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Protein

Collagen alpha-1(II) chain

Gene

COL2A1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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
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

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

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-1442490. Collagen degradation.
R-HSA-1474244. Extracellular matrix organization.
R-HSA-1650814. Collagen biosynthesis and modifying enzymes.
R-HSA-186797. Signaling by PDGF.
R-HSA-198933. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
R-HSA-2022090. Assembly of collagen fibrils and other multimeric structures.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-3000171. Non-integrin membrane-ECM interactions.
R-HSA-3000178. ECM proteoglycans.
R-HSA-419037. NCAM1 interactions.
SIGNORiP02458.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:2200. COL2A1.

Subcellular locationi

GO - Cellular componenti

  • basement membrane Source: Ensembl
  • collagen type II trimer Source: BHF-UCL
  • endoplasmic reticulum lumen Source: Reactome
  • extracellular matrix Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Spondyloepiphyseal dysplasia congenital type (SEDC)8 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionDisorder characterized by disproportionate short stature and pleiotropic involvement of the skeletal and ocular systems.
See also OMIM:183900
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
Corresponds to variant rs121912867 [ dbSNP | Ensembl ].
VAR_001749
Natural varianti855 – 8551G → S in SEDC.
VAR_023930
Natural varianti891 – 8911G → R in ACG2 and SEDC. 2 Publications
Corresponds to variant rs121912879 [ dbSNP | Ensembl ].
VAR_001752
Natural varianti989 – 9891R → C in SEDC. 1 Publication
Corresponds to variant rs121912874 [ dbSNP | Ensembl ].
VAR_001755
Natural varianti1164 – 119936Missing in SEDC.
VAR_001762Add
BLAST
Natural varianti1173 – 11731G → R in SEDC. 1 Publication
Corresponds to variant rs121912883 [ dbSNP | Ensembl ].
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
Corresponds to variant rs121912870 [ dbSNP | Ensembl ].
VAR_001765
Natural varianti1439 – 14391T → M in SEDC. 1 Publication
Corresponds to variant rs121912886 [ dbSNP | Ensembl ].
VAR_017105
Spondyloepiphyseal dysplasia, Stanescu type (SEDSTN)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant spondyloepiphyseal dysplasia characterized by glycoproteins accumulation in chondrocytes. Clinical features include progressive joint contractures, premature degenerative joint disease particularly in the knee, hip and finger joints, and osseous distention of the metaphyseal ends of the phalanges causing swolling of interphalangeal joints of the hands. Radiological features include generalized platyspondyly, hypoplastic pelvis, epiphyseal flattening with metaphyseal splaying of the long bones, and enlarged phalangeal epimetaphyses of the hands.
See also OMIM:616583
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti207 – 2071G → R in SEDSTN. 1 Publication
VAR_075729
Spondyloepimetaphyseal dysplasia, Strudwick type (SEMDSTWK)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:184250
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti492 – 4921G → V in SEMDSTWK. 1 Publication
Corresponds to variant rs121912881 [ dbSNP | Ensembl ].
VAR_001745
Natural varianti504 – 5041G → C in SEMDSTWK. 1 Publication
Corresponds to variant rs121912880 [ dbSNP | Ensembl ].
VAR_001746
Natural varianti897 – 8971G → V in SEMDSTWK. 1 Publication
VAR_023931
Natural varianti909 – 9091G → C in SEMDSTWK. 2 Publications
Corresponds to variant rs121912875 [ dbSNP | Ensembl ].
VAR_001753
Natural varianti992 – 9921R → G in SEMDSTWK. 1 Publication
Corresponds to variant rs121912895 [ dbSNP | Ensembl ].
VAR_023932
Achondrogenesis 2 (ACG2)7 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disease characterized by the absence of ossification in the vertebral column, sacrum and pubic bones.
See also OMIM:200610
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 varianti516 – 5161G → D in ACG2. 1 Publication
Corresponds to variant rs121912888 [ dbSNP | Ensembl ].
VAR_023926
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
Corresponds to variant rs121912879 [ dbSNP | Ensembl ].
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
Corresponds to variant rs121912878 [ dbSNP | Ensembl ].
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)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionCharacterized 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.
See also OMIM:150600
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1170 – 11701G → S in ANFH and in LCPD. 2 Publications
Corresponds to variant rs121912891 [ dbSNP | Ensembl ].
VAR_023933
Kniest dysplasia (KD)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionModerately 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.
See also OMIM:156550
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti303 – 3031G → D in KD; abnormal allele expressed in the cartilage. 1 Publication
Corresponds to variant rs121912877 [ dbSNP | Ensembl ].
VAR_001741
Natural varianti1207 – 12126Missing in KD. 1 Publication
VAR_001766
Avascular necrosis of the femoral head, primary (ANFH)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disease characterized by mechanical failure of the subchondral bone, and degeneration of the hip joint. It usually leads to destruction of the hip joint in the third to fifth decade of life. The clinical manifestations, such as pain on exertion, a limping gait, and a discrepancy in leg length, cause considerable disability.
See also OMIM:608805
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti717 – 7171G → S in ANFH. 1 Publication
Corresponds to variant rs387906558 [ dbSNP | Ensembl ].
VAR_023929
Natural varianti1170 – 11701G → S in ANFH and in LCPD. 2 Publications
Corresponds to variant rs121912891 [ dbSNP | Ensembl ].
VAR_023933
Natural varianti1383 – 13831T → M in ANFH. 1 Publication
Corresponds to variant rs138498898 [ dbSNP | Ensembl ].
VAR_075730
Osteoarthritis with mild chondrodysplasia (OSCDP)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionOsteoarthritis is a common disease that produces joint pain and stiffness together with radiologic evidence of progressive degeneration of joint cartilage.
See also OMIM:604864
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti719 – 7191R → C in OSCDP; also in mild spondyloepiphyseal dysplasia and precocious osteoarthritis. 5 Publications
Corresponds to variant rs121912865 [ dbSNP | Ensembl ].
VAR_001748
Platyspondylic lethal skeletal dysplasia Torrance type (PLSD-T)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionPlatyspondylic 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.
See also OMIM:151210
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1390 – 13901T → N in PLSD-T; phenotype previously considered as achondrogenesis-hypochondrogenesis type 2. 2 Publications
VAR_024822
Natural varianti1391 – 13911Y → C in PLSD-T. 1 Publication
Corresponds to variant rs121912889 [ dbSNP | Ensembl ].
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)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:132450
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti904 – 9041R → C in EDMMD and STL1. 2 Publications
Corresponds to variant rs121912882 [ dbSNP | Ensembl ].
VAR_017645
Spondyloperipheral dysplasia (SPD)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionSPD patients manifest short stature, midface hypoplasia, sensorineural hearing loss, spondyloepiphyseal dysplasia, platyspondyly and brachydactyly.
See also OMIM:271700
Stickler syndrome 1 (STL1)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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. Pierre 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.
See also OMIM:108300
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti57 – 571C → Y in STL1O. 1 Publication
Corresponds to variant rs121912898 [ dbSNP | Ensembl ].
VAR_063891
Natural varianti240 – 2401G → D in STL1. 1 Publication
VAR_063892
Natural varianti267 – 2671G → D in STL1O. 1 Publication
Corresponds to variant rs121912872 [ dbSNP | Ensembl ].
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
Corresponds to variant rs794727339 [ dbSNP | Ensembl ].
VAR_063895
Natural varianti501 – 5011G → R in STL1. 1 Publication
VAR_063896
Natural varianti565 – 5651R → C in STL1. 1 Publication
Corresponds to variant rs121912884 [ dbSNP | Ensembl ].
VAR_023927
Natural varianti904 – 9041R → C in EDMMD and STL1. 2 Publications
Corresponds to variant rs121912882 [ dbSNP | Ensembl ].
VAR_017645
Natural varianti1158 – 11581G → A in STL1. 1 Publication
VAR_063898
Stickler syndrome 1 non-syndromic ocular (STL1O)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:609508
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti57 – 571C → Y in STL1O. 1 Publication
Corresponds to variant rs121912898 [ dbSNP | Ensembl ].
VAR_063891
Natural varianti267 – 2671G → D in STL1O. 1 Publication
Corresponds to variant rs121912872 [ dbSNP | Ensembl ].
VAR_001738
Rhegmatogenous retinal detachment autosomal dominant (DRRD)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:609508
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti318 – 3181G → R in DRRD. 1 Publication
Corresponds to variant rs121912894 [ dbSNP | Ensembl ].
VAR_023925
Natural varianti667 – 6671L → F in DRRD. 2 Publications
Corresponds to variant rs121912885 [ dbSNP | Ensembl ].
VAR_023928
Czech dysplasia (CZECHD)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA skeletal dysplasia characterized by early-onset, progressive pseudorheumatoid arthritis, platyspondyly, and short third and fourth toes.
See also OMIM:609162
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti275 – 2751R → C in CZECHD. 4 Publications
Corresponds to variant rs121912876 [ dbSNP | Ensembl ].
VAR_001739

Keywords - Diseasei

Cataract, Deafness, Disease mutation, Dwarfism, Stickler syndrome

Organism-specific databases

MalaCardsiCOL2A1.
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.
616583. 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.
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.
3450. Weissenbacher- Zweymuller syndrome.
PharmGKBiPA26715.

Chemistry

ChEMBLiCHEMBL2364188.
DrugBankiDB00048. Collagenase clostridium histolyticum.

Polymorphism and mutation databases

BioMutaiCOL2A1.
DMDMi124056489.

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei181 – 1822Cleavage; by procollagen N-endopeptidaseBy similarity
Sitei1241 – 12422Cleavage; by procollagen C-endopeptidaseBy similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

EPDiP02458.
MaxQBiP02458.
PaxDbiP02458.
PeptideAtlasiP02458.
PRIDEiP02458.

PTM databases

iPTMnetiP02458.
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.
GenevisibleiP02458. HS.

Organism-specific databases

HPAiCAB002214.
HPA045939.

Interactioni

Subunit structurei

Homotrimers of alpha 1(II) chains.

GO - Molecular functioni

  • identical protein binding Source: BHF-UCL
  • platelet-derived growth factor binding Source: MGI

Protein-protein interaction databases

BioGridi107677. 24 interactions.
IntActiP02458. 3 interactions.
MINTiMINT-6796075.
STRINGi9606.ENSP00000369889.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

eggNOGiKOG3544. Eukaryota.
ENOG410XNMM. LUCA.
GeneTreeiENSGT00840000129673.
HOVERGENiHBG004933.
InParanoidiP02458.
KOiK19719.
OMAiLRCQGQD.
OrthoDBiEOG7TJ3HH.
PhylomeDBiP02458.
TreeFamiTF344135.

Family and domain databases

InterProiIPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_dom.
[Graphical view]
PfamiPF01410. COLFI. 1 hit.
PF01391. Collagen. 6 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. AlignAdd to basket

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. Curated

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 (Ref. 16) Curated
Sequence conflicti677 – 6771G → A in CAA32030 (Ref. 16) Curated
Sequence conflicti784 – 7841G → A in CAA32030 (Ref. 16) Curated
Sequence conflicti832 – 8354PAGF → TSGI in CAA34488 (PubMed:2587267).Curated
Sequence conflicti1006 – 10061K → Q in CAA34488 (PubMed:2587267).Curated
Sequence conflicti1006 – 10061K → Q in CAA32030 (Ref. 16) Curated
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
Corresponds to variant rs121912898 [ dbSNP | Ensembl ].
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 varianti207 – 2071G → R in SEDSTN. 1 Publication
VAR_075729
Natural varianti240 – 2401G → D in STL1. 1 Publication
VAR_063892
Natural varianti267 – 2671G → D in STL1O. 1 Publication
Corresponds to variant rs121912872 [ dbSNP | Ensembl ].
VAR_001738
Natural varianti270 – 2701G → R in STL1. 1 Publication
VAR_063893
Natural varianti275 – 2751R → C in CZECHD. 4 Publications
Corresponds to variant rs121912876 [ dbSNP | Ensembl ].
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
Corresponds to variant rs121912877 [ dbSNP | Ensembl ].
VAR_001741
Natural varianti318 – 3181G → R in DRRD. 1 Publication
Corresponds to variant rs121912894 [ dbSNP | Ensembl ].
VAR_023925
Natural varianti354 – 3541G → R in spondylometaphyseal dysplasia; congenital type. 1 Publication
Corresponds to variant rs121912871 [ dbSNP | Ensembl ].
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
Corresponds to variant rs794727339 [ dbSNP | Ensembl ].
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
Corresponds to variant rs121912881 [ dbSNP | Ensembl ].
VAR_001745
Natural varianti501 – 5011G → R in STL1. 1 Publication
VAR_063896
Natural varianti504 – 5041G → C in SEMDSTWK. 1 Publication
Corresponds to variant rs121912880 [ dbSNP | Ensembl ].
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 ACG2. 1 Publication
Corresponds to variant rs121912888 [ dbSNP | Ensembl ].
VAR_023926
Natural varianti547 – 5471D → V in ACG2. 1 Publication
VAR_063897
Natural varianti565 – 5651R → C in STL1. 1 Publication
Corresponds to variant rs121912884 [ dbSNP | Ensembl ].
VAR_023927
Natural varianti638 – 6381T → I.1 Publication
Corresponds to variant rs41263847 [ dbSNP | Ensembl ].
VAR_033783
Natural varianti667 – 6671L → F in DRRD. 2 Publications
Corresponds to variant rs121912885 [ dbSNP | Ensembl ].
VAR_023928
Natural varianti717 – 7171G → S in ANFH. 1 Publication
Corresponds to variant rs387906558 [ dbSNP | Ensembl ].
VAR_023929
Natural varianti717 – 7171G → V in ACG2. 1 Publication
VAR_024820
Natural varianti719 – 7191R → C in OSCDP; also in mild spondyloepiphyseal dysplasia and precocious osteoarthritis. 5 Publications
Corresponds to variant rs121912865 [ dbSNP | Ensembl ].
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
Corresponds to variant rs121912867 [ dbSNP | Ensembl ].
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
Corresponds to variant rs121912879 [ dbSNP | Ensembl ].
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
Corresponds to variant rs121912882 [ dbSNP | Ensembl ].
VAR_017645
Natural varianti909 – 9091G → C in SEMDSTWK. 2 Publications
Corresponds to variant rs121912875 [ dbSNP | Ensembl ].
VAR_001753
Natural varianti948 – 9481G → D in ACG2. 1 Publication
VAR_017646
Natural varianti969 – 9691G → S in ACG2. 1 Publication
Corresponds to variant rs121912878 [ dbSNP | Ensembl ].
VAR_001754
Natural varianti981 – 9811G → S in ACG2. 1 Publication
VAR_017647
Natural varianti989 – 9891R → C in SEDC. 1 Publication
Corresponds to variant rs121912874 [ dbSNP | Ensembl ].
VAR_001755
Natural varianti992 – 9921R → G in SEMDSTWK. 1 Publication
Corresponds to variant rs121912895 [ dbSNP | Ensembl ].
VAR_023932
Natural varianti1005 – 10051G → S in hypochondrogenesis.
Corresponds to variant rs753342774 [ dbSNP | Ensembl ].
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
Corresponds to variant rs121912868 [ dbSNP | Ensembl ].
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
Corresponds to variant rs121912891 [ dbSNP | Ensembl ].
VAR_023933
Natural varianti1173 – 11731G → R in SEDC. 1 Publication
Corresponds to variant rs121912883 [ dbSNP | Ensembl ].
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
Corresponds to variant rs121912870 [ dbSNP | Ensembl ].
VAR_001765
Natural varianti1207 – 12126Missing in KD. 1 Publication
VAR_001766
Natural varianti1305 – 13051G → D in vitreoretinopathy; with phalangeal epiphyseal dysplasia. 1 Publication
Corresponds to variant rs121912887 [ dbSNP | Ensembl ].
VAR_023934
Natural varianti1331 – 13311V → I.2 Publications
Corresponds to variant rs12721427 [ dbSNP | Ensembl ].
VAR_017652
Natural varianti1383 – 13831T → M in ANFH. 1 Publication
Corresponds to variant rs138498898 [ dbSNP | Ensembl ].
VAR_075730
Natural varianti1390 – 13901T → N in PLSD-T; phenotype previously considered as achondrogenesis-hypochondrogenesis type 2. 2 Publications
VAR_024822
Natural varianti1391 – 13911Y → C in PLSD-T. 1 Publication
Corresponds to variant rs121912889 [ dbSNP | Ensembl ].
VAR_023935
Natural varianti1405 – 14051G → S.1 Publication
Corresponds to variant rs2070739 [ dbSNP | Ensembl ].
VAR_033785
Natural varianti1439 – 14391T → M in SEDC. 1 Publication
Corresponds to variant rs121912886 [ dbSNP | Ensembl ].
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:
EMBLi
GenBanki
DDBJi
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.
UCSCiuc001rqu.4. human. [P02458-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi107677. 24 interactions.
IntActiP02458. 3 interactions.
MINTiMINT-6796075.
STRINGi9606.ENSP00000369889.

Chemistry

ChEMBLiCHEMBL2364188.
DrugBankiDB00048. Collagenase clostridium histolyticum.

PTM databases

iPTMnetiP02458.
PhosphoSiteiP02458.

Polymorphism and mutation databases

BioMutaiCOL2A1.
DMDMi124056489.

Proteomic databases

EPDiP02458.
MaxQBiP02458.
PaxDbiP02458.
PeptideAtlasiP02458.
PRIDEiP02458.

Protocols and materials databases

DNASUi1280.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000337299; ENSP00000338213; ENSG00000139219. [P02458-1]
ENST00000380518; ENSP00000369889; ENSG00000139219. [P02458-2]
GeneIDi1280.
KEGGihsa:1280.
UCSCiuc001rqu.4. human. [P02458-2]

Organism-specific databases

CTDi1280.
GeneCardsiCOL2A1.
GeneReviewsiCOL2A1.
HGNCiHGNC:2200. COL2A1.
HPAiCAB002214.
HPA045939.
MalaCardsiCOL2A1.
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.
616583. phenotype.
neXtProtiNX_P02458.
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.
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.
3450. Weissenbacher- Zweymuller syndrome.
PharmGKBiPA26715.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3544. Eukaryota.
ENOG410XNMM. LUCA.
GeneTreeiENSGT00840000129673.
HOVERGENiHBG004933.
InParanoidiP02458.
KOiK19719.
OMAiLRCQGQD.
OrthoDBiEOG7TJ3HH.
PhylomeDBiP02458.
TreeFamiTF344135.

Enzyme and pathway databases

ReactomeiR-HSA-1442490. Collagen degradation.
R-HSA-1474244. Extracellular matrix organization.
R-HSA-1650814. Collagen biosynthesis and modifying enzymes.
R-HSA-186797. Signaling by PDGF.
R-HSA-198933. Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
R-HSA-2022090. Assembly of collagen fibrils and other multimeric structures.
R-HSA-216083. Integrin cell surface interactions.
R-HSA-3000171. Non-integrin membrane-ECM interactions.
R-HSA-3000178. ECM proteoglycans.
R-HSA-419037. NCAM1 interactions.
SIGNORiP02458.

Miscellaneous databases

ChiTaRSiCOL2A1. human.
EvolutionaryTraceiP02458.
GeneWikiiCollagen,_type_II,_alpha_1.
GenomeRNAii1280.
PMAP-CutDBP02458.
PROiP02458.
SOURCEiSearch...

Gene expression databases

BgeeiP02458.
GenevisibleiP02458. HS.

Family and domain databases

InterProiIPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_dom.
[Graphical view]
PfamiPF01410. COLFI. 1 hit.
PF01391. Collagen. 6 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]
ProtoNetiSearch...

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: