P02458 (CO2A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Collagen alpha-1(II) chain

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

Cleaved into the following 2 chains:

1. Collagen alpha-1(II) chain
2. Chondrocalcin

Gene names

Name:

COL2A1

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	1487 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 II collagen is specific for cartilaginous tissues. It is essential for the normal embryonic development of the skeleton, for linear growth and for the ability of cartilage to resist compressive forces.
Subunit structure	Homotrimers of alpha 1(II) chains.
Subcellular location	Secreted › extracellular space › extracellular matrix By similarity.
Tissue specificity	Isoform 2 is highly expressed in juvenile chondrocyte and low in fetal chondrocyte. Ref.11
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	Probably 3-hydroxylated on prolines by LEPREL1 By similarity. 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. The N-telopeptide is covalently linked to the helical COL2 region of alpha 1(IX), alpha 2(IX) and alpha 3(IX) chain. The C-telopeptide is covalently linked to an another site in the helical region of alpha 3(IX) COL2.
Involvement in disease	Spondyloepiphyseal dysplasia congenital type (SEDC) [MIM:183900]: Disorder characterized by disproportionate short stature and pleiotropic involvement of the skeletal and ocular systems. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.22 Ref.23 Ref.42 Ref.43 Ref.46 Ref.48 Ref.56 Ref.59 Spondyloepimetaphyseal dysplasia, Strudwick type (SEMDSTWK) [MIM:184250]: A bone disease characterized by disproportionate short stature from birth, with a very short trunk and shortened limbs, and skeletal abnormalities including lordosis, scoliosis, flattened vertebrae, pectus carinatum, coxa vara, clubfoot, and abnormal epiphyses or metaphyses. A distinctive radiographic feature is irregular sclerotic changes, described as dappled in the metaphyses of the long bones. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.38 Ref.50 Ref.65 Achondrogenesis 2 (ACG2) [MIM:200610]: A disease characterized by the absence of ossification in the vertebral column, sacrum and pubic bones. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.33 Ref.47 Ref.48 Ref.49 Ref.57 Ref.58 Ref.69 Legg-Calve-Perthes disease (LCPD) [MIM:150600]: Characterized by loss of circulation to the femoral head, resulting in avascular necrosis in a growing child. Clinical pictures of the disease vary, depending on the phase of disease progression through ischemia, revascularization, fracture and collapse, and repair and remodeling of the bone. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.70 Kniest dysplasia (KD) [MIM:156550]: Moderately severe chondrodysplasia phenotype that results from mutations in the COL2A1 gene. Characteristics of the disorder include a short trunk and extremities, mid-face hypoplasia, cleft palate, myopia, retinal detachment, and hearing loss. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.45 Ref.52 Primary avascular necrosis of femoral head (ANFH) [MIM:608805]: Causes disability that often requires surgical intervention. Most cases are sporadic, but families in which there is an autosomal dominant inheritance of the disease have been identified. It has been estimated that 300,000 to 600,000 people in the United States have ANFH. Approximately 15,000 new cases of this common and disabling disorder are reported annually. The age at the onset is earlier than that for osteoarthritis. The diagnosis is typically made when patients are between the ages of 30 and 60 years. The clinical manifestations, such as pain on exertion, a limping gait, and a discrepancy in leg length, cause considerable disability. Moreover, nearly 10 percent of the 500,000 total-hip arthroplasties performed each year in the United States involve patients with ANFH. As a result, this disease creates a substantial socioeconomic cost as well as a burden for patients and their families. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.67 Osteoarthritis with mild chondrodysplasia (OACD) [MIM:604864]: Osteoarthritis is a common disease that produces joint pain and stiffness together with radiologic evidence of progressive degeneration of joint cartilage. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.34 Ref.35 Ref.39 Ref.48 Platyspondylic lethal skeletal dysplasia Torrance type (PLSD-T) [MIM:151210]: Platyspondylic lethal skeletal dysplasias (PLSDs) are a heterogeneous group of chondrodysplasias characterized by severe platyspondyly and limb shortening. PLSD-T is characterized by varying platyspondyly, short ribs with anterior cupping, hypoplasia of the lower ilia with broad ischial and pubic bones, and shortening of the tubular bones with splayed and cupped metaphyses. Histology of the growth plate typically shows focal hypercellularity with slightly enlarged chondrocytes in the resting cartilage and relatively well-preserved columnar formation and ossification at the chondro-osseous junction. PLSD-T is generally a perinatally lethal disease, but a few long-term survivors have been reported. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.58 Ref.63 Ref.64 Multiple epiphyseal dysplasia with myopia and conductive deafness (EDMMD) [MIM:132450]: A generalized skeletal dysplasia associated with significant morbidity. Joint pain, joint deformity, waddling gait, and short stature are the main clinical signs and symptoms. EDMMD is an autosomal dominant disorder characterized by epiphyseal dysplasia associated with progressive myopia, retinal thinning, crenated cataracts, conductive deafness. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.53 Spondyloperipheral dysplasia (SPD) [MIM:271700]: SPD patients manifest short stature, midface hypoplasia, sensorineural hearing loss, spondyloepiphyseal dysplasia, platyspondyly and brachydactyly. Note: The disease is caused by mutations affecting the gene represented in this entry. Stickler syndrome 1 (STL1) [MIM:108300]: An autosomal dominant form of Stickler syndrome, an inherited disorder that associates ocular signs with more or less complete forms of Pierre Robin sequence, bone disorders and sensorineural deafness. Ocular disorders may include juvenile cataract, myopia, strabismus, vitreoretinal or chorioretinal degeneration, retinal detachment, and chronic uveitis. Robin sequence includes an opening in the roof of the mouth (a cleft palate), a large tongue (macroglossia), and a small lower jaw (micrognathia). Bones are affected by slight platyspondylisis and large, often defective epiphyses. Juvenile joint laxity is followed by early signs of arthrosis. The degree of hearing loss varies among affected individuals and may become more severe over time. Syndrome expressivity is variable. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.37 Ref.44 Ref.55 Ref.68 Ref.73 Ref.75 Stickler syndrome 1 non-syndromic ocular (STL1O) [MIM:609508]: An autosomal dominant form of Stickler syndrome characterized by the ocular signs typically seen in Stickler syndrome type 1 such as cataract, myopia, retinal detachment. Systemic features of premature osteoarthritis, cleft palate, hearing impairment, and craniofacial abnormalities are either absent or very mild. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.37 Ref.68 Ref.73 Rhegmatogenous retinal detachment autosomal dominant (DRRD) [MIM:609508]: A eye disease that most frequently results from a break or tear in the retina that allows fluid from the vitreous humor to enter the potential space beneath the retina. It is often associated with pathologic myopia and in most cases leads to visual impairment or blindness if untreated. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.55 Ref.66 Czech dysplasia (CZECHD) [MIM:609162]: A skeletal dysplasia characterized by early-onset, progressive pseudorheumatoid arthritis, platyspondyly, and short third and fourth toes. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.41 Ref.48 Ref.71 Ref.74
Sequence similarities	Belongs to the fibrillar collagen family. Contains 1 fibrillar collagen NC1 domain. Contains 1 VWFC domain.
Sequence caution	The sequence AAH07252.1 differs from that shown. Reason: Frameshift at position 1198.

Ontologies

Keywords
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Cataract Deafness Disease mutation Dwarfism Stickler syndrome
Domain	Collagen Repeat Signal
Ligand	Calcium Metal-binding
PTM	Disulfide bond Glycoprotein Hydroxylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	axon guidance Traceable author statement. Source: Reactome cartilage condensation Inferred from electronic annotation. Source: Compara cartilage development Traceable author statement Ref.50. Source: BHF-UCL cartilage development involved in endochondral bone morphogenesis Inferred from electronic annotation. Source: Compara cellular response to BMP stimulus Inferred from electronic annotation. Source: Compara central nervous system development Inferred from electronic annotation. Source: Compara chondrocyte differentiation Inferred from electronic annotation. Source: Compara collagen fibril organization Inferred from mutant phenotype Ref.20. Source: BHF-UCL embryonic skeletal joint morphogenesis Inferred from mutant phenotype Ref.68. Source: BHF-UCL endochondral ossification Inferred from electronic annotation. Source: Compara heart morphogenesis Inferred from electronic annotation. Source: Compara inner ear morphogenesis Inferred from electronic annotation. Source: Compara limb bud formation Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara notochord development Inferred from electronic annotation. Source: Compara otic vesicle development Inferred from electronic annotation. Source: Compara palate development Inferred from electronic annotation. Source: Compara proteoglycan metabolic process Inferred from electronic annotation. Source: Compara regulation of gene expression Inferred from electronic annotation. Source: Compara sensory perception of sound Inferred from mutant phenotype Ref.68. Source: BHF-UCL tissue homeostasis Inferred from electronic annotation. Source: Compara visual perception Inferred from mutant phenotype PubMed 10486316. Source: UniProtKB
Cellular_component	basement membrane Inferred from electronic annotation. Source: Compara collagen type II Inferred from direct assay Ref.13. Source: BHF-UCL endoplasmic reticulum lumen Traceable author statement. Source: Reactome extracellular space Inferred from electronic annotation. Source: Compara
Molecular_function	extracellular matrix structural constituent conferring tensile strength Inferred by curator Ref.13. Source: BHF-UCL identical protein binding Non-traceable author statement Ref.1. Source: BHF-UCL 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...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 2 (identifier: P02458-2)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 1 (identifier: P02458-1)

The sequence of this isoform differs from the canonical sequence as follows:
     29-98: QEAGSCVQDGQRYNDKDVWKPEPCRICVCDTGTVLCDDIICEDVKDCLSPEIPFGECCPICPTDLATASG → R

Isoform 3 (identifier: P02458-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1219: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

25

Potential

Propeptide

26 – 181

156

N-terminal propeptide

PRO_0000005729

Chain

182 – 1241

1060

Collagen alpha-1(II) chain

PRO_0000005730

Chain

1242 – 1487

246

Chondrocalcin

PRO_0000005731

Regions

Domain

32 – 90

59

VWFC

Domain

1253 – 1487

235

Fibrillar collagen NC1

Region

201 – 1214

1014

Triple-helical region

Region

1215 – 1241

27

Nonhelical region (C-terminal)

Sites

Metal binding

1301

1

Calcium By similarity

Metal binding

1303

1

Calcium By similarity

Metal binding

1304

1

Calcium; via carbonyl oxygen By similarity

Metal binding

1306

1

Calcium; via carbonyl oxygen By similarity

Metal binding

1309

1

Calcium By similarity

Site

181 – 182

2

Cleavage; by procollagen N-endopeptidase By similarity

Site

1241 – 1242

2

Cleavage; by procollagen C-endopeptidase By similarity

Amino acid modifications

Modified residue

190

1

5-hydroxylysine By similarity

Modified residue

287

1

5-hydroxylysine By similarity

Modified residue

299

1

5-hydroxylysine By similarity

Modified residue

308

1

5-hydroxylysine By similarity

Modified residue

374

1

5-hydroxylysine By similarity

Modified residue

608

1

5-hydroxylysine By similarity

Modified residue

620

1

5-hydroxylysine By similarity

Modified residue

670

1

3-hydroxyproline By similarity

Modified residue

907

1

3-hydroxyproline By similarity

Modified residue

1130

1

5-hydroxylysine By similarity

Modified residue

1144

1

3-hydroxyproline By similarity

Modified residue

1186

1

3-hydroxyproline By similarity

Modified residue

1201

1

3-hydroxyproline By similarity

Modified residue

1207

1

3-hydroxyproline By similarity

Modified residue

1213

1

3-hydroxyproline By similarity

Glycosylation

190

1

O-linked (Gal...) By similarity

Glycosylation

287

1

O-linked (Gal...) By similarity

Glycosylation

299

1

O-linked (Gal...) By similarity

Glycosylation

308

1

O-linked (Gal...) By similarity

Glycosylation

374

1

O-linked (Gal...) By similarity

Glycosylation

608

1

O-linked (Gal...) By similarity

Glycosylation

620

1

O-linked (Gal...) By similarity

Glycosylation

1130

1

O-linked (Gal...) By similarity

Glycosylation

1388

1

N-linked (GlcNAc...)

Disulfide bond

1283 ↔ 1315

By similarity

Disulfide bond

1289

Interchain (with C-1306) By similarity

Disulfide bond

1306

Interchain (with C-1289) By similarity

Disulfide bond

1323 ↔ 1485

By similarity

Disulfide bond

1393 ↔ 1438

By similarity

Natural variations

Alternative sequence

1 – 1219

1219

Missing in isoform 3.

VSP_022365

Alternative sequence

29 – 98

70

QEAGS…ATASG → R in isoform 1.

VSP_022366

Natural variant

9

1

T → S. Ref.1 Ref.2 Ref.6 Ref.7 Ref.8 Ref.72
Corresponds to variant rs3803183 [ dbSNP | Ensembl ].

VAR_017638

Natural variant

57

1

C → Y in STL1O. Ref.73

VAR_063891

Natural variant

142

1

E → D. Ref.72
Corresponds to variant rs34392760 [ dbSNP | Ensembl ].

VAR_033782

Natural variant

158

1

P → L. Ref.1
Corresponds to variant rs1050861 [ dbSNP | Ensembl ].

VAR_019836

Natural variant

240

1

G → D in STL1. Ref.75

VAR_063892

Natural variant

267

1

G → D in STL1O. Ref.37

VAR_001738

Natural variant

270

1

G → R in STL1. Ref.75

VAR_063893

Natural variant

275

1

R → C in CZECHD. Ref.41 Ref.48 Ref.71 Ref.74

VAR_001739

Natural variant

282

1

G → D in STL1. Ref.75

VAR_063894

Natural variant

302 – 308

7

Missing in STL1.

VAR_001740

Natural variant

303

1

G → D in KD; abnormal allele expressed in the cartilage. Ref.45

VAR_001741

Natural variant

318

1

G → R in DRRD. Ref.66

VAR_023925

Natural variant

354

1

G → R in spondylometaphyseal dysplasia; congenital type. Ref.40

VAR_001742

Natural variant

375

1

G → R in SEDC.

VAR_001743

Natural variant

447

1

G → S in SEDC. Ref.46

VAR_001744

Natural variant

453

1

G → A in STL1. Ref.75

VAR_063895

Natural variant

453

1

G → D in ACG2. Ref.57

VAR_017639

Natural variant

453

1

G → V in ACG2. Ref.57

VAR_017640

Natural variant

492

1

G → V in SEMDSTWK. Ref.50

VAR_001745

Natural variant

501

1

G → R in STL1. Ref.75

VAR_063896

Natural variant

504

1

G → C in SEMDSTWK. Ref.50

VAR_001746

Natural variant

510

1

G → D in ACG2.

VAR_001747

Natural variant

513

1

G → S in ACG2. Ref.58

VAR_024819

Natural variant

516

1

G → D in ACGA2. Ref.61

VAR_023926

Natural variant

547

1

D → V in ACG2. Ref.69

VAR_063897

Natural variant

565

1

R → C in STL1. Ref.55

VAR_023927

Natural variant

638

1

T → I. Ref.72
Corresponds to variant rs41263847 [ dbSNP | Ensembl ].

VAR_033783

Natural variant

667

1

L → F in DRRD. Ref.55 Ref.66

VAR_023928

Natural variant

717

1

G → S in ANFH. Ref.67

VAR_023929

Natural variant

717

1

G → V in ACG2. Ref.58

VAR_024820

Natural variant

719

1

R → C in OACD; also in mild spondyloepiphyseal dysplasia and precocious osteoarthritis. Ref.34 Ref.35 Ref.39 Ref.48 Ref.54

VAR_001748

Natural variant

771

1

G → A in ACG2. Ref.58

VAR_024821

Natural variant

771

1

G → D in ACG2. Ref.57

VAR_017641

Natural variant

774

1

G → S in SEDC and hypochondrogenesis; lethal. Ref.36

VAR_001749

Natural variant

780

1

G → R in ACG2. Ref.57

VAR_017642

Natural variant

795

1

G → R in ACG2. Ref.57

VAR_017643

Natural variant

804

1

G → A in hypochondrogenesis.

VAR_001751

Natural variant

855

1

G → S in SEDC.

VAR_023930

Natural variant

891

1

G → R in ACG2 and SEDC. Ref.47 Ref.48

VAR_001752

Natural variant

894

1

G → E in ACG2. Ref.57

VAR_017644

Natural variant

897

1

G → V in SEMDSTWK. Ref.38

VAR_023931

Natural variant

904

1

R → C in EDMMD and STL1. Ref.53 Ref.75

VAR_017645

Natural variant

909

1

G → C in SEMDSTWK. Ref.38 Ref.50

VAR_001753

Natural variant

948

1

G → D in ACG2. Ref.57

VAR_017646

Natural variant

969

1

G → S in ACG2. Ref.49

VAR_001754

Natural variant

981

1

G → S in ACG2. Ref.57

VAR_017647

Natural variant

989

1

R → C in SEDC. Ref.42

VAR_001755

Natural variant

992

1

R → G in SEMDSTWK. Ref.65

VAR_023932

Natural variant

1005

1

G → S in hypochondrogenesis.

VAR_001756

Natural variant

1017 – 1022

6

Missing in hypochondrogenesis.

VAR_017648

Natural variant

1017

1

G → V in ACG2.

VAR_001757

Natural variant

1051

1

A → T. Ref.72
Corresponds to variant rs41272041 [ dbSNP | Ensembl ].

VAR_033784

Natural variant

1053

1

G → E in hypochondrogenesis; lethal. Ref.20

VAR_001758

Natural variant

1065

1

G → V in ACG2. Ref.57

VAR_017649

Natural variant

1110

1

G → C in ACG2. Ref.58

VAR_001759

Natural variant

1113

1

G → C in hypochondrogenesis. Ref.51

VAR_001760

Natural variant

1119

1

G → R in ACG2. Ref.57

VAR_017650

Natural variant

1143

1

G → S in ACG2. Ref.33 Ref.58

VAR_001761

Natural variant

1158

1

G → A in STL1. Ref.75

VAR_063898

Natural variant

1164 – 1199

36

Missing in SEDC.

VAR_001762

Natural variant

1170

1

G → S in ANFH and in LCPD. Ref.67 Ref.70

VAR_023933

Natural variant

1173

1

G → R in SEDC. Ref.56

VAR_017651

Natural variant

1176

1

G → S in SEDC. Ref.48

VAR_001763

Natural variant

1176

1

G → V Mutation found in a patient with features of multiple epiphyseal dysplasia; features overlap with SEDC. Ref.76

VAR_066836

Natural variant

1179

1

G → R Mutation found in a patient with features of multiple epiphyseal dysplasia; features overlap with SEDC. Ref.76

VAR_066837

Natural variant

1184

1

I → IGPSGKDGANGIPGPI in SEDC.

VAR_019837

Natural variant

1188

1

G → R in ACG2. Ref.48

VAR_001764

Natural variant

1197

1

G → S in SEDC. Ref.43

VAR_001765

Natural variant

1207 – 1212

6

Missing in KD.

VAR_001766

Natural variant

1305

1

G → D in vitreoretinopathy; with phalangeal epiphyseal dysplasia. Ref.60

VAR_023934

Natural variant

1331

1

V → I. Ref.57 Ref.72
Corresponds to variant rs12721427 [ dbSNP | Ensembl ].

VAR_017652

Natural variant

1390

1

T → N in PLSD-T; phenotype previously considered as achondrogenesis-hypochondrogenesis type 2. Ref.58 Ref.64

VAR_024822

Natural variant

1391

1

Y → C in PLSD-T. Ref.63

VAR_023935

Natural variant

1405

1

G → S. Ref.72
Corresponds to variant rs2070739 [ dbSNP | Ensembl ].

VAR_033785

Natural variant

1439

1

T → M in SEDC. Ref.59

VAR_017105

Natural variant

1448

1

T → P in PLSD-T. Ref.64

VAR_024823

Natural variant

1469

1

D → H in PLSD-T. Ref.64

VAR_024824

Natural variant

1484

1

Missing in PLSD-T. Ref.64

VAR_024825

Natural variant

1485

1

C → G in PLSD-T. Ref.64

VAR_024826

Experimental info

Sequence conflict

441

1

G → D in CAA34488. Ref.1

Sequence conflict

457

1

E → K in CAA34488. Ref.1

Sequence conflict

481

1

A → P in AAB60370. Ref.15

Sequence conflict

641

1

A → E in CAA34488. Ref.1

Sequence conflict

641

1

A → E in CAA32030. Ref.16

Sequence conflict

677

1

G → A in CAA32030. Ref.16

Sequence conflict

784

1

G → A in CAA32030. Ref.16

Sequence conflict

832 – 835

4

PAGF → TSGI in CAA34488. Ref.1

Sequence conflict

1006

1

K → Q in CAA34488. Ref.1

Sequence conflict

1006

1

K → Q in CAA32030. Ref.16

Sequence conflict

1037

1

E → Q in CAA34683. Ref.6

Sequence conflict

1057

1

D → N in AAD15287. Ref.17

Sequence conflict

1057

1

D → N in CAA26223. Ref.17

Sequence conflict

1057

1

D → N in AAA51997. Ref.19

Sequence conflict

1069

1

A → T in CAA34683. Ref.6

Sequence conflict

1069

1

A → T in AAD15287. Ref.17

Sequence conflict

1069

1

A → T in CAA26223. Ref.17

Sequence conflict

1069

1

A → T in AAA51997. Ref.19

Sequence conflict

1243

1

Q → E in CAA29604. Ref.24

Sequence conflict

1247

1

G → N in CAA29604. Ref.24

Sequence conflict

1271

1

S → T in AAA52038. Ref.21

Sequence conflict

1274

1

G → A in AAA52038. Ref.21

Sequence conflict

1333

1

K → R in M12048. Ref.28

Sequence conflict

1350

1

G → A in M12048. Ref.28

Sequence conflict

1372

1

N → D in CAA26223. Ref.17

Sequence conflict

1383

1

T → A in CAA26223. Ref.17

Sequence conflict

1400

1

L → M in CAA26223. Ref.17

Secondary structure

1

.

.

.

.

.

.

.

.

.

1487

Helix Strand Turn

Details...

Beta strand

34 – 38

5

Beta strand

51 – 58

8

Beta strand

61 – 66

6

Beta strand

91 – 94

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 2 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: A8312503825BF0BB	FASTA	1,487	141,785
	10 20 30 40 50 60 MIRLGAPQTL VLLTLLVAAV LRCQGQDVQE AGSCVQDGQR YNDKDVWKPE PCRICVCDTG 70 80 90 100 110 120 TVLCDDIICE DVKDCLSPEI PFGECCPICP TDLATASGQP GPKGQKGEPG DIKDIVGPKG 130 140 150 160 170 180 PPGPQGPAGE QGPRGDRGDK GEKGAPGPRG RDGEPGTPGN PGPPGPPGPP GPPGLGGNFA 190 200 210 220 230 240 AQMAGGFDEK AGGAQLGVMQ GPMGPMGPRG PPGPAGAPGP QGFQGNPGEP GEPGVSGPMG 250 260 270 280 290 300 PRGPPGPPGK PGDDGEAGKP GKAGERGPPG PQGARGFPGT PGLPGVKGHR GYPGLDGAKG 310 320 330 340 350 360 EAGAPGVKGE SGSPGENGSP GPMGPRGLPG ERGRTGPAGA AGARGNDGQP GPAGPPGPVG 370 380 390 400 410 420 PAGGPGFPGA PGAKGEAGPT GARGPEGAQG PRGEPGTPGS PGPAGASGNP GTDGIPGAKG 430 440 450 460 470 480 SAGAPGIAGA PGFPGPRGPP GPQGATGPLG PKGQTGEPGI AGFKGEQGPK GEPGPAGPQG 490 500 510 520 530 540 APGPAGEEGK RGARGEPGGV GPIGPPGERG APGNRGFPGQ DGLAGPKGAP GERGPSGLAG 550 560 570 580 590 600 PKGANGDPGR PGEPGLPGAR GLTGRPGDAG PQGKVGPSGA PGEDGRPGPP GPQGARGQPG 610 620 630 640 650 660 VMGFPGPKGA NGEPGKAGEK GLPGAPGLRG LPGKDGETGA AGPPGPAGPA GERGEQGAPG 670 680 690 700 710 720 PSGFQGLPGP PGPPGEGGKP GDQGVPGEAG APGLVGPRGE RGFPGERGSP GAQGLQGPRG 730 740 750 760 770 780 LPGTPGTDGP KGASGPAGPP GAQGPPGLQG MPGERGAAGI AGPKGDRGDV GEKGPEGAPG 790 800 810 820 830 840 KDGGRGLTGP IGPPGPAGAN GEKGEVGPPG PAGSAGARGA PGERGETGPP GPAGFAGPPG 850 860 870 880 890 900 ADGQPGAKGE QGEAGQKGDA GAPGPQGPSG APGPQGPTGV TGPKGARGAQ GPPGATGFPG 910 920 930 940 950 960 AAGRVGPPGS NGNPGPPGPP GPSGKDGPKG ARGDSGPPGR AGEPGLQGPA GPPGEKGEPG 970 980 990 1000 1010 1020 DDGPSGAEGP PGPQGLAGQR GIVGLPGQRG ERGFPGLPGP SGEPGKQGAP GASGDRGPPG 1030 1040 1050 1060 1070 1080 PVGPPGLTGP AGEPGREGSP GADGPPGRDG AAGVKGDRGE TGAVGAPGAP GPPGSPGPAG 1090 1100 1110 1120 1130 1140 PTGKQGDRGE AGAQGPMGPS GPAGARGIQG PQGPRGDKGE AGEPGERGLK GHRGFTGLQG 1150 1160 1170 1180 1190 1200 LPGPPGPSGD QGASGPAGPS GPRGPPGPVG PSGKDGANGI PGPIGPPGPR GRSGETGPAG 1210 1220 1230 1240 1250 1260 PPGNPGPPGP PGPPGPGIDM SAFAGLGPRE KGPDPLQYMR ADQAAGGLRQ HDAEVDATLK 1270 1280 1290 1300 1310 1320 SLNNQIESIR SPEGSRKNPA RTCRDLKLCH PEWKSGDYWI DPNQGCTLDA MKVFCNMETG 1330 1340 1350 1360 1370 1380 ETCVYPNPAN VPKKNWWSSK SKEKKHIWFG ETINGGFHFS YGDDNLAPNT ANVQMTFLRL 1390 1400 1410 1420 1430 1440 LSTEGSQNIT YHCKNSIAYL DEAAGNLKKA LLIQGSNDVE IRAEGNSRFT YTALKDGCTK 1450 1460 1470 1480 HTGKWGKTVI EYRSQKTSRL PIIDIAPMDI GGPEQEFGVD IGPVCFL
	Isoform 1 [UniParc]. Checksum: 1A9E7505AEC4168A	FASTA	1,418	134,389
	10 20 30 40 50 60 MIRLGAPQTL VLLTLLVAAV LRCQGQDVRQ PGPKGQKGEP GDIKDIVGPK GPPGPQGPAG 70 80 90 100 110 120 EQGPRGDRGD KGEKGAPGPR GRDGEPGTPG NPGPPGPPGP PGPPGLGGNF AAQMAGGFDE 130 140 150 160 170 180 KAGGAQLGVM QGPMGPMGPR GPPGPAGAPG PQGFQGNPGE PGEPGVSGPM GPRGPPGPPG 190 200 210 220 230 240 KPGDDGEAGK PGKAGERGPP GPQGARGFPG TPGLPGVKGH RGYPGLDGAK GEAGAPGVKG 250 260 270 280 290 300 ESGSPGENGS PGPMGPRGLP GERGRTGPAG AAGARGNDGQ PGPAGPPGPV GPAGGPGFPG 310 320 330 340 350 360 APGAKGEAGP TGARGPEGAQ GPRGEPGTPG SPGPAGASGN PGTDGIPGAK GSAGAPGIAG 370 380 390 400 410 420 APGFPGPRGP PGPQGATGPL GPKGQTGEPG IAGFKGEQGP KGEPGPAGPQ GAPGPAGEEG 430 440 450 460 470 480 KRGARGEPGG VGPIGPPGER GAPGNRGFPG QDGLAGPKGA PGERGPSGLA GPKGANGDPG 490 500 510 520 530 540 RPGEPGLPGA RGLTGRPGDA GPQGKVGPSG APGEDGRPGP PGPQGARGQP GVMGFPGPKG 550 560 570 580 590 600 ANGEPGKAGE KGLPGAPGLR GLPGKDGETG AAGPPGPAGP AGERGEQGAP GPSGFQGLPG 610 620 630 640 650 660 PPGPPGEGGK PGDQGVPGEA GAPGLVGPRG ERGFPGERGS PGAQGLQGPR GLPGTPGTDG 670 680 690 700 710 720 PKGASGPAGP PGAQGPPGLQ GMPGERGAAG IAGPKGDRGD VGEKGPEGAP GKDGGRGLTG 730 740 750 760 770 780 PIGPPGPAGA NGEKGEVGPP GPAGSAGARG APGERGETGP PGPAGFAGPP GADGQPGAKG 790 800 810 820 830 840 EQGEAGQKGD AGAPGPQGPS GAPGPQGPTG VTGPKGARGA QGPPGATGFP GAAGRVGPPG 850 860 870 880 890 900 SNGNPGPPGP PGPSGKDGPK GARGDSGPPG RAGEPGLQGP AGPPGEKGEP GDDGPSGAEG 910 920 930 940 950 960 PPGPQGLAGQ RGIVGLPGQR GERGFPGLPG PSGEPGKQGA PGASGDRGPP GPVGPPGLTG 970 980 990 1000 1010 1020 PAGEPGREGS PGADGPPGRD GAAGVKGDRG ETGAVGAPGA PGPPGSPGPA GPTGKQGDRG 1030 1040 1050 1060 1070 1080 EAGAQGPMGP SGPAGARGIQ GPQGPRGDKG EAGEPGERGL KGHRGFTGLQ GLPGPPGPSG 1090 1100 1110 1120 1130 1140 DQGASGPAGP SGPRGPPGPV GPSGKDGANG IPGPIGPPGP RGRSGETGPA GPPGNPGPPG 1150 1160 1170 1180 1190 1200 PPGPPGPGID MSAFAGLGPR EKGPDPLQYM RADQAAGGLR QHDAEVDATL KSLNNQIESI 1210 1220 1230 1240 1250 1260 RSPEGSRKNP ARTCRDLKLC HPEWKSGDYW IDPNQGCTLD AMKVFCNMET GETCVYPNPA 1270 1280 1290 1300 1310 1320 NVPKKNWWSS KSKEKKHIWF GETINGGFHF SYGDDNLAPN TANVQMTFLR LLSTEGSQNI 1330 1340 1350 1360 1370 1380 TYHCKNSIAY LDEAAGNLKK ALLIQGSNDV EIRAEGNSRF TYTALKDGCT KHTGKWGKTV 1390 1400 1410 IEYRSQKTSR LPIIDIAPMD IGGPEQEFGV DIGPVCFL
	Isoform 3 [UniParc]. Checksum: E8337954D719ACBF	FASTA	268	29,781
	10 20 30 40 50 60 MSAFAGLGPR EKGPDPLQYM RADQAAGGLR QHDAEVDATL KSLNNQIESI RSPEGSRKNP 70 80 90 100 110 120 ARTCRDLKLC HPEWKSGDYW IDPNQGCTLD AMKVFCNMET GETCVYPNPA NVPKKNWWSS 130 140 150 160 170 180 KSKEKKHIWF GETINGGFHF SYGDDNLAPN TANVQMTFLR LLSTEGSQNI TYHCKNSIAY 190 200 210 220 230 240 LDEAAGNLKK ALLIQGSNDV EIRAEGNSRF TYTALKDGCT KHTGKWGKTV IEYRSQKTSR 250 260 LPIIDIAPMD IGGPEQEFGV DIGPVCFL

References

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[1]	"Nucleotide sequence of the full length cDNA encoding for human type II procollagen." Su M.W., Lee B., Ramirez F., Machado M.A., Horton W.A. Nucleic Acids Res. 17:9473-9473(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS SER-9 AND LEU-158.
[2]	"Conservation of the sizes of 53 introns and over 100 intronic sequences for the binding of common transcription factors in the human and mouse genes for type II procollagen (COL2A1)." Ala-Kokko L., Kvist A.-P., Metsaranta M., Kivirikko K.I., de Crombrugghe B., Prockop D.J., Vuorio E. Biochem. J. 308:923-929(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), VARIANT SER-9. Tissue: Blood.
[3]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[4]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1109-1487 (ISOFORMS 1/2). Tissue: Embryonic stem cell and Muscle.
[6]	"Structure of cDNA clones coding for human type II procollagen. The alpha 1(II) chain is more similar to the alpha 1(I) chain than two other alpha chains of fibrillar collagens." Baldwin C.T., Reginato A.M., Smith C., Jimenez S.A., Prockop D.J. Biochem. J. 262:521-528(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1229 (ISOFORM 1), VARIANT SER-9.
[7]	"Organization of the exons coding for pro alpha 1(II) collagen N-propeptide confirms a distinct evolutionary history of this domain of the fibrillar collagen genes." Su M.W., Benson-Chanda V., Vissing H., Ramirez F. Genomics 4:438-441(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-236 (ISOFORM 1), VARIANT SER-9.
[8]	"The human type II procollagen gene: identification of an additional protein-coding domain and location of potential regulatory sequences in the promoter and first intron." Ryan M.C., Sieraski M., Sandell L.J. Genomics 8:41-48(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-103 (ISOFORM 2), VARIANT SER-9.
[9]	"Promoter region of the human pro-alpha 1(II)-collagen gene." Nunez A.M., Kohno K., Martin G.R., Yamada Y. Gene 44:11-16(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28 (ISOFORMS 1/2).
[10]	"Structural analysis of the regulatory elements of the type-II procollagen gene. Conservation of promoter and first intron sequences between human and mouse." Vikkula M., Metsaranta M., Syvaenen A.-C., Ala-Kokko L., Vuorio E., Peltonen L. Biochem. J. 285:287-294(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28 (ISOFORMS 1/2).
[11]	"Differential expression of a cysteine-rich domain in the amino-terminal propeptide of type II (cartilage) procollagen by alternative splicing of mRNA." Ryan M.C., Sandell L.J. J. Biol. Chem. 265:10334-10339(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 27-103 (ISOFORM 2), TISSUE SPECIFICITY.
[12]	"Genomic organization of the human procollagen alpha 1(II) collagen gene." Huang M.C., Seyer J.M., Thompson J.P., Spinella D.G., Cheah K.S., Kang A.H. Eur. J. Biochem. 195:593-600(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 99-341 (ISOFORMS 1/2). Tissue: Fetal sternum.
[13]	"Collagen type IX from human cartilage: a structural profile of intermolecular cross-linking sites." Diab M., Wu J.J., Eyre D.R. Biochem. J. 314:327-332(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 188-195 AND 1224-1236.
[14]	"Immunohistochemical and biochemical analyses of 20,000-25,000-year-old fossil cartilage." Franc S., Marzin E., Boutillon M.-M., Lafont R., Lechene de la Porte P., Herbage D. Eur. J. Biochem. 234:125-131(1995) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 243-261; 575-590 AND 756-779.
[15]	"An RNA-splicing mutation (G+5IVS20) in the type II collagen gene (COL2A1) in a family with spondyloepiphyseal dysplasia congenita." Tiller G.E., Weis M.A., Polumbo P.A., Gruber H.E., Rimoin D.L., Cohn D.H., Eyre D.R. Am. J. Hum. Genet. 56:388-395(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 440-509 (ISOFORMS 1/2).
[16]	Ramirez F. Submitted (DEC-1988) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 501-1214 (ISOFORMS 1/2).
[17]	"Isolation and partial characterization of the entire human pro alpha 1(II) collagen gene." Sangiorgi F.O., Benson-Chanda V., de Wet W.J., Sobel M.E., Tsipouras P., Ramirez F. Nucleic Acids Res. 13:2207-2225(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 541-578; 784-803; 1056-1109 AND 1200-1487 (ISOFORMS 1/2).
[18]	"Structural analyses of the polymorphic area in type II collagen gene." Vikkula M., Peltonen L. FEBS Lett. 250:171-174(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 630-785 (ISOFORMS 1/2).
[19]	"Identification and characterization of the human type II collagen gene (COL2A1)." Cheah K.S.E., Stoker N.G., Griffin J.R., Grosveld F.G., Solomon E. Proc. Natl. Acad. Sci. U.S.A. 82:2555-2559(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1032-1487 (ISOFORMS 1/2).
[20]	"An amino acid substitution (Gly853-->Glu) in the collagen alpha 1(II) chain produces hypochondrogenesis." Bogaert R., Tiller G.E., Wies M.A., Gruber H.E., Rimoin D.L., Cohn D.H., Eyre D.R. J. Biol. Chem. 267:22522-22526(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1038-1055 (ISOFORMS 1/2), VARIANT HYPOCHONDROGENESIS GLU-1053.
[21]	"Low basal transcription of genes for tissue-specific collagens by fibroblasts and lymphoblastoid cells. Application to the characterization of a glycine 997 to serine substitution in alpha 1(II) collagen chains of a patient with spondyloepiphyseal dysplasia." Chan D., Cole W.G. J. Biol. Chem. 266:12487-12494(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1082-1288 (ISOFORMS 1/2).
[22]	"Identification of the molecular defect in a family with spondyloepiphyseal dysplasia." Lee B., Vissing H., Ramirez F., Rogers D., Rimoin D.L. Science 244:978-980(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1146-1199 (ISOFORMS 1/2), VARIANT SEDC 1164-GLY--TYR-1399 DEL.
[23]	"Tandem duplication within a type II collagen gene (COL2A1) exon in an individual with spondyloepiphyseal dysplasia." Tiller G.E., Rimoin D.L., Murray L.W., Cohn D.H. Proc. Natl. Acad. Sci. U.S.A. 87:3889-3893(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 1164-1199 (ISOFORMS 1/2), VARIANT SEDC GLY-PRO-SER-GLY-LYS-ASP-GLY-ALA-ASN-GLY-ILE-PRO-GLY-PRO-ILE-1184 INS.
[24]	"Determination of the single polyadenylation site of the human pro alpha 1(II) collagen gene." Elima K., Vuorio T., Vuorio E. Nucleic Acids Res. 15:9499-9504(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1175-1487 (ISOFORMS 1/2).
[25]	"Construction and identification of a cDNA clone for human type II procollagen mRNA." Elima K., Maekelae J.K., Vuorio T., Kauppinen S., Knowles J., Vuorio E. Biochem. J. 229:183-188(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1189-1467 (ISOFORMS 1/2).
[26]	"Chondrocalcin is identical with the C-propeptide of type II procollagen." Van der Rest M., Rosenberg L.C., Olsen B.R., Poole A.R. Biochem. J. 237:923-925(1986) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1242-1265; 1295-1305 AND 1395-1408.
[27]	"Isolation and characterization of genomic clones corresponding to the human type II procollagen gene." Strom C.M., Upholt W.B. Nucleic Acids Res. 12:1025-1038(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1245-1295 (ISOFORMS 1/2/3).
[28]	"Isolation and partial characterization of genomic clones coding for a human pro-alpha 1 (II) collagen chain and demonstration of restriction fragment length polymorphism at the 3' end of the gene." Nunez A.M., Francomano C., Young M.F., Martin G.R., Yamada Y. Biochemistry 24:6343-6348(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1296-1358 (ISOFORMS 1/2/3).
[29]	"X-ray crystal structure of HLA-DR4 (DRA*0101, DRB1*0401) complexed with a peptide from human collagen II." Dessen A., Lawrence C.M., Cupo S., Zaller D.M., Wiley D.C. Immunity 7:473-481(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1238-1247.
[30]	"Solution structure and dynamics of a prototypical chordin-like cysteine-rich repeat (von Willebrand Factor type C module) from collagen IIA." O'Leary J.M., Hamilton J.M., Deane C.M., Valeyev N.V., Sandell L.J., Downing A.K. J. Biol. Chem. 279:53857-53866(2004) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 25-162 (ISOFORM 2), DISULFIDE BONDS.
[31]	"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.
[32]	"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.
[33]	"Glycine to serine substitution in the triple helical domain of pro-alpha 1 (II) collagen results in a lethal perinatal form of short-limbed dwarfism." Vissing H., D'Alessio M., Lee B., Ramirez F., Godfrey M., Hollister D.W. J. Biol. Chem. 264:18265-18267(1989) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ACG2 SER-1143.
[34]	"Single base mutation in the type II procollagen gene (COL2A1) as a cause of primary osteoarthritis associated with a mild chondrodysplasia." Ala-Kokko L., Baldwin C.T., Moskowitz R.W., Prockop D.J. Proc. Natl. Acad. Sci. U.S.A. 87:6565-6568(1990) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT OACD CYS-719.
[35]	"Cartilage expression of a type II collagen mutation in an inherited form of osteoarthritis associated with a mild chondrodysplasia." Eyre D.R., Weis M.A., Moskowitz R.W. J. Clin. Invest. 87:357-361(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT OACD CYS-719.
[36]	"Characterization of a type II collagen gene (COL2A1) mutation identified in cultured chondrocytes from human hypochondrogenesis." Horton W.A., Machado M.A., Ellard J., Campbell D., Bartley J., Ramirez F., Vitale E., Lee B. Proc. Natl. Acad. Sci. U.S.A. 89:4583-4587(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HYPOCHONDROGENESIS SER-774.
[37]	"Mutation in type II procollagen (COL2A1) that substitutes aspartate for glycine alpha 1-67 and that causes cataracts and retinal detachment: evidence for molecular heterogeneity in the Wagner syndrome and the Stickler syndrome (arthro-ophthalmopathy)." Koerkkoe J., Ritvaniemi P., Haataja L., Kaeaeriaeinen H., Kivirikko K.I., Prockop D.J., Ala-Kokko L. Am. J. Hum. Genet. 53:55-61(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT STL1O ASP-267.
[38]	"A dominant mutation in the type II collagen gene (COL2A1) produces spondyloepimetaphyseal dysplasia (SEMD), Strudwick type." Tiller G.E., Weis M.A., Lachman R.S., Cohn D.H., Rimoin D.L., Eyre D.R. Am. J. Hum. Genet. 53:A209-A209(1993) Cited for: VARIANTS SEMDSTWK VAL-897 AND CYS-909.
[39]	"Human cartilage from late stage familial osteoarthritis transcribes type II collagen mRNA encoding a cysteine in position 519." Holderbaum D., Malemud C.J., Moskowitz R.W., Haqqi T.M. Biochem. Biophys. Res. Commun. 192:1169-1174(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT OACD CYS-719.
[40]	"A mutation in the amino-terminal end of the triple helix of type II collagen causing severe osteochondrodysplasia." Vikkula M., Ritvaniemi P., Vuorio A.F., Kaitila I., Ala-Kokko L., Peltonen L. Genomics 16:282-285(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT SPONDYLOMETAPHYSEAL DYSPLASIA ARG-354.
[41]	"Spondyloepiphyseal dysplasia and precocious osteoarthritis in a family with an Arg75-->Cys mutation in the procollagen type II gene (COL2A1)." Williams C.J., Considine E.L., Knowlton R.G., Reginato A., Neumann G., Harrison D., Buxton P., Jimenez S.A., Prockop D.J. Hum. Genet. 92:499-505(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CZECHD CYS-275.
[42]	"Characterization of an arginine 789 to cysteine substitution in alpha 1 (II) collagen chains of a patient with spondyloepiphyseal dysplasia." Chan D., Taylor T.K.F., Cole W.G. J. Biol. Chem. 268:15238-15245(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT SEDC CYS-989.
[43]	"The clinical features of spondyloepiphyseal dysplasia congenita resulting from the substitution of glycine 997 by serine in the alpha 1(II) chain of type II collagen." Cole W.G., Hall R.K., Rogers J.G. J. Med. Genet. 30:27-35(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT SEDC SER-1197.
[44]	"Expression, in cartilage, of a 7-amino-acid deletion in type II collagen from two unrelated individuals with Kniest dysplasia." Bogaert R., Wilkin D.J., Wilcox W.R., Lachman R.S., Rimoin D.L., Cohn D.H., Eyre D.R. Am. J. Hum. Genet. 55:1128-1136(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT STL1 302-ALA--LYS-308 DEL.
[45]	"A single amino acid substitution (G103D) in the type II collagen triple helix produces Kniest dysplasia." Wilkin D.J., Bogaert R., Lachman R.S., Rimoin D.L., Eyres D.R., Cohn D.H. Hum. Mol. Genet. 3:1999-2003(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT KD ASP-303.
[46]	"A single base mutation in the type II procollagen gene (COL2A1) that converts glycine alpha 1-247 to serine in a family with late-onset spondyloepiphyseal dysplasia." Ritvaniemi P., Sokolov B.P., Williams C.J., Considine W., Yurgenev L., Meerson E.M., Ala-Kokko L., Prockop D.J. Hum. Mutat. 3:261-267(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT SEDC SER-447.
[47]	"A radiographic, morphologic, biochemical and molecular analysis of a case of achondrogenesis type II resulting from substitution for a glycine residue (Gly691-->Arg) in the type II collagen trimer." Mortier G.R., Wilkin D.J., Wilcox W.R., Rimoin D.L., Lachman R.S., Eyre D.R., Cohn D.H. Hum. Mol. Genet. 4:285-288(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ACG2 ARG-891.
[48]	"Three new point mutations in type II procollagen (COL2A1) and identification of a fourth family with the COL2A1 Arg519-->Cys base substitution using conformation sensitive gel electrophoresis." Williams C.J., Rock M., Considine E.L., McCarron S., Gow P., Ladda R., McLain D., Michels V.M., Murphy W., Prockop D.J., Ganguly A. Hum. Mol. Genet. 4:309-312(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CZECHD CYS-275, VARIANT SEDC SER-1176, VARIANT OACD CYS-719, VARIANT HYPOCHONDROGENESIS ARG-891, VARIANT ACG2 ARG-1188.
[49]	"A COL2A1 mutation in achondrogenesis type II results in the replacement of type II collagen by type I and III collagens in cartilage." Chan D., Cole W.G., Chow C.W., Mundlos S., Bateman J.F. J. Biol. Chem. 270:1747-1753(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ACG2 SER-969.
[50]	"Dominant mutations in the type II collagen gene, COL2A1, produce spondyloepimetaphyseal dysplasia, Strudwick type." Tiller G.E., Polumbo P.A., Weis M.A., Bogaert R., Lachman R.S., Cohn D.H., Rimoin D.L., Eyre D.R. Nat. Genet. 11:87-89(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS SEMDSTWK VAL-492; CYS-504 AND CYS-909.
[51]	"An alpha 1(II) Gly913 to Cys substitution prevents the matrix incorporation of type II collagen which is replaced with type I and III collagens in cartilage from a patient with hypochondrogenesis." Mundlos S., Chan D., McGill J., Bateman J.F. Am. J. Med. Genet. 63:129-136(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HYPOCHONDROGENESIS CYS-1113.
[52]	"The deletion of six amino acids at the C-terminus of the alpha 1 (II) chain causes overmodification of type II and type XI collagen: further evidence for the association between small deletions in COL2A1 and Kniest dysplasia." Winterpacht A., Superti-Furga A., Schwarze U., Stoess H., Steinmann B., Spranger J., Zabel B. J. Med. Genet. 33:649-654(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT KD 1207-PRO--GLY-1212 DEL.
[53]	"Stickler-like syndrome due to a dominant negative mutation in the COL2A1 gene." Ballo R., Beighton P.H., Ramesar R.S. Am. J. Med. Genet. 80:6-11(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT EDMMD CYS-904.
[54]	"Five families with arginine 519-cysteine mutation in COL2A1: evidence for three distinct founders." Bleasel J.F., Holderbaum D., Brancolini V., Moskowitz R.W., Considine E.L., Prockop D.J., Devoto M., Williams C.J. Hum. Mutat. 12:172-176(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT SPONDYLOEPIPHYSEAL DYSPLASIA CYS-719.
[55]	"Variation in the vitreous phenotype of Stickler syndrome can be caused by different amino acid substitutions in the X position of the type II collagen Gly-X-Y triple helix." Richards A.J., Baguley D.M., Yates J.R.W., Lane C., Nicol M., Harper P.S., Scott J.D., Snead M.P. Am. J. Hum. Genet. 67:1083-1094(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT STL1 CYS-565, VARIANT DRRD PHE-667.
[56]	"Boy with syndactylies, macrocephaly, and severe skeletal dysplasia: not a new syndrome, but two dominant mutations (GLI3 E543X and COL2A1 G973R) in the same individual." Sobetzko D., Eich G., Kalff-Suske M., Grzeschik K.-H., Superti-Furga A. Am. J. Med. Genet. 90:239-242(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT SEDC ARG-1173.
[57]	"Widely distributed mutations in the COL2A1 gene produce achondrogenesis type II/hypochondrogenesis." Koerkkoe J., Cohn D.H., Ala-Kokko L., Krakow D., Prockop D.J. Am. J. Med. Genet. 92:95-100(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ACG2 VAL-453; ASP-453; ASP-771; ARG-780; ARG-795; GLU-894; ASP-948; SER-981; VAL-1065 AND ARG-1119, VARIANT HYPOCHONDROGENESIS 1017-GLY--VAL-1022 DEL, VARIANT ILE-1331.
[58]	"Report of five novel and one recurrent COL2A1 mutations with analysis of genotype-phenotype correlation in patients with a lethal type II collagen disorder." Mortier G.R., Weis M., Nuytinck L., King L.M., Wilkin D.J., De Paepe A., Lachman R.S., Rimoin D.L., Eyre D.R., Cohn D.H. J. Med. Genet. 37:263-271(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ACG2 SER-513; VAL-717; ALA-771; CYS-1110 AND SER-1143, VARIANT PLSD-T ASN-1390.
[59]	"Double heterozygosity for pseudoachondroplasia and spondyloepiphyseal dysplasia congenita." Unger S., Koerkkoe J., Krakow D., Lachman R.S., Rimoin D.L., Cohn D.H. Am. J. Med. Genet. 104:140-146(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT SEDC MET-1439.
[60]	"Vitreoretinopathy with phalangeal epiphyseal dysplasia, a type II collagenopathy resulting from a novel mutation in the C-propeptide region of the molecule." Richards A.J., Morgan J., Bearcroft P.W.P., Pickering E., Owen M.J., Holmans P., Williams N., Tysoe C., Pope F.M., Snead M.P., Hughes H. J. Med. Genet. 39:661-665(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT VITREORETINOPATHY ASP-1305.
[61]	"Recurrence of achondrogenesis type II within the same family: evidence for germline mosaicism." Faivre L., Le Merrer M., Douvier S., Laurent N., Thauvin-Robinet C., Rousseau T., Vereecke I., Sagot P., Delezoide A.-L., Coucke P., Mortier G. Am. J. Med. Genet. A 126:308-312(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ACGA2 ASP-516.
[62]	"Spondyloperipheral dysplasia is caused by truncating mutations in the C-propeptide of COL2A1." Zankl A., Zabel B., Hilbert K., Wildhardt G., Cuenot S., Xavier B., Ha-Vinh R., Bonafe L., Spranger J., Superti-Furga A. Am. J. Med. Genet. A 129:144-148(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN SPONDYLOPERIPHERAL DYSPLASIA.
[63]	"Identification of COL2A1 mutations in platyspondylic skeletal dysplasia, Torrance type." Nishimura G., Nakashima E., Mabuchi A., Shimamoto K., Shimamoto T., Shimao Y., Nagai T., Yamaguchi T., Kosaki R., Ohashi H., Makita Y., Ikegawa S. J. Med. Genet. 41:75-79(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PLSD-T CYS-1391.
[64]	"Dominant negative mutations in the C-propeptide of COL2A1 cause platyspondylic lethal skeletal dysplasia, torrance type, and define a novel subfamily within the type 2 collagenopathies." Zankl A., Neumann L., Ignatius J., Nikkels P., Schrander-Stumpel C., Mortier G., Omran H., Wright M., Hilbert K., Bonafe L., Spranger J., Zabel B., Superti-Furga A. Am. J. Med. Genet. A 133:61-67(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PLSD-T PRO-1448; HIS-1469; VAL-1484 DEL AND GLY-1485, DISCUSSION OF VARIANT ASN-1390.
[65]	"Novel amino acid substitution in the Y-position of collagen type II causes spondyloepimetaphyseal dysplasia congenita." Sulko J., Czarny-Ratajczak M., Wozniak A., Latos-Bielenska A., Kozlowski K. Am. J. Med. Genet. A 137:292-297(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT SEMDSTWK GLY-992.
[66]	"A novel mutation of COL2A1 resulting in dominantly inherited rhegmatogenous retinal detachment." Richards A.J., Meredith S., Poulson A., Bearcroft P., Crossland G., Baguley D.M., Scott J.D., Snead M.P. Invest. Ophthalmol. Vis. Sci. 46:663-668(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS DRRD ARG-318 AND PHE-667.
[67]	"Type II collagen gene variants and inherited osteonecrosis of the femoral head." Liu Y.-F., Chen W.-M., Lin Y.-F., Yang R.-C., Lin M.-W., Li L.-H., Chang Y.-H., Jou Y.-S., Lin P.-Y., Su J.-S., Huang S.-F., Hsiao K.-J., Fann C.S.J., Hwang H.-W., Chen Y.-T., Tsai S.-F. N. Engl. J. Med. 352:2294-2301(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ANFH SER-717 AND SER-1170.
[68]	"High efficiency of mutation detection in type 1 stickler syndrome using a two-stage approach: vitreoretinal assessment coupled with exon sequencing for screening COL2A1." Richards A.J., Laidlaw M., Whittaker J., Treacy B., Rai H., Bearcroft P., Baguley D.M., Poulson A., Ang A., Scott J.D., Snead M.P. Hum. Mutat. 27:696-704(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN STL1O.
[69]	"A familial case of achondrogenesis type II caused by a dominant COL2A1 mutation and 'patchy' expression in the mosaic father." Forzano F., Lituania M., Viassolo A., Superti-Furga V., Wildhardt G., Zabel B., Faravelli F. Am. J. Med. Genet. A 143:2815-2820(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ACG2 VAL-547.
[70]	"A recurrent mutation in type II collagen gene causes Legg-Calve-Perthes disease in a Japanese family." Miyamoto Y., Matsuda T., Kitoh H., Haga N., Ohashi H., Nishimura G., Ikegawa S. Hum. Genet. 121:625-629(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT LCPD SER-1170.
[71]	"Czech dysplasia: report of a large family and further delineation of the phenotype." Tzschach A., Tinschert S., Kaminsky E., Lusga E., Mundlos S., Graul-Neumann L.M. Am. J. Med. Genet. A 146:1859-1864(2008) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CZECHD CYS-275.
[72]	"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 SER-9; ASP-142; ILE-638; THR-1051; ILE-1331 AND SER-1405.
[73]	"Missense and nonsense mutations in the alternatively-spliced exon 2 of COL2A1 cause the ocular variant of Stickler syndrome." McAlinden A., Majava M., Bishop P.N., Perveen R., Black G.C.M., Pierpont M.E., Ala-Kokko L., Maennikkoe M. Hum. Mutat. 29:83-90(2008) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT STL1O TYR-57.
[74]	"Czech dysplasia occurring in a Japanese family." Matsui Y., Michigami T., Tachikawa K., Yamazaki M., Kawabata H., Nishimura G. Am. J. Med. Genet. A 149:2285-2289(2009) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CZECHD CYS-275.
[75]	"Stickler syndrome and the vitreous phenotype: mutations in COL2A1 and COL11A1." Richards A.J., McNinch A., Martin H., Oakhill K., Rai H., Waller S., Treacy B., Whittaker J., Meredith S., Poulson A., Snead M.P. Hum. Mutat. 31:E1461-E1471(2010) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS STL1 ASP-240; ARG-270; ASP-282; ALA-453; ARG-501; CYS-904 AND ALA-1158.
[76]	"Pseudoachondroplasia and multiple epiphyseal dysplasia: A 7-year comprehensive analysis of the known disease genes identify novel and recurrent mutations and provides an accurate assessment of their relative contribution." Jackson G.C., Mittaz-Crettol L., Taylor J.A., Mortier G.R., Spranger J., Zabel B., Le Merrer M., Cormier-Daire V., Hall C.M., Offiah A., Wright M.J., Savarirayan R., Nishimura G., Ramsden S.C., Elles R., Bonafe L., Superti-Furga A., Unger S., Zankl A., Briggs M.D. Hum. Mutat. 33:144-157(2012) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS VAL-1176 AND ARG-1179.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X16468 mRNA. Translation: CAA34488.1.
L10347 Genomic DNA. Translation: AAC41772.1.
BT007205 mRNA. Translation: AAP35869.1.
AC004801 Genomic DNA. No translation available.
BC007252 mRNA. Translation: AAH07252.1. Frameshift.
BC116449 mRNA. Translation: AAI16450.1.
X16711 mRNA. Translation: CAA34683.1.
M25730 , M32168, M25655, M25656, M64345 Genomic DNA. Translation: AAA58428.2.
M60299 Genomic DNA. Translation: AAA73873.1.
M25698 Genomic DNA. Translation: AAA52051.1.
X58709 Genomic DNA. No translation available.
X57010 Genomic DNA. Translation: CAA40330.1.
U15195 Genomic DNA. Translation: AAB60370.1.
X13783 mRNA. Translation: CAA32030.1.
M25728 Genomic DNA. Translation: AAD15287.1.
X02371 , X02372, X02373, X02374 Genomic DNA. Translation: CAA26223.1.
X02375 Genomic DNA. Translation: CAA26224.1.
X02376 Genomic DNA. Translation: CAA26225.1.
X02377 Genomic DNA. Translation: CAA26226.1.
X02378 Genomic DNA. Translation: CAA26227.1.
X16158 Genomic DNA. Translation: CAA34278.1.
X16158 Genomic DNA. Translation: CAA34279.1.
X16158 Genomic DNA. Translation: CAA34280.1.
X16158 Genomic DNA. Translation: CAA34281.1.
X16158 Genomic DNA. Translation: CAA34282.1.
X16158 Genomic DNA. Translation: CAA34283.1.
X16158 Genomic DNA. Translation: CAA34284.1.
J00116 Genomic DNA. Translation: AAA51997.1.
L00977 Genomic DNA. No translation available.
M63281 mRNA. Translation: AAA52038.1.
M27468 Genomic DNA. Translation: AAA52039.1.
X06268 mRNA. Translation: CAA29604.1.
X00339 Genomic DNA. Translation: CAA25092.1.
M12048 Genomic DNA. No translation available.

IPI

IPI00186460.
IPI00748487.
IPI00936892.

PIR

CGHU6C. A38513.

RefSeq

NP_001835.3. NM_001844.4.
NP_149162.2. NM_033150.2.

UniGene

Hs.408182.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1U5M	NMR	-	A	29-94	[»]
2FSE	X-ray	3.10	E/F	461-474	[»]
2SEB	X-ray	2.50	E	1238-1247	[»]

ProteinModelPortal

P02458.

ModBase

Search...

Protein-protein interaction databases

IntAct

P02458. 2 interactions.

MINT

MINT-6796075.

PTM databases

PhosphoSite

P02458.

Polymorphism databases

DMDM

124056489.

Proteomic databases

PaxDb

P02458.

PRIDE

P02458.

Protocols and materials databases

DNASU

1280.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000337299; ENSP00000338213; ENSG00000139219.
ENST00000380518; ENSP00000369889; ENSG00000139219.

GeneID

1280.

KEGG

hsa:1280.

UCSC

uc001rqt.3. human.
uc001rqu.3. human.
uc001rqv.3. human.

Organism-specific databases

CTD

1280.

GeneCards

GC12M048266.

HGNC

HGNC:2200. COL2A1.

HPA

CAB002214.

MIM

108300. phenotype.
120140. gene+phenotype.
132450. phenotype.
150600. phenotype.
151210. phenotype.
156550. phenotype.
183900. phenotype.
184250. phenotype.
200610. phenotype.
271700. phenotype.
604864. phenotype.
608805. phenotype.
609162. phenotype.
609508. phenotype.

neXtProt

NX_P02458.

Orphanet

93296. Achondrogenesis type 2.
209867. Autosomal dominant rhegmatogenous retinal detachment.
137678. Czech dysplasia, metatarsal type.
86820. Familial avascular necrosis of femoral head.
93297. Hypochondrogenesis.
485. Kniest dysplasia.
2380. Legg-Calve-Perthes disease.
93279. Mild spondyloepiphyseal dysplasia due to COL2A1 mutation with early-onset osteoarthritis.
166011. Multiple epiphyseal dysplasia, Beighton type.
1427. Otospondylomegaepiphyseal dysplasia.
85166. Platyspondylic dysplasia, Torrance type.
93346. Spondyloepimetaphyseal dysplasia congenita, Strudwick type.
94068. Spondyloepiphyseal dysplasia congenita.
93315. Spondylometaphyseal dysplasia, 'corner fracture' type.
1856. Spondyloperipheral dysplasia - short ulna.
90653. Stickler syndrome type 1.

PharmGKB

PA26715.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG12793.

HOVERGEN

HBG004933.

KO

K06236.

OMA

SSCRICV.

OrthoDB

EOG4FTW1C.

Enzyme and pathway databases

Reactome

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

Gene expression databases

Bgee

P02458.

Genevestigator

P02458.

GermOnline

ENSG00000139219. 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. 9 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

ChiTaRS

COL2A1. human.

DrugBank

DB00048. Collagenase.

EvolutionaryTrace

P02458.

GenomeRNAi

1280.

NextBio

5171.

PMAP-CutDB

P02458.

SOURCE

Search...

Entry information

Entry name

CO2A1_HUMAN

Accession

Primary (citable) accession number: P02458
Secondary accession number(s): A6NGA0 , Q12985, Q14009, Q14044, Q14045, Q14046, Q14047, Q14056, Q14058, Q16672, Q1JQ82, Q2V4X7, Q6LBY1, Q6LBY2, Q6LBY3, Q96IT5, Q99227, Q9UE38, Q9UE39, Q9UE40, Q9UE41, Q9UE42, Q9UE43

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 167 of the entry and version 3 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.