Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
COMP (human)

Overview
COMP May play 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. Could play a role in the pathogenesis of osteoarthritis. 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). 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. Defects in COMP are the cause of multiple epiphyseal dysplasia type 1 (EDM1). EDM is a generalized skeletal dysplasia associated with significant morbidity. Joint pain, joint deformity, waddling gait, and short stature are the main clinical signs and symptoms. EDM is broadly categorized into the more severe Fairbank and the milder Ribbing types. Defects in COMP are the cause of pseudoachondroplasia (PSACH). PSAC is a dominantly inherited chondrodysplasia characterized by short stature and early-onset osteoarthrosis. PSACH is more severe than EDM1 and is recognized in early childhood. Belongs to the thrombospondin family. Note: This description may include information from UniProtKB.
Protein type: Secreted, signal peptide; Secreted
Chromosomal Location of Human Ortholog: 19p13.1
Cellular Component: extracellular matrix; extracellular space; proteinaceous extracellular matrix; extracellular region
Molecular Function: heparin binding; collagen binding; heparan sulfate proteoglycan binding; protein binding; protease binding; extracellular matrix structural constituent; calcium ion binding
Biological Process: limb development; organ morphogenesis; extracellular matrix organization and biogenesis; apoptosis; cell adhesion; skeletal development; negative regulation of apoptosis
Reference #:  P49747 (UniProtKB)
Alt. Names/Synonyms: Cartilage oligomeric matrix protein; cartilage oligomeric matrix protein (pseudoachondroplasia, epiphyseal dysplasia 1, multiple); cartilage oligomeric matrix protein(pseudoachondroplasia, epiphyseal dysplasia 1, multiple); COMP; EDM1; EPD1; MED; MGC131819; MGC149768; PSACH; pseudoachondroplasia (epiphyseal dysplasia 1, multiple); THBS5; Thrombospondin-5; TSP5
Gene Symbols: COMP
Molecular weight: 82,860 Da
Basal Isoelectric point: 4.36  Predict pI for various phosphorylation states
Select Structure to View Below

COMP

Protein Structure Not Found.


STRING  |  Wikipedia  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  DISEASE  |  Scansite  |  Pfam  |  RCSB PDB  |  Phospho3D  |  Phospho.ELM  |  NetworKIN  |  UCSD-Nature  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


Modification Sites and Domains  

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 K396 RVPNSDQKDSDGDGI
0 1 S398 PNSDQKDSDGDGIGD
  mouse

 
S394-p RVPNFDQsDsDGDGV
S396-p PNFDQsDsDGDGVGD
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.