| Predicate | Object |
|---|---|
| rdf:type | |
| biopax3:comment |
FUNCTION: Type I collagen is a member of group I collagen (fibrillar forming collagen). SUBUNIT: Trimers of one alpha 2(I) and two alpha 1(I) chains. SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix (By similarity). TISSUE SPECIFICITY: Forms the fibrils of tendon, ligaments and bones. In bones the fibrils are mineralized with calcium hydroxyapatite. PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. DISEASE: Defects in COL1A2 are the cause of Ehlers-Danlos syndrome type 7B (EDS7B) [MIM:130060]. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS7B is marked by bilateral congenital hip dislocation, hyperlaxity of the joints, and recurrent partial dislocations. DISEASE: Defects in COL1A2 are a cause of osteogenesis imperfecta type 1 (OI1) [MIM:166200]. A dominantly inherited connective tissue disorder characterized by bone fragility and blue sclerae. Osteogenesis imperfecta type 1 is non-deforming with normal height or mild short stature, and no dentinogenesis imperfecta. DISEASE: Defects in COL1A2 are a cause of osteogenesis imperfecta type 2 (OI2) [MIM:166210]; also known as osteogenesis imperfecta congenita (OIC) or lethal perinatal. A connective tissue disorder characterized by bone fragility, with many perinatal fractures, severe bowing of long bones, undermineralization, and death in the perinatal period due to respiratory insufficiency. DISEASE: Defects in COL1A2 are the cause of Ehlers-Danlos syndrome autosomal recessive cardiac valvular form (EDSCV) [MIM:225320]. A connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. In addition to joint laxity, skin hyperextensibility and friability, and abnormal scar formation, patients have mitral valve prolapse and insufficiency, mitral regurgitation, and aortic insufficiency. DISEASE: Defects in COL1A2 are a cause of osteogenesis imperfecta type 3 (OI3) [MIM:259420]. A connective tissue disorder characterized by progressively deforming bones, very short stature, a triangular face, severe scoliosis, grayish sclera, and dentinogenesis imperfecta. DISEASE: Defects in COL1A2 are a cause of osteogenesis imperfecta type 4 (OI4) [MIM:166220]; also known as osteogenesis imperfecta with normal sclerae. A connective tissue disorder characterized by moderately short stature, mild to moderate scoliosis, grayish or white sclera and dentinogenesis imperfecta. DISEASE: Note=A chromosomal aberration involving COL1A2 may be a cause of lipoblastomas, which are benign tumors resulting from transformation of adipocytes, usually diagnosed in children. Translocation t(7;8)(p22;q13) with PLAG1. SIMILARITY: Belongs to the fibrillar collagen family. SIMILARITY: Contains 1 fibrillar collagen NC1 domain. WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/COL1A2ID411ch7q22.html"; WEB RESOURCE: Name=Osteogenesis imperfecta variant database; Note=Collagen type I alpha 2 (COL1A2); URL="http://oi.gene.le.ac.uk/home.php?select_db=COL1A2"; WEB RESOURCE: Name=GeneReviews; URL="http://www.ncbi.nlm.nih.gov/sites/GeneTests/lab/gene/COL1A2"; GENE SYNONYMS:COL1A2. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.,
SEQUENCE 1366 AA; 129314 MW; 1E68A5970FB4210A CRC64;
|
| biopax3:xref |
urn:biopax:RelationshipXref:HGNC_HGNC:2198,
urn:biopax:RelationshipXref:NCBI GENE_1278,
urn:biopax:RelationshipXref:REFSEQ_NP_000080,
urn:biopax:UnificationXref:UNIPROT_P02464,
urn:biopax:UnificationXref:UNIPROT_P08123,
urn:biopax:UnificationXref:UNIPROT_Q13897,
urn:biopax:UnificationXref:UNIPROT_Q13997,
urn:biopax:UnificationXref:UNIPROT_Q13998,
urn:biopax:UnificationXref:UNIPROT_Q14038,
urn:biopax:UnificationXref:UNIPROT_Q14057,
urn:biopax:UnificationXref:UNIPROT_Q15177,
urn:biopax:UnificationXref:UNIPROT_Q15947,
urn:biopax:UnificationXref:UNIPROT_Q16480,
urn:biopax:UnificationXref:UNIPROT_Q16511,
urn:biopax:UnificationXref:UNIPROT_Q7Z5S6,
urn:biopax:UnificationXref:UNIPROT_Q9UEB6,
urn:biopax:UnificationXref:UNIPROT_Q9UEF9,
urn:biopax:UnificationXref:UNIPROT_Q9UM83,
urn:biopax:UnificationXref:UNIPROT_Q9UMI1,
urn:biopax:UnificationXref:UNIPROT_Q9UML5,
urn:biopax:UnificationXref:UNIPROT_Q9UMM6,
urn:biopax:UnificationXref:UNIPROT_Q9UPH0
|
| biopax3:displayName |
CO1A2_HUMAN
|
| biopax3:name |
Alpha-2 type I collagen,
COL1A2
|
| biopax3:entityFeature | |
| biopax3:organism | |
| biopax3:sequence |
MLSFVDTRTLLLLAVTLCLATCQSLQEETVRKGPAGDRGPRGERGPPGPPGRDGEDGPTGPPGPPGPPGPPGLGGNFAAQYDGKGVGLGPGPMGLMGPRGPPGAAGAPGPQGFQGPAGEPGEPGQTGPAGARGPAGPPGKAGEDGHPGKPGRPGERGVVGPQGARGFPGTPGLPGFKGIRGHNGLDGLKGQPGAPGVKGEPGAPGENGTPGQTGARGLPGERGRVGAPGPAGARGSDGSVGPVGPAGPIGSAGPPGFPGAPGPKGEIGAVGNAGPAGPAGPRGEVGLPGLSGPVGPPGNPGANGLTGAKGAAGLPGVAGAPGLPGPRGIPGPVGAAGATGARGLVGEPGPAGSKGESGNKGEPGSAGPQGPPGPSGEEGKRGPNGEAGSAGPPGPPGLRGSPGSRGLPGADGRAGVMGPPGSRGASGPAGVRGPNGDAGRPGEPGLMGPRGLPGSPGNIGPAGKEGPVGLPGIDGRPGPIGPAGARGEPGNIGFPGPKGPTGDPGKNGDKGHAGLAGARGAPGPDGNNGAQGPPGPQGVQGGKGEQGPPGPPGFQGLPGPSGPAGEVGKPGERGLHGEFGLPGPAGPRGERGPPGESGAAGPTGPIGSRGPSGPPGPDGNKGEPGVVGAVGTAGPSGPSGLPGERGAAGIPGGKGEKGEPGLRGEIGNPGRDGARGAPGAVGAPGPAGATGDRGEAGAAGPAGPAGPRGSPGERGEVGPAGPNGFAGPAGAAGQPGAKGERGAKGPKGENGVVGPTGPVGAAGPAGPNGPPGPAGSRGDGGPPGMTGFPGAAGRTGPPGPSGISGPPGPPGPAGKEGLRGPRGDQGPVGRTGEVGAVGPPGFAGEKGPSGEAGTAGPPGTPGPQGLLGAPGILGLPGSRGERGLPGVAGAVGEPGPLGIAGPPGARGPPGAVGSPGVNGAPGEAGRDGNPGNDGPPGRDGQPGHKGERGYPGNIGPVGAAGAPGPHGPVGPAGKHGNRGETGPSGPVGPAGAVGPRGPSGPQGIRGDKGEPGEKGPRGLPGLKGHNGLQGLPGIAGHHGDQGAPGSVGPAGPRGPAGPSGPAGKDGRTGHPGTVGPAGIRGPQGHQGPAGPPGPPGPPGPPGVSGGGYDFGYDGDFYRADQPRSAPSLRPKDYEVDATLKSLNNQIETLLTPEGSRKNPARTCRDLRLSHPEWSSGYYWIDPNQGCTMDAIKVYCDFSTGETCIRAQPENIPAKNWYRSSKDKKHVWLGETINAGSQFEYNVEGVTSKEMATQLAFMRLLANYASQNITYHCKNSIAYMDEETGNLKKAVILQGSNDVELVAEGNSRFTYTVLVDGCSKKTNEWGKTIIEYKTNKPSRLPFLDIAPLDIGGADQEFFVDIGPVCFK
|
| biopax3:standardName |
Collagen alpha-2(I) chain
|