SynDB Home Page
SynDB Home Page
Browse
Search
Download
Help
People
links

blue bulletSynDB protein details  


Parse error: syntax error, unexpected T_VARIABLE in /home/kongl/syndb/www/sdb_nats.php on line 52
0COMP_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameCOMP
DescriptionCartilage oligomeric matrix protein precursor (comp).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005578 extracellular matrix (sensu Metazoa) (TAS)
0005509 calcium ion binding (TAS)
0005201 extracellular matrix structural constituent (TAS)
0001501 skeletal development (TAS)

Warning: fopen(/home/kongl/syndb/www/temp/870880944.dot) [function.fopen]: failed to open stream: Permission denied in /home/kongl/syndb/www/sdb_pro.php on line 269

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 270

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 271

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 272

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 273

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 274

Warning: fwrite(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 299

Warning: fclose(): supplied argument is not a valid stream resource in /home/kongl/syndb/www/sdb_pro.php on line 300
schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains unassigned to SynO:
This region is found at the C terminus of thrombospondin and related proteins.
  IPR008859:Thrombospondin, C-terminal
A sequence of about forty amino-acid residues found in epidermal growth factor (EGF) has been shown .o be present in a large number of membrane-bound and extracellular.ostly animal.roteins. Many of these proteins require calcium for their biological function and a calcium-binding site has been found at the N-terminus of some EGF-like domains . Calcium-binding may be crucial for numerous protein-protein interactions.For human coagulation factor IX it has been shown that the calcium-ligands form a pentagonal bipyramid. The first.hird and fourth conserved negatively charged or polar residues are side chain ligands. The latter is possibly hydroxylated (see aspartic acid and asparagine hydroxylation site) . A conserved aromatic residue.s well as the second conserved negative residue.re thought to be involved in stabilizing the calcium-binding site.As in non-calcium binding EGF-like domains.here are six conserved cysteines and the structure of both types is very similar as calcium-binding induces only strictly local structural changes .
  IPR013091:EGF calcium-binding
A sequence of about forty amino-acid residues found in epidermal growth factor (EGF) has been shown .o be present in a large number of membrane-bound and extracellular.ostly animal.roteins. Many of these proteins require calcium for their biological function and a calcium-binding site has been found at the N-terminus of some EGF-like domains . Calcium-binding may be crucial for numerous protein-protein interactions.For human coagulation factor IX it has been shown that the calcium-ligands form a pentagonal bipyramid. The first.hird and fourth conserved negatively charged or polar residues are side chain ligands. The latter is possibly hydroxylated (see aspartic acid and asparagine hydroxylation site) . A conserved aromatic residue.s well as the second conserved negative residue.re thought to be involved in stabilizing the calcium-binding site.As in non-calcium binding EGF-like domains.here are six conserved cysteines and the structure of both types is very similar as calcium-binding induces only strictly local structural changes .
  IPR001881:EGF-like calcium-binding
A sequence of about thirty to forty amino-acid residues long found in the sequence of epidermal growth factor (EGF)has been shown to be present.n a moreor less conserved form.n a large number of other.ostly animal proteins. The list of proteins currently known tocontain one or more copies of an EGF-like pattern is large and varied. The functional significance of EGF domains inwhat appear to be unrelated proteins is not yet clear. However. common feature is that these repeats are found inthe extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandinG/H synthase). The EGF domain includes six cysteine residues which have been shown (in EGF) to be involved in disulphidebonds. The main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet.Subdomains between the conserved cysteines vary in length.
  IPR006209:EGF-like
Epidermal growth factors and transforming growth factors belong to a general class of proteins that share a repeat pattern involving a number of conserved Cys residues. Growth factors are involved in cell recognition and division . The repeating pattern.specially of cysteines (the so-called EGF repeat).s thought to be important to the 3D structure of the proteins.nd hence its recognition by receptors and other molecules. The type 1 EGF signature includes six conserved cysteines believed to be involved in disulphide bond formation. The EGF motif is found frequently in nature.articularly in extracellular proteins.
  IPR006210:EGF
The growth factor receptor domain is a cysteine-rich region that is found in a variety of eukaryotic proteins that are involved in the mechanism of signal transduction by receptor tyrosine kinases. Proteins containing the growth factor receptor domain include the insulin-like growth factor-binding proteins (IGFBP) .he type-1 insulin-like growth-factor receptor (IGF-1R) .nd the receptor protein-tyrosine kinase Erbb-3 (ErbB3) . The general structure of the growth factor receptor domain is a disulphide-bound fold containing a beta-hairpin with two adjacent disulphides. IGFBPs control the distribution.unction and activity of insulin-like growth factors (IGFs) IGF-I and IGF-II.hich are key regulators of cell proliferation.ifferentiation and transformation. All IGFBPs share a common domain organization.here the highest conservation is found in the N-terminal Cys-rich IGF-binding domain. The N-terminal domain contains 10-12 conserved cysteine residues. IGF-1R is a member of the tyrosine-kinase receptor superfamily that is involved in both normal growth and development and malignant transformation. The Cys-rich domain is flanked by two L-domains.nd together they contribute to hormone binding and ligand specificity.ven though they do not bind ligand directly. The Cys-rich region is composed of eight disulphide-bonded modules.even of which form a rod-shaped domain. ErbB3 is a member of the epidermal growth factor receptor (EGFR) family of receptor tyrosine kinases. The extracellular region of ErbB3 is made up of two Cys-rich domains and two L-domains.rranged alternately. The two L-domains and the first Cys-rich domain are structurally homologous to those found in IGF-1R. The two Cys-rich domains are extended repeats of seven small disulphide-containing modules. A beta-hairpin loop extends from the first Cys-rich domain to contact the C-terminal portion of the second Cys-rich domain.reating a large pore structure. The SSF signature in this entry is currently under review. Please be aware that some of the protein hits may be false positives.
  IPR009030:Growth factor, receptor
Thrombospondin is an adhesive glycoprotein that mediates cell-to-cell and cell-to-matrix interactions. It can bind to fibrinogen.ibronectin.aminin and type V collagen. This repeat is found in the thrombospondin family of proteins and probably binds to calcium . Cartilage oligomeric matrix protein is also part of this family.
  IPR003367:Thrombospondin type 3 repeat
IPR008859:TSP_C 
Evalue:-168.769546508789 
Location:546-746IPR013091:EGF_CA 
Evalue:-10.1549015045166 
Location:180-221IPR001881:EGF_CA 
Evalue:-6.76955107862173 
Location:127-179IPR003367:TSP_3 
Evalue:-2.04095864295959 
Location:396-408IPR006209:EGF 
Evalue:-2.01772880554199 
Location:229-266IPR003367:TSP_3 
Evalue:-1.88605666160583 
Location:301-313IPR003367:TSP_3 
Evalue:-1.58502662181854 
Location:493-505IPR003367:TSP_3 
Evalue:-1.53760194778442 
Location:457-469IPR003367:TSP_3 
Evalue:-1.37675070762634 
Location:360-372IPR003367:TSP_3 
Evalue:-1.24412512779236 
Location:419-431IPR003367:TSP_3 
Evalue:-0.958607316017151 
Location:337-349IPR003367:TSP_3 
Evalue:-0.76955109834671 
Location:434-449IPR003367:TSP_3 
Evalue:-0.537602007389069 
Location:314-329IPR006210:EGF 
Evalue:-0.537602002101044 
Location:90-126IPR003367:TSP_3 
Evalue:-0.283996641635895 
Location:373-388IPR003367:TSP_3 
Evalue:0 
Location:470-485IPR009030:Grow_fac_recept 
Evalue:0 
Location:7-21IPR002048:EF_HAND_1 
Evalue:0 
Location:507-519IPR013032:EGF_1 
Evalue:0 
Location:0-0IPR003367:TSP_3 
Evalue:0.698970019817352 
Location:268-283
SequencesProtein: COMP_HUMAN (757 aa)
mRNA: NM_000095
Local Annotation
Synapse Ontology
Calcium release from RyR (Ryanodine Receptor) in the SR (Sarcoplasmic Reticulum) is activated by the calcium induced-calcium-release
sdb:0325 RyR-CICR  (Evidence:keywords)
KO assignmentK04659
  Level 3 annotation:
    thrombospondin
  Level 2 annotation:
    TGF-beta signaling pathway
    ECM-receptor interaction
    CAM ligands
    Focal adhesion
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 64 residues, 18754582-18754771Exon2: 48 residues, 18754863-18755003Exon3: 59 residues, 18756000-18756173Exon4: 67 residues, 18756705-18756902Exon5: 18 residues, 18757307-18757356Exon6: 61 residues, 18757482-18757661Exon7: 62 residues, 18757774-18757956Exon8: 19 residues, 18758048-18758101Exon9: 41 residues, 18758341-18758460Exon10: 55 residues, 18759299-18759459Exon11: 38 residues, 18760020-18760128Exon12: 37 residues, 18760218-18760323Exon13: 55 residues, 18760400-18760559Exon14: 27 residues, 18760647-18760722Exon15: 48 residues, 18760968-18761106Exon16: 59 residues, 18761750-18761923Exon17: 19 residues, 18762370-18762422Exon18: 30 residues, 18762658-18762744Exon19: 40 residues, 18762999-18763114Exon20: 2 residues, -Jump to COMP_HUMAN  
Tune and view alternative isoforms
Loci Cluster (Details)Loci: 4381 18754582-18763114 ~-9K 18371(COMP)(-)Loci: 3100 18803787-18840038 ~-36K 18373(RENT1)(+)Loci: 4382 18871323-18891199 ~-20K 18381(COPE)(-)Loci: 4383 18901011-18912983 ~-12K 18385(HOMER3)(-)Loci: 3101 19035807-19084697 ~-49K 18393(+)Loci: 3099 18655487-18749762 ~-94K 18368(MECT1)(+)Link out to UCSC