MGP Database

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MGP000614

UniProt Annotations

Entry Information
Gene Namecollagen, type I, alpha 1
Protein EntryCO1A1_HUMAN
UniProt IDP02452
SpeciesHuman
Comments
Comment typeDescription
DiseaseCaffey disease (CAFFD) [MIM:114000]: Characterized by an infantile episode of massive subperiosteal new bone formation that typically involves the diaphyses of the long bones, mandible, and clavicles. The involved bones may also appear inflamed, with painful swelling and systemic fever often accompanying the illness. The bone changes usually begin before 5 months of age and resolve before 2 years of age. {ECO:0000269|PubMed:15864348}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DiseaseEhlers-Danlos syndrome 1 (EDS1) [MIM:130000]: A connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS1 is the severe form of classic Ehlers-Danlos syndrome. {ECO:0000269|PubMed:10739762, ECO:0000269|PubMed:17211858}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DiseaseEhlers-Danlos syndrome 7A (EDS7A) [MIM:130060]: A connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. Marked by bilateral congenital hip dislocation, hyperlaxity of the joints, and recurrent partial dislocations. Note=The disease is caused by mutations affecting the gene represented in this entry.
DiseaseNote=A chromosomal aberration involving COL1A1 is found in dermatofibrosarcoma protuberans. Translocation t(17;22)(q22;q13) with PDGF.
DiseaseOsteogenesis imperfecta 1 (OI1) [MIM:166200]: An autosomal dominant form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI1 is a non-deforming form with normal height or mild short stature, and no dentinogenesis imperfecta. {ECO:0000269|PubMed:1634225, ECO:0000269|PubMed:16638323, ECO:0000269|PubMed:16705691, ECO:0000269|PubMed:16786509, ECO:0000269|PubMed:1718984, ECO:0000269|PubMed:1737847, ECO:0000269|PubMed:17875077, ECO:0000269|PubMed:18670065, ECO:0000269|PubMed:2794057, ECO:0000269|PubMed:3244312, ECO:0000269|PubMed:8223589}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DiseaseOsteogenesis imperfecta 2 (OI2) [MIM:166210]: An autosomal dominant form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI2 is characterized by bone fragility, with many perinatal fractures, severe bowing of long bones, undermineralization, and death in the perinatal period due to respiratory insufficiency. {ECO:0000269|PubMed:10627137, ECO:0000269|PubMed:1460047, ECO:0000269|PubMed:1511982, ECO:0000269|PubMed:1613761, ECO:0000269|PubMed:16566045, ECO:0000269|PubMed:16786509, ECO:0000269|PubMed:18670065, ECO:0000269|PubMed:1874719, ECO:0000269|PubMed:18996919, ECO:0000269|PubMed:1939261, ECO:0000269|PubMed:1953667, ECO:0000269|PubMed:2035536, ECO:0000269|PubMed:2036375, ECO:0000269|PubMed:2037280, ECO:0000269|PubMed:2116413, ECO:0000269|PubMed:2211725, ECO:0000269|PubMed:2339700, ECO:0000269|PubMed:2470760, ECO:0000269|PubMed:2777764, ECO:0000269|PubMed:2794057, ECO:0000269|PubMed:2913053, ECO:0000269|PubMed:3016737, ECO:0000269|PubMed:3108247, ECO:0000269|PubMed:3403550, ECO:0000269|PubMed:3667599, ECO:0000269|PubMed:7520724, ECO:0000269|PubMed:7679635, ECO:0000269|PubMed:7691343, ECO:0000269|PubMed:7961597, ECO:0000269|PubMed:8100209, ECO:0000269|PubMed:8349697, ECO:0000269|PubMed:8349698, ECO:0000269|PubMed:8364588, ECO:0000269|PubMed:8456808, ECO:0000269|PubMed:8786074, ECO:0000269|PubMed:9143923, ECO:0000269|Ref.45, ECO:0000269|Ref.48}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DiseaseOsteogenesis imperfecta 3 (OI3) [MIM:259420]: An autosomal dominant form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI3 is characterized by progressively deforming bones, very short stature, a triangular face, severe scoliosis, grayish sclera and dentinogenesis imperfecta. {ECO:0000269|PubMed:10408781, ECO:0000269|PubMed:16879195, ECO:0000269|PubMed:1770532, ECO:0000269|PubMed:18670065, ECO:0000269|PubMed:2037280, ECO:0000269|PubMed:2511192, ECO:0000269|PubMed:2794057, ECO:0000269|PubMed:7691343, ECO:0000269|PubMed:7881420, ECO:0000269|PubMed:8019571, ECO:0000269|PubMed:8364588, ECO:0000269|PubMed:8456809, ECO:0000269|PubMed:8669434, ECO:0000269|PubMed:8723681, ECO:0000269|PubMed:9101304}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DiseaseOsteogenesis imperfecta 4 (OI4) [MIM:166220]: An autosomal dominant form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI4 is characterized by moderately short stature, mild to moderate scoliosis, grayish or white sclera and dentinogenesis imperfecta. {ECO:0000269|PubMed:16786509, ECO:0000269|PubMed:16879195, ECO:0000269|PubMed:1770532, ECO:0000269|PubMed:17875077, ECO:0000269|PubMed:1988452, ECO:0000269|PubMed:2745420, ECO:0000269|PubMed:7691343, ECO:0000269|PubMed:7982948, ECO:0000269|PubMed:8094076, ECO:0000269|PubMed:8339541, ECO:0000269|PubMed:9600458}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DiseaseOsteoporosis (OSTEOP) [MIM:166710]: A systemic skeletal disorder characterized by decreased bone mass and deterioration of bone microarchitecture without alteration in the composition of bone. The result is fragile bones and an increased risk of fractures, even after minimal trauma. Osteoporosis is a chronic condition of multifactorial etiology and is usually clinically silent until a fracture occurs. {ECO:0000269|PubMed:8841196, ECO:0000269|PubMed:9535665}. Note=Disease susceptibility is associated with variations affecting the gene represented in this entry.
DomainThe C-terminal propeptide, also known as COLFI domain, have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. It binds a calcium ion which is essential for its function (By similarity). {ECO:0000250}.
FunctionType I collagen is a member of group I collagen (fibrillar forming collagen).
InteractionO01949:AAEL010235 (xeno); NbExp=5; IntAct=EBI-982999, EBI-7685554;
PtmO-linked glycan consists of a Glc-Gal disaccharide bound to the oxygen atom of a post-translationally added hydroxyl group. {ECO:0000269|PubMed:4319110}.
PtmProline residues at the third position of the tripeptide repeating unit (G-X-P) are hydroxylated in some or all of the chains. Proline residues at the second position of the tripeptide repeating unit (G-P-X) are hydroxylated in some of the chains. {ECO:0000269|PubMed:4319110}.
Sequence CautionSequence=BAD92834.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
SimilarityBelongs to the fibrillar collagen family. {ECO:0000255|PROSITE-ProRule:PRU00793}.
SimilarityContains 1 fibrillar collagen NC1 domain. {ECO:0000255|PROSITE-ProRule:PRU00793}.
SimilarityContains 1 VWFC domain. {ECO:0000255|PROSITE- ProRule:PRU00220}.
Subcellular LocationSecreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
SubunitTrimers of one alpha 2(I) and two alpha 1(I) chains. Interacts with MRC2 (By similarity). Interacts with TRAM2. {ECO:0000250, ECO:0000269|PubMed:14749390}.
Tissue SpecificityForms the fibrils of tendon, ligaments and bones. In bones the fibrils are mineralized with calcium hydroxyapatite.
Web ResourceName=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/COL1A1ID186.html";
Web ResourceName=Osteogenesis imperfecta variant database; Note=Collagen type I alpha 1 (COL1A1); URL="http://oi.gene.le.ac.uk/home.php?select_db=COL1A1";
Web ResourceName=Wikipedia; Note=Type-I collagen entry; URL="http://en.wikipedia.org/wiki/Type-I_collagen";
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