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P02458

- CO2A1_HUMAN

UniProt

P02458 - CO2A1_HUMAN

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Protein

Collagen alpha-1(II) chain

Gene

COL2A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei181 – 1822Cleavage; by procollagen N-endopeptidaseBy similarity
Sitei1241 – 12422Cleavage; by procollagen C-endopeptidaseBy similarity
Metal bindingi1301 – 13011CalciumBy similarity
Metal bindingi1303 – 13031CalciumBy similarity
Metal bindingi1304 – 13041Calcium; via carbonyl oxygenBy similarity
Metal bindingi1306 – 13061Calcium; via carbonyl oxygenBy similarity
Metal bindingi1309 – 13091CalciumBy similarity

GO - Molecular functioni

  1. extracellular matrix structural constituent conferring tensile strength Source: BHF-UCL
  2. identical protein binding Source: BHF-UCL
  3. metal ion binding Source: UniProtKB-KW
  4. platelet-derived growth factor binding Source: MGI

GO - Biological processi

  1. axon guidance Source: Reactome
  2. cartilage condensation Source: Ensembl
  3. cartilage development Source: BHF-UCL
  4. cartilage development involved in endochondral bone morphogenesis Source: Ensembl
  5. cellular response to BMP stimulus Source: Ensembl
  6. central nervous system development Source: Ensembl
  7. chondrocyte differentiation Source: Ensembl
  8. collagen catabolic process Source: Reactome
  9. collagen fibril organization Source: BHF-UCL
  10. embryonic skeletal joint morphogenesis Source: BHF-UCL
  11. endochondral ossification Source: Ensembl
  12. extracellular matrix disassembly Source: Reactome
  13. extracellular matrix organization Source: Reactome
  14. heart morphogenesis Source: Ensembl
  15. inner ear morphogenesis Source: Ensembl
  16. limb bud formation Source: Ensembl
  17. negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
  18. notochord development Source: Ensembl
  19. otic vesicle development Source: Ensembl
  20. palate development Source: Ensembl
  21. proteoglycan metabolic process Source: Ensembl
  22. regulation of gene expression Source: Ensembl
  23. sensory perception of sound Source: BHF-UCL
  24. skeletal system development Source: BHF-UCL
  25. tissue homeostasis Source: Ensembl
  26. visual perception Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_118779. Extracellular matrix organization.
REACT_121139. Collagen biosynthesis and modifying enzymes.
REACT_13552. Integrin cell surface interactions.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_150401. Collagen degradation.
REACT_163874. Non-integrin membrane-ECM interactions.
REACT_163906. ECM proteoglycans.
REACT_16888. Signaling by PDGF.
REACT_18312. NCAM1 interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-1(II) chain
Alternative name(s):
Alpha-1 type II collagen
Cleaved into the following 2 chains:
Gene namesi
Name:COL2A1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:2200. COL2A1.

Subcellular locationi

Secretedextracellular spaceextracellular matrix PROSITE-ProRule annotation

GO - Cellular componenti

  1. basement membrane Source: Ensembl
  2. collagen type II trimer Source: BHF-UCL
  3. endoplasmic reticulum lumen Source: Reactome
  4. extracellular matrix Source: UniProtKB
  5. extracellular region Source: Reactome
  6. extracellular space Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Spondyloepiphyseal dysplasia congenital type (SEDC) [MIM:183900]: Disorder characterized by disproportionate short stature and pleiotropic involvement of the skeletal and ocular systems.8 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti375 – 3751G → R in SEDC.
VAR_001743
Natural varianti447 – 4471G → S in SEDC. 1 Publication
VAR_001744
Natural varianti774 – 7741G → S in SEDC and hypochondrogenesis; lethal. 1 Publication
VAR_001749
Natural varianti855 – 8551G → S in SEDC.
VAR_023930
Natural varianti891 – 8911G → R in ACG2 and SEDC. 2 Publications
VAR_001752
Natural varianti989 – 9891R → C in SEDC. 1 Publication
VAR_001755
Natural varianti1164 – 119936Missing in SEDC.
VAR_001762Add
BLAST
Natural varianti1173 – 11731G → R in SEDC. 1 Publication
VAR_017651
Natural varianti1176 – 11761G → S in SEDC. 1 Publication
VAR_001763
Natural varianti1176 – 11761G → V Mutation found in a patient with features of multiple epiphyseal dysplasia; features overlap with SEDC. 1 Publication
VAR_066836
Natural varianti1179 – 11791G → R Mutation found in a patient with features of multiple epiphyseal dysplasia; features overlap with SEDC. 1 Publication
VAR_066837
Natural varianti1184 – 11841I → IGPSGKDGANGIPGPI in SEDC. 1 Publication
VAR_019837
Natural varianti1197 – 11971G → S in SEDC. 1 Publication
VAR_001765
Natural varianti1439 – 14391T → M in SEDC. 1 Publication
VAR_017105
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.3 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti492 – 4921G → V in SEMDSTWK. 1 Publication
VAR_001745
Natural varianti504 – 5041G → C in SEMDSTWK. 1 Publication
VAR_001746
Natural varianti897 – 8971G → V in SEMDSTWK. 1 Publication
VAR_023931
Natural varianti909 – 9091G → C in SEMDSTWK. 2 Publications
VAR_001753
Natural varianti992 – 9921R → G in SEMDSTWK. 1 Publication
VAR_023932
Achondrogenesis 2 (ACG2) [MIM:200610]: A disease characterized by the absence of ossification in the vertebral column, sacrum and pubic bones.7 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti453 – 4531G → D in ACG2. 1 Publication
VAR_017639
Natural varianti453 – 4531G → V in ACG2. 1 Publication
VAR_017640
Natural varianti510 – 5101G → D in ACG2.
VAR_001747
Natural varianti513 – 5131G → S in ACG2. 1 Publication
VAR_024819
Natural varianti547 – 5471D → V in ACG2. 1 Publication
VAR_063897
Natural varianti717 – 7171G → V in ACG2. 1 Publication
VAR_024820
Natural varianti771 – 7711G → A in ACG2. 1 Publication
VAR_024821
Natural varianti771 – 7711G → D in ACG2. 1 Publication
VAR_017641
Natural varianti780 – 7801G → R in ACG2. 1 Publication
VAR_017642
Natural varianti795 – 7951G → R in ACG2. 1 Publication
VAR_017643
Natural varianti891 – 8911G → R in ACG2 and SEDC. 2 Publications
VAR_001752
Natural varianti894 – 8941G → E in ACG2. 1 Publication
VAR_017644
Natural varianti948 – 9481G → D in ACG2. 1 Publication
VAR_017646
Natural varianti969 – 9691G → S in ACG2. 1 Publication
VAR_001754
Natural varianti981 – 9811G → S in ACG2. 1 Publication
VAR_017647
Natural varianti1017 – 10171G → V in ACG2.
VAR_001757
Natural varianti1065 – 10651G → V in ACG2. 1 Publication
VAR_017649
Natural varianti1110 – 11101G → C in ACG2. 1 Publication
VAR_001759
Natural varianti1119 – 11191G → R in ACG2. 1 Publication
VAR_017650
Natural varianti1143 – 11431G → S in ACG2. 2 Publications
VAR_001761
Natural varianti1188 – 11881G → R in ACG2. 1 Publication
VAR_001764
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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1170 – 11701G → S in ANFH and in LCPD. 2 Publications
VAR_023933
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.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti303 – 3031G → D in KD; abnormal allele expressed in the cartilage. 1 Publication
VAR_001741
Natural varianti1207 – 12126Missing in KD. 1 Publication
VAR_001766
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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti717 – 7171G → S in ANFH. 1 Publication
VAR_023929
Natural varianti1170 – 11701G → S in ANFH and in LCPD. 2 Publications
VAR_023933
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.4 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti719 – 7191R → C in OACD; also in mild spondyloepiphyseal dysplasia and precocious osteoarthritis. 5 Publications
VAR_001748
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.3 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1390 – 13901T → N in PLSD-T; phenotype previously considered as achondrogenesis-hypochondrogenesis type 2. 1 Publication
VAR_024822
Natural varianti1391 – 13911Y → C in PLSD-T. 1 Publication
VAR_023935
Natural varianti1448 – 14481T → P in PLSD-T. 1 Publication
VAR_024823
Natural varianti1469 – 14691D → H in PLSD-T. 1 Publication
VAR_024824
Natural varianti1484 – 14841Missing in PLSD-T. 1 Publication
VAR_024825
Natural varianti1485 – 14851C → G in PLSD-T. 1 Publication
VAR_024826
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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti904 – 9041R → C in EDMMD and STL1. 2 Publications
VAR_017645
Spondyloperipheral dysplasia (SPD) [MIM:271700]: SPD patients manifest short stature, midface hypoplasia, sensorineural hearing loss, spondyloepiphyseal dysplasia, platyspondyly and brachydactyly.1 Publication
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.3 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti57 – 571C → Y in STL1O. 1 Publication
VAR_063891
Natural varianti240 – 2401G → D in STL1. 1 Publication
VAR_063892
Natural varianti267 – 2671G → D in STL1O. 1 Publication
VAR_001738
Natural varianti270 – 2701G → R in STL1. 1 Publication
VAR_063893
Natural varianti282 – 2821G → D in STL1. 1 Publication
VAR_063894
Natural varianti302 – 3087Missing in STL1. 1 Publication
VAR_001740
Natural varianti453 – 4531G → A in STL1. 1 Publication
VAR_063895
Natural varianti501 – 5011G → R in STL1. 1 Publication
VAR_063896
Natural varianti565 – 5651R → C in STL1. 1 Publication
VAR_023927
Natural varianti904 – 9041R → C in EDMMD and STL1. 2 Publications
VAR_017645
Natural varianti1158 – 11581G → A in STL1. 1 Publication
VAR_063898
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.3 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti57 – 571C → Y in STL1O. 1 Publication
VAR_063891
Natural varianti267 – 2671G → D in STL1O. 1 Publication
VAR_001738
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.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti318 – 3181G → R in DRRD. 1 Publication
VAR_023925
Natural varianti667 – 6671L → F in DRRD. 2 Publications
VAR_023928
Czech dysplasia (CZECHD) [MIM:609162]: A skeletal dysplasia characterized by early-onset, progressive pseudorheumatoid arthritis, platyspondyly, and short third and fourth toes.4 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti275 – 2751R → C in CZECHD. 4 Publications
VAR_001739

Keywords - Diseasei

Cataract, Deafness, Disease mutation, Dwarfism, Stickler syndrome

Organism-specific databases

MIMi108300. 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.
Orphaneti93296. Achondrogenesis type 2.
209867. Autosomal dominant rhegmatogenous retinal detachment.
137678. Czech dysplasia, metatarsal type.
85198. Dysspondyloenchondromatosis.
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.
93316. Spondylometaphyseal dysplasia, Schmidt type.
1856. Spondyloperipheral dysplasia - short ulna.
90653. Stickler syndrome type 1.
PharmGKBiPA26715.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence AnalysisAdd
BLAST
Propeptidei26 – 181156N-terminal propeptidePRO_0000005729Add
BLAST
Chaini182 – 12411060Collagen alpha-1(II) chainPRO_0000005730Add
BLAST
Chaini1242 – 1487246ChondrocalcinPRO_0000005731Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei190 – 19015-hydroxylysineBy similarity
Glycosylationi190 – 1901O-linked (Gal...)By similarity
Modified residuei287 – 28715-hydroxylysineBy similarity
Glycosylationi287 – 2871O-linked (Gal...)By similarity
Modified residuei299 – 29915-hydroxylysineBy similarity
Glycosylationi299 – 2991O-linked (Gal...)By similarity
Modified residuei308 – 30815-hydroxylysineBy similarity
Glycosylationi308 – 3081O-linked (Gal...)By similarity
Modified residuei374 – 37415-hydroxylysineBy similarity
Glycosylationi374 – 3741O-linked (Gal...)By similarity
Modified residuei608 – 60815-hydroxylysineBy similarity
Glycosylationi608 – 6081O-linked (Gal...)By similarity
Modified residuei620 – 62015-hydroxylysineBy similarity
Glycosylationi620 – 6201O-linked (Gal...)By similarity
Modified residuei670 – 67013-hydroxyprolineBy similarity
Modified residuei907 – 90713-hydroxyprolineBy similarity
Modified residuei1130 – 113015-hydroxylysineBy similarity
Glycosylationi1130 – 11301O-linked (Gal...)By similarity
Modified residuei1144 – 114413-hydroxyprolineBy similarity
Modified residuei1186 – 118613-hydroxyprolineBy similarity
Modified residuei1201 – 120113-hydroxyprolineBy similarity
Modified residuei1207 – 120713-hydroxyprolineBy similarity
Modified residuei1213 – 121313-hydroxyprolineBy similarity
Disulfide bondi1283 ↔ 1315PROSITE-ProRule annotation
Disulfide bondi1289 – 1289Interchain (with C-1306)PROSITE-ProRule annotation
Disulfide bondi1306 – 1306Interchain (with C-1289)PROSITE-ProRule annotation
Disulfide bondi1323 ↔ 1485PROSITE-ProRule annotation
Glycosylationi1388 – 13881N-linked (GlcNAc...)
Disulfide bondi1393 ↔ 1438PROSITE-ProRule annotation

Post-translational modificationi

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.By similarity
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.

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

MaxQBiP02458.
PaxDbiP02458.
PRIDEiP02458.

PTM databases

PhosphoSiteiP02458.

Miscellaneous databases

PMAP-CutDBP02458.

Expressioni

Tissue specificityi

Isoform 2 is highly expressed in juvenile chondrocyte and low in fetal chondrocyte.1 Publication

Gene expression databases

BgeeiP02458.
GenevestigatoriP02458.

Organism-specific databases

HPAiCAB002214.
HPA045939.

Interactioni

Subunit structurei

Homotrimers of alpha 1(II) chains.

Protein-protein interaction databases

BioGridi107677. 18 interactions.
IntActiP02458. 3 interactions.
MINTiMINT-6796075.

Structurei

Secondary structure

1
1487
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi34 – 385
Beta strandi51 – 588
Beta strandi61 – 666
Beta strandi91 – 944

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1U5MNMR-A29-97[»]
2FSEX-ray3.10E/F461-474[»]
2SEBX-ray2.50E1238-1247[»]
DisProtiDP00274.
ProteinModelPortaliP02458.
SMRiP02458. Positions 27-97, 1271-1487.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02458.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini32 – 9059VWFCPROSITE-ProRule annotationAdd
BLAST
Domaini1253 – 1487235Fibrillar collagen NC1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni201 – 12141014Triple-helical regionAdd
BLAST
Regioni1215 – 124127Nonhelical region (C-terminal)Add
BLAST

Domaini

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).By similarity

Sequence similaritiesi

Belongs to the fibrillar collagen family.PROSITE-ProRule annotation
Contains 1 fibrillar collagen NC1 domain.PROSITE-ProRule annotation
Contains 1 VWFC domain.PROSITE-ProRule annotation

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00760000118776.
HOVERGENiHBG004933.
InParanoidiP02458.
KOiK06236.
OMAiPLQYMRA.
OrthoDBiEOG7TJ3HH.
PhylomeDBiP02458.
TreeFamiTF344135.

Family and domain databases

InterProiIPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_C.
[Graphical view]
PfamiPF01410. COLFI. 1 hit.
PF01391. Collagen. 9 hits.
PF00093. VWC. 1 hit.
[Graphical view]
ProDomiPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00038. COLFI. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
PROSITEiPS51461. NC1_FIB. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 2 (identifier: P02458-2) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MIRLGAPQTL VLLTLLVAAV LRCQGQDVQE AGSCVQDGQR YNDKDVWKPE
60 70 80 90 100
PCRICVCDTG TVLCDDIICE DVKDCLSPEI PFGECCPICP TDLATASGQP
110 120 130 140 150
GPKGQKGEPG DIKDIVGPKG PPGPQGPAGE QGPRGDRGDK GEKGAPGPRG
160 170 180 190 200
RDGEPGTPGN PGPPGPPGPP GPPGLGGNFA AQMAGGFDEK AGGAQLGVMQ
210 220 230 240 250
GPMGPMGPRG PPGPAGAPGP QGFQGNPGEP GEPGVSGPMG PRGPPGPPGK
260 270 280 290 300
PGDDGEAGKP GKAGERGPPG PQGARGFPGT PGLPGVKGHR GYPGLDGAKG
310 320 330 340 350
EAGAPGVKGE SGSPGENGSP GPMGPRGLPG ERGRTGPAGA AGARGNDGQP
360 370 380 390 400
GPAGPPGPVG PAGGPGFPGA PGAKGEAGPT GARGPEGAQG PRGEPGTPGS
410 420 430 440 450
PGPAGASGNP GTDGIPGAKG SAGAPGIAGA PGFPGPRGPP GPQGATGPLG
460 470 480 490 500
PKGQTGEPGI AGFKGEQGPK GEPGPAGPQG APGPAGEEGK RGARGEPGGV
510 520 530 540 550
GPIGPPGERG APGNRGFPGQ DGLAGPKGAP GERGPSGLAG PKGANGDPGR
560 570 580 590 600
PGEPGLPGAR GLTGRPGDAG PQGKVGPSGA PGEDGRPGPP GPQGARGQPG
610 620 630 640 650
VMGFPGPKGA NGEPGKAGEK GLPGAPGLRG LPGKDGETGA AGPPGPAGPA
660 670 680 690 700
GERGEQGAPG PSGFQGLPGP PGPPGEGGKP GDQGVPGEAG APGLVGPRGE
710 720 730 740 750
RGFPGERGSP GAQGLQGPRG LPGTPGTDGP KGASGPAGPP GAQGPPGLQG
760 770 780 790 800
MPGERGAAGI AGPKGDRGDV GEKGPEGAPG KDGGRGLTGP IGPPGPAGAN
810 820 830 840 850
GEKGEVGPPG PAGSAGARGA PGERGETGPP GPAGFAGPPG ADGQPGAKGE
860 870 880 890 900
QGEAGQKGDA GAPGPQGPSG APGPQGPTGV TGPKGARGAQ GPPGATGFPG
910 920 930 940 950
AAGRVGPPGS NGNPGPPGPP GPSGKDGPKG ARGDSGPPGR AGEPGLQGPA
960 970 980 990 1000
GPPGEKGEPG DDGPSGAEGP PGPQGLAGQR GIVGLPGQRG ERGFPGLPGP
1010 1020 1030 1040 1050
SGEPGKQGAP GASGDRGPPG PVGPPGLTGP AGEPGREGSP GADGPPGRDG
1060 1070 1080 1090 1100
AAGVKGDRGE TGAVGAPGAP GPPGSPGPAG PTGKQGDRGE AGAQGPMGPS
1110 1120 1130 1140 1150
GPAGARGIQG PQGPRGDKGE AGEPGERGLK GHRGFTGLQG LPGPPGPSGD
1160 1170 1180 1190 1200
QGASGPAGPS GPRGPPGPVG PSGKDGANGI PGPIGPPGPR GRSGETGPAG
1210 1220 1230 1240 1250
PPGNPGPPGP PGPPGPGIDM SAFAGLGPRE KGPDPLQYMR ADQAAGGLRQ
1260 1270 1280 1290 1300
HDAEVDATLK SLNNQIESIR SPEGSRKNPA RTCRDLKLCH PEWKSGDYWI
1310 1320 1330 1340 1350
DPNQGCTLDA MKVFCNMETG ETCVYPNPAN VPKKNWWSSK SKEKKHIWFG
1360 1370 1380 1390 1400
ETINGGFHFS YGDDNLAPNT ANVQMTFLRL LSTEGSQNIT YHCKNSIAYL
1410 1420 1430 1440 1450
DEAAGNLKKA LLIQGSNDVE IRAEGNSRFT YTALKDGCTK HTGKWGKTVI
1460 1470 1480
EYRSQKTSRL PIIDIAPMDI GGPEQEFGVD IGPVCFL
Length:1,487
Mass (Da):141,785
Last modified:January 23, 2007 - v3
Checksum:iA8312503825BF0BB
GO
Isoform 1 (identifier: P02458-1) [UniParc]FASTAAdd to Basket

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

Show »
Length:1,418
Mass (Da):134,389
Checksum:i1A9E7505AEC4168A
GO
Isoform 3 (identifier: P02458-3) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:268
Mass (Da):29,781
Checksum:iE8337954D719ACBF
GO

Sequence cautioni

The sequence AAH07252.1 differs from that shown. Reason: Frameshift at position 1198.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti441 – 4411G → D in CAA34488. (PubMed:2587267)Curated
Sequence conflicti457 – 4571E → K in CAA34488. (PubMed:2587267)Curated
Sequence conflicti481 – 4811A → P in AAB60370. (PubMed:7847372)Curated
Sequence conflicti641 – 6411A → E in CAA34488. (PubMed:2587267)Curated
Sequence conflicti641 – 6411A → E in CAA32030. 1 PublicationCurated
Sequence conflicti677 – 6771G → A in CAA32030. 1 PublicationCurated
Sequence conflicti784 – 7841G → A in CAA32030. 1 PublicationCurated
Sequence conflicti832 – 8354PAGF → TSGI in CAA34488. (PubMed:2587267)Curated
Sequence conflicti1006 – 10061K → Q in CAA34488. (PubMed:2587267)Curated
Sequence conflicti1006 – 10061K → Q in CAA32030. 1 PublicationCurated
Sequence conflicti1037 – 10371E → Q in CAA34683. (PubMed:2803268)Curated
Sequence conflicti1057 – 10571D → N in AAD15287. (PubMed:2987845)Curated
Sequence conflicti1057 – 10571D → N in CAA26223. (PubMed:2987845)Curated
Sequence conflicti1057 – 10571D → N in AAA51997. (PubMed:3857598)Curated
Sequence conflicti1069 – 10691A → T in CAA34683. (PubMed:2803268)Curated
Sequence conflicti1069 – 10691A → T in AAD15287. (PubMed:2987845)Curated
Sequence conflicti1069 – 10691A → T in CAA26223. (PubMed:2987845)Curated
Sequence conflicti1069 – 10691A → T in AAA51997. (PubMed:3857598)Curated
Sequence conflicti1243 – 12431Q → E in CAA29604. (PubMed:2825137)Curated
Sequence conflicti1247 – 12471G → N in CAA29604. (PubMed:2825137)Curated
Sequence conflicti1271 – 12711S → T in AAA52038. (PubMed:1905723)Curated
Sequence conflicti1274 – 12741G → A in AAA52038. (PubMed:1905723)Curated
Sequence conflicti1333 – 13331K → R in M12048. (PubMed:3002437)Curated
Sequence conflicti1350 – 13501G → A in M12048. (PubMed:3002437)Curated
Sequence conflicti1372 – 13721N → D in CAA26223. (PubMed:2987845)Curated
Sequence conflicti1383 – 13831T → A in CAA26223. (PubMed:2987845)Curated
Sequence conflicti1400 – 14001L → M in CAA26223. (PubMed:2987845)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti9 – 91T → S.6 Publications
Corresponds to variant rs3803183 [ dbSNP | Ensembl ].
VAR_017638
Natural varianti57 – 571C → Y in STL1O. 1 Publication
VAR_063891
Natural varianti142 – 1421E → D.1 Publication
Corresponds to variant rs34392760 [ dbSNP | Ensembl ].
VAR_033782
Natural varianti158 – 1581P → L.1 Publication
Corresponds to variant rs1050861 [ dbSNP | Ensembl ].
VAR_019836
Natural varianti240 – 2401G → D in STL1. 1 Publication
VAR_063892
Natural varianti267 – 2671G → D in STL1O. 1 Publication
VAR_001738
Natural varianti270 – 2701G → R in STL1. 1 Publication
VAR_063893
Natural varianti275 – 2751R → C in CZECHD. 4 Publications
VAR_001739
Natural varianti282 – 2821G → D in STL1. 1 Publication
VAR_063894
Natural varianti302 – 3087Missing in STL1. 1 Publication
VAR_001740
Natural varianti303 – 3031G → D in KD; abnormal allele expressed in the cartilage. 1 Publication
VAR_001741
Natural varianti318 – 3181G → R in DRRD. 1 Publication
VAR_023925
Natural varianti354 – 3541G → R in spondylometaphyseal dysplasia; congenital type. 1 Publication
VAR_001742
Natural varianti375 – 3751G → R in SEDC.
VAR_001743
Natural varianti447 – 4471G → S in SEDC. 1 Publication
VAR_001744
Natural varianti453 – 4531G → A in STL1. 1 Publication
VAR_063895
Natural varianti453 – 4531G → D in ACG2. 1 Publication
VAR_017639
Natural varianti453 – 4531G → V in ACG2. 1 Publication
VAR_017640
Natural varianti492 – 4921G → V in SEMDSTWK. 1 Publication
VAR_001745
Natural varianti501 – 5011G → R in STL1. 1 Publication
VAR_063896
Natural varianti504 – 5041G → C in SEMDSTWK. 1 Publication
VAR_001746
Natural varianti510 – 5101G → D in ACG2.
VAR_001747
Natural varianti513 – 5131G → S in ACG2. 1 Publication
VAR_024819
Natural varianti516 – 5161G → D in ACGA2. 1 Publication
VAR_023926
Natural varianti547 – 5471D → V in ACG2. 1 Publication
VAR_063897
Natural varianti565 – 5651R → C in STL1. 1 Publication
VAR_023927
Natural varianti638 – 6381T → I.1 Publication
Corresponds to variant rs41263847 [ dbSNP | Ensembl ].
VAR_033783
Natural varianti667 – 6671L → F in DRRD. 2 Publications
VAR_023928
Natural varianti717 – 7171G → S in ANFH. 1 Publication
VAR_023929
Natural varianti717 – 7171G → V in ACG2. 1 Publication
VAR_024820
Natural varianti719 – 7191R → C in OACD; also in mild spondyloepiphyseal dysplasia and precocious osteoarthritis. 5 Publications
VAR_001748
Natural varianti771 – 7711G → A in ACG2. 1 Publication
VAR_024821
Natural varianti771 – 7711G → D in ACG2. 1 Publication
VAR_017641
Natural varianti774 – 7741G → S in SEDC and hypochondrogenesis; lethal. 1 Publication
VAR_001749
Natural varianti780 – 7801G → R in ACG2. 1 Publication
VAR_017642
Natural varianti795 – 7951G → R in ACG2. 1 Publication
VAR_017643
Natural varianti804 – 8041G → A in hypochondrogenesis.
VAR_001751
Natural varianti855 – 8551G → S in SEDC.
VAR_023930
Natural varianti891 – 8911G → R in ACG2 and SEDC. 2 Publications
VAR_001752
Natural varianti894 – 8941G → E in ACG2. 1 Publication
VAR_017644
Natural varianti897 – 8971G → V in SEMDSTWK. 1 Publication
VAR_023931
Natural varianti904 – 9041R → C in EDMMD and STL1. 2 Publications
VAR_017645
Natural varianti909 – 9091G → C in SEMDSTWK. 2 Publications
VAR_001753
Natural varianti948 – 9481G → D in ACG2. 1 Publication
VAR_017646
Natural varianti969 – 9691G → S in ACG2. 1 Publication
VAR_001754
Natural varianti981 – 9811G → S in ACG2. 1 Publication
VAR_017647
Natural varianti989 – 9891R → C in SEDC. 1 Publication
VAR_001755
Natural varianti992 – 9921R → G in SEMDSTWK. 1 Publication
VAR_023932
Natural varianti1005 – 10051G → S in hypochondrogenesis.
VAR_001756
Natural varianti1017 – 10226Missing in hypochondrogenesis. 1 Publication
VAR_017648
Natural varianti1017 – 10171G → V in ACG2.
VAR_001757
Natural varianti1051 – 10511A → T.1 Publication
Corresponds to variant rs41272041 [ dbSNP | Ensembl ].
VAR_033784
Natural varianti1053 – 10531G → E in hypochondrogenesis; lethal. 1 Publication
VAR_001758
Natural varianti1065 – 10651G → V in ACG2. 1 Publication
VAR_017649
Natural varianti1110 – 11101G → C in ACG2. 1 Publication
VAR_001759
Natural varianti1113 – 11131G → C in hypochondrogenesis. 1 Publication
VAR_001760
Natural varianti1119 – 11191G → R in ACG2. 1 Publication
VAR_017650
Natural varianti1143 – 11431G → S in ACG2. 2 Publications
VAR_001761
Natural varianti1158 – 11581G → A in STL1. 1 Publication
VAR_063898
Natural varianti1164 – 119936Missing in SEDC.
VAR_001762Add
BLAST
Natural varianti1170 – 11701G → S in ANFH and in LCPD. 2 Publications
VAR_023933
Natural varianti1173 – 11731G → R in SEDC. 1 Publication
VAR_017651
Natural varianti1176 – 11761G → S in SEDC. 1 Publication
VAR_001763
Natural varianti1176 – 11761G → V Mutation found in a patient with features of multiple epiphyseal dysplasia; features overlap with SEDC. 1 Publication
VAR_066836
Natural varianti1179 – 11791G → R Mutation found in a patient with features of multiple epiphyseal dysplasia; features overlap with SEDC. 1 Publication
VAR_066837
Natural varianti1184 – 11841I → IGPSGKDGANGIPGPI in SEDC. 1 Publication
VAR_019837
Natural varianti1188 – 11881G → R in ACG2. 1 Publication
VAR_001764
Natural varianti1197 – 11971G → S in SEDC. 1 Publication
VAR_001765
Natural varianti1207 – 12126Missing in KD. 1 Publication
VAR_001766
Natural varianti1305 – 13051G → D in vitreoretinopathy; with phalangeal epiphyseal dysplasia. 1 Publication
VAR_023934
Natural varianti1331 – 13311V → I.2 Publications
Corresponds to variant rs12721427 [ dbSNP | Ensembl ].
VAR_017652
Natural varianti1390 – 13901T → N in PLSD-T; phenotype previously considered as achondrogenesis-hypochondrogenesis type 2. 1 Publication
VAR_024822
Natural varianti1391 – 13911Y → C in PLSD-T. 1 Publication
VAR_023935
Natural varianti1405 – 14051G → S.1 Publication
Corresponds to variant rs2070739 [ dbSNP | Ensembl ].
VAR_033785
Natural varianti1439 – 14391T → M in SEDC. 1 Publication
VAR_017105
Natural varianti1448 – 14481T → P in PLSD-T. 1 Publication
VAR_024823
Natural varianti1469 – 14691D → H in PLSD-T. 1 Publication
VAR_024824
Natural varianti1484 – 14841Missing in PLSD-T. 1 Publication
VAR_024825
Natural varianti1485 – 14851C → G in PLSD-T. 1 Publication
VAR_024826

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 12191219Missing in isoform 3. 1 PublicationVSP_022365Add
BLAST
Alternative sequencei29 – 9870QEAGS…ATASG → R in isoform 1. 2 PublicationsVSP_022366Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS41778.1. [P02458-2]
CCDS8759.1. [P02458-1]
PIRiA38513. CGHU6C.
RefSeqiNP_001835.3. NM_001844.4. [P02458-2]
NP_149162.2. NM_033150.2. [P02458-1]
UniGeneiHs.408182.

Genome annotation databases

EnsembliENST00000337299; ENSP00000338213; ENSG00000139219. [P02458-1]
ENST00000380518; ENSP00000369889; ENSG00000139219. [P02458-2]
GeneIDi1280.
KEGGihsa:1280.
UCSCiuc001rqt.3. human. [P02458-3]
uc001rqu.3. human. [P02458-2]
uc001rqv.3. human. [P02458-1]

Polymorphism databases

DMDMi124056489.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS41778.1. [P02458-2 ]
CCDS8759.1. [P02458-1 ]
PIRi A38513. CGHU6C.
RefSeqi NP_001835.3. NM_001844.4. [P02458-2 ]
NP_149162.2. NM_033150.2. [P02458-1 ]
UniGenei Hs.408182.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1U5M NMR - A 29-97 [» ]
2FSE X-ray 3.10 E/F 461-474 [» ]
2SEB X-ray 2.50 E 1238-1247 [» ]
DisProti DP00274.
ProteinModelPortali P02458.
SMRi P02458. Positions 27-97, 1271-1487.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107677. 18 interactions.
IntActi P02458. 3 interactions.
MINTi MINT-6796075.

Chemistry

ChEMBLi CHEMBL2364188.
DrugBanki DB00048. Collagenase.

PTM databases

PhosphoSitei P02458.

Polymorphism databases

DMDMi 124056489.

Proteomic databases

MaxQBi P02458.
PaxDbi P02458.
PRIDEi P02458.

Protocols and materials databases

DNASUi 1280.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000337299 ; ENSP00000338213 ; ENSG00000139219 . [P02458-1 ]
ENST00000380518 ; ENSP00000369889 ; ENSG00000139219 . [P02458-2 ]
GeneIDi 1280.
KEGGi hsa:1280.
UCSCi uc001rqt.3. human. [P02458-3 ]
uc001rqu.3. human. [P02458-2 ]
uc001rqv.3. human. [P02458-1 ]

Organism-specific databases

CTDi 1280.
GeneCardsi GC12M048366.
GeneReviewsi COL2A1.
HGNCi HGNC:2200. COL2A1.
HPAi CAB002214.
HPA045939.
MIMi 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.
neXtProti NX_P02458.
Orphaneti 93296. Achondrogenesis type 2.
209867. Autosomal dominant rhegmatogenous retinal detachment.
137678. Czech dysplasia, metatarsal type.
85198. Dysspondyloenchondromatosis.
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.
93316. Spondylometaphyseal dysplasia, Schmidt type.
1856. Spondyloperipheral dysplasia - short ulna.
90653. Stickler syndrome type 1.
PharmGKBi PA26715.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00760000118776.
HOVERGENi HBG004933.
InParanoidi P02458.
KOi K06236.
OMAi PLQYMRA.
OrthoDBi EOG7TJ3HH.
PhylomeDBi P02458.
TreeFami TF344135.

Enzyme and pathway databases

Reactomei REACT_118779. Extracellular matrix organization.
REACT_121139. Collagen biosynthesis and modifying enzymes.
REACT_13552. Integrin cell surface interactions.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_150401. Collagen degradation.
REACT_163874. Non-integrin membrane-ECM interactions.
REACT_163906. ECM proteoglycans.
REACT_16888. Signaling by PDGF.
REACT_18312. NCAM1 interactions.

Miscellaneous databases

ChiTaRSi COL2A1. human.
EvolutionaryTracei P02458.
GeneWikii Collagen,_type_II,_alpha_1.
GenomeRNAii 1280.
NextBioi 5171.
PMAP-CutDB P02458.
PROi P02458.
SOURCEi Search...

Gene expression databases

Bgeei P02458.
Genevestigatori P02458.

Family and domain databases

InterProi IPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_C.
[Graphical view ]
Pfami PF01410. COLFI. 1 hit.
PF01391. Collagen. 9 hits.
PF00093. VWC. 1 hit.
[Graphical view ]
ProDomi PD002078. Fib_collagen_C. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00038. COLFI. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view ]
PROSITEi PS51461. NC1_FIB. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: VARIANT CZECHD CYS-275.
  75. 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.

Entry informationi

Entry nameiCO2A1_HUMAN
AccessioniPrimary (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 historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 184 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for prof