P02452 (CO1A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Collagen alpha-1(I) chain

Alternative name(s):
Alpha-1 type I collagen

Gene names

Name:

COL1A1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1464 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	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.
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]: 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. 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]: 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. 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]: A connective tissue disorder 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]: A connective tissue disorder 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 component	Extracellular matrix Secreted
Coding sequence diversity	Chromosomal rearrangement Polymorphism
Disease	Disease mutation Dwarfism Ehlers-Danlos syndrome Osteogenesis imperfecta
Domain	Collagen Repeat Signal
Ligand	Calcium Metal-binding
PTM	Disulfide bond Glycoprotein Hydroxylation Pyrrolidone carboxylic acid
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	axon guidance Traceable author statement. Source: Reactome blood vessel development Inferred from mutant phenotype Ref.97. Source: UniProtKB bone trabecula formation Inferred from electronic annotation. Source: Compara cartilage development involved in endochondral bone morphogenesis Inferred from electronic annotation. Source: Compara cellular response to amino acid stimulus Inferred from electronic annotation. Source: Compara cellular response to mechanical stimulus Inferred from electronic annotation. Source: Compara cellular response to retinoic acid Inferred from electronic annotation. Source: Compara cellular response to transforming growth factor beta stimulus Inferred from electronic annotation. Source: Compara collagen biosynthetic process Inferred from mutant phenotype PubMed 15095409. Source: UniProtKB 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: Compara face morphogenesis Inferred from electronic annotation. Source: Compara intramembranous ossification Inferred from electronic annotation. Source: Compara leukocyte migration Traceable author statement. Source: Reactome negative regulation of cell-substrate adhesion Inferred from electronic annotation. Source: Compara osteoblast differentiation Inferred from electronic annotation. Source: Compara platelet activation Traceable author statement. Source: Reactome positive regulation of canonical Wnt receptor 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-dependent Inferred from direct assay PubMed 20018240. Source: UniProtKB protein heterotrimerization Inferred from electronic annotation. Source: Compara protein localization to nucleus Inferred from direct assay PubMed 20018240. Source: UniProtKB protein transport Inferred from electronic annotation. Source: Compara response to cAMP Inferred from electronic annotation. Source: Compara response to corticosteroid stimulus Inferred from electronic annotation. Source: Compara response to hydrogen peroxide Inferred from electronic annotation. Source: Compara response to nutrient Inferred from electronic annotation. Source: Compara response to peptide hormone stimulus Inferred from electronic annotation. Source: Compara sensory perception of sound Inferred from mutant phenotype PubMed 17489845. 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_component	collagen type I Inferred from mutant phenotype PubMed 14976317PubMed 17576241. Source: UniProtKB endoplasmic reticulum lumen Traceable author statement. Source: Reactome extracellular space Inferred from direct assay PubMed 20551380. Source: BHF-UCL
Molecular_function	extracellular matrix structural constituent Inferred from electronic annotation. Source: Compara 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...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

22

Propeptide

23 – 161

139

N-terminal propeptide

PRO_0000005719

Chain

162 – 1218

1057

Collagen alpha-1(I) chain

PRO_0000005720

Propeptide

1219 – 1464

246

C-terminal propeptide

PRO_0000005721

Regions

Domain

38 – 96

59

VWFC

Domain

1229 – 1464

236

Fibrillar collagen NC1

Region

162 – 178

17

Nonhelical region (N-terminal)

Region

179 – 1192

1014

Triple-helical region

Region

1193 – 1218

26

Nonhelical region (C-terminal)

Motif

745 – 747

3

Cell attachment site Potential

Motif

1093 – 1095

3

Cell attachment site Potential

Sites

Metal binding

1277

1

Calcium By similarity

Metal binding

1279

1

Calcium By similarity

Metal binding

1280

1

Calcium; via carbonyl oxygen By similarity

Metal binding

1282

1

Calcium; via carbonyl oxygen By similarity

Metal binding

1285

1

Calcium By similarity

Site

161 – 162

2

Cleavage; by procollagen N-endopeptidase

Site

953 – 954

2

Cleavage; by collagenase By similarity

Site

1218 – 1219

2

Cleavage; by procollagen C-endopeptidase

Amino acid modifications

Modified residue

162

1

Pyrrolidone carboxylic acid

Modified residue

170

1

Allysine

Modified residue

265

1

5-hydroxylysine

Modified residue

1108

1

5-hydroxylysine By similarity

Modified residue

1164

1

3-hydroxyproline By similarity

Modified residue

1208

1

Allysine By similarity

Glycosylation

265

1

O-linked (Gal...)

Glycosylation

1108

1

O-linked (Gal...) By similarity

Glycosylation

1365

1

N-linked (GlcNAc...)

Disulfide bond

1259 ↔ 1291

By similarity

Disulfide bond

1265

Interchain By similarity

Disulfide bond

1282

Interchain By similarity

Disulfide bond

1299 ↔ 1462

By similarity

Disulfide bond

1370 ↔ 1415

By similarity

Natural variations

Natural variant

22

1

G → R in OI2. Ref.94

VAR_063290

Natural variant

146

1

P → T in a patient with osteogenesis imperfecta type 2; rare variant of unknown pathological significance. Ref.102

VAR_063291

Natural variant

194

1

G → R in OI1. Ref.93

VAR_063292

Natural variant

197

1

G → C.
Corresponds to variant rs8179178 [ dbSNP | Ensembl ].

VAR_001642

Natural variant

197

1

G → R in OI4. Ref.94

VAR_063293

Natural variant

200

1

G → V in OI1; patient diagnosed with OI1/OI4. Ref.101

VAR_063294

Natural variant

203

1

G → V in OI3. Ref.92

VAR_063295

Natural variant

205

1

P → A. Ref.94

VAR_001643

Natural variant

221

1

G → C in OI1; mild form. Ref.62

VAR_001644

Natural variant

224

1

G → C in OI1; mild phenotype.

VAR_001645

Natural variant

242

1

G → D in OI. Ref.93

VAR_063296

Natural variant

257

1

G → R in OI4. Ref.92 Ref.93

VAR_063297

Natural variant

263

1

G → R in OI1; mild form. Ref.55

VAR_001646

Natural variant

263

1

G → V in OI1; mild form. Ref.68

VAR_001647

Natural variant

266

1

G → E in OI1. Ref.99

VAR_063298

Natural variant

272

1

G → C in OI1. Ref.44

VAR_001648

Natural variant

275

1

G → D in OI2.

VAR_001649

Natural variant

287

1

G → S in OI1. Ref.99

VAR_063299

Natural variant

288

1

E → K in a patient with osteogenesis imperfecta type 1 carrying also mutation Glu-1219; unknown pathological significance. Ref.94

VAR_063300

Natural variant

288

1

E → V in a patient with osteogenesis imperfecta type 2; rare variant of unknown pathological significance. Ref.102

VAR_063301

Natural variant

312

1

R → C in EDS1. Ref.88 Ref.97

VAR_013579

Natural variant

320

1

G → V in OI1. Ref.94

VAR_063302

Natural variant

332

1

G → R in OI3; mild to moderate form. Ref.52 Ref.78

VAR_001650

Natural variant

338

1

G → C in OI4. Ref.94

VAR_063303

Natural variant

349

1

V → F in OI1. Ref.101

VAR_063304

Natural variant

350

1

G → R in OI3. Ref.75

VAR_001651

Natural variant

353

1

G → C in OI4. Ref.66

VAR_001652

Natural variant

353

1

G → D in OI2. Ref.102

VAR_063305

Natural variant

353

1

G → S in OI4. Ref.99

VAR_063306

Natural variant

356

1

G → C in OI4; mild form. Ref.53

VAR_001653

Natural variant

368

1

G → V in OI2. Ref.102

VAR_063307

Natural variant

383

1

G → C in OI4.

VAR_001654

Natural variant

389

1

G → C in OI; moderate form.

VAR_001655

Natural variant

389

1

G → R in OI2. Ref.74

VAR_001656

Natural variant

390

1

A → T in a patient with osteogenesis imperfecta type 2; rare variant of unknown pathological significance. Ref.102

VAR_063308

Natural variant

398

1

G → A in OI4. Ref.84

VAR_001657

Natural variant

398

1

G → D in OI2.

VAR_001658

Natural variant

401

1

G → C in OI4.

VAR_001659

Natural variant

404

1

G → C in OI; moderate form.

VAR_001660

Natural variant

422

1

G → C in OI2. Ref.45

VAR_001661

Natural variant

425

1

G → S in OI2; lethal form. Ref.70 Ref.102

VAR_001662

Natural variant

434

1

G → V in OI2. Ref.39 Ref.63

VAR_001663

Natural variant

455

1

G → D in OI2. Ref.102

VAR_063309

Natural variant

470

1

G → V in OI2. Ref.102

VAR_063310

Natural variant

476

1

G → R in OI2.
Corresponds to variant rs57377812 [ dbSNP | Ensembl ].

VAR_001664

Natural variant

509

1

G → V in OI2. Ref.102

VAR_063311

Natural variant

527

1

G → C in OI4. Ref.84

VAR_001665

Natural variant

530

1

G → S in OI2, OI3 and OI4; mild to lethal form. Ref.65 Ref.70 Ref.72

VAR_001666

Natural variant

533

1

G → D in OI2.

VAR_001667

Natural variant

548

1

G → A in OI2. Ref.102

VAR_063312

Natural variant

555

1

P → R in OI1. Ref.94

VAR_063313

Natural variant

560

1

G → C in OI4.

VAR_001669

Natural variant

560

1

G → R in OI2.

VAR_001670

Natural variant

560

1

G → S in OI4. Ref.70

VAR_001668

Natural variant

564

1

R → H.
Corresponds to variant rs1800211 [ dbSNP | Ensembl ].

VAR_001671

Natural variant

569

1

G → R in OI2. Ref.35

VAR_001672

Natural variant

574

1

R → C in a patient with isolated osteopenia and vascular rupture. Ref.97

VAR_063314

Natural variant

581

1

G → R in OI2. Ref.94

VAR_063315

Natural variant

593

1

G → C in OI3 and OI4. Ref.57

VAR_001673

Natural variant

593

1

G → S in OI2 and OI3; moderate to lethal form. Ref.71

VAR_001674

Natural variant

602

1

G → R in OI2. Ref.102

VAR_063316

Natural variant

605

1

G → D in OI2. Ref.102

VAR_063317

Natural variant

614

1

G → R in OI2. Ref.102

VAR_063318

Natural variant

647

1

G → S in OI1. Ref.94

VAR_063319

Natural variant

656

1

G → S in OI2. Ref.85

VAR_001676

Natural variant

683

1

G → S in OI4. Ref.92

VAR_063320

Natural variant

701

1

G → C in OI4. Ref.84

VAR_001677

Natural variant

704

1

G → C in OI3. Ref.44

VAR_001678

Natural variant

719

1

G → D in OI2. Ref.49

VAR_001679

Natural variant

719

1

G → S in OI3. Ref.70

VAR_001680

Natural variant

722

1

G → S in OI1. Ref.93

VAR_063321

Natural variant

728

1

G → R in OI2. Ref.22

VAR_001681

Natural variant

734

1

G → V in OI2. Ref.94

VAR_063322

Natural variant

737

1

G → D in OI2.

VAR_001682

Natural variant

740

1

G → R in OI2. Ref.102

VAR_063323

Natural variant

743

1

G → S in OI2.

VAR_001683

Natural variant

743

1

G → V in OI2. Ref.69

VAR_001684

Natural variant

764

1

G → V in OI2. Ref.83

VAR_001685

Natural variant

767

1

G → S in OI3; severe. Ref.23 Ref.93

VAR_001686

Natural variant

776

1

G → S in OI2. Ref.46

VAR_001687

Natural variant

809

1

G → S in OI2. Ref.46 Ref.102

VAR_001688

Natural variant

815

1

G → V in OI2. Ref.54

VAR_001689

Natural variant

821

1

G → S in OI3. Ref.82 Ref.92 Ref.93

VAR_001690

Natural variant

823

1

P → A. Ref.70
Corresponds to variant rs1800214 [ dbSNP | Ensembl ].

VAR_001691

Natural variant

824

1

G → R in OI2. Ref.102

VAR_063324

Natural variant

833

1

G → D in OI2. Ref.95

VAR_063325

Natural variant

839

1

G → S in OI2; mild to moderate form. Ref.79

VAR_001692

Natural variant

842

1

G → R in OI2. Ref.37

VAR_001693

Natural variant

845

1

G → R in OI2. Ref.102

VAR_001694

Natural variant

848

1

G → R in OI2. Ref.102

VAR_063342

Natural variant

851

1

G → D in OI2.

VAR_001695

Natural variant

855

1

N → H in a patient with osteogenesis imperfecta type 2; rare variant of unknown pathological significance. Ref.102

VAR_063326

Natural variant

866

1

G → S in OI3 and OI2. Ref.87 Ref.101 Ref.102

VAR_008118

Natural variant

869

1

G → C in OI2. Ref.50

VAR_001696

Natural variant

875

1

G → S in OI2. Ref.102

VAR_063327

Natural variant

884

1

G → S in OI2 and OI3; extremely severe form. Ref.102

VAR_001697

Natural variant

896

1

G → C in OI2. Ref.44

VAR_001698

Natural variant

896

1

G → D in OI2. Ref.102

VAR_063328

Natural variant

906

1

G → S in a patient with mild osteogenesis imperfecta; uncertain pathological significance. Ref.94

VAR_063329

Natural variant

926

1

G → C in OI2. Ref.36 Ref.51

VAR_001699

Natural variant

947

1

G → C in OI2. Ref.102

VAR_063330

Natural variant

977

1

G → D in OI2. Ref.102

VAR_063331

Natural variant

980

1

G → V in OI2. Ref.60

VAR_001700

Natural variant

1001

1

G → C in OI2. Ref.102

VAR_063332

Natural variant

1010

1

G → S in OI4. Ref.40

VAR_001701

Natural variant

1014

1

R → C in CAFFD. Ref.91

VAR_033097

Natural variant

1019

1

G → A. Ref.1 Ref.18
Corresponds to variant rs1135348 [ dbSNP | Ensembl ].

VAR_030013

Natural variant

1022

1

G → S in OI3; severe form. Ref.42

VAR_001702

Natural variant

1022

1

G → V in OI2. Ref.102

VAR_001703

Natural variant

1025

1

G → R in OI2. Ref.47

VAR_001704

Natural variant

1040

1

G → S in OI2 and OI3; moderate to lethal form. Ref.82 Ref.101

VAR_001705

Natural variant

1043

1

G → S in OI2.

VAR_001706

Natural variant

1046 – 1048

3

Missing in OI2.

VAR_001707

Natural variant

1049

1

G → S in OI3. Ref.82

VAR_001708

Natural variant

1052

1

G → GAPG in OI2.

VAR_063333

Natural variant

1055

1

G → D in OI2. Ref.102

VAR_063334

Natural variant

1058

1

G → S in OI3 and OI4; mild form. Ref.82 Ref.93

VAR_001709

Natural variant

1061

1

G → D in OI2.

VAR_001710

Natural variant

1061

1

G → S in OI4. Ref.77

VAR_001711

Natural variant

1066

1

R → 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 variant

1075

1

T → 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 variant

1076

1

G → S in OI3; severe form. Ref.82

VAR_001713

Natural variant

1079

1

G → S in OI1 and OI2; mild to moderate form. Ref.59

VAR_001714

Natural variant

1082

1

G → C in OI2. Ref.43

VAR_001715

Natural variant

1088

1

G → A in OI2. Ref.67

VAR_001716

Natural variant

1091

1

G → S in OI2. Ref.48

VAR_001717

Natural variant

1093

1

R → C in a patient with isolated osteopenia and vascular rupture. Ref.97

VAR_063336

Natural variant

1094

1

G → S in OI2. Ref.102

VAR_063337

Natural variant

1100

1

G → D in OI2. Ref.102

VAR_001718

Natural variant

1106

1

G → A in OI2. Ref.41

VAR_001719

Natural variant

1124

1

G → C in OI2. Ref.76

VAR_001720

Natural variant

1141

1

R → Q. Ref.100
Corresponds to variant rs41316713 [ dbSNP | Ensembl ].

VAR_033778

Natural variant

1142

1

G → S in OI2.

VAR_001721

Natural variant

1151

1

G → S in OI3.

VAR_001722

Natural variant

1151

1

G → V in OI2. Ref.41 Ref.63

VAR_001723

Natural variant

1154

1

G → R in OI2. Ref.41

VAR_001724

Natural variant

1157

1

G → D in OI1. Ref.96

VAR_063338

Natural variant

1166

1

G → C in OI2. Ref.34

VAR_001725

Natural variant

1172

1

G → D in OI2. Ref.85

VAR_001726

Natural variant

1177

1

V → I. Ref.100
Corresponds to variant rs41316719 [ dbSNP | Ensembl ].

VAR_033779

Natural variant

1181

1

G → S in OI2. Ref.48 Ref.52

VAR_001727

Natural variant

1184

1

G → V in OI2. Ref.41 Ref.63

VAR_001728

Natural variant

1187

1

G → S in OI2 and OI3; extremely severe form. Ref.48

VAR_001729

Natural variant

1187

1

G → V in OI2. Ref.48

VAR_001730

Natural variant

1195

1

G → C in OI1; mild form. Ref.26 Ref.38

VAR_001731

Natural variant

1219

1

D → E in OI1. Ref.94

VAR_063339

Natural variant

1219

1

D → 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 variant

1251

1

S → T. Ref.25
Corresponds to variant rs3205325 [ dbSNP | Ensembl ].

VAR_030014

Natural variant

1277

1

D → H in OI2; impaired pro-alpha chain association. Ref.25

VAR_001732

Natural variant

1312

1

W → C in OI2. Ref.64

VAR_001733

Natural variant

1337 – 1338

2

Missing in OI2; impaired pro-alpha chain association.

VAR_001734

Natural variant

1356

1

R → H. Ref.94

VAR_063340

Natural variant

1388

1

L → R in OI2; impaired pro-alpha chain association. Ref.25

VAR_001735

Natural variant

1391

1

Q → K. Ref.1 Ref.2 Ref.27
Corresponds to variant rs2586486 [ dbSNP | Ensembl ].

VAR_030015

Natural variant

1413

1

D → N in OI2. Ref.94 Ref.102

VAR_063341

Natural variant

1430

1

K → N.
Corresponds to variant rs1059454 [ dbSNP | Ensembl ].

VAR_033780

Natural variant

1431

1

T → P.
Corresponds to variant rs1059454 [ dbSNP | Ensembl ].

VAR_033781

Natural variant

1434

1

T → S. Ref.1 Ref.25
Corresponds to variant rs1800220 [ dbSNP | Ensembl ].

VAR_001736

Natural variant

1438

1

P → R. Ref.5
Corresponds to variant rs17857117 [ dbSNP | Ensembl ].

VAR_030016

Natural variant

1460

1

P → H. Ref.5
Corresponds to variant rs17853657 [ dbSNP | Ensembl ].

VAR_030017

Natural variant

1464

1

L → P in OI3. Ref.80

VAR_001737

Experimental info

Sequence conflict

59

1

R → Q in CAA25394. Ref.8

Sequence conflict

112 – 114

3

Missing in AAB94054. Ref.2

Sequence conflict

288

1

E → P AA sequence Ref.15

Sequence conflict

370

1

R → L in AAB59373. Ref.6

Sequence conflict

484

1

P → L in AAA52289. Ref.19

Sequence conflict

595

1

A → R in AAA51847. Ref.20

Sequence conflict

721

1

Q → E no nucleotide entry Ref.22

Sequence conflict

738

1

L → E no nucleotide entry Ref.22

Sequence conflict

975 – 976

2

LP → PL in AAA52291. Ref.19

Sequence conflict

1081

1

V → A in AAA51995. Ref.18

Sequence conflict

1329

1

S → T in AAB27856. Ref.25

Secondary structure

1

.

.

.

.

.

1464

Helix Strand Turn

Details...

Beta strand

263 – 266

4

Beta strand

966 – 968

3

Sequences

	Sequence		Length	Mass (Da)
	P02452 [UniParc]. Last modified May 18, 2010. Version 5. Checksum: F0EC4DE778FFFC11	FASTA	1,464	138,941
	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

References

	« Hide 'large scale' referencesShow '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, 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.

Web resources

Osteogenesis imperfecta variant database

Collagen type I alpha 1 (COL1A1)

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

Wikipedia

Type-I collagen entry

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.

IPI

IPI00297646.

PIR

CGHU1S. I60114.

RefSeq

NP_000079.2. NM_000088.3.

UniGene

Hs.172928.
Hs.681002.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Q7D	X-ray	1.80	A/B/C	914-930	[»]
2LLP	NMR	-	A/B/C	949-965	[»]
3EJH	X-ray	2.10	E/F	956-977	[»]
3GXE	X-ray	2.60	E/F	254-275	[»]

ProteinModelPortal

P02452.

SMR

P02452. Positions 1247-1464.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-36077N.

IntAct

P02452. 10 interactions.

PTM databases

PhosphoSite

P02452.

Polymorphism databases

DMDM

296439504.

2D gel databases

DOSAC-COBS-2DPAGE

P02452.

Proteomic databases

PaxDb

P02452.

PRIDE

P02452.

Protocols and materials databases

DNASU

1277.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000225964; ENSP00000225964; ENSG00000108821.

GeneID

1277.

KEGG

hsa:1277.

UCSC

uc002iqm.3. human.

Organism-specific databases

CTD

1277.

GeneCards

GC17M048260.

HGNC

HGNC:2197. COL1A1.

HPA

HPA008405.
HPA011795.

MIM

114000. phenotype.
120150. gene.
130000. phenotype.
130060. phenotype.
166200. phenotype.
166210. phenotype.
166220. phenotype.
166710. phenotype.
259420. phenotype.
607907. phenotype.

neXtProt

NX_P02452.

Orphanet

1310. 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.
216796. Osteogenesis imperfecta type 1.
216804. Osteogenesis imperfecta type 2.
216812. Osteogenesis imperfecta type 3.
216820. Osteogenesis imperfecta type 4.

PharmGKB

PA35041.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG12793.

HOVERGEN

HBG004933.

InParanoid

P02452.

KO

K06236.

OMA

VAYMDQQ.

OrthoDB

EOG4S4PHP.

PhylomeDB

P02452.

Enzyme and pathway databases

Pathway_Interaction_DB

il4_2pathway. IL4-mediated signaling events.
lymphangiogenesis_pathway. VEGFR3 signaling in lymphatic endothelium.

Reactome

REACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_118779. Extracellular matrix organization.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P02452.

Bgee

P02452.

Genevestigator

P02452.

GermOnline

ENSG00000108821. Homo sapiens.

Family and domain databases

InterPro

IPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_C.
[Graphical view]

Pfam

PF01410. COLFI. 1 hit.
PF01391. Collagen. 13 hits.
PF00093. VWC. 1 hit.
[Graphical view]

ProDom

PD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00038. COLFI. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]

PROSITE

PS51461. NC1_FIB. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL3030.

ChiTaRS

COL1A1. human.

DrugBank

DB00048. Collagenase.
DB00039. Palifermin.

EvolutionaryTrace

P02452.

GenomeRNAi

1277.

NextBio

5161.

PMAP-CutDB

P02452.

SOURCE

Search...

Entry information

Entry name

CO1A1_HUMAN

Accession

Primary (citable) accession number: P02452
Secondary accession number(s): O76045 , 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:	May 1, 2013
This is version 174 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.