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P02452 (CO1A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 185. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Collagen alpha-1(I) chain
Alternative name(s):
Alpha-1 type I collagen
Gene names
Name:COL1A1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1464 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Type I collagen is a member of group I collagen (fibrillar forming collagen).

Subunit structure

Trimers of one alpha 2(I) and two alpha 1(I) chains. Interacts with MRC2 By similarity. Interacts with TRAM2. Ref.33

Subcellular location

Secretedextracellular spaceextracellular matrix By similarity.

Tissue specificity

Forms the fibrils of tendon, ligaments and bones. In bones the fibrils are mineralized with calcium hydroxyapatite.

Domain

The 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.

Post-translational modification

Proline 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.

O-linked glycan consists of a Glc-Gal disaccharide bound to the oxygen atom of a post-translationally added hydroxyl group.

Involvement in disease

Caffey 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.89 Ref.90 Ref.91

Ehlers-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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.88 Ref.89 Ref.90 Ref.97

Ehlers-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. Ref.89 Ref.90

Osteogenesis 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.38 Ref.44 Ref.55 Ref.59 Ref.62 Ref.68 Ref.89 Ref.90 Ref.93 Ref.94 Ref.96 Ref.99 Ref.101

Osteogenesis 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.22 Ref.25 Ref.34 Ref.35 Ref.36 Ref.37 Ref.39 Ref.41 Ref.43 Ref.44 Ref.45 Ref.46 Ref.47 Ref.48 Ref.49 Ref.50 Ref.51 Ref.52 Ref.54 Ref.56 Ref.60 Ref.61 Ref.63 Ref.64 Ref.67 Ref.69 Ref.70 Ref.71 Ref.73 Ref.74 Ref.76 Ref.79 Ref.83 Ref.85 Ref.89 Ref.90 Ref.94 Ref.95 Ref.101 Ref.102

Osteogenesis 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.23 Ref.42 Ref.44 Ref.52 Ref.57 Ref.65 Ref.70 Ref.71 Ref.75 Ref.78 Ref.80 Ref.82 Ref.87 Ref.89 Ref.90 Ref.92 Ref.101

Osteogenesis 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.40 Ref.53 Ref.57 Ref.66 Ref.70 Ref.72 Ref.77 Ref.84 Ref.89 Ref.90 Ref.92 Ref.94 Ref.99

Osteoporosis (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.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.81 Ref.86 Ref.89 Ref.90

A chromosomal aberration involving COL1A1 is found in dermatofibrosarcoma protuberans. Translocation t(17;22)(q22;q13) with PDGF. Ref.89 Ref.90

Sequence similarities

Belongs to the fibrillar collagen family.

Contains 1 fibrillar collagen NC1 domain.

Contains 1 VWFC domain.

Sequence caution

The sequence BAD92834.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityChromosomal rearrangement
Polymorphism
   DiseaseDisease mutation
Dwarfism
Ehlers-Danlos syndrome
Osteogenesis imperfecta
   DomainCollagen
Repeat
Signal
   LigandCalcium
Metal-binding
   PTMDisulfide bond
Glycoprotein
Hydroxylation
Pyrrolidone carboxylic acid
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Traceable author statement. Source: Reactome

blood vessel development

Inferred from mutant phenotype Ref.97. Source: UniProtKB

bone trabecula formation

Inferred from electronic annotation. Source: Ensembl

cartilage development involved in endochondral bone morphogenesis

Inferred from electronic annotation. Source: Ensembl

cellular response to amino acid stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to retinoic acid

Inferred from electronic annotation. Source: Ensembl

cellular response to transforming growth factor beta stimulus

Inferred from electronic annotation. Source: Ensembl

collagen biosynthetic process

Inferred from mutant phenotype PubMed 15095409. Source: UniProtKB

collagen catabolic process

Traceable author statement. Source: Reactome

collagen fibril organization

Inferred from mutant phenotype PubMed 14976317PubMed 15095409Ref.97PubMed 18375391. Source: UniProtKB

embryonic skeletal system development

Inferred from mutant phenotype PubMed 18553566. Source: UniProtKB

endochondral ossification

Inferred from electronic annotation. Source: Ensembl

extracellular matrix disassembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

face morphogenesis

Inferred from electronic annotation. Source: Ensembl

intramembranous ossification

Inferred from electronic annotation. Source: Ensembl

leukocyte migration

Traceable author statement. Source: Reactome

negative regulation of cell-substrate adhesion

Inferred from electronic annotation. Source: Ensembl

osteoblast differentiation

Inferred from electronic annotation. Source: Ensembl

platelet activation

Traceable author statement. Source: Reactome

positive regulation of canonical Wnt signaling pathway

Inferred from direct assay PubMed 20018240. Source: UniProtKB

positive regulation of cell migration

Inferred from direct assay PubMed 20018240. Source: UniProtKB

positive regulation of epithelial to mesenchymal transition

Inferred from direct assay PubMed 20018240. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 20018240. Source: UniProtKB

protein heterotrimerization

Inferred from electronic annotation. Source: Ensembl

protein localization to nucleus

Inferred from direct assay PubMed 20018240. Source: UniProtKB

protein transport

Inferred from electronic annotation. Source: Ensembl

response to cAMP

Inferred from electronic annotation. Source: Ensembl

response to corticosteroid

Inferred from electronic annotation. Source: Ensembl

response to estradiol

Inferred from electronic annotation. Source: Ensembl

response to hydrogen peroxide

Inferred from electronic annotation. Source: Ensembl

response to nutrient

Inferred from electronic annotation. Source: Ensembl

response to peptide hormone

Inferred from electronic annotation. Source: Ensembl

sensory perception of sound

Inferred from mutant phenotype PubMed 17489845. Source: UniProtKB

skeletal system development

Inferred from mutant phenotype PubMed 14976317Ref.54. Source: UniProtKB

skin morphogenesis

Inferred from mutant phenotype Ref.97. Source: UniProtKB

tooth mineralization

Inferred from mutant phenotype PubMed 17118335. Source: UniProtKB

visual perception

Inferred from mutant phenotype PubMed 17557158. Source: UniProtKB

   Cellular_componentcollagen type I

Inferred from mutant phenotype PubMed 14976317PubMed 17576241. Source: UniProtKB

endoplasmic reticulum lumen

Traceable author statement. Source: Reactome

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 20551380. Source: BHF-UCL

   Molecular_functionextracellular matrix structural constituent

Inferred from electronic annotation. Source: Ensembl

identical protein binding

Inferred from direct assay Ref.97. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

platelet-derived growth factor binding

Inferred from direct assay PubMed 8900172. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

AAEL010235O019495EBI-982999,EBI-7685554From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222
Propeptide23 – 161139N-terminal propeptide
PRO_0000005719
Chain162 – 12181057Collagen alpha-1(I) chain
PRO_0000005720
Propeptide1219 – 1464246C-terminal propeptide
PRO_0000005721

Regions

Domain38 – 9659VWFC
Domain1229 – 1464236Fibrillar collagen NC1
Region162 – 17817Nonhelical region (N-terminal)
Region179 – 11921014Triple-helical region
Region1193 – 121826Nonhelical region (C-terminal)
Motif745 – 7473Cell attachment site Potential
Motif1093 – 10953Cell attachment site Potential

Sites

Metal binding12771Calcium By similarity
Metal binding12791Calcium By similarity
Metal binding12801Calcium; via carbonyl oxygen By similarity
Metal binding12821Calcium; via carbonyl oxygen By similarity
Metal binding12851Calcium By similarity
Site161 – 1622Cleavage; by procollagen N-endopeptidase
Site953 – 9542Cleavage; by collagenase By similarity
Site1218 – 12192Cleavage; by procollagen C-endopeptidase

Amino acid modifications

Modified residue1621Pyrrolidone carboxylic acid
Modified residue1701Allysine
Modified residue26515-hydroxylysine
Modified residue110815-hydroxylysine By similarity
Modified residue116413-hydroxyproline By similarity
Modified residue12081Allysine By similarity
Glycosylation2651O-linked (Gal...)
Glycosylation11081O-linked (Gal...) By similarity
Glycosylation13651N-linked (GlcNAc...)
Disulfide bond1259 ↔ 1291 By similarity
Disulfide bond1265Interchain By similarity
Disulfide bond1282Interchain By similarity
Disulfide bond1299 ↔ 1462 By similarity
Disulfide bond1370 ↔ 1415 By similarity

Natural variations

Natural variant221G → R in OI2. Ref.94
VAR_063290
Natural variant1461P → T in a patient with osteogenesis imperfecta type 2; rare variant of unknown pathological significance. Ref.102
VAR_063291
Natural variant1941G → R in OI1. Ref.93
VAR_063292
Natural variant1971G → C.
Corresponds to variant rs8179178 [ dbSNP | Ensembl ].
VAR_001642
Natural variant1971G → R in OI4. Ref.94
VAR_063293
Natural variant2001G → V in OI1; patient diagnosed with OI1/OI4. Ref.101
VAR_063294
Natural variant2031G → V in OI3. Ref.92
VAR_063295
Natural variant2051P → A. Ref.94
Corresponds to variant rs72667032 [ dbSNP | Ensembl ].
VAR_001643
Natural variant2211G → C in OI1; mild form. Ref.62
VAR_001644
Natural variant2241G → C in OI1; mild phenotype.
VAR_001645
Natural variant2421G → D in OI. Ref.93
VAR_063296
Natural variant2571G → R in OI4. Ref.92 Ref.93
VAR_063297
Natural variant2631G → R in OI1; mild form. Ref.55
VAR_001646
Natural variant2631G → V in OI1; mild form. Ref.68
VAR_001647
Natural variant2661G → E in OI1. Ref.99
VAR_063298
Natural variant2721G → C in OI1. Ref.44
VAR_001648
Natural variant2751G → D in OI2.
VAR_001649
Natural variant2871G → S in OI1. Ref.99
VAR_063299
Natural variant2881E → K in a patient with osteogenesis imperfecta type 1 carrying also mutation Glu-1219; unknown pathological significance. Ref.94
VAR_063300
Natural variant2881E → V in a patient with osteogenesis imperfecta type 2; rare variant of unknown pathological significance. Ref.102
VAR_063301
Natural variant3121R → C in EDS1. Ref.88 Ref.97
VAR_013579
Natural variant3201G → V in OI1. Ref.94
VAR_063302
Natural variant3321G → R in OI3; mild to moderate form. Ref.52 Ref.78
VAR_001650
Natural variant3381G → C in OI4. Ref.94
VAR_063303
Natural variant3491V → F in OI1. Ref.101
VAR_063304
Natural variant3501G → R in OI3. Ref.75
VAR_001651
Natural variant3531G → C in OI4. Ref.66
VAR_001652
Natural variant3531G → D in OI2. Ref.102
VAR_063305
Natural variant3531G → S in OI4. Ref.99
VAR_063306
Natural variant3561G → C in OI4; mild form. Ref.53
VAR_001653
Natural variant3681G → V in OI2. Ref.102
VAR_063307
Natural variant3831G → C in OI4.
VAR_001654
Natural variant3891G → C in OI; moderate form.
VAR_001655
Natural variant3891G → R in OI2. Ref.74
VAR_001656
Natural variant3901A → T in a patient with osteogenesis imperfecta type 2; rare variant of unknown pathological significance. Ref.102
Corresponds to variant rs116794104 [ dbSNP | Ensembl ].
VAR_063308
Natural variant3981G → A in OI4. Ref.84
VAR_001657
Natural variant3981G → D in OI2.
VAR_001658
Natural variant4011G → C in OI4.
VAR_001659
Natural variant4041G → C in OI; moderate form.
VAR_001660
Natural variant4221G → C in OI2. Ref.45
VAR_001661
Natural variant4251G → S in OI2; lethal form. Ref.70 Ref.102
VAR_001662
Natural variant4341G → V in OI2. Ref.39 Ref.63
VAR_001663
Natural variant4551G → D in OI2. Ref.102
VAR_063309
Natural variant4701G → V in OI2. Ref.102
VAR_063310
Natural variant4761G → R in OI2.
Corresponds to variant rs57377812 [ dbSNP | Ensembl ].
VAR_001664
Natural variant5091G → V in OI2. Ref.102
VAR_063311
Natural variant5271G → C in OI4. Ref.84
VAR_001665
Natural variant5301G → S in OI2, OI3 and OI4; mild to lethal form. Ref.65 Ref.70 Ref.72
VAR_001666
Natural variant5331G → D in OI2.
VAR_001667
Natural variant5481G → A in OI2. Ref.102
VAR_063312
Natural variant5551P → R in OI1. Ref.94
VAR_063313
Natural variant5601G → C in OI4.
VAR_001669
Natural variant5601G → R in OI2.
VAR_001670
Natural variant5601G → S in OI4. Ref.70
VAR_001668
Natural variant5641R → H.
Corresponds to variant rs1800211 [ dbSNP | Ensembl ].
VAR_001671
Natural variant5691G → R in OI2. Ref.35
VAR_001672
Natural variant5741R → C in a patient with isolated osteopenia and vascular rupture. Ref.97
VAR_063314
Natural variant5811G → R in OI2. Ref.94
VAR_063315
Natural variant5931G → C in OI3 and OI4. Ref.57
VAR_001673
Natural variant5931G → S in OI2 and OI3; moderate to lethal form. Ref.71
VAR_001674
Natural variant6021G → R in OI2. Ref.102
VAR_063316
Natural variant6051G → D in OI2. Ref.102
VAR_063317
Natural variant6141G → R in OI2. Ref.102
VAR_063318
Natural variant6471G → S in OI1. Ref.94
VAR_063319
Natural variant6561G → S in OI2. Ref.85
VAR_001676
Natural variant6831G → S in OI4. Ref.92
VAR_063320
Natural variant7011G → C in OI4. Ref.84
VAR_001677
Natural variant7041G → C in OI3. Ref.44
VAR_001678
Natural variant7191G → D in OI2. Ref.49
VAR_001679
Natural variant7191G → S in OI3. Ref.70
VAR_001680
Natural variant7221G → S in OI1. Ref.93
VAR_063321
Natural variant7281G → R in OI2. Ref.22
VAR_001681
Natural variant7341G → V in OI2. Ref.94
VAR_063322
Natural variant7371G → D in OI2.
VAR_001682
Natural variant7401G → R in OI2. Ref.102
VAR_063323
Natural variant7431G → S in OI2.
VAR_001683
Natural variant7431G → V in OI2. Ref.69
VAR_001684
Natural variant7641G → V in OI2. Ref.83
VAR_001685
Natural variant7671G → S in OI3; severe. Ref.23 Ref.93
VAR_001686
Natural variant7761G → S in OI2. Ref.46
VAR_001687
Natural variant8091G → S in OI2. Ref.46 Ref.102
VAR_001688
Natural variant8151G → V in OI2. Ref.54
VAR_001689
Natural variant8211G → S in OI3. Ref.82 Ref.92 Ref.93
VAR_001690
Natural variant8231P → A. Ref.70
Corresponds to variant rs1800214 [ dbSNP | Ensembl ].
VAR_001691
Natural variant8241G → R in OI2. Ref.102
VAR_063324
Natural variant8331G → D in OI2. Ref.95
VAR_063325
Natural variant8391G → S in OI2; mild to moderate form. Ref.79
VAR_001692
Natural variant8421G → R in OI2. Ref.37
VAR_001693
Natural variant8451G → R in OI2. Ref.102
VAR_001694
Natural variant8481G → R in OI2. Ref.102
VAR_063342
Natural variant8511G → D in OI2.
VAR_001695
Natural variant8551N → H in a patient with osteogenesis imperfecta type 2; rare variant of unknown pathological significance. Ref.102
VAR_063326
Natural variant8661G → S in OI3 and OI2. Ref.87 Ref.101 Ref.102
VAR_008118
Natural variant8691G → C in OI2. Ref.50
VAR_001696
Natural variant8751G → S in OI2. Ref.102
VAR_063327
Natural variant8841G → S in OI2 and OI3; extremely severe form. Ref.102
VAR_001697
Natural variant8961G → C in OI2. Ref.44
VAR_001698
Natural variant8961G → D in OI2. Ref.102
VAR_063328
Natural variant9061G → S in a patient with mild osteogenesis imperfecta; uncertain pathological significance. Ref.94
VAR_063329
Natural variant9261G → C in OI2. Ref.36 Ref.51
VAR_001699
Natural variant9471G → C in OI2. Ref.102
VAR_063330
Natural variant9771G → D in OI2. Ref.102
VAR_063331
Natural variant9801G → V in OI2. Ref.60
VAR_001700
Natural variant10011G → C in OI2. Ref.102
VAR_063332
Natural variant10101G → S in OI4. Ref.40
VAR_001701
Natural variant10141R → C in CAFFD. Ref.91
VAR_033097
Natural variant10191G → A. Ref.1 Ref.18
Corresponds to variant rs1135348 [ dbSNP | Ensembl ].
VAR_030013
Natural variant10221G → S in OI3; severe form. Ref.42
VAR_001702
Natural variant10221G → V in OI2. Ref.102
VAR_001703
Natural variant10251G → R in OI2. Ref.47
VAR_001704
Natural variant10401G → S in OI2 and OI3; moderate to lethal form. Ref.82 Ref.101
VAR_001705
Natural variant10431G → S in OI2.
VAR_001706
Natural variant1046 – 10483Missing in OI2.
VAR_001707
Natural variant10491G → S in OI3. Ref.82
VAR_001708
Natural variant10521G → GAPG in OI2.
VAR_063333
Natural variant10551G → D in OI2. Ref.102
VAR_063334
Natural variant10581G → S in OI3 and OI4; mild form. Ref.82 Ref.93
VAR_001709
Natural variant10611G → D in OI2.
VAR_001710
Natural variant10611G → S in OI4. Ref.77
VAR_001711
Natural variant10661R → C in a patient with overlapping features of osteogenesis imperfecta and Ehlers-Danlos syndrome; pathogenic mutation; affects dimer formation, helix stability and organization of collagen fibrils. Ref.98
VAR_063335
Natural variant10751T → A. Ref.1 Ref.2 Ref.5 Ref.18 Ref.24 Ref.29 Ref.45 Ref.58 Ref.100 Ref.102
Corresponds to variant rs1800215 [ dbSNP | Ensembl ].
VAR_001712
Natural variant10761G → S in OI3; severe form. Ref.82
VAR_001713
Natural variant10791G → S in OI1 and OI2; mild to moderate form. Ref.59
VAR_001714
Natural variant10821G → C in OI2. Ref.43
VAR_001715
Natural variant10881G → A in OI2. Ref.67
VAR_001716
Natural variant10911G → S in OI2. Ref.48
VAR_001717
Natural variant10931R → C in a patient with isolated osteopenia and vascular rupture. Ref.97
VAR_063336
Natural variant10941G → S in OI2. Ref.102
VAR_063337
Natural variant11001G → D in OI2. Ref.102
VAR_001718
Natural variant11061G → A in OI2. Ref.41
VAR_001719
Natural variant11241G → C in OI2. Ref.76
VAR_001720
Natural variant11411R → Q. Ref.100
Corresponds to variant rs41316713 [ dbSNP | Ensembl ].
VAR_033778
Natural variant11421G → S in OI2.
VAR_001721
Natural variant11511G → S in OI3.
VAR_001722
Natural variant11511G → V in OI2. Ref.41 Ref.63
VAR_001723
Natural variant11541G → R in OI2. Ref.41
VAR_001724
Natural variant11571G → D in OI1. Ref.96
VAR_063338
Natural variant11661G → C in OI2. Ref.34
VAR_001725
Natural variant11721G → D in OI2. Ref.85
VAR_001726
Natural variant11771V → I. Ref.100
Corresponds to variant rs41316719 [ dbSNP | Ensembl ].
VAR_033779
Natural variant11811G → S in OI2. Ref.48 Ref.52
VAR_001727
Natural variant11841G → V in OI2. Ref.41 Ref.63
VAR_001728
Natural variant11871G → S in OI2 and OI3; extremely severe form. Ref.48
VAR_001729
Natural variant11871G → V in OI2. Ref.48
VAR_001730
Natural variant11951G → C in OI1; mild form. Ref.26 Ref.38
VAR_001731
Natural variant12191D → E in OI1. Ref.94
VAR_063339
Natural variant12191D → N in a patient with mild osteogenesis imperfecta associated with increased bone mineral density; results in defective type I procollagen processing; incorporation of the immature procollagen into the matrix leads to increased bone matrix mineralization and altered collagen fibril structure. Ref.103
VAR_066385
Natural variant12511S → T. Ref.25
Corresponds to variant rs3205325 [ dbSNP | Ensembl ].
VAR_030014
Natural variant12771D → H in OI2; impaired pro-alpha chain association. Ref.25
VAR_001732
Natural variant13121W → C in OI2. Ref.64
VAR_001733
Natural variant1337 – 13382Missing in OI2; impaired pro-alpha chain association.
VAR_001734
Natural variant13561R → H. Ref.94
VAR_063340
Natural variant13881L → R in OI2; impaired pro-alpha chain association. Ref.25
VAR_001735
Natural variant13911Q → K. Ref.1 Ref.2 Ref.27
Corresponds to variant rs2586486 [ dbSNP | Ensembl ].
VAR_030015
Natural variant14131D → N in OI2. Ref.94 Ref.102
VAR_063341
Natural variant14301K → N.
Corresponds to variant rs1059454 [ dbSNP | Ensembl ].
VAR_033780
Natural variant14311T → P.
Corresponds to variant rs1059454 [ dbSNP | Ensembl ].
VAR_033781
Natural variant14341T → S. Ref.1 Ref.25
Corresponds to variant rs1800220 [ dbSNP | Ensembl ].
VAR_001736
Natural variant14381P → R. Ref.5
Corresponds to variant rs17857117 [ dbSNP | Ensembl ].
VAR_030016
Natural variant14601P → H. Ref.5
Corresponds to variant rs17853657 [ dbSNP | Ensembl ].
VAR_030017
Natural variant14641L → P in OI3. Ref.80
VAR_001737

Experimental info

Sequence conflict591R → Q in CAA25394. Ref.8
Sequence conflict112 – 1143Missing in AAB94054. Ref.2
Sequence conflict2881E → P AA sequence Ref.15
Sequence conflict3701R → L in AAB59373. Ref.6
Sequence conflict4841P → L in AAA52289. Ref.19
Sequence conflict5951A → R in AAA51847. Ref.20
Sequence conflict7211Q → E no nucleotide entry Ref.22
Sequence conflict7381L → E no nucleotide entry Ref.22
Sequence conflict975 – 9762LP → PL in AAA52291. Ref.19
Sequence conflict10811V → A in AAA51995. Ref.18
Sequence conflict13291S → T in AAB27856. Ref.25

Secondary structure

..... 1464
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02452 [UniParc].

Last modified May 18, 2010. Version 5.
Checksum: F0EC4DE778FFFC11

FASTA1,464138,941
        10         20         30         40         50         60 
MFSFVDLRLL LLLAATALLT HGQEEGQVEG QDEDIPPITC VQNGLRYHDR DVWKPEPCRI 

        70         80         90        100        110        120 
CVCDNGKVLC DDVICDETKN CPGAEVPEGE CCPVCPDGSE SPTDQETTGV EGPKGDTGPR 

       130        140        150        160        170        180 
GPRGPAGPPG RDGIPGQPGL PGPPGPPGPP GPPGLGGNFA PQLSYGYDEK STGGISVPGP 

       190        200        210        220        230        240 
MGPSGPRGLP GPPGAPGPQG FQGPPGEPGE PGASGPMGPR GPPGPPGKNG DDGEAGKPGR 

       250        260        270        280        290        300 
PGERGPPGPQ GARGLPGTAG LPGMKGHRGF SGLDGAKGDA GPAGPKGEPG SPGENGAPGQ 

       310        320        330        340        350        360 
MGPRGLPGER GRPGAPGPAG ARGNDGATGA AGPPGPTGPA GPPGFPGAVG AKGEAGPQGP 

       370        380        390        400        410        420 
RGSEGPQGVR GEPGPPGPAG AAGPAGNPGA DGQPGAKGAN GAPGIAGAPG FPGARGPSGP 

       430        440        450        460        470        480 
QGPGGPPGPK GNSGEPGAPG SKGDTGAKGE PGPVGVQGPP GPAGEEGKRG ARGEPGPTGL 

       490        500        510        520        530        540 
PGPPGERGGP GSRGFPGADG VAGPKGPAGE RGSPGPAGPK GSPGEAGRPG EAGLPGAKGL 

       550        560        570        580        590        600 
TGSPGSPGPD GKTGPPGPAG QDGRPGPPGP PGARGQAGVM GFPGPKGAAG EPGKAGERGV 

       610        620        630        640        650        660 
PGPPGAVGPA GKDGEAGAQG PPGPAGPAGE RGEQGPAGSP GFQGLPGPAG PPGEAGKPGE 

       670        680        690        700        710        720 
QGVPGDLGAP GPSGARGERG FPGERGVQGP PGPAGPRGAN GAPGNDGAKG DAGAPGAPGS 

       730        740        750        760        770        780 
QGAPGLQGMP GERGAAGLPG PKGDRGDAGP KGADGSPGKD GVRGLTGPIG PPGPAGAPGD 

       790        800        810        820        830        840 
KGESGPSGPA GPTGARGAPG DRGEPGPPGP AGFAGPPGAD GQPGAKGEPG DAGAKGDAGP 

       850        860        870        880        890        900 
PGPAGPAGPP GPIGNVGAPG AKGARGSAGP PGATGFPGAA GRVGPPGPSG NAGPPGPPGP 

       910        920        930        940        950        960 
AGKEGGKGPR GETGPAGRPG EVGPPGPPGP AGEKGSPGAD GPAGAPGTPG PQGIAGQRGV 

       970        980        990       1000       1010       1020 
VGLPGQRGER GFPGLPGPSG EPGKQGPSGA SGERGPPGPM GPPGLAGPPG ESGREGAPGA 

      1030       1040       1050       1060       1070       1080 
EGSPGRDGSP GAKGDRGETG PAGPPGAPGA PGAPGPVGPA GKSGDRGETG PAGPTGPVGP 

      1090       1100       1110       1120       1130       1140 
VGARGPAGPQ GPRGDKGETG EQGDRGIKGH RGFSGLQGPP GPPGSPGEQG PSGASGPAGP 

      1150       1160       1170       1180       1190       1200 
RGPPGSAGAP GKDGLNGLPG PIGPPGPRGR TGDAGPVGPP GPPGPPGPPG PPSAGFDFSF 

      1210       1220       1230       1240       1250       1260 
LPQPPQEKAH DGGRYYRADD ANVVRDRDLE VDTTLKSLSQ QIENIRSPEG SRKNPARTCR 

      1270       1280       1290       1300       1310       1320 
DLKMCHSDWK SGEYWIDPNQ GCNLDAIKVF CNMETGETCV YPTQPSVAQK NWYISKNPKD 

      1330       1340       1350       1360       1370       1380 
KRHVWFGESM TDGFQFEYGG QGSDPADVAI QLTFLRLMST EASQNITYHC KNSVAYMDQQ 

      1390       1400       1410       1420       1430       1440 
TGNLKKALLL QGSNEIEIRA EGNSRFTYSV TVDGCTSHTG AWGKTVIEYK TTKTSRLPII 

      1450       1460 
DVAPLDVGAP DQEFGFDVGP VCFL 

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References

« Hide 'large scale' references
[1]Dalgleish R.
Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ALA-1019; ALA-1075; LYS-1391 AND SER-1434.
[2]"Analysis of the COL1A1 and COL1A2 genes by PCR amplification and scanning by conformation-sensitive gel electrophoresis identifies only COL1A1 mutations in 15 patients with osteogenesis imperfecta type I: identification of common sequences of null-allele mutations."
Korkko J.M., Ala-Kokko L., De Paepe A., Nuytinck L., Earley J.J., Prockop D.J.
Am. J. Hum. Genet. 62:98-110(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ALA-1075 AND LYS-1391.
[3]Korkko J.M., Earley J.J., Nuytinck L., DePaepe A., Prockop D.J., Ala-Kokko L.
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 1049.
[4]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-1075.
Tissue: Spleen.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ALA-1075; ARG-1438 AND HIS-1460.
Tissue: Brain.
[6]"Complete nucleotide sequence of the region encompassing the first twenty-five exons of the human pro alpha 1(I) collagen gene (COL1A1)."
D'Alessio M., Bernard M.P., Pretorius P.J., de Wet W., Ramirez F., Pretorious P.J.
Gene 67:105-115(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-589.
[7]"Structure of a full-length cDNA clone for the prepro alpha 1(I) chain of human type I procollagen."
Tromp G., Kuivaniemi H., Stacey A., Shikata H., Baldwin C.T., Jaenisch R., Prockup D.J.
Biochem. J. 253:919-922(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-472.
[8]"Human pro alpha 1(I) collagen gene structure reveals evolutionary conservation of a pattern of introns and exons."
Chu M.-L., de Wet W.J., Bernard M.P., Ding J.-F., Morabito M., Myers J., Williams C., Ramirez F.
Nature 310:337-340(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-181.
[9]"DNA sequences in the first intron of the human pro-alpha 1(I) collagen gene enhance transcription."
Rossouw C.M.S., Vergeer W.P., du Plooy S.J., Bernard M.P., Ramirez F., de Wet W.
J. Biol. Chem. 262:15151-15157(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44.
[10]"Fine structural analysis of the human pro-alpha 1 (I) collagen gene. Promoter structure, AluI repeats, and polymorphic transcripts."
Chu M.-L., de Wet W., Bernard M.P., Ramirez F.
J. Biol. Chem. 260:2315-2320(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
[11]"Regulatory elements in the first intron contribute to transcriptional control of the human alpha 1(I) collagen gene."
Bornstein P., McKay J., Morishima J.K., Devarayalu S., Gelinas R.E.
Proc. Natl. Acad. Sci. U.S.A. 84:8869-8873(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
[12]"In vivo and in vitro noncovalent association of excised alpha 1 (I) amino-terminal propeptides with mutant pN alpha 2(I) collagen chains in native mutant collagen in a case of Ehlers-Danlos syndrome, type VII."
Wirtz M.K., Keene D.R., Hori H., Glanville R.W., Steinmann B., Rao V.H., Hollister D.W.
J. Biol. Chem. 265:6312-6317(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 33-52.
[13]"A base substitution in the exon of a collagen gene causes alternative splicing and generates a structurally abnormal polypeptide in a patient with Ehlers-Danlos syndrome type VII."
Weil D., D'Alessio M., Ramirez F., de Wet W., Cole W.G., Chan D., Bateman J.F.
EMBO J. 8:1705-1710(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 156-183.
[14]"Isolation and characterization of the cyanogen bromide peptides from the alpha 1 and alpha 2 chains of human skin collagen."
Click E.M., Bornstein P.
Biochemistry 9:4699-4706(1970) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 162-301, ALLYSINE AT LYS-170, PYROGLUTAMATE FORMATION AT GLN-162.
Tissue: Skin.
[15]"A critical crosslink region in human-bone-derived collagen type I. Specific cleavage site at residue Leu95."
Baetge B., Notbohm H., Diebold J., Lehmann H., Bodo M., Deutzmann R., Muller P.K.
Eur. J. Biochem. 192:153-159(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 175-187 AND 274-289.
[16]"A comparative study of glycopeptides derived from selected vertebrate collagens. A possible role of the carbohydrate in fibril formation."
Morgan P.H., Jacobs H.G., Segrest J.P., Cunningham L.W.
J. Biol. Chem. 245:5042-5048(1970) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 263-268.
Tissue: Skin.
[17]"Segmental amplification of the entire helical and telopeptide regions of the cDNA for human alpha 1 (I) collagen."
Labhard M.E., Hollister D.W.
Matrix 10:124-130(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 281-302; 402-420; 823-842; 924-944; 1026-1045 AND 1143-1162.
[18]"Nucleotide sequences of complementary deoxyribonucleic acids for the pro alpha 1 chain of human type I procollagen. Statistical evaluation of structures that are conserved during evolution."
Bernard M.P., Chu M.-L., Myers J.C., Ramirez F., Eikenberry E.F., Prockop D.J.
Biochemistry 22:5213-5223(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 425-1464, VARIANTS ALA-1019 AND ALA-1075.
[19]"Cloning and characterization of five overlapping cDNAs specific for the human pro alpha 1(I) collagen chain."
Chu M.-L., Myers J.C., Bernard M.P., Ding J.-F., Ramirez F.
Nucleic Acids Res. 10:5925-5934(1982) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 425-490; 965-1024; 999-1039 AND 1453-1464.
[20]"Multiexon deletion in an osteogenesis imperfecta variant with increased type III collagen mRNA."
Chu M.-L., Gargiulo V., Williams C.J., Ramirez F.
J. Biol. Chem. 260:691-694(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 472-607.
[21]"Intron-mediated recombination may cause a deletion in an alpha 1 type I collagen chain in a lethal form of osteogenesis imperfecta."
Barsh G.S., Roush C.L., Bonadio J., Byers P.H., Gelinas R.E.
Proc. Natl. Acad. Sci. U.S.A. 82:2870-2874(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 488-625.
[22]"Variable expression of osteogenesis imperfecta in a nuclear family is explained by somatic mosaicism for a lethal point mutation in the alpha 1(I) gene (COL1A1) of type I collagen in a parent."
Wallis G.A., Starman B.J., Zinn A.B., Byers P.H.
Am. J. Hum. Genet. 46:1034-1040(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 710-745, VARIANT OI2 ARG-728.
[23]"Severe (type III) osteogenesis imperfecta due to glycine substitutions in the central domain of the collagen triple helix."
Forlino A., Zolezzi F., Valli M., Pignatti P.F., Cetta G., Brunelli P.C., Mottes M.
Hum. Mol. Genet. 3:2201-2206(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 746-781, VARIANT OI3 SER-767.
[24]Lubec G., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1063-1084, IDENTIFICATION BY MASS SPECTROMETRY, VARIANT ALA-1075.
Tissue: Fetal brain cortex.
[25]"Mutations in the carboxyl-terminal propeptide of the pro alpha 1(I) chain of type I collagen result in defective chain association and produce lethal osteogenesis imperfecta."
Chessler S.D., Wallis G.A., Byers P.H.
J. Biol. Chem. 268:18218-18225(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1179-1464, VARIANTS OI2 HIS-1277; ARG-1388 AND 1337-GLU-TYR-1338 DEL, VARIANTS THR-1251 AND SER-1434.
[26]"Substitution of cysteine for glycine within the carboxyl-terminal telopeptide of the alpha 1 chain of type I collagen produces mild osteogenesis imperfecta."
Cohn D.H., Apone S., Eyre D.R., Starman B.J., Andreassen P., Charbonneau H., Nicholls A.C., Pope F.M., Byers P.H.
J. Biol. Chem. 263:14605-14607(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1187-1220, VARIANT CYS-1195.
[27]"Human pro alpha 1(I) collagen: cDNA sequence for the C-propeptide domain."
Maekelae J.K., Raassina M., Virta A., Vuorio E.
Nucleic Acids Res. 16:349-349(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1229-1454, VARIANT LYS-1391.
Tissue: Bone.
[28]"Frameshift mutation near the 3' end of the COL1A1 gene of type I collagen predicts an elongated Pro alpha 1(I) chain and results in osteogenesis imperfecta type I."
Willing M.C., Cohn D.H., Byers P.H.
J. Clin. Invest. 85:282-290(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1440-1464.
[29]"Highly conserved sequences in the 3'-untranslated region of the COL1A1 gene bind cell-specific nuclear proteins."
Maatta A., Bornstein P., Penttinen R.P.
FEBS Lett. 279:9-13(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1454-1464, VARIANT ALA-1075.
[30]"Mutations in collagen genes: causes of rare and some common diseases in humans."
Kuivaniemi H., Tromp G., Prockop D.J.
FASEB J. 5:2052-2060(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[31]"Mutations in fibrillar collagens (types I, II, III, and XI), fibril-associated collagen (type IX), and network-forming collagen (type X) cause a spectrum of diseases of bone, cartilage, and blood vessels."
Kuivaniemi H., Tromp G., Prockop D.J.
Hum. Mutat. 9:300-315(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[32]"Osteogenesis imperfecta: translation of mutation to phenotype."
Byers P.H., Wallis G.A., Willing M.C.
J. Med. Genet. 28:433-442(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[33]"TRAM2 protein interacts with endoplasmic reticulum Ca2+ pump Serca2b and is necessary for collagen type I synthesis."
Stefanovic B., Stefanovic L., Schnabl B., Bataller R., Brenner D.A.
Mol. Cell. Biol. 24:1758-1768(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRAM2.
[34]"Lethal osteogenesis imperfecta resulting from a single nucleotide change in one human pro alpha 1(I) collagen allele."
Cohn D.H., Byers P.H., Steinmann B., Gelinas R.E.
Proc. Natl. Acad. Sci. U.S.A. 83:6045-6047(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI2 CYS-1166.
[35]"Lethal perinatal osteogenesis imperfecta due to the substitution of arginine for glycine at residue 391 of the alpha 1(I) chain of type I collagen."
Bateman J.F., Chan D., Walkers I.D., Rogers J.G., Cole W.G.
J. Biol. Chem. 262:7021-7027(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI2 ARG-569.
[36]"A point mutation in a type I procollagen gene converts glycine 748 of the alpha 1 chain to cysteine and destabilizes the triple helix in a lethal variant of osteogenesis imperfecta."
Vogel B.E., Minor R.R., Freund M., Prockop D.J.
J. Biol. Chem. 262:14737-14744(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI2 CYS-926.
[37]"Substitution of arginine for glycine 664 in the collagen alpha 1(I) chain in lethal perinatal osteogenesis imperfecta. Demonstration of the peptide defect by in vitro expression of the mutant cDNA."
Bateman J.F., Lamande S.R., Dahl H.-H.M., Chan D., Cole W.G.
J. Biol. Chem. 263:11627-11630(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI2 ARG-842.
[38]"A cysteine for glycine substitution at position 1017 in an alpha 1(I) chain of type I collagen in a patient with mild dominantly inherited osteogenesis imperfecta."
Labhard M.E., Wirtz M.K., Pope F.M., Nicholls A.C., Hollister D.W.
Mol. Biol. Med. 5:197-207(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI1 CYS-1195.
[39]"RNA sequence analysis of a perinatal lethal osteogenesis imperfecta mutation."
Patterson E., Smiley E., Bonadio J.
J. Biol. Chem. 264:10083-10087(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI2 VAL-434.
[40]"Osteogenesis imperfecta type IV. Detection of a point mutation in one alpha 1(I) collagen allele (COL1A1) by RNA/RNA hybrid analysis."
Marini J.C., Grange D.K., Gottesman G.S., Lewis M.B., Koeplin D.A.
J. Biol. Chem. 264:11893-11900(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI4 SER-1010.
[41]"Characterization of point mutations in the collagen COL1A1 and COL1A2 genes causing lethal perinatal osteogenesis imperfecta."
Lamande S.R., Dahl H.-H.M., Cole W.G., Bateman J.F.
J. Biol. Chem. 264:15809-15812(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OI2 ALA-1106; VAL-1151; ARG-1154 AND VAL-1184.
[42]"Substitution of serine for alpha 1(I)-glycine 844 in a severe variant of osteogenesis imperfecta minimally destabilizes the triple helix of type I procollagen. The effects of glycine substitutions on thermal stability are either position of amino acid specific."
Pack M., Constantinou C.D., Kalia K., Nielsen K.B., Prockop D.J.
J. Biol. Chem. 264:19694-19699(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI3 SER-1022.
[43]"A lethal variant of osteogenesis imperfecta has a single base mutation that substitutes cysteine for glycine 904 of the alpha 1(I) chain of type I procollagen. The asymptomatic mother has an unidentified mutation producing an overmodified and unstable type I procollagen."
Constantinou C.D., Nielsen K.B., Prockop D.J.
J. Clin. Invest. 83:574-584(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI2 CYS-1082.
[44]"Osteogenesis imperfecta. The position of substitution for glycine by cysteine in the triple helical domain of the pro alpha 1(I) chains of type I collagen determines the clinical phenotype."
Starman B.J., Eyre D.R., Charbonneau H., Harrylock M., Weis M.A., Weiss L., Graham J.M. Jr., Byers P.H.
J. Clin. Invest. 84:1206-1214(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI1 CYS-272, VARIANT OI3 CYS-704, VARIANT OI2 CYS-896.
[45]"Two cysteine substitutions in the type I procollagen genes (COL1A1 and COL1A2) that cause lethal osteogenesis imperfecta. The location of glycine substitutions does not in any simple way predict their effects on protein function or phenotype."
Fertala A., Westerhausen A., Morris G.M., Rooney J.E., Prockop D.J.
Am. J. Hum. Genet. 47:A216-A216(1990)
Cited for: VARIANT OI2 CYS-422.
[46]"Mutations that substitute serine for glycine alpha 1-598 and glycine alpha 1-631 in type I procollagen. The effects on thermal unfolding of the triple helix are position-specific and demonstrate that the protein unfolds through a series of cooperative blocks."
Westerhausen A., Kishi J., Prockop D.J.
J. Biol. Chem. 265:13995-14000(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OI2 SER-776 AND SER-809.
[47]"Substitution of arginine for glycine at position 847 in the triple-helical domain of the alpha 1 (I) chain of type I collagen produces lethal osteogenesis imperfecta. Molecules that contain one or two abnormal chains differ in stability and secretion."
Wallis G.A., Starman B.J., Schwartz M.F., Byers P.H.
J. Biol. Chem. 265:18628-18633(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI2 ARG-1025.
[48]"Serine for glycine substitutions in the alpha1(I) chain of type I collagen: biological plasticity in the Gly-Pro-Hyp clamp at the carboxyl-terminal end of triple helicalH domain."
Cohn D.H., Wallis G.A., Zhang X., Byers P.H.
Matrix 10:236-236(1990)
Cited for: VARIANTS OI2 SER-1091; SER-1181; SER-1187 AND VAL-1187.
[49]"A single base mutation in type I procollagen (COL1A1) that converts glycine alpha 1-541 to aspartate in a lethal variant of osteogenesis imperfecta: detection of the mutation with a carbodiimide reaction of DNA heteroduplexes and direct sequencing of products of the PCR."
Zhuang J., Constantinou C.D., Ganguly A., Prockop D.J.
Am. J. Hum. Genet. 48:1186-1191(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI2 ASP-719.
[50]"Substitution of cysteine for glycine-alpha 1-691 in the pro alpha 1(I) chain of type I procollagen in a proband with lethal osteogenesis imperfecta destabilizes the triple helix at a site C-terminal to the substitution."
Steinmann B., Westerhausen A., Constantinou C.D., Superti-Furga A., Prockop D.J.
Biochem. J. 279:747-752(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI2 CYS-869.
[51]"A type I collagen with substitution of a cysteine for glycine-748 in the alpha 1(I) chain copolymerizes with normal type I collagen and can generate fractallike structures."
Kadler K.E., Torre-Blanco A., Adachi E., Vogel B.E., Hojima Y., Prockop D.J.
Biochemistry 30:5081-5088(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI2 CYS-926.
[52]"Osteogenesis imperfecta due to recurrent point mutations at CpG dinucleotides in the COL1A1 gene of type I collagen."
Pruchno C.J., Cohn D.H., Wallis G.A., Willing M.C., Starman B.J., Zhang X., Byers P.H.
Hum. Genet. 87:33-40(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI3 ARG-332, VARIANT OI2 SER-1181.
[53]"A de novo G to T transversion in a pro-alpha 1 (I) collagen gene for a moderate case of osteogenesis imperfecta. Substitution of cysteine for glycine 178 in the triple helical domain."
Valli M., Mottes M., Tenni R., Sangalli A., Gomez Lira M., Rossi A., Antoniazzi F., Cetta G., Pignatti P.F.
J. Biol. Chem. 266:1872-1878(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI4 CYS-356.
[54]"Substitutions for glycine alpha 1-637 and glycine alpha 2-694 of type I procollagen in lethal osteogenesis imperfecta. The conformational strain on the triple helix introduced by a glycine substitution can be transmitted along the helix."
Tsuneyoshi T., Westerhausen A., Constantinou C.D., Prockop D.J.
J. Biol. Chem. 266:15608-15613(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI2 VAL-815.
[55]"The substitution of arginine for glycine 85 of the alpha 1(I) procollagen chain results in mild osteogenesis imperfecta. The mutation provides direct evidence for three discrete domains of cooperative melting of intact type I collagen."
Deak S.B., Scholz P.M., Amenta P.S., Constantinou C.D., Levi-Minzi S.A., Gonzalez-Lavin L., MacKenzie J.W.
J. Biol. Chem. 266:21827-21832(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI1 ARG-263.
[56]"A 9-base pair deletion in COL1A1 in a lethal variant of osteogenesis imperfecta."
Hawkins J.R., Superti-Furga A., Steinmann B., Dalgleish R.
J. Biol. Chem. 266:22370-22374(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI2 1046-GLY--PRO-1048 DEL.
[57]"Substitution of cysteine for glycine at residue 415 of one allele of the alpha 1(I) chain of type I procollagen in type III/IV osteogenesis imperfecta."
Nicholls A.C., Oliver J.E., Renouf D.V., Keston M., Pope F.M.
J. Med. Genet. 28:757-764(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI3 CYS-593, VARIANT OI4 CYS-593.
[58]"G to A polymorphism in exon 45 of the COL1A1 gene."
Sokolov B.P., Constantinou C.D., Tsuneyoshi T., Zhuang J., Prockop D.J.
Nucleic Acids Res. 19:4302-4302(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ALA-1075.
[59]"Mild dominant osteogenesis imperfecta with intrafamilial variability: the cause is a serine for glycine alpha 1(I) 901 substitution in a type-I collagen gene."
Mottes M., Sangalli A., Valli M., Gomez Lira M., Tenni R., Buttitta P., Pignatti P.F., Cetta G.
Hum. Genet. 89:480-484(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI1 SER-1079.
[60]"A dominant mutation in the COL1A1 gene that substitutes glycine for valine causes recurrent lethal osteogenesis imperfecta."
Bonaventure J., Cohen-Solal L., Lasselin C., Maroteaux P.
Hum. Genet. 89:640-646(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI2 VAL-980.
[61]"A tripeptide deletion in the triple-helical domain of the pro alpha 1(I) chain of type I procollagen in a patient with lethal osteogenesis imperfecta does not alter cleavage of the molecule by N-proteinase."
Wallis G.A., Kadler K.E., Starman B.J., Byers P.H.
J. Biol. Chem. 267:25529-25534(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI2 1046-GLY--PRO-1048 DEL.
[62]"An osteopenic nonfracture syndrome with features of mild osteogenesis imperfecta associated with the substitution of a cysteine for glycine at triple helix position 43 in the pro alpha 1(I) chain of type I collagen."
Shapiro J.R., Stover M.L., Burn V.E., McKinstry M.B., Burshell A.L., Chipman S.D., Rowe D.W.
J. Clin. Invest. 89:567-573(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI1 CYS-221.
[63]"The clinicopathological features of three babies with osteogenesis imperfecta resulting from the substitution of glycine by valine in the pro alpha 1 (I) chain of type I procollagen."
Cole W.G., Patterson E., Bonadio J., Campbell P.E., Fortune D.W.
J. Med. Genet. 29:112-118(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OI2 VAL-434; VAL-1151 AND VAL-1184.
[64]"Chemical cleavage method for the detection of RNA base changes: experience in the application to collagen mutations in osteogenesis imperfecta."
Bateman J.F., Lamande S.R., Hannagan M., Moeller I., Dahl H.-H.M., Cole W.G.
Am. J. Med. Genet. 45:233-240(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI2 CYS-1312.
[65]"Moderately severe osteogenesis imperfecta associated with substitutions of serine for glycine in the alpha 1(I) chain of type I collagen."
Marini J.C., Lewis M.B., Chen K.J.
Am. J. Med. Genet. 45:241-245(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI3 SER-530.
[66]"A cysteine for glycine substitution at position 175 in an alpha 1 (I) chain of type I collagen produces a clinically heterogeneous form of osteogenesis imperfecta."
Wirtz M.K., Rao V.H., Glanville R.W., Labhard M.E., Pretorius P.J., de Vries W.N., de Wet W., Hollister D.W.
Connect. Tissue Res. 29:1-11(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI4 CYS-353.
[67]"Osteogenesis imperfecta and type-I collagen mutations. A lethal variant caused by a Gly910-->Ala substitution in the alpha 1 (I) chain."
Valli M., Sangalli A., Rossi A., Mottes M., Forlino A., Tenni R., Pignatti P.F., Cetta G.
Eur. J. Biochem. 211:415-419(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI2 ALA-1088.
[68]"Gly85 to Val substitution in pro alpha 1(I) chain causes mild osteogenesis imperfecta and introduces a susceptibility to protease digestion."
Valli M., Zolezzi F., Mottes M., Antoniazzi F., Stanzial F., Tenni R., Pignatti P.F., Cetta G.
Eur. J. Biochem. 217:77-82(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI1 VAL-263.
[69]"SSCP detection of a Gly565Val substitution in the pro alpha 1(I) collagen chain resulting in osteogenesis imperfecta type II."
Mackay K., Lund A.M., Raghunath M., Steinmann B., Dalgleish R.
Hum. Genet. 91:439-444(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI2 VAL-743.
[70]"An RT-PCR-SSCP screening strategy for detection of mutations in the gene encoding the alpha 1 chain of type I collagen: application to four patients with osteogenesis imperfecta."
Mackay K., Byers P.H., Dalgleish R.
Hum. Mol. Genet. 2:1155-1160(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OI2 SER-425 AND SER-530, VARIANT OI4 SER-560, VARIANT OI3 SER-719, VARIANT ALA-823.
[71]"Paternal mosaicism for a COL1A1 dominant mutation (alpha 1 Ser-415) causes recurrent osteogenesis imperfecta."
Mottes M., Gomez Lira M., Valli M., Scarano G., Lonardo F., Forlino A., Cetta G., Pignatti P.F.
Hum. Mutat. 2:196-204(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI2 SER-593, VARIANT OI3 SER-593.
[72]"Serine for glycine substitutions in type I collagen in two cases of type IV osteogenesis imperfecta (OI). Additional evidence for a regional model of OI pathophysiology."
Marini J.C., Lewis M.B., Wang Q., Chen K.J., Orrison B.M.
J. Biol. Chem. 268:2667-2673(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI4 SER-530.
[73]"BiP binds type I procollagen pro alpha chains with mutations in the carboxyl-terminal propeptide synthesized by cells from patients with osteogenesis imperfecta."
Chessler S.D., Byers P.H.
J. Biol. Chem. 268:18226-18233(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OI2.
[74]"Osteogenesis imperfecta: comparison of molecular defects with bone histological changes."
Sztrolovics R., Glorieux F.H., Travers R., van der Rest M., Roughley P.J.
Bone 15:321-328(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI2 ARG-389.
[75]"Substitution of glycine-172 by arginine in the alpha 1 chain of type I collagen in a patient with osteogenesis imperfecta, type III."
Mackay K., de Paepe A., Nuytinck L., Dalgleish R.
Hum. Mutat. 3:324-326(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI3 ARG-350.
[76]"Substitution of cysteine for glycine-946 in the alpha 1(I) chain of type I procollagen causes lethal osteogenesis imperfecta."
Kurosaka D., Hattori S., Hori H., Yamaguchi N., Hasegawa T., Akimoto H., Nagai Y.
J. Biochem. 115:853-857(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI2 CYS-1124.
[77]"Substitution of serine for glycine 883 in the triple helix of the pro alpha 1 (I) chain of type I procollagen produces osteogenesis imperfecta type IV and introduces a structural change in the triple helix that does not alter cleavage of the molecule by procollagen N-proteinase."
Lightfoot S.J., Atkinson M.S., Murphy G., Byers P.H., Kadler K.E.
J. Biol. Chem. 269:30352-30357(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI4 SER-1061.
[78]"Substitution of arginine for glycine at position 154 of the alpha 1 chain of type I collagen in a variant of osteogenesis imperfecta: comparison to previous cases with the same mutation."
Zhuang J., Tromp G., Kuivaniemi H., Castells S., Prockop D.J.
Am. J. Med. Genet. 61:111-116(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI3 ARG-332.
[79]"Substitution of glycine-661 by serine in the alpha1(I) and alpha2(I) chains of type I collagen results in different clinical and biochemical phenotypes."
Nuytinck L., Dalgleish R., Spotila L., Renard J.-P., van Regemorter N., de Paepe A.
Hum. Genet. 97:324-329(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI2 SER-839.
[80]"Mutation in the carboxy-terminal propeptide of the Pro alpha 1(I) chain of type I collagen in a child with severe osteogenesis imperfecta (OI type III): possible implications for protein folding."
Oliver J.E., Thompson E.M., Pope F.M., Nicholls A.C.
Hum. Mutat. 7:318-326(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI3 PRO-1464.
[81]"Reduced bone density and osteoporosis associated with a polymorphic Sp1 binding site in the collagen type I alpha 1 gene."
Grant S.F.A., Reid D.M., Blake G., Herd R., Fogelman I., Ralston S.H.
Nat. Genet. 14:203-205(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN OSTEOPOROSIS.
[82]"Serine for glycine substitutions in the C-terminal third of the alpha 1(I) chain of collagen I in five patients with nonlethal osteogenesis imperfecta."
Lund A.M., Skovby F., Schwartz M.
Hum. Mutat. 9:378-382(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OI3 SER-821; SER-1040; SER-1049; SER-1058 AND SER-1076.
[83]"(G586V) substitutions in the alpha 1 and alpha 2 chains of collagen I: effect of alpha-chain stoichiometry on the phenotype of osteogenesis imperfecta?"
Lund A.M., Skovby F., Schwartz M.
Hum. Mutat. 9:431-436(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI2 VAL-764.
[84]"Three novel type I collagen mutations in osteogenesis imperfecta type IV probands are associated with discrepancies between electrophoretic migration of osteoblast and fibroblast collagen."
Sarafova A.P., Choi H., Forlino A., Gajko A., Cabral W.A., Tosi L., Reing C.M., Marini J.C.
Hum. Mutat. 11:395-403(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OI4 ALA-398; CYS-527 AND CYS-701.
[85]"Four new cases of lethal osteogenesis imperfecta due to glycine substitutions in COL1A1 and genes."
Mottes M., Gomez Lira M., Zolezzi F., Valli M., Lisi V., Freising P.
Hum. Mutat. 12:71-72(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OI2 SER-656 AND ASP-1172.
[86]"Relation of alleles of the collagen type Ialpha1 gene to bone density and the risk of osteoporotic fractures in postmenopausal women."
Uitterlinden A.G., Burger H., Huang Q., Yue F., McGuigan F.E.A., Grant S.F.A., Hofman A., van Leeuwen J.P.T.M., Pols H.A.P., Ralston S.H.
N. Engl. J. Med. 338:1016-1021(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN INVOLUTIONAL OSTEOPOROSIS.
[87]"Osteogenesis imperfecta: mosaicism and refinement of the genotype-phenotype map in OI type III."
Lund A.M., Astroem E., Soederhaell S., Schwartz M., Skovby F.
Hum. Mutat. 13:503-503(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI3 SER-866.
[88]"Classical Ehlers-Danlos syndrome caused by a mutation in type I collagen."
Nuytinck L., Freund M., Lagae L., Pierard G.E., Hermanns-Le T., De Paepe A.
Am. J. Hum. Genet. 66:1398-1402(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EDS1 CYS-312.
[89]"Deregulation of the platelet-derived growth factor B-chain gene via fusion with collagen gene COL1A1 in dermatofibrosarcoma protuberans and giant-cell fibroblastoma."
Simon M.-P., Pedeutour F., Sirvent N., Grosgeorge J., Minoletti F., Coindre J.-M., Terrier-Lacombe M.-J., Mandahl N., Craver R.D., Blin N., Sozzi G., Turc-Carel C., O'Brien K.P., Kedra D., Fransson I., Guilbaud C., Dumanski J.P.
Nat. Genet. 15:95-98(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: DISEASE, CHROMOSOMAL TRANSLOCATION WITH PDGFB.
[90]"Dermatofibrosarcoma protuberans of breast."
Sandberg A.A., Anderson W.D., Fredenberg C., Hashimoto H.
Cancer Genet. Cytogenet. 142:56-59(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: DISEASE, CHROMOSOMAL TRANSLOCATION WITH PDGFB.
[91]"A novel COL1A1 mutation in infantile cortical hyperostosis (Caffey disease) expands the spectrum of collagen-related disorders."
Gensure R.C., Maekitie O., Barclay C., Chan C., Depalma S.R., Bastepe M., Abuzahra H., Couper R., Mundlos S., Sillence D., Ala-Kokko L., Seidman J.G., Cole W.G., Jueppner H.
J. Clin. Invest. 115:1250-1257(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CAFFD CYS-1014.
[92]"Osteogenesis imperfecta: clinical, biochemical and molecular findings."
Venturi G., Tedeschi E., Mottes M., Valli M., Camilot M., Viglio S., Antoniazzi F., Tato L.
Clin. Genet. 70:131-139(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OI3 VAL-203 AND SER-821, VARIANTS OI4 ARG-257 AND SER-683.
[93]"Mutational spectrum of type I collagen genes in Korean patients with osteogenesis imperfecta."
Lee K.S., Song H.R., Cho T.J., Kim H.J., Lee T.M., Jin H.S., Park H.Y., Kang S., Jung S.C., Koo S.K.
Hum. Mutat. 27:599-599(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OI1/OI3/OI4 ARG-194; ASP-242; ARG-257; SER-722; SER-767; SER-821 AND SER-1058.
[94]"Mutation analysis of COL1A1 and COL1A2 in patients diagnosed with osteogenesis imperfecta type I-IV."
Pollitt R., McMahon R., Nunn J., Bamford R., Afifi A., Bishop N., Dalton A.
Hum. Mutat. 27:716-716(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OI2 ARG-22; ARG-581; VAL-734 AND ASN-1413, VARIANTS OI4 ARG-197 AND CYS-338, VARIANTS OI1 VAL-320; ARG-555; SER-647 AND GLU-1219, VARIANTS ALA-205; LYS-288; SER-906 AND HIS-1356.
[95]"Prenatal diagnosis of type II osteogenesis imperfecta, describing a new mutation in the COL1A1 gene."
Aerts M., Van Holsbeke C., de Ravel T., Devlieger R.
Prenat. Diagn. 26:394-394(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI2 ASP-833.
[96]"A new mutation in COL1A1 gene in a family with osteogenesis imperfecta."
Wang Z., Xu D.L., Chen Z., Hu J.Y., Yang Z., Wang L.T.
Zhonghua Yi Xue Za Zhi 86:170-173(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OI1 ASP-1157.
[97]"Three arginine to cysteine substitutions in the pro-alpha (I)-collagen chain cause Ehlers-Danlos syndrome with a propensity to arterial rupture in early adulthood."
Malfait F., Symoens S., De Backer J., Hermanns-Le T., Sakalihasan N., Lapiere C.M., Coucke P., De Paepe A.
Hum. Mutat. 28:387-395(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EDS1 CYS-312, VARIANTS CYS-574 AND CYS-1093.
[98]"Y-position cysteine substitution in type I collagen (alpha1(I) R888C/p.R1066C) is associated with osteogenesis imperfecta/Ehlers-Danlos syndrome phenotype."
Cabral W.A., Makareeva E., Letocha A.D., Scribanu N., Fertala A., Steplewski A., Keene D.R., Persikov A.V., Leikin S., Marini J.C.
Hum. Mutat. 28:396-405(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CYS-1066.
[99]"Mutations in type I collagen genes in Japanese osteogenesis imperfecta patients."
Kataoka K., Ogura E., Hasegawa K., Inoue M., Seino Y., Morishima T., Tanaka H.
Pediatr. Int. 49:564-569(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OI1 GLU-266 AND SER-287, VARIANT OI4 SER-353.
[100]"Natural variation in four human collagen genes across an ethnically diverse population."
Chan T.F., Poon A., Basu A., Addleman N.R., Chen J., Phong A., Byers P.H., Klein T.E., Kwok P.Y.
Genomics 91:307-314(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ALA-1075; GLN-1141 AND ILE-1177.
[101]"Two novel COL1A1 mutations in patients with osteogenesis imperfecta (OI) affect the stability of the collagen type I triple-helix."
Witecka J., Augusciak-Duma A.M., Kruczek A., Szydlo A., Lesiak M., Krzak M., Pietrzyk J.J., Mannikko M., Sieron A.L.
J. Appl. Genet. 49:283-295(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OI1 VAL-200 AND PHE-349, VARIANT OI2 SER-866, VARIANT OI3 SER-1040.
[102]"Mutation and polymorphism spectrum in osteogenesis imperfecta type II: implications for genotype-phenotype relationships."
Bodian D.L., Chan T.F., Poon A., Schwarze U., Yang K., Byers P.H., Kwok P.Y., Klein T.E.
Hum. Mol. Genet. 18:463-471(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OI2 THR-146; VAL-288; ASP-353; VAL-368; THR-390; SER-425; ASP-455; VAL-470; VAL-509; ALA-548; ARG-602; ASP-605; ARG-614; ARG-740; SER-809; ARG-824; ARG-845; ARG-848; HIS-855; SER-866; SER-875; SER-884; ASP-896; CYS-947; ASP-977; CYS-1001; VAL-1022; ALA-PRO-GLY-1052 INS; ASP-1055; SER-1094; ASP-1100 AND ASN-1413, VARIANT ALA-1075.
[103]"COL1 C-propeptide cleavage site mutations cause high bone mass osteogenesis imperfecta."
Lindahl K., Barnes A.M., Fratzl-Zelman N., Whyte M.P., Hefferan T.E., Makareeva E., Brusel M., Yaszemski M.J., Rubin C.J., Kindmark A., Roschger P., Klaushofer K., McAlister W.H., Mumm S., Leikin S., Kessler E., Boskey A.L., Ljunggren O., Marini J.C.
Hum. Mutat. 32:598-609(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ASN-1219, CHARACTERIZATION OF VARIANT ASN-1219.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z74615 mRNA. Translation: CAA98968.1.
AF017178 Genomic DNA. Translation: AAB94054.3.
AB209597 mRNA. Translation: BAD92834.1. Different initiation.
BC036531 mRNA. Translation: AAH36531.1.
M20789 Genomic DNA. Translation: AAB59373.1.
M36546 mRNA. Translation: AAA60150.1.
X07884 mRNA. Translation: CAA30731.1.
X00820 Genomic DNA. Translation: CAA25394.1.
J02829 Genomic DNA. Translation: AAA51993.1.
M10627 Genomic DNA. Translation: AAA51992.1.
J03559 Genomic DNA. Translation: AAA52052.1.
K01228 mRNA. Translation: AAA51995.1.
J00110 mRNA. Translation: AAA52289.1.
J00111 mRNA. Translation: AAA52290.1.
J00112 mRNA. Translation: AAA52291.1.
J00113 mRNA. Translation: AAN86574.1.
K03179 Genomic DNA. Translation: AAA51847.1.
M11162 Genomic DNA. Translation: AAA75386.1.
L47667 Genomic DNA. Translation: AAB59576.1.
S64596 mRNA. Translation: AAB27856.1.
M23213 Genomic DNA. Translation: AAB59363.1.
X06269 mRNA. Translation: CAA29605.1.
M32798 mRNA. Translation: AAA52049.1.
M55998 Genomic DNA. Translation: AAA52036.1.
PIRCGHU1S. I60114.
RefSeqNP_000079.2. NM_000088.3.
UniGeneHs.172928.
Hs.681002.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Q7DX-ray1.80A/B/C914-930[»]
2LLPNMR-A/B/C949-965[»]
3EJHX-ray2.10E/F956-977[»]
3GXEX-ray2.60E/F254-275[»]
ProteinModelPortalP02452.
SMRP02452. Positions 34-101, 1247-1464.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107674. 29 interactions.
DIPDIP-36077N.
IntActP02452. 15 interactions.

Chemistry

ChEMBLCHEMBL2364188.
DrugBankDB00048. Collagenase.
DB00039. Palifermin.

PTM databases

PhosphoSiteP02452.

Polymorphism databases

DMDM296439504.

2D gel databases

DOSAC-COBS-2DPAGEP02452.

Proteomic databases

PaxDbP02452.
PRIDEP02452.

Protocols and materials databases

DNASU1277.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000225964; ENSP00000225964; ENSG00000108821.
GeneID1277.
KEGGhsa:1277.
UCSCuc002iqm.3. human.

Organism-specific databases

CTD1277.
GeneCardsGC17M048260.
HGNCHGNC:2197. COL1A1.
HPAHPA008405.
HPA011795.
MIM114000. phenotype.
120150. gene.
130000. phenotype.
130060. phenotype.
166200. phenotype.
166210. phenotype.
166220. phenotype.
166710. phenotype.
259420. phenotype.
607907. phenotype.
neXtProtNX_P02452.
Orphanet1310. Caffey disease.
31112. Dermatofibrosarcoma protuberans.
90309. Ehlers-Danlos syndrome type 1.
99875. Ehlers-Danlos syndrome type 7A.
230845. Ehlers-Danlos syndrome, vascular-like type.
230857. Ehlers-Danlos/osteogenesis imperfecta syndrome.
314029. High bone mass osteogenesis imperfecta.
216796. Osteogenesis imperfecta type 1.
216804. Osteogenesis imperfecta type 2.
216812. Osteogenesis imperfecta type 3.
216820. Osteogenesis imperfecta type 4.
PharmGKBPA35041.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOVERGENHBG004933.
InParanoidP02452.
KOK06236.
OMAGSTMGTD.
OrthoDBEOG7TJ3HH.
PhylomeDBP02452.
TreeFamTF344135.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.
REACT_160300. Binding and Uptake of Ligands by Scavenger Receptors.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP02452.
BgeeP02452.
GenevestigatorP02452.

Family and domain databases

InterProIPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_C.
[Graphical view]
PfamPF01410. COLFI. 1 hit.
PF01391. Collagen. 13 hits.
PF00093. VWC. 1 hit.
[Graphical view]
ProDomPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00038. COLFI. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
PROSITEPS51461. NC1_FIB. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCOL1A1. human.
EvolutionaryTraceP02452.
GeneWikiCollagen,_type_I,_alpha_1.
GenomeRNAi1277.
NextBio5161.
PMAP-CutDBP02452.
PROP02452.
SOURCESearch...

Entry information

Entry nameCO1A1_HUMAN
AccessionPrimary (citable) accession number: P02452
Secondary accession number(s): O76045 expand/collapse secondary AC list , P78441, Q13896, Q13902, Q13903, Q14037, Q14992, Q15176, Q15201, Q16050, Q59F64, Q7KZ30, Q7KZ34, Q8IVI5, Q8N473, Q9UML6, Q9UMM7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: May 18, 2010
Last modified: April 16, 2014
This is version 185 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM