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P02458

- CO2A1_HUMAN

UniProt

P02458 - CO2A1_HUMAN

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
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    • History
      Entry version 183 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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

    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 region Source: Reactome
    5. extracellular space Source: Ensembl

    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. 15 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.
    HOVERGENiHBG004933.
    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.

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    MIRLGAPQTL VLLTLLVAAV LRCQGQDVQE AGSCVQDGQR YNDKDVWKPE     50
    PCRICVCDTG TVLCDDIICE DVKDCLSPEI PFGECCPICP TDLATASGQP 100
    GPKGQKGEPG DIKDIVGPKG PPGPQGPAGE QGPRGDRGDK GEKGAPGPRG 150
    RDGEPGTPGN PGPPGPPGPP GPPGLGGNFA AQMAGGFDEK AGGAQLGVMQ 200
    GPMGPMGPRG PPGPAGAPGP QGFQGNPGEP GEPGVSGPMG PRGPPGPPGK 250
    PGDDGEAGKP GKAGERGPPG PQGARGFPGT PGLPGVKGHR GYPGLDGAKG 300
    EAGAPGVKGE SGSPGENGSP GPMGPRGLPG ERGRTGPAGA AGARGNDGQP 350
    GPAGPPGPVG PAGGPGFPGA PGAKGEAGPT GARGPEGAQG PRGEPGTPGS 400
    PGPAGASGNP GTDGIPGAKG SAGAPGIAGA PGFPGPRGPP GPQGATGPLG 450
    PKGQTGEPGI AGFKGEQGPK GEPGPAGPQG APGPAGEEGK RGARGEPGGV 500
    GPIGPPGERG APGNRGFPGQ DGLAGPKGAP GERGPSGLAG PKGANGDPGR 550
    PGEPGLPGAR GLTGRPGDAG PQGKVGPSGA PGEDGRPGPP GPQGARGQPG 600
    VMGFPGPKGA NGEPGKAGEK GLPGAPGLRG LPGKDGETGA AGPPGPAGPA 650
    GERGEQGAPG PSGFQGLPGP PGPPGEGGKP GDQGVPGEAG APGLVGPRGE 700
    RGFPGERGSP GAQGLQGPRG LPGTPGTDGP KGASGPAGPP GAQGPPGLQG 750
    MPGERGAAGI AGPKGDRGDV GEKGPEGAPG KDGGRGLTGP IGPPGPAGAN 800
    GEKGEVGPPG PAGSAGARGA PGERGETGPP GPAGFAGPPG ADGQPGAKGE 850
    QGEAGQKGDA GAPGPQGPSG APGPQGPTGV TGPKGARGAQ GPPGATGFPG 900
    AAGRVGPPGS NGNPGPPGPP GPSGKDGPKG ARGDSGPPGR AGEPGLQGPA 950
    GPPGEKGEPG DDGPSGAEGP PGPQGLAGQR GIVGLPGQRG ERGFPGLPGP 1000
    SGEPGKQGAP GASGDRGPPG PVGPPGLTGP AGEPGREGSP GADGPPGRDG 1050
    AAGVKGDRGE TGAVGAPGAP GPPGSPGPAG PTGKQGDRGE AGAQGPMGPS 1100
    GPAGARGIQG PQGPRGDKGE AGEPGERGLK GHRGFTGLQG LPGPPGPSGD 1150
    QGASGPAGPS GPRGPPGPVG PSGKDGANGI PGPIGPPGPR GRSGETGPAG 1200
    PPGNPGPPGP PGPPGPGIDM SAFAGLGPRE KGPDPLQYMR ADQAAGGLRQ 1250
    HDAEVDATLK SLNNQIESIR SPEGSRKNPA RTCRDLKLCH PEWKSGDYWI 1300
    DPNQGCTLDA MKVFCNMETG ETCVYPNPAN VPKKNWWSSK SKEKKHIWFG 1350
    ETINGGFHFS YGDDNLAPNT ANVQMTFLRL LSTEGSQNIT YHCKNSIAYL 1400
    DEAAGNLKKA LLIQGSNDVE IRAEGNSRFT YTALKDGCTK HTGKWGKTVI 1450
    EYRSQKTSRL PIIDIAPMDI GGPEQEFGVD IGPVCFL 1487
    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. 15 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 GC12M048266.
    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.
    HOVERGENi HBG004933.
    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

    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 1, 2014
    This is version 183 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 professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3