferred from biological aspect of ancestori
Keywords - Cellular componenti
Extracellular matrix, Secreted<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei
Multiple epiphyseal dysplasia 1 (EDM1)9 PublicationsManual assertion based on experiment ini
- Ref.7"Pseudoachondroplasia and multiple epiphyseal dysplasia due to mutations in the cartilage oligomeric matrix protein gene."
Briggs M.D., Hoffman S.M.G., King L.M., Olsen A.S., Mohrenweiser H., Leroy J.G., Mortier G.R., Rimoin D.L., Lachman R.S., Gaines E.S., Cekleniak J.A., Knowlton R.G., Cohn D.H.
Nat. Genet. 10:330-336(1995) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 326-344, VARIANT EDM1 TYR-342, VARIANT PSACH ARG-328. - Ref.9"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]Cited for: PROTEIN SEQUENCE, CALCIUM-BINDING, INTERACTION WITH COLLAGEN I; COLLAGEN II AND COLLAGEN IX, CHARACTERIZATION OF VARIANT PSACH ASP-469 DEL, CHARACTERIZATION OF VARIANT EDM1 TYR-361. - Ref.20"Multiple epiphyseal dysplasia, ribbing type: a novel point mutation in the COMP gene in a South African family."
Ballo R., Briggs M.D., Cohn D.H., Knowlton R.G., Beighton P.H., Ramesar R.S.
Am. J. Med. Genet. 68:396-400(1997) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT EDM1 LYS-523. - Ref.21"Multiple epiphyseal dysplasia and pseudoachondroplasia due to novel mutations in the calmodulin-like repeats of cartilage oligomeric matrix protein."
Susic S., McGrory J., Ahier J., Cole W.G.
Clin. Genet. 51:219-224(1997) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT EDM1 SER-371, VARIANT PSACH 513-VAL--LYS-516 DEL. - Ref.22"Diverse mutations in the gene for cartilage oligomeric matrix protein in the pseudoachondroplasia-multiple epiphyseal dysplasia disease spectrum."
Briggs M.D., Mortier G.R., Cole W.G., King L.M., Golik S.S., Bonaventure J., Nuytinck L., de Paepe A., Leroy J.G., Biesecker L., Lipson M., Wilcox W.R., Lachman R.S., Rimoin D.L., Knowlton R.G., Cohn D.H.
Am. J. Hum. Genet. 62:311-319(1998) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS PSACH, VARIANTS EDM1 SER-453 AND ARG-585. - Ref.23"Novel and recurrent COMP (cartilage oligomeric matrix protein) mutations in pseudoachondroplasia and multiple epiphyseal dysplasia."
Ikegawa S., Ohashi H., Nishimura G., Kim K.C., Sannohe A., Kimizuka M., Fukushima Y., Nagai T., Nakamura Y.
Hum. Genet. 103:633-638(1998) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS PSACH AND EDM1. - Ref.24"Identification of five novel mutations in cartilage oligomeric matrix protein gene in pseudoachondroplasia and multiple epiphyseal dysplasia."
Loughlin J., Irven C., Mustafa Z., Briggs M.D., Carr A., Lynch S.-A., Knowlton R.G., Cohn D.H., Sykes B.
Hum. Mutat. Suppl. 1:S10-S17(1998) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS PSACH ARG-328; ASP-372 DEL; 391-PRO--ASP-394 DELINS VAL; ARG-440; SER-459 DEL; TYR-468; ASP-469 DEL AND TYR-472, VARIANTS EDM1 TYR-342; TYR-361; 367-ARG-GLY-368 DEL AND TYR-408. - Ref.28"A mutation in COL9A1 causes multiple epiphyseal dysplasia: further evidence for locus heterogeneity."
Czarny-Ratajczak M., Lohiniva J., Rogala P., Kozlowski K., Peraelae M., Carter L., Spector T.D., Kolodziej L., Seppaenen U., Glazar R., Krolewski J., Latos-Bielenska A., Ala-Kokko L.
Am. J. Hum. Genet. 69:969-980(2001) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS EDM1 ARG-276; ALA-420 AND MET-585. - Ref.29"Pseudoachondroplasia and multiple epiphyseal dysplasia: A 7-year comprehensive analysis of the known disease genes identify novel and recurrent mutations and provides an accurate assessment of their relative contribution."
Jackson G.C., Mittaz-Crettol L., Taylor J.A., Mortier G.R., Spranger J., Zabel B., Le Merrer M., Cormier-Daire V., Hall C.M., Offiah A., Wright M.J., Savarirayan R., Nishimura G., Ramsden S.C., Elles R., Bonafe L., Superti-Furga A., Unger S., Zankl A., Briggs M.D.
Hum. Mutat. 33:144-157(2012) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS PSACH SER-234; GLY-290; ARG-299; TYR-326; 341-GLU-ASP-342 DEL; 350-ASN--ASP-372 DEL; VAL-378; ARG-387; 402-GLY--GLY-404 DELINS VAL-CYS; ARG-440; ASN-446; SER-448; ASP-473 DEL; HIS-473; ASN-475; GLY-482; GLY-507; GLY-511; GLY-515; ILE-529; ARG-585 AND SER-719, VARIANTS EDM1 GLU-167; ARG-276; LEU-298; ASP-311; GLY-317; GLY-326; PHE-348; SER-371; TYR-371; ASN-374; ASN-376; ASN-385; ASP-385 DEL; TYR-385; HIS-397; ARG-404; TYR-410; LYS-415; GLU-427; 430-CYS--SER-432 DELINS LEU-TRP-CYS; GLU-457 DEL; ASP-473 INS; ASP-501; LYS-523; MET-585; PRO-718 AND TRP-718, VARIANT ARG-756.
Ref.7
"Pseudoachondroplasia and multiple epiphyseal dysplasia due to mutations in the cartilage oligomeric matrix protein gene."
Briggs M.D., Hoffman S.M.G., King L.M., Olsen A.S., Mohrenweiser H., Leroy J.G., Mortier G.R., Rimoin D.L., Lachman R.S., Gaines E.S., Cekleniak J.A., Knowlton R.G., Cohn D.H.
Nat. Genet. 10:330-336(1995) [PubMed] [Europe PMC] [Abstract]
Briggs M.D., Hoffman S.M.G., King L.M., Olsen A.S., Mohrenweiser H., Leroy J.G., Mortier G.R., Rimoin D.L., Lachman R.S., Gaines E.S., Cekleniak J.A., Knowlton R.G., Cohn D.H.
Nat. Genet. 10:330-336(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 326-344, VARIANT EDM1 TYR-342, VARIANT PSACH ARG-328.
Ref.9
"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]
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]
Cited for: PROTEIN SEQUENCE, CALCIUM-BINDING, INTERACTION WITH COLLAGEN I; COLLAGEN II AND COLLAGEN IX, CHARACTERIZATION OF VARIANT PSACH ASP-469 DEL, CHARACTERIZATION OF VARIANT EDM1 TYR-361.
Ref.20
"Multiple epiphyseal dysplasia, ribbing type: a novel point mutation in the COMP gene in a South African family."
Ballo R., Briggs M.D., Cohn D.H., Knowlton R.G., Beighton P.H., Ramesar R.S.
Am. J. Med. Genet. 68:396-400(1997) [PubMed] [Europe PMC] [Abstract]
Ballo R., Briggs M.D., Cohn D.H., Knowlton R.G., Beighton P.H., Ramesar R.S.
Am. J. Med. Genet. 68:396-400(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EDM1 LYS-523.
Ref.21
"Multiple epiphyseal dysplasia and pseudoachondroplasia due to novel mutations in the calmodulin-like repeats of cartilage oligomeric matrix protein."
Susic S., McGrory J., Ahier J., Cole W.G.
Clin. Genet. 51:219-224(1997) [PubMed] [Europe PMC] [Abstract]
Susic S., McGrory J., Ahier J., Cole W.G.
Clin. Genet. 51:219-224(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EDM1 SER-371, VARIANT PSACH 513-VAL--LYS-516 DEL.
Ref.22
"Diverse mutations in the gene for cartilage oligomeric matrix protein in the pseudoachondroplasia-multiple epiphyseal dysplasia disease spectrum."
Briggs M.D., Mortier G.R., Cole W.G., King L.M., Golik S.S., Bonaventure J., Nuytinck L., de Paepe A., Leroy J.G., Biesecker L., Lipson M., Wilcox W.R., Lachman R.S., Rimoin D.L., Knowlton R.G., Cohn D.H.
Am. J. Hum. Genet. 62:311-319(1998) [PubMed] [Europe PMC] [Abstract]
Briggs M.D., Mortier G.R., Cole W.G., King L.M., Golik S.S., Bonaventure J., Nuytinck L., de Paepe A., Leroy J.G., Biesecker L., Lipson M., Wilcox W.R., Lachman R.S., Rimoin D.L., Knowlton R.G., Cohn D.H.
Am. J. Hum. Genet. 62:311-319(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PSACH, VARIANTS EDM1 SER-453 AND ARG-585.
Ref.23
"Novel and recurrent COMP (cartilage oligomeric matrix protein) mutations in pseudoachondroplasia and multiple epiphyseal dysplasia."
Ikegawa S., Ohashi H., Nishimura G., Kim K.C., Sannohe A., Kimizuka M., Fukushima Y., Nagai T., Nakamura Y.
Hum. Genet. 103:633-638(1998) [PubMed] [Europe PMC] [Abstract]
Ikegawa S., Ohashi H., Nishimura G., Kim K.C., Sannohe A., Kimizuka M., Fukushima Y., Nagai T., Nakamura Y.
Hum. Genet. 103:633-638(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PSACH AND EDM1.
Ref.24
"Identification of five novel mutations in cartilage oligomeric matrix protein gene in pseudoachondroplasia and multiple epiphyseal dysplasia."
Loughlin J., Irven C., Mustafa Z., Briggs M.D., Carr A., Lynch S.-A., Knowlton R.G., Cohn D.H., Sykes B.
Hum. Mutat. Suppl. 1:S10-S17(1998) [PubMed] [Europe PMC] [Abstract]
Loughlin J., Irven C., Mustafa Z., Briggs M.D., Carr A., Lynch S.-A., Knowlton R.G., Cohn D.H., Sykes B.
Hum. Mutat. Suppl. 1:S10-S17(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PSACH ARG-328; ASP-372 DEL; 391-PRO--ASP-394 DELINS VAL; ARG-440; SER-459 DEL; TYR-468; ASP-469 DEL AND TYR-472, VARIANTS EDM1 TYR-342; TYR-361; 367-ARG-GLY-368 DEL AND TYR-408.
Ref.28
"A mutation in COL9A1 causes multiple epiphyseal dysplasia: further evidence for locus heterogeneity."
Czarny-Ratajczak M., Lohiniva J., Rogala P., Kozlowski K., Peraelae M., Carter L., Spector T.D., Kolodziej L., Seppaenen U., Glazar R., Krolewski J., Latos-Bielenska A., Ala-Kokko L.
Am. J. Hum. Genet. 69:969-980(2001) [PubMed] [Europe PMC] [Abstract]
Czarny-Ratajczak M., Lohiniva J., Rogala P., Kozlowski K., Peraelae M., Carter L., Spector T.D., Kolodziej L., Seppaenen U., Glazar R., Krolewski J., Latos-Bielenska A., Ala-Kokko L.
Am. J. Hum. Genet. 69:969-980(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS EDM1 ARG-276; ALA-420 AND MET-585.
Ref.29
"Pseudoachondroplasia and multiple epiphyseal dysplasia: A 7-year comprehensive analysis of the known disease genes identify novel and recurrent mutations and provides an accurate assessment of their relative contribution."
Jackson G.C., Mittaz-Crettol L., Taylor J.A., Mortier G.R., Spranger J., Zabel B., Le Merrer M., Cormier-Daire V., Hall C.M., Offiah A., Wright M.J., Savarirayan R., Nishimura G., Ramsden S.C., Elles R., Bonafe L., Superti-Furga A., Unger S., Zankl A., Briggs M.D.
Hum. Mutat. 33:144-157(2012) [PubMed] [Europe PMC] [Abstract]
Jackson G.C., Mittaz-Crettol L., Taylor J.A., Mortier G.R., Spranger J., Zabel B., Le Merrer M., Cormier-Daire V., Hall C.M., Offiah A., Wright M.J., Savarirayan R., Nishimura G., Ramsden S.C., Elles R., Bonafe L., Superti-Furga A., Unger S., Zankl A., Briggs M.D.
Hum. Mutat. 33:144-157(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PSACH SER-234; GLY-290; ARG-299; TYR-326; 341-GLU-ASP-342 DEL; 350-ASN--ASP-372 DEL; VAL-378; ARG-387; 402-GLY--GLY-404 DELINS VAL-CYS; ARG-440; ASN-446; SER-448; ASP-473 DEL; HIS-473; ASN-475; GLY-482; GLY-507; GLY-511; GLY-515; ILE-529; ARG-585 AND SER-719, VARIANTS EDM1 GLU-167; ARG-276; LEU-298; ASP-311; GLY-317; GLY-326; PHE-348; SER-371; TYR-371; ASN-374; ASN-376; ASN-385; ASP-385 DEL; TYR-385; HIS-397; ARG-404; TYR-410; LYS-415; GLU-427; 430-CYS--SER-432 DELINS LEU-TRP-CYS; GLU-457 DEL; ASP-473 INS; ASP-501; LYS-523; MET-585; PRO-718 AND TRP-718, VARIANT ARG-756.
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionA generalized skeletal dysplasia associated with significant morbidity. Joint pain, joint deformity, waddling gait, and short stature are the main clinical signs and symptoms. Radiological examination of the skeleton shows delayed, irregular mineralization of the epiphyseal ossification centers and of the centers of the carpal and tarsal bones. Multiple epiphyseal dysplasia is broadly categorized into the more severe Fairbank and the milder Ribbing types. The Fairbank type is characterized by shortness of stature, short and stubby fingers, small epiphyses in several joints, including the knee, ankle, hand, and hip. The Ribbing type is confined predominantly to the hip joints and is characterized by hands that are normal and stature that is normal or near-normal.
Related information in OMIM| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_066789 | 167 | G → E in EDM1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_026239 | 276 | P → R in EDM1. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066792 | 298 | S → L in EDM1; phenotypic features overlapping with mild PSACH. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066793 | 311 | A → D in EDM1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066794 | 317 | D → G in EDM1; atypical form. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066795 | 326 | D → G in EDM1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007617 | 342 | D → Y in EDM1; Fairbank type. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066798 | 348 | C → F in EDM1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007619 | 361 | D → V in EDM1; Fairbank type. | 1 | |
| Natural variantiVAR_007620 | 361 | D → Y in EDM1; binds less calcium. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007621 | 367 – 368 | Missing in EDM1. 1 Publication Manual assertion based on experiment ini
| 2 | |
| Natural variantiVAR_007622 | 371 | C → S in EDM1; Fairbank type. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066800 | 371 | C → Y in EDM1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066801 | 374 | D → N in EDM1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066802 | 376 | D → N in EDM1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066804 | 385 | D → N in EDM1; atypical form. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066805 | 385 | D → Y in EDM1; atypical form. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066806 | 385 | Missing in EDM1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066808 | 397 | D → H in EDM1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066810 | 404 | G → R in EDM1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007627 | 408 | D → Y in EDM1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066811 | 410 | C → Y in EDM1; phenotype overlapping with mild PSACH. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066812 | 415 | N → K in EDM1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_026240 | 420 | D → A in EDM1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066813 | 427 | G → E in EDM1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066814 | 430 – 432 | CDS → LWC in EDM1. 1 Publication Manual assertion based on experiment ini
| 3 | |
| Natural variantiVAR_007630 | 453 | N → S in EDM1; Fairbank type. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066817 | 457 | Missing in EDM1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066818 | 473 | D → DD in EDM1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066821 | 501 | G → D in EDM1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007640 | 523 | N → K in EDM1; Ribbing type. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007642 | 585 | T → R in EDM1 and PSACH. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066826 | 718 | R → P in EDM1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066827 | 718 | R → W in EDM1 and CTS2; reduced secretion in tendon cells and chondrocytes. 2 Publications Manual assertion based on experiment ini
| 1 |
Pseudoachondroplasia (PSACH)12 PublicationsManual assertion based on experiment ini
- Ref.7"Pseudoachondroplasia and multiple epiphyseal dysplasia due to mutations in the cartilage oligomeric matrix protein gene."
Briggs M.D., Hoffman S.M.G., King L.M., Olsen A.S., Mohrenweiser H., Leroy J.G., Mortier G.R., Rimoin D.L., Lachman R.S., Gaines E.S., Cekleniak J.A., Knowlton R.G., Cohn D.H.
Nat. Genet. 10:330-336(1995) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 326-344, VARIANT EDM1 TYR-342, VARIANT PSACH ARG-328. - Ref.8"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]Cited for: PROTEIN SEQUENCE OF 80-89, SUBUNIT, CALCIUM-BINDING, CHARACTERIZATION OF VARIANT PSACH ASP-469 DEL. - Ref.9"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]Cited for: PROTEIN SEQUENCE, CALCIUM-BINDING, INTERACTION WITH COLLAGEN I; COLLAGEN II AND COLLAGEN IX, CHARACTERIZATION OF VARIANT PSACH ASP-469 DEL, CHARACTERIZATION OF VARIANT EDM1 TYR-361. - Ref.19"Mutations in exon 17B of cartilage oligomeric matrix protein (COMP) cause pseudoachondroplasia."
Hecht J.T., Nelson L.D., Crowder E., Wang Y., Elder F.F.B., Harrison W.R., Francomano C.A., Prange C.K., Lennon G.G., Deere M., Lawler J.
Nat. Genet. 10:325-329(1995) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS PSACH SER-459 DEL; TYR-468 AND TYR-472. - Ref.21"Multiple epiphyseal dysplasia and pseudoachondroplasia due to novel mutations in the calmodulin-like repeats of cartilage oligomeric matrix protein."
Susic S., McGrory J., Ahier J., Cole W.G.
Clin. Genet. 51:219-224(1997) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT EDM1 SER-371, VARIANT PSACH 513-VAL--LYS-516 DEL. - Ref.22"Diverse mutations in the gene for cartilage oligomeric matrix protein in the pseudoachondroplasia-multiple epiphyseal dysplasia disease spectrum."
Briggs M.D., Mortier G.R., Cole W.G., King L.M., Golik S.S., Bonaventure J., Nuytinck L., de Paepe A., Leroy J.G., Biesecker L., Lipson M., Wilcox W.R., Lachman R.S., Rimoin D.L., Knowlton R.G., Cohn D.H.
Am. J. Hum. Genet. 62:311-319(1998) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS PSACH, VARIANTS EDM1 SER-453 AND ARG-585. - Ref.23"Novel and recurrent COMP (cartilage oligomeric matrix protein) mutations in pseudoachondroplasia and multiple epiphyseal dysplasia."
Ikegawa S., Ohashi H., Nishimura G., Kim K.C., Sannohe A., Kimizuka M., Fukushima Y., Nagai T., Nakamura Y.
Hum. Genet. 103:633-638(1998) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS PSACH AND EDM1. - Ref.24"Identification of five novel mutations in cartilage oligomeric matrix protein gene in pseudoachondroplasia and multiple epiphyseal dysplasia."
Loughlin J., Irven C., Mustafa Z., Briggs M.D., Carr A., Lynch S.-A., Knowlton R.G., Cohn D.H., Sykes B.
Hum. Mutat. Suppl. 1:S10-S17(1998) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS PSACH ARG-328; ASP-372 DEL; 391-PRO--ASP-394 DELINS VAL; ARG-440; SER-459 DEL; TYR-468; ASP-469 DEL AND TYR-472, VARIANTS EDM1 TYR-342; TYR-361; 367-ARG-GLY-368 DEL AND TYR-408. - Ref.25"Pseudoachondroplasia due to the substitution of the highly conserved Asp482 by Gly in the seventh calmodulin-like repeat of cartilage oligomeric matrix protein."
Susic S., Ahier J., Cole W.G.
Hum. Mutat. Suppl. 1:S125-S127(1998) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT PSACH GLY-482. - Ref.26"Double heterozygosity for pseudoachondroplasia and spondyloepiphyseal dysplasia congenita."
Unger S., Koerkkoe J., Krakow D., Lachman R.S., Rimoin D.L., Cohn D.H.
Am. J. Med. Genet. 104:140-146(2001) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT PSACH ARG-348. - Ref.27"Novel mutation in exon 18 of the cartilage oligomeric matrix protein gene causes a severe pseudoachondroplasia."
Mabuchi A., Haga N., Ikeda T., Manabe N., Ohashi H., Takatori Y., Nakamura K., Ikegawa S.
Am. J. Med. Genet. 104:135-139(2001) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT PSACH ASP-719. - Ref.29"Pseudoachondroplasia and multiple epiphyseal dysplasia: A 7-year comprehensive analysis of the known disease genes identify novel and recurrent mutations and provides an accurate assessment of their relative contribution."
Jackson G.C., Mittaz-Crettol L., Taylor J.A., Mortier G.R., Spranger J., Zabel B., Le Merrer M., Cormier-Daire V., Hall C.M., Offiah A., Wright M.J., Savarirayan R., Nishimura G., Ramsden S.C., Elles R., Bonafe L., Superti-Furga A., Unger S., Zankl A., Briggs M.D.
Hum. Mutat. 33:144-157(2012) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS PSACH SER-234; GLY-290; ARG-299; TYR-326; 341-GLU-ASP-342 DEL; 350-ASN--ASP-372 DEL; VAL-378; ARG-387; 402-GLY--GLY-404 DELINS VAL-CYS; ARG-440; ASN-446; SER-448; ASP-473 DEL; HIS-473; ASN-475; GLY-482; GLY-507; GLY-511; GLY-515; ILE-529; ARG-585 AND SER-719, VARIANTS EDM1 GLU-167; ARG-276; LEU-298; ASP-311; GLY-317; GLY-326; PHE-348; SER-371; TYR-371; ASN-374; ASN-376; ASN-385; ASP-385 DEL; TYR-385; HIS-397; ARG-404; TYR-410; LYS-415; GLU-427; 430-CYS--SER-432 DELINS LEU-TRP-CYS; GLU-457 DEL; ASP-473 INS; ASP-501; LYS-523; MET-585; PRO-718 AND TRP-718, VARIANT ARG-756.
Ref.7
"Pseudoachondroplasia and multiple epiphyseal dysplasia due to mutations in the cartilage oligomeric matrix protein gene."
Briggs M.D., Hoffman S.M.G., King L.M., Olsen A.S., Mohrenweiser H., Leroy J.G., Mortier G.R., Rimoin D.L., Lachman R.S., Gaines E.S., Cekleniak J.A., Knowlton R.G., Cohn D.H.
Nat. Genet. 10:330-336(1995) [PubMed] [Europe PMC] [Abstract]
Briggs M.D., Hoffman S.M.G., King L.M., Olsen A.S., Mohrenweiser H., Leroy J.G., Mortier G.R., Rimoin D.L., Lachman R.S., Gaines E.S., Cekleniak J.A., Knowlton R.G., Cohn D.H.
Nat. Genet. 10:330-336(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 326-344, VARIANT EDM1 TYR-342, VARIANT PSACH ARG-328.
Ref.8
"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]
Chen H., Deere M., Hecht J.T., Lawler J.
J. Biol. Chem. 275:26538-26544(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 80-89, SUBUNIT, CALCIUM-BINDING, CHARACTERIZATION OF VARIANT PSACH ASP-469 DEL.
Ref.9
"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]
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]
Cited for: PROTEIN SEQUENCE, CALCIUM-BINDING, INTERACTION WITH COLLAGEN I; COLLAGEN II AND COLLAGEN IX, CHARACTERIZATION OF VARIANT PSACH ASP-469 DEL, CHARACTERIZATION OF VARIANT EDM1 TYR-361.
Ref.19
"Mutations in exon 17B of cartilage oligomeric matrix protein (COMP) cause pseudoachondroplasia."
Hecht J.T., Nelson L.D., Crowder E., Wang Y., Elder F.F.B., Harrison W.R., Francomano C.A., Prange C.K., Lennon G.G., Deere M., Lawler J.
Nat. Genet. 10:325-329(1995) [PubMed] [Europe PMC] [Abstract]
Hecht J.T., Nelson L.D., Crowder E., Wang Y., Elder F.F.B., Harrison W.R., Francomano C.A., Prange C.K., Lennon G.G., Deere M., Lawler J.
Nat. Genet. 10:325-329(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PSACH SER-459 DEL; TYR-468 AND TYR-472.
Ref.21
"Multiple epiphyseal dysplasia and pseudoachondroplasia due to novel mutations in the calmodulin-like repeats of cartilage oligomeric matrix protein."
Susic S., McGrory J., Ahier J., Cole W.G.
Clin. Genet. 51:219-224(1997) [PubMed] [Europe PMC] [Abstract]
Susic S., McGrory J., Ahier J., Cole W.G.
Clin. Genet. 51:219-224(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EDM1 SER-371, VARIANT PSACH 513-VAL--LYS-516 DEL.
Ref.22
"Diverse mutations in the gene for cartilage oligomeric matrix protein in the pseudoachondroplasia-multiple epiphyseal dysplasia disease spectrum."
Briggs M.D., Mortier G.R., Cole W.G., King L.M., Golik S.S., Bonaventure J., Nuytinck L., de Paepe A., Leroy J.G., Biesecker L., Lipson M., Wilcox W.R., Lachman R.S., Rimoin D.L., Knowlton R.G., Cohn D.H.
Am. J. Hum. Genet. 62:311-319(1998) [PubMed] [Europe PMC] [Abstract]
Briggs M.D., Mortier G.R., Cole W.G., King L.M., Golik S.S., Bonaventure J., Nuytinck L., de Paepe A., Leroy J.G., Biesecker L., Lipson M., Wilcox W.R., Lachman R.S., Rimoin D.L., Knowlton R.G., Cohn D.H.
Am. J. Hum. Genet. 62:311-319(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PSACH, VARIANTS EDM1 SER-453 AND ARG-585.
Ref.23
"Novel and recurrent COMP (cartilage oligomeric matrix protein) mutations in pseudoachondroplasia and multiple epiphyseal dysplasia."
Ikegawa S., Ohashi H., Nishimura G., Kim K.C., Sannohe A., Kimizuka M., Fukushima Y., Nagai T., Nakamura Y.
Hum. Genet. 103:633-638(1998) [PubMed] [Europe PMC] [Abstract]
Ikegawa S., Ohashi H., Nishimura G., Kim K.C., Sannohe A., Kimizuka M., Fukushima Y., Nagai T., Nakamura Y.
Hum. Genet. 103:633-638(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PSACH AND EDM1.
Ref.24
"Identification of five novel mutations in cartilage oligomeric matrix protein gene in pseudoachondroplasia and multiple epiphyseal dysplasia."
Loughlin J., Irven C., Mustafa Z., Briggs M.D., Carr A., Lynch S.-A., Knowlton R.G., Cohn D.H., Sykes B.
Hum. Mutat. Suppl. 1:S10-S17(1998) [PubMed] [Europe PMC] [Abstract]
Loughlin J., Irven C., Mustafa Z., Briggs M.D., Carr A., Lynch S.-A., Knowlton R.G., Cohn D.H., Sykes B.
Hum. Mutat. Suppl. 1:S10-S17(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PSACH ARG-328; ASP-372 DEL; 391-PRO--ASP-394 DELINS VAL; ARG-440; SER-459 DEL; TYR-468; ASP-469 DEL AND TYR-472, VARIANTS EDM1 TYR-342; TYR-361; 367-ARG-GLY-368 DEL AND TYR-408.
Ref.25
"Pseudoachondroplasia due to the substitution of the highly conserved Asp482 by Gly in the seventh calmodulin-like repeat of cartilage oligomeric matrix protein."
Susic S., Ahier J., Cole W.G.
Hum. Mutat. Suppl. 1:S125-S127(1998) [PubMed] [Europe PMC] [Abstract]
Susic S., Ahier J., Cole W.G.
Hum. Mutat. Suppl. 1:S125-S127(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PSACH GLY-482.
Ref.26
"Double heterozygosity for pseudoachondroplasia and spondyloepiphyseal dysplasia congenita."
Unger S., Koerkkoe J., Krakow D., Lachman R.S., Rimoin D.L., Cohn D.H.
Am. J. Med. Genet. 104:140-146(2001) [PubMed] [Europe PMC] [Abstract]
Unger S., Koerkkoe J., Krakow D., Lachman R.S., Rimoin D.L., Cohn D.H.
Am. J. Med. Genet. 104:140-146(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PSACH ARG-348.
Ref.27
"Novel mutation in exon 18 of the cartilage oligomeric matrix protein gene causes a severe pseudoachondroplasia."
Mabuchi A., Haga N., Ikeda T., Manabe N., Ohashi H., Takatori Y., Nakamura K., Ikegawa S.
Am. J. Med. Genet. 104:135-139(2001) [PubMed] [Europe PMC] [Abstract]
Mabuchi A., Haga N., Ikeda T., Manabe N., Ohashi H., Takatori Y., Nakamura K., Ikegawa S.
Am. J. Med. Genet. 104:135-139(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PSACH ASP-719.
Ref.29
"Pseudoachondroplasia and multiple epiphyseal dysplasia: A 7-year comprehensive analysis of the known disease genes identify novel and recurrent mutations and provides an accurate assessment of their relative contribution."
Jackson G.C., Mittaz-Crettol L., Taylor J.A., Mortier G.R., Spranger J., Zabel B., Le Merrer M., Cormier-Daire V., Hall C.M., Offiah A., Wright M.J., Savarirayan R., Nishimura G., Ramsden S.C., Elles R., Bonafe L., Superti-Furga A., Unger S., Zankl A., Briggs M.D.
Hum. Mutat. 33:144-157(2012) [PubMed] [Europe PMC] [Abstract]
Jackson G.C., Mittaz-Crettol L., Taylor J.A., Mortier G.R., Spranger J., Zabel B., Le Merrer M., Cormier-Daire V., Hall C.M., Offiah A., Wright M.J., Savarirayan R., Nishimura G., Ramsden S.C., Elles R., Bonafe L., Superti-Furga A., Unger S., Zankl A., Briggs M.D.
Hum. Mutat. 33:144-157(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PSACH SER-234; GLY-290; ARG-299; TYR-326; 341-GLU-ASP-342 DEL; 350-ASN--ASP-372 DEL; VAL-378; ARG-387; 402-GLY--GLY-404 DELINS VAL-CYS; ARG-440; ASN-446; SER-448; ASP-473 DEL; HIS-473; ASN-475; GLY-482; GLY-507; GLY-511; GLY-515; ILE-529; ARG-585 AND SER-719, VARIANTS EDM1 GLU-167; ARG-276; LEU-298; ASP-311; GLY-317; GLY-326; PHE-348; SER-371; TYR-371; ASN-374; ASN-376; ASN-385; ASP-385 DEL; TYR-385; HIS-397; ARG-404; TYR-410; LYS-415; GLU-427; 430-CYS--SER-432 DELINS LEU-TRP-CYS; GLU-457 DEL; ASP-473 INS; ASP-501; LYS-523; MET-585; PRO-718 AND TRP-718, VARIANT ARG-756.
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionA skeletal dysplasia usually manifesting in the second year of life and characterized by moderate to severe disproportionate short stature, deformity of the lower limbs, brachydactyly, ligamentous laxity, and degenerative joint disease.
Related information in OMIM| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Natural variantiVAR_066790 | 234 | P → S in PSACH. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066791 | 290 | D → G in PSACH. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007614 | 290 | D → N in PSACH; mild form. | 1 | |
| Natural variantiVAR_007615 | 299 | G → R in PSACH. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066796 | 326 | D → Y in PSACH. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007616 | 328 | C → R in PSACH; mild form. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066797 | 341 – 342 | Missing in PSACH. 1 Publication Manual assertion based on experiment ini
| 2 | |
| Natural variantiVAR_017102 | 348 | C → R in PSACH. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007618 | 349 | D → V in PSACH; mild form. | 1 | |
| Natural variantiVAR_066799 | 350 – 372 | Missing in PSACH. 1 Publication Manual assertion based on experiment ini
| 23 | |
| Natural variantiVAR_007623 | 372 | Missing in PSACH. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007624 | 374 | Missing in PSACH; mild form. | 1 | |
| Natural variantiVAR_066803 | 378 | D → V in PSACH. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007625 | 387 | C → G in PSACH; mild form. | 1 | |
| Natural variantiVAR_066807 | 387 | C → R in PSACH. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007626 | 391 – 394 | PNSD → V in PSACH. 1 Publication Manual assertion based on experiment ini
| 4 | |
| Natural variantiVAR_066809 | 402 – 404 | GIG → VC in PSACH. 1 Publication Manual assertion based on experiment ini
| 3 | |
| Natural variantiVAR_007628 | 440 | G → E in PSACH; mild form. | 1 | |
| Natural variantiVAR_007629 | 440 | G → R in PSACH. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066815 | 446 | D → N in PSACH. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066816 | 448 | C → S in PSACH. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007631 | 459 | Missing in PSACH; severe form. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007632 | 468 | C → Y in PSACH; severe form. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007633 | 469 | Missing in PSACH; severe form; MUT3 mutant; most common mutation; binds less calcium and causes misfolding of the protein; greatly reduced interaction with ACAN; reduced interaction with collagen. 3 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007634 | 472 | D → Y in PSACH; severe form. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007635 | 473 | D → G in PSACH; severe form. Corresponds to variant dbSNP:rs28936669EnsemblClinVar. | 1 | |
| Natural variantiVAR_066819 | 473 | D → H in PSACH. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007636 | 473 | Missing in PSACH; severe form. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066820 | 475 | D → N in PSACH. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007637 | 482 | D → G in PSACH. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066822 | 507 | D → G in PSACH. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066823 | 511 | D → G in PSACH. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007638 | 513 – 516 | Missing in PSACH; mild form. 1 Publication Manual assertion based on experiment ini
| 4 | |
| Natural variantiVAR_066824 | 515 | D → G in PSACH. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007639 | 518 | D → N in PSACH; mild form. Corresponds to variant dbSNP:rs1359984033Ensembl. | 1 | |
| Natural variantiVAR_066825 | 529 | T → I in PSACH. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007641 | 585 | T → M in PSACH; mild form and EDM1. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007642 | 585 | T → R in EDM1 and PSACH. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_017103 | 719 | G → D in PSACH; severe. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066828 | 719 | G → S in PSACH. 1 Publication Manual assertion based on experiment ini
| 1 |
Carpal tunnel syndrome 2 (CTS2)1 PublicationManual assertion based on experiment ini
- Ref.30"Mutations in COMP cause familial carpal tunnel syndrome."
Li C., Wang N., Schaeffer A.A., Liu X., Zhao Z., Elliott G., Garrett L., Choi N.T., Wang Y., Wang Y., Wang C., Wang J., Chan D., Su P., Cui S., Yang Y., Gao B.
Nat. Commun. 11:3642-3642(2020) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS CTS2 GLU-66 AND TRP-718, CHARACTERIZATION OF VARIANTS CTS2 GLU-66 AND TRP-718, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Ref.30
"Mutations in COMP cause familial carpal tunnel syndrome."
Li C., Wang N., Schaeffer A.A., Liu X., Zhao Z., Elliott G., Garrett L., Choi N.T., Wang Y., Wang Y., Wang C., Wang J., Chan D., Su P., Cui S., Yang Y., Gao B.
Nat. Commun. 11:3642-3642(2020) [PubMed] [Europe PMC] [Abstract]
Li C., Wang N., Schaeffer A.A., Liu X., Zhao Z., Elliott G., Garrett L., Choi N.T., Wang Y., Wang Y., Wang C., Wang J., Chan D., Su P., Cui S., Yang Y., Gao B.
Nat. Commun. 11:3642-3642(2020) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CTS2 GLU-66 AND TRP-718, CHARACTERIZATION OF VARIANTS CTS2 GLU-66 AND TRP-718, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant form of carpal tunnel syndrome, a condition characterized by entrapment of the median nerve within the carpal tunnel. Symptoms include burning pain and paresthesias involving the ventral surface of the hand and fingers which may radiate proximally. Impairment of sensation in the distribution of the median nerve and thenar muscle atrophy may occur. This condition may be associated with repetitive occupational trauma, wrist injuries, amyloid neuropathies, rheumatoid arthritis.
Related information in OMIM| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Natural variantiVAR_085230 | 66 | V → E in CTS2; reduced secretion in tendon cells; no effect on secretion in chondrocytes; disrupted pentamerization; induced ER stress. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066827 | 718 | R → W in EDM1 and CTS2; reduced secretion in tendon cells and chondrocytes. 2 Publications Manual assertion based on experiment ini
| 1 |
Keywords - Diseasei
Disease variant, DwarfismOrganism-specific databases
DisGeNET More...DisGeNETi | 1311 |
GeneReviews a resource of expert-authored, peer-reviewed disease descriptions. More...GeneReviewsi | COMP |
MalaCards human disease database More...MalaCardsi | COMP |
| MIMi | 132400, phenotype 177170, phenotype 619161, phenotype |
Open Targets More...OpenTargetsi | ENSG00000105664 |
Orphanet; a database dedicated to information on rare diseases and orphan drugs More...Orphaneti | 93308, Multiple epiphyseal dysplasia type 1 750, Pseudoachondroplasia |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA26744 |
Miscellaneous databases
Pharos NIH Druggable Genome Knowledgebase More...Pharosi | P49747, Tbio |
Chemistry databases
Drug and drug target database More...DrugBanki | DB01373, Calcium |
Genetic variation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | COMP |
Domain mapping of disease mutations (DMDM) More...DMDMi | 209572601 |
<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
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei | 1 – 20 | Sequence analysisAdd BLAST | 20 | |
| <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000035857 | 21 – 757 | Cartilage oligomeric matrix proteinAdd BLAST | 737 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi | 69 | Interchain1 Publication <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| ||
| Disulfide bondi | 72 | Interchain1 Publication Manual assertion inferred by curator fromi
| ||
| Disulfide bondi | 91 ↔ 102 | PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | ||
| Disulfide bondi | 96 ↔ 111 | PROSITE-ProRule annotation Manual assertion according to rulesi | ||
| Disulfide bondi | 114 ↔ 125 | PROSITE-ProRule annotation Manual assertion according to rulesi | ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi | 121 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
| Disulfide bondi | 131 ↔ 142 | PROSITE-ProRule annotation Manual assertion according to rulesi | ||
| Disulfide bondi | 136 ↔ 151 | PROSITE-ProRule annotation Manual assertion according to rulesi | ||
| Disulfide bondi | 154 ↔ 178 | PROSITE-ProRule annotation Manual assertion according to rulesi | ||
| Disulfide bondi | 184 ↔ 197 | PROSITE-ProRule annotation Manual assertion according to rulesi | ||
| Disulfide bondi | 191 ↔ 206 | PROSITE-ProRule annotation Manual assertion according to rulesi | ||
| Disulfide bondi | 209 ↔ 221 | PROSITE-ProRule annotation Manual assertion according to rulesi | ||
| Disulfide bondi | 229 ↔ 243 | PROSITE-ProRule annotation Manual assertion according to rulesi 1 PublicationManual assertion based on experiment ini
| ||
| Disulfide bondi | 237 ↔ 253 | PROSITE-ProRule annotation Manual assertion according to rulesi 1 PublicationManual assertion based on experiment ini
| ||
| Disulfide bondi | 255 ↔ 266 | PROSITE-ProRule annotation Manual assertion according to rulesi 1 PublicationManual assertion based on experiment ini
| ||
| Disulfide bondi | 282 ↔ 287 | PROSITE-ProRule annotation Manual assertion according to rulesi 1 PublicationManual assertion based on experiment ini
| ||
| Disulfide bondi | 292 ↔ 312 | PROSITE-ProRule annotation Manual assertion according to rulesi 1 PublicationManual assertion based on experiment ini
| ||
| Disulfide bondi | 328 ↔ 348 | PROSITE-ProRule annotation Manual assertion according to rulesi 1 PublicationManual assertion based on experiment ini
| ||
| Disulfide bondi | 351 ↔ 371 | PROSITE-ProRule annotation Manual assertion according to rulesi 1 PublicationManual assertion based on experiment ini
| ||
| Disulfide bondi | 387 ↔ 407 | PROSITE-ProRule annotation Manual assertion according to rulesi 1 PublicationManual assertion based on experiment ini
| ||
| Disulfide bondi | 410 ↔ 430 | PROSITE-ProRule annotation Manual assertion according to rulesi 1 PublicationManual assertion based on experiment ini
| ||
| Disulfide bondi | 448 ↔ 468 | PROSITE-ProRule annotation Manual assertion according to rulesi 1 PublicationManual assertion based on experiment ini
| ||
| Disulfide bondi | 484 ↔ 504 | PROSITE-ProRule annotation Manual assertion according to rulesi 1 PublicationManual assertion based on experiment ini
| ||
| Disulfide bondi | 520 ↔ 741 | PROSITE-ProRule annotation Manual assertion according to rulesi 1 PublicationManual assertion based on experiment ini
| ||
| Glycosylationi | 742 | N-linked (GlcNAc...) asparagine1 Publication Manual assertion based on experiment ini
| 1 |
Keywords - PTMi
Disulfide bond, GlycoproteinProteomic databases
jPOST - Japan Proteome Standard Repository/Database More...jPOSTi | P49747 |
MassIVE - Mass Spectrometry Interactive Virtual Environment More...MassIVEi | P49747 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P49747 |
PeptideAtlas More...PeptideAtlasi | P49747 |
PRoteomics IDEntifications database More...PRIDEi | P49747 |
ProteomicsDB: a multi-organism proteome resource More...ProteomicsDBi | 4464 56060 [P49747-1] |
PTM databases
GlyConnect protein glycosylation platform More...GlyConnecti | 1076, 7 N-Linked glycans (2 sites) |
GlyGen: Computational and Informatics Resources for Glycoscience More...GlyGeni | P49747, 2 sites, 8 N-linked glycans (2 sites) |
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P49747 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P49747 |
<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
Abundantly expressed in the chondrocyte extracellular matrix, and is also found in bone, tendon, ligament and synovium and blood vessels. Increased amounts are produced during late stages of osteoarthritis in the area adjacent to the main defect.2 Publications
Manual assertion based on experiment ini
- Ref.13"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]Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. - Ref.30"Mutations in COMP cause familial carpal tunnel syndrome."
Li C., Wang N., Schaeffer A.A., Liu X., Zhao Z., Elliott G., Garrett L., Choi N.T., Wang Y., Wang Y., Wang C., Wang J., Chan D., Su P., Cui S., Yang Y., Gao B.
Nat. Commun. 11:3642-3642(2020) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS CTS2 GLU-66 AND TRP-718, CHARACTERIZATION OF VARIANTS CTS2 GLU-66 AND TRP-718, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei
Present during the earliest stages of limb maturation and is later found in regions where the joints develop.1 Publication
Manual assertion based on experiment ini
- Ref.13"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]Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000105664, Expressed in tendon of biceps brachii and 153 other tissues |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P49747, baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P49747, HS |
Organism-specific databases
Human Protein Atlas More...HPAi | ENSG00000105664, Tissue enhanced (adipose tissue, skin) |
<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
Pentamer; disulfide-linked (PubMed:32686688). Exists in a more compact conformation in the presence of calcium and shows a more extended conformation in the absence of calcium (PubMed:19276170).
Interacts with ITGB3, ITGA5 and FN1. Binding to FN1 requires the presence of divalent cations (Ca2+, Mg2+ or Mn2+). The greatest amount of binding is seen in the presence of Mn2+ (PubMed:16051604, PubMed:12225811).
Interacts with MATN1, MATN3, MATN4 and ACAN (PubMed:15075323, PubMed:17588949). Binds heparin, heparan sulfate and chondroitin sulfate. EDTA dimishes significantly its binding to ACAN and abolishes its binding to MATN3, MATN4 and chondroitin sulfate (PubMed:17588949).
Interacts with collagen I, II and IX, and interaction with these collagens is dependent on the presence of zinc ions (PubMed:11084047).
Interacts with ADAMTS12 (PubMed:16611630).
Interacts with ITGA7 (By similarity).
By similarityManual assertion inferred from sequence similarity toi
8 PublicationsManual assertion based on experiment ini
- Ref.9"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]Cited for: PROTEIN SEQUENCE, CALCIUM-BINDING, INTERACTION WITH COLLAGEN I; COLLAGEN II AND COLLAGEN IX, CHARACTERIZATION OF VARIANT PSACH ASP-469 DEL, CHARACTERIZATION OF VARIANT EDM1 TYR-361. - Ref.10"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]Cited for: INTERACTION WITH FN1. - Ref.11"Interactions between the cartilage oligomeric matrix protein and matrilins. Implications for matrix assembly and the pathogenesis of chondrodysplasias."
Mann H.H., Oezbek S., Engel J., Paulsson M., Wagener R.
J. Biol. Chem. 279:25294-25298(2004) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH MATN1; MATN3 AND MATN4. - Ref.12"Cartilage oligomeric matrix protein/thrombospondin 5 supports chondrocyte attachment through interaction with integrins."
Chen F.-H., Thomas A.O., Hecht J.T., Goldring M.B., Lawler J.
J. Biol. Chem. 280:32655-32661(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH ITGB3 AND ITGA5. - Ref.14"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]Cited for: INTERACTION WITH ADAMTS12. - Ref.15"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]Cited for: INTERACTION WITH ACAN; HEPARIN; HEPARAN SULFATE AND CHONDROITIN SULFATE. - Ref.18"The crystal structure of the signature domain of cartilage oligomeric matrix protein: implications for collagen, glycosaminoglycan and integrin binding."
Tan K., Duquette M., Joachimiak A., Lawler J.
FASEB J. 23:2490-2501(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) OF 225-757 IN COMPLEX WITH CALCIUM IONS, DISULFIDE BONDS, GLYCOSYLATION AT ASN-742. - Ref.30"Mutations in COMP cause familial carpal tunnel syndrome."
Li C., Wang N., Schaeffer A.A., Liu X., Zhao Z., Elliott G., Garrett L., Choi N.T., Wang Y., Wang Y., Wang C., Wang J., Chan D., Su P., Cui S., Yang Y., Gao B.
Nat. Commun. 11:3642-3642(2020) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS CTS2 GLU-66 AND TRP-718, CHARACTERIZATION OF VARIANTS CTS2 GLU-66 AND TRP-718, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
P49747
GO - Molecular functioni
- BMP binding Source: Ensembl
- heparan sulfate proteoglycan binding Source: UniProtKBInferred from direct assayi
- Ref.15"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]Cited for: INTERACTION WITH ACAN; HEPARIN; HEPARAN SULFATE AND CHONDROITIN SULFATE.
- integrin binding Source: Ensembl
- protease binding Source: BHF-UCLInferred from physical interactioni
- "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: MGIInferred from direct assayi
- "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
The Biological General Repository for Interaction Datasets (BioGRID) More...BioGRIDi | 107706, 11 interactors |
ComplexPortal: manually curated resource of macromolecular complexes More...ComplexPortali | CPX-1791, Thrombospondin 5 complex |
Protein interaction database and analysis system More...IntActi | P49747, 18 interactors |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000222271 |
Miscellaneous databases
RNAct, Protein-RNA interaction predictions for model organisms. More...RNActi | P49747, protein |
<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
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 232 – 234 | Combined sources <p>Information inferred from a combination of experimental and computational evidence, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000213">More...</a></p> Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 241 – 245 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 251 – 255 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 259 – 265 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 | |
| Beta strandi | 272 – 274 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 285 – 287 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 291 – 295 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 306 – 308 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 310 – 312 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code 'T'.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 314 – 317 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 319 – 321 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 323 – 325 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 327 – 331 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 342 – 344 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 346 – 348 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 364 – 367 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Helixi | 369 – 371 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 378 – 380 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 401 – 403 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 405 – 407 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 424 – 426 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Turni | 428 – 430 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 443 – 445 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 462 – 464 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Turni | 466 – 468 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 470 – 473 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 475 – 477 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 479 – 481 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 495 – 500 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Turni | 503 – 506 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 4 | |
| Beta strandi | 511 – 513 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 515 – 517 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 532 – 540 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 9 | |
| Beta strandi | 551 – 553 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Turni | 555 – 557 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 560 – 562 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 567 – 588 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 22 | |
| Beta strandi | 596 – 605 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 10 | |
| Beta strandi | 608 – 617 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 10 | |
| Beta strandi | 625 – 627 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 636 – 641 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 648 – 655 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
| Beta strandi | 656 – 658 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Turni | 661 – 663 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 664 – 669 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 681 – 689 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 9 | |
| Helixi | 690 – 692 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 694 – 701 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 8 | |
| Beta strandi | 704 – 708 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 716 – 728 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 13 | |
| Beta strandi | 732 – 741 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 10 | |
| Helixi | 748 – 754 | Combined sources Automatic assertion inferred from combination of experimental and computational evidencei | 7 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P49747 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P49747 |
<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
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 87 – 126 | EGF-like 1PROSITE-ProRule annotation Manual assertion according to rulesi Add BLAST | 40 | |
| Domaini | 127 – 179 | EGF-like 2; calcium-bindingPROSITE-ProRule annotation Manual assertion according to rulesi Add BLAST | 53 | |
| Domaini | 180 – 222 | EGF-like 3; calcium-bindingPROSITE-ProRule annotation Manual assertion according to rulesi Add BLAST | 43 | |
| Domaini | 225 – 267 | EGF-like 4PROSITE-ProRule annotation Manual assertion according to rulesi Add BLAST | 43 | |
| <p>This subsection of the 'Family and Domains' section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati | 268 – 300 | TSP type-3 1Add BLAST | 33 | |
| Repeati | 301 – 336 | TSP type-3 2Add BLAST | 36 | |
| Repeati | 337 – 359 | TSP type-3 3Add BLAST | 23 | |
| Repeati | 360 – 395 | TSP type-3 4Add BLAST | 36 | |
| Repeati | 396 – 418 | TSP type-3 5Add BLAST | 23 | |
| Repeati | 419 – 456 | TSP type-3 6Add BLAST | 38 | |
| Repeati | 457 – 492 | TSP type-3 7Add BLAST | 36 | |
| Repeati | 493 – 528 | TSP type-3 8Add BLAST | 36 | |
| Domaini | 532 – 746 | TSP C-terminalPROSITE-ProRule annotation Manual assertion according to rulesi Add BLAST | 215 |
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 22 – 86 | COMP N-terminalAdd BLAST | 65 | |
| Regioni | 298 – 503 | DisorderedSequence analysis <p>Information which has been generated by the UniProtKB automatic annotation system, without manual validation.</p> <p><a href="/manual/evidences#ECO:0000256">More...</a></p> Automatic assertion according to sequence analysisi Add BLAST | 206 | |
| Regioni | 527 – 757 | Mediates cell survival and induction of the IAP family of survival proteinsAdd BLAST | 231 |
Motif
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi | 367 – 369 | Cell attachment siteSequence analysis | 3 |
Compositional bias
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 303 – 322 | Basic and acidic residuesSequence analysis Automatic assertion according to sequence analysisi Add BLAST | 20 | |
| Compositional biasi | 335 – 383 | Basic and acidic residuesSequence analysis Automatic assertion according to sequence analysisi Add BLAST | 49 | |
| Compositional biasi | 417 – 444 | Basic and acidic residuesSequence analysis Automatic assertion according to sequence analysisi Add BLAST | 28 | |
| Compositional biasi | 463 – 477 | Acidic residuesSequence analysis Automatic assertion according to sequence analysisi Add BLAST | 15 |
<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
The cell attachment motif mediates the attachment to chondrocytes. It mediates the induction of both the IAP family of survival proteins and the antiapoptotic response.1 Publication
Manual assertion based on experiment ini
- Ref.16"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]Cited for: FUNCTION, DOMAINS.
The TSP C-terminal domain mediates interaction with FN1 and ACAN.1 Publication
Manual assertion based on experiment ini
- Ref.16"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]Cited for: FUNCTION, DOMAINS.
Each of the eight TSP type-3 repeats binds two calcium ions. The TSP C-terminal domain binds three calcium ions.1 Publication
Manual assertion based on experiment ini
- Ref.16"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]Cited for: FUNCTION, DOMAINS.
<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
Belongs to the thrombospondin family.Curated
Keywords - Domaini
EGF-like domain, Repeat, SignalPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG502QRK8, Eukaryota |
Ensembl GeneTree More...GeneTreei | ENSGT00940000162169 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P49747 |
Identification of Orthologs from Complete Genome Data More...OMAi | CPERNCN |
Database of Orthologous Groups More...OrthoDBi | 120983at2759 |
Database for complete collections of gene phylogenies More...PhylomeDBi | P49747 |
TreeFam database of animal gene trees More...TreeFami | TF324917 |
Family and domain databases
Conserved Domains Database More...CDDi | cd16077, TSP-5cc, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 4.10.1080.10, 2 hits |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR013320, ConA-like_dom_sf IPR001881, EGF-like_Ca-bd_dom IPR000742, EGF-like_dom IPR018097, EGF_Ca-bd_CS IPR009030, Growth_fac_rcpt_cys_sf IPR024665, Thbs/COMP_coiled-coil IPR003367, Thrombospondin_3-like_rpt IPR017897, Thrombospondin_3_rpt IPR008859, Thrombospondin_C IPR028492, TSP-5 IPR039081, TSP-5_cc IPR028974, TSP_type-3_rpt |
The PANTHER Classification System More...PANTHERi | PTHR10199:SF88, PTHR10199:SF88, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF11598, COMP, 1 hit PF07645, EGF_CA, 2 hits PF02412, TSP_3, 5 hits PF05735, TSP_C, 1 hit |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00181, EGF, 4 hits SM00179, EGF_CA, 3 hits |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF103647, SSF103647, 3 hits SSF49899, SSF49899, 1 hit SSF57184, SSF57184, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS01186, EGF_2, 1 hit PS50026, EGF_3, 3 hits PS01187, EGF_CA, 2 hits PS51234, TSP3, 8 hits PS51236, TSP_CTER, 1 hit |
<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>Sequences (2+)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 describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded to basketThis entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All
Isoform 1 (identifier: P49747-1) [UniParc]FASTAAdd to basketAdded to basket
This isoform has been chosen as the <p><strong>What is the canonical sequence?</strong><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
« Hide
Show »10 20 30 40 50
MVPDTACVLL LTLAALGASG QGQSPLGSDL GPQMLRELQE TNAALQDVRE
60 70 80 90 100
LLRQQVREIT FLKNTVMECD ACGMQQSVRT GLPSVRPLLH CAPGFCFPGV
110 120 130 140 150
ACIQTESGAR CGPCPAGFTG NGSHCTDVNE CNAHPCFPRV RCINTSPGFR
160 170 180 190 200
CEACPPGYSG PTHQGVGLAF AKANKQVCTD INECETGQHN CVPNSVCINT
210 220 230 240 250
RGSFQCGPCQ PGFVGDQASG CQRRAQRFCP DGSPSECHEH ADCVLERDGS
260 270 280 290 300
RSCVCAVGWA GNGILCGRDT DLDGFPDEKL RCPERQCRKD NCVTVPNSGQ
310 320 330 340 350
EDVDRDGIGD ACDPDADGDG VPNEKDNCPL VRNPDQRNTD EDKWGDACDN
360 370 380 390 400
CRSQKNDDQK DTDQDGRGDA CDDDIDGDRI RNQADNCPRV PNSDQKDSDG
410 420 430 440 450
DGIGDACDNC PQKSNPDQAD VDHDFVGDAC DSDQDQDGDG HQDSRDNCPT
460 470 480 490 500
VPNSAQEDSD HDGQGDACDD DDDNDGVPDS RDNCRLVPNP GQEDADRDGV
510 520 530 540 550
GDVCQDDFDA DKVVDKIDVC PENAEVTLTD FRAFQTVVLD PEGDAQIDPN
560 570 580 590 600
WVVLNQGREI VQTMNSDPGL AVGYTAFNGV DFEGTFHVNT VTDDDYAGFI
610 620 630 640 650
FGYQDSSSFY VVMWKQMEQT YWQANPFRAV AEPGIQLKAV KSSTGPGEQL
660 670 680 690 700
RNALWHTGDT ESQVRLLWKD PRNVGWKDKK SYRWFLQHRP QVGYIRVRFY
710 720 730 740 750
EGPELVADSN VVLDTTMRGG RLGVFCFSQE NIIWANLRYR CNDTIPEDYE
THQLRQA
Length:757
Mass (Da):82,860
Last modified:October 14, 2008 - v2
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:iA0B73AADB39FBC7B
Isoform 2 (identifier: P49747-2) [UniParc]FASTAAdd to basketAdded to basket
The sequence of this isoform differs from the canonical sequence as follows:
129-181: Missing.
« Hide
Show »10 20 30 40 50
MVPDTACVLL LTLAALGASG QGQSPLGSDL GPQMLRELQE TNAALQDVRE
60 70 80 90 100
LLRQQVREIT FLKNTVMECD ACGMQQSVRT GLPSVRPLLH CAPGFCFPGV
110 120 130 140 150
ACIQTESGAR CGPCPAGFTG NGSHCTDVNE CETGQHNCVP NSVCINTRGS
160 170 180 190 200
FQCGPCQPGF VGDQASGCQR RAQRFCPDGS PSECHEHADC VLERDGSRSC
210 220 230 240 250
VCAVGWAGNG ILCGRDTDLD GFPDEKLRCP ERQCRKDNCV TVPNSGQEDV
260 270 280 290 300
DRDGIGDACD PDADGDGVPN EKDNCPLVRN PDQRNTDEDK WGDACDNCRS
310 320 330 340 350
QKNDDQKDTD QDGRGDACDD DIDGDRIRNQ ADNCPRVPNS DQKDSDGDGI
360 370 380 390 400
GDACDNCPQK SNPDQADVDH DFVGDACDSD QDQDGDGHQD SRDNCPTVPN
410 420 430 440 450
SAQEDSDHDG QGDACDDDDD NDGVPDSRDN CRLVPNPGQE DADRDGVGDV
460 470 480 490 500
CQDDFDADKV VDKIDVCPEN AEVTLTDFRA FQTVVLDPEG DAQIDPNWVV
510 520 530 540 550
LNQGREIVQT MNSDPGLAVG YTAFNGVDFE GTFHVNTVTD DDYAGFIFGY
560 570 580 590 600
QDSSSFYVVM WKQMEQTYWQ ANPFRAVAEP GIQLKAVKSS TGPGEQLRNA
610 620 630 640 650
LWHTGDTESQ VRLLWKDPRN VGWKDKKSYR WFLQHRPQVG YIRVRFYEGP
660 670 680 690 700
ELVADSNVVL DTTMRGGRLG VFCFSQENII WANLRYRCND TIPEDYETHQ
LRQA
<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi
There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket| Entry | Entry name | Protein names | Gene names | Length | Annotation | ||
|---|---|---|---|---|---|---|---|
| G3XAP6 | G3XAP6_HUMAN | Cartilage oligomeric matrix protein Cartilage oligomeric matrix protein (Cartilage oligomeric matrix protein, isoform CRA_b) | COMP hCG_37043 | 724 | Annotation score: Annotation score:2 out of 5 <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p> | ||
<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni
The sequence AAB86501 differs from that shown. Reason: Erroneous gene model prediction.Curated
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 256 | A → R in AAA57253 (PubMed:7713493).Curated | 1 | |
| Sequence conflicti | 256 | A → R in BAC53888 (Ref. 2) Curated | 1 | |
| Sequence conflicti | 340 | D → Y in AAB35270 (PubMed:7670472).Curated | 1 |
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| Natural variantiVAR_016254 | 50 | E → D2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_016255 | 51 | L → W2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_085230 | 66 | V → E in CTS2; reduced secretion in tendon cells; no effect on secretion in chondrocytes; disrupted pentamerization; induced ER stress. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_016257 | 109 | A → G2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066789 | 167 | G → E in EDM1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_016258 | 224 | R → G2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066790 | 234 | P → S in PSACH. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_026239 | 276 | P → R in EDM1. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_016261 | 285 | R → P2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066791 | 290 | D → G in PSACH. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007614 | 290 | D → N in PSACH; mild form. | 1 | |
| Natural variantiVAR_066792 | 298 | S → L in EDM1; phenotypic features overlapping with mild PSACH. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007615 | 299 | G → R in PSACH. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066793 | 311 | A → D in EDM1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066794 | 317 | D → G in EDM1; atypical form. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066795 | 326 | D → G in EDM1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066796 | 326 | D → Y in PSACH. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007616 | 328 | C → R in PSACH; mild form. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066797 | 341 – 342 | Missing in PSACH. 1 Publication Manual assertion based on experiment ini
| 2 | |
| Natural variantiVAR_007617 | 342 | D → Y in EDM1; Fairbank type. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066798 | 348 | C → F in EDM1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_017102 | 348 | C → R in PSACH. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007618 | 349 | D → V in PSACH; mild form. | 1 | |
| Natural variantiVAR_066799 | 350 – 372 | Missing in PSACH. 1 Publication Manual assertion based on experiment ini
| 23 | |
| Natural variantiVAR_007619 | 361 | D → V in EDM1; Fairbank type. | 1 | |
| Natural variantiVAR_007620 | 361 | D → Y in EDM1; binds less calcium. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007621 | 367 – 368 | Missing in EDM1. 1 Publication Manual assertion based on experiment ini
| 2 | |
| Natural variantiVAR_007622 | 371 | C → S in EDM1; Fairbank type. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066800 | 371 | C → Y in EDM1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007623 | 372 | Missing in PSACH. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066801 | 374 | D → N in EDM1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007624 | 374 | Missing in PSACH; mild form. | 1 | |
| Natural variantiVAR_066802 | 376 | D → N in EDM1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066803 | 378 | D → V in PSACH. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_046796 | 381 | R → C. Corresponds to variant dbSNP:rs3179763Ensembl. | 1 | |
| Natural variantiVAR_066804 | 385 | D → N in EDM1; atypical form. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066805 | 385 | D → Y in EDM1; atypical form. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066806 | 385 | Missing in EDM1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007625 | 387 | C → G in PSACH; mild form. | 1 | |
| Natural variantiVAR_066807 | 387 | C → R in PSACH. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007626 | 391 – 394 | PNSD → V in PSACH. 1 Publication Manual assertion based on experiment ini
| 4 | |
| Natural variantiVAR_066808 | 397 | D → H in EDM1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066809 | 402 – 404 | GIG → VC in PSACH. 1 Publication Manual assertion based on experiment ini
| 3 | |
| Natural variantiVAR_066810 | 404 | G → R in EDM1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007627 | 408 | D → Y in EDM1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066811 | 410 | C → Y in EDM1; phenotype overlapping with mild PSACH. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066812 | 415 | N → K in EDM1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_026240 | 420 | D → A in EDM1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066813 | 427 | G → E in EDM1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066814 | 430 – 432 | CDS → LWC in EDM1. 1 Publication Manual assertion based on experiment ini
| 3 | |
| Natural variantiVAR_007628 | 440 | G → E in PSACH; mild form. | 1 | |
| Natural variantiVAR_007629 | 440 | G → R in PSACH. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066815 | 446 | D → N in PSACH. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066816 | 448 | C → S in PSACH. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007630 | 453 | N → S in EDM1; Fairbank type. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066817 | 457 | Missing in EDM1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007631 | 459 | Missing in PSACH; severe form. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007632 | 468 | C → Y in PSACH; severe form. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007633 | 469 | Missing in PSACH; severe form; MUT3 mutant; most common mutation; binds less calcium and causes misfolding of the protein; greatly reduced interaction with ACAN; reduced interaction with collagen. 3 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007634 | 472 | D → Y in PSACH; severe form. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066818 | 473 | D → DD in EDM1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007635 | 473 | D → G in PSACH; severe form. Corresponds to variant dbSNP:rs28936669EnsemblClinVar. | 1 | |
| Natural variantiVAR_066819 | 473 | D → H in PSACH. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007636 | 473 | Missing in PSACH; severe form. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066820 | 475 | D → N in PSACH. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007637 | 482 | D → G in PSACH. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066821 | 501 | G → D in EDM1. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066822 | 507 | D → G in PSACH. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_066823 | 511 | D → G in PSACH. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007638 | 513 – 516 | Missing in PSACH; mild form. 1 Publication Manual assertion based on experiment ini
| 4 | |
| Natural variantiVAR_066824 | 515 | D → G in PSACH. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Natural variantiVAR_007639 | 518 | D → N in PSACH; mild form. Corresponds to variant dbSNP:rs1359984033Ensembl. | 1 | |
| Natural variantiVAR_007640 | 523 | N → K in EDM1; Ribbing type. 2 Publications Manual assertion based on experiment ini
| 1 | |
| Natural varianti |