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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)DescriptionActionsGraphical viewLength
Metal bindingi1301CalciumBy similarity1
Metal bindingi1303CalciumBy similarity1
Metal bindingi1304Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1306Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1309CalciumBy similarity1

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

BioCyciZFISH:ENSG00000139219-MONOMER.
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.
R-HSA-8874081. MET activates PTK2 signaling.
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)DescriptionActionsGraphical viewLength
Natural variantiVAR_001743375G → R in SEDC. 1
Natural variantiVAR_001744447G → S in SEDC. 1 Publication1
Natural variantiVAR_001749774G → S in SEDC and hypochondrogenesis; lethal. 1 PublicationCorresponds to variant rs121912867dbSNPEnsembl.1
Natural variantiVAR_023930855G → S in SEDC. 1
Natural variantiVAR_001752891G → R in ACG2 and SEDC. 2 PublicationsCorresponds to variant rs121912879dbSNPEnsembl.1
Natural variantiVAR_001755989R → C in SEDC. 1 PublicationCorresponds to variant rs121912874dbSNPEnsembl.1
Natural variantiVAR_0017621164 – 1199Missing in SEDC. Add BLAST36
Natural variantiVAR_0176511173G → R in SEDC. 1 PublicationCorresponds to variant rs121912883dbSNPEnsembl.1
Natural variantiVAR_0017631176G → S in SEDC. 1 Publication1
Natural variantiVAR_0668361176G → V Mutation found in a patient with features of multiple epiphyseal dysplasia; features overlap with SEDC. 1 Publication1
Natural variantiVAR_0668371179G → R Mutation found in a patient with features of multiple epiphyseal dysplasia; features overlap with SEDC. 1 Publication1
Natural variantiVAR_0198371184I → IGPSGKDGANGIPGPI in SEDC. 1 Publication1
Natural variantiVAR_0017651197G → S in SEDC. 1 PublicationCorresponds to variant rs121912870dbSNPEnsembl.1
Natural variantiVAR_0171051439T → M in SEDC. 1 PublicationCorresponds to variant rs121912886dbSNPEnsembl.1
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)DescriptionActionsGraphical viewLength
Natural variantiVAR_075729207G → R in SEDSTN. 1 Publication1
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)DescriptionActionsGraphical viewLength
Natural variantiVAR_001745492G → V in SEMDSTWK. 1 PublicationCorresponds to variant rs121912881dbSNPEnsembl.1
Natural variantiVAR_001746504G → C in SEMDSTWK. 1 PublicationCorresponds to variant rs121912880dbSNPEnsembl.1
Natural variantiVAR_023931897G → V in SEMDSTWK. 1 Publication1
Natural variantiVAR_001753909G → C in SEMDSTWK. 2 PublicationsCorresponds to variant rs121912875dbSNPEnsembl.1
Natural variantiVAR_023932992R → G in SEMDSTWK. 1 PublicationCorresponds to variant rs121912895dbSNPEnsembl.1
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)DescriptionActionsGraphical viewLength
Natural variantiVAR_017639453G → D in ACG2. 1 Publication1
Natural variantiVAR_017640453G → V in ACG2. 1 Publication1
Natural variantiVAR_001747510G → D in ACG2. 1
Natural variantiVAR_024819513G → S in ACG2. 1 Publication1
Natural variantiVAR_023926516G → D in ACG2. 1 PublicationCorresponds to variant rs121912888dbSNPEnsembl.1
Natural variantiVAR_063897547D → V in ACG2. 1 Publication1
Natural variantiVAR_024820717G → V in ACG2. 1 Publication1
Natural variantiVAR_024821771G → A in ACG2. 1 Publication1
Natural variantiVAR_017641771G → D in ACG2. 1 Publication1
Natural variantiVAR_017642780G → R in ACG2. 1 Publication1
Natural variantiVAR_017643795G → R in ACG2. 1 Publication1
Natural variantiVAR_001752891G → R in ACG2 and SEDC. 2 PublicationsCorresponds to variant rs121912879dbSNPEnsembl.1
Natural variantiVAR_017644894G → E in ACG2. 1 Publication1
Natural variantiVAR_017646948G → D in ACG2. 1 Publication1
Natural variantiVAR_001754969G → S in ACG2. 1 PublicationCorresponds to variant rs121912878dbSNPEnsembl.1
Natural variantiVAR_017647981G → S in ACG2. 1 Publication1
Natural variantiVAR_0017571017G → V in ACG2. 1
Natural variantiVAR_0176491065G → V in ACG2. 1 Publication1
Natural variantiVAR_0017591110G → C in ACG2. 1 Publication1
Natural variantiVAR_0176501119G → R in ACG2. 1 Publication1
Natural variantiVAR_0017611143G → S in ACG2. 2 Publications1
Natural variantiVAR_0017641188G → R in ACG2. 1 Publication1
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)DescriptionActionsGraphical viewLength
Natural variantiVAR_0239331170G → S in ANFH and in LCPD. 2 PublicationsCorresponds to variant rs121912891dbSNPEnsembl.1
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)DescriptionActionsGraphical viewLength
Natural variantiVAR_001741303G → D in KD; abnormal allele expressed in the cartilage. 1 PublicationCorresponds to variant rs121912877dbSNPEnsembl.1
Natural variantiVAR_0017661207 – 1212Missing in KD. 1 Publication6
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)DescriptionActionsGraphical viewLength
Natural variantiVAR_023929717G → S in ANFH. 1 PublicationCorresponds to variant rs387906558dbSNPEnsembl.1
Natural variantiVAR_0239331170G → S in ANFH and in LCPD. 2 PublicationsCorresponds to variant rs121912891dbSNPEnsembl.1
Natural variantiVAR_0757301383T → M in ANFH. 1 PublicationCorresponds to variant rs138498898dbSNPEnsembl.1
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)DescriptionActionsGraphical viewLength
Natural variantiVAR_001748719R → C in OSCDP; also in mild spondyloepiphyseal dysplasia and precocious osteoarthritis. 5 PublicationsCorresponds to variant rs121912865dbSNPEnsembl.1
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)DescriptionActionsGraphical viewLength
Natural variantiVAR_0248221390T → N in PLSD-T; phenotype previously considered as achondrogenesis-hypochondrogenesis type 2. 2 Publications1
Natural variantiVAR_0239351391Y → C in PLSD-T. 1 PublicationCorresponds to variant rs121912889dbSNPEnsembl.1
Natural variantiVAR_0248231448T → P in PLSD-T. 1 Publication1
Natural variantiVAR_0248241469D → H in PLSD-T. 1 Publication1
Natural variantiVAR_0248251484Missing in PLSD-T. 1 Publication1
Natural variantiVAR_0248261485C → G in PLSD-T. 1 Publication1
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)DescriptionActionsGraphical viewLength
Natural variantiVAR_017645904R → C in EDMMD and STL1. 2 PublicationsCorresponds to variant rs121912882dbSNPEnsembl.1
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)DescriptionActionsGraphical viewLength
Natural variantiVAR_06389157C → Y in STL1O. 1 PublicationCorresponds to variant rs121912898dbSNPEnsembl.1
Natural variantiVAR_063892240G → D in STL1. 1 Publication1
Natural variantiVAR_001738267G → D in STL1O. 1 PublicationCorresponds to variant rs121912872dbSNPEnsembl.1
Natural variantiVAR_063893270G → R in STL1. 1 Publication1
Natural variantiVAR_063894282G → D in STL1. 1 Publication1
Natural variantiVAR_001740302 – 308Missing in STL1. 1 Publication7
Natural variantiVAR_063895453G → A in STL1. 1 PublicationCorresponds to variant rs794727339dbSNPEnsembl.1
Natural variantiVAR_063896501G → R in STL1. 1 Publication1
Natural variantiVAR_023927565R → C in STL1. 1 PublicationCorresponds to variant rs121912884dbSNPEnsembl.1
Natural variantiVAR_017645904R → C in EDMMD and STL1. 2 PublicationsCorresponds to variant rs121912882dbSNPEnsembl.1
Natural variantiVAR_0638981158G → A in STL1. 1 Publication1
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)DescriptionActionsGraphical viewLength
Natural variantiVAR_06389157C → Y in STL1O. 1 PublicationCorresponds to variant rs121912898dbSNPEnsembl.1
Natural variantiVAR_001738267G → D in STL1O. 1 PublicationCorresponds to variant rs121912872dbSNPEnsembl.1
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)DescriptionActionsGraphical viewLength
Natural variantiVAR_023925318G → R in DRRD. 1 PublicationCorresponds to variant rs121912894dbSNPEnsembl.1
Natural variantiVAR_023928667L → F in DRRD. 2 PublicationsCorresponds to variant rs121912885dbSNPEnsembl.1
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)DescriptionActionsGraphical viewLength
Natural variantiVAR_001739275R → C in CZECHD. 4 PublicationsCorresponds to variant rs121912876dbSNPEnsembl.1

Keywords - Diseasei

Cataract, Deafness, Disease mutation, Dwarfism, Stickler syndrome

Organism-specific databases

DisGeNETi1280.
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.
OpenTargetsiENSG00000139219.
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 databases

ChEMBLiCHEMBL2364188.
DrugBankiDB00048. Collagenase clostridium histolyticum.

Polymorphism and mutation databases

BioMutaiCOL2A1.
DMDMi124056489.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 25Sequence analysisAdd BLAST25
PropeptideiPRO_000000572926 – 181N-terminal propeptideAdd BLAST156
ChainiPRO_0000005730182 – 1241Collagen alpha-1(II) chainAdd BLAST1060
ChainiPRO_00000057311242 – 1487ChondrocalcinAdd BLAST246

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1905-hydroxylysineBy similarity1
Glycosylationi190O-linked (Gal...)By similarity1
Modified residuei2875-hydroxylysineBy similarity1
Glycosylationi287O-linked (Gal...)By similarity1
Modified residuei2995-hydroxylysineBy similarity1
Glycosylationi299O-linked (Gal...)By similarity1
Modified residuei3085-hydroxylysineBy similarity1
Glycosylationi308O-linked (Gal...)By similarity1
Modified residuei3745-hydroxylysineBy similarity1
Glycosylationi374O-linked (Gal...)By similarity1
Modified residuei6085-hydroxylysineBy similarity1
Glycosylationi608O-linked (Gal...)By similarity1
Modified residuei6205-hydroxylysineBy similarity1
Glycosylationi620O-linked (Gal...)By similarity1
Modified residuei6703-hydroxyprolineBy similarity1
Modified residuei9073-hydroxyprolineBy similarity1
Modified residuei11305-hydroxylysineBy similarity1
Glycosylationi1130O-linked (Gal...)By similarity1
Modified residuei11443-hydroxyprolineBy similarity1
Modified residuei11863-hydroxyprolineBy similarity1
Modified residuei12013-hydroxyprolineBy similarity1
Modified residuei12073-hydroxyprolineBy similarity1
Modified residuei12133-hydroxyprolineBy similarity1
Disulfide bondi1283 ↔ 1315PROSITE-ProRule annotation
Disulfide bondi1289Interchain (with C-1306)PROSITE-ProRule annotation
Disulfide bondi1306Interchain (with C-1289)PROSITE-ProRule annotation
Disulfide bondi1323 ↔ 1485PROSITE-ProRule annotation
Glycosylationi1388N-linked (GlcNAc...)1
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)DescriptionActionsGraphical viewLength
Sitei181 – 182Cleavage; by procollagen N-endopeptidaseBy similarity2
Sitei1241 – 1242Cleavage; by procollagen C-endopeptidaseBy similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

EPDiP02458.
PaxDbiP02458.
PeptideAtlasiP02458.
PRIDEiP02458.

PTM databases

iPTMnetiP02458.
PhosphoSitePlusiP02458.

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

BgeeiENSG00000139219.
GenevisibleiP02458. HS.

Organism-specific databases

HPAiCAB002214.

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 interactors.
IntActiP02458. 4 interactors.
MINTiMINT-6796075.
STRINGi9606.ENSP00000369889.

Structurei

Secondary structure

11487
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi34 – 38Combined sources5
Beta strandi51 – 58Combined sources8
Beta strandi61 – 66Combined sources6
Beta strandi91 – 94Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1U5MNMR-A29-97[»]
2FSEX-ray3.10E/F461-474[»]
2SEBX-ray2.50E1238-1247[»]
DisProtiDP00274.
ProteinModelPortaliP02458.
SMRiP02458.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02458.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini32 – 90VWFCPROSITE-ProRule annotationAdd BLAST59
Domaini1253 – 1487Fibrillar collagen NC1PROSITE-ProRule annotationAdd BLAST235

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni201 – 1214Triple-helical regionAdd BLAST1014
Regioni1215 – 1241Nonhelical region (C-terminal)Add BLAST27

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.
OMAiLQDGCTK.
OrthoDBiEOG091G03LV.
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 differs from that shown. Reason: Frameshift at position 1198.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti441G → D in CAA34488 (PubMed:2587267).Curated1
Sequence conflicti457E → K in CAA34488 (PubMed:2587267).Curated1
Sequence conflicti481A → P in AAB60370 (PubMed:7847372).Curated1
Sequence conflicti641A → E in CAA34488 (PubMed:2587267).Curated1
Sequence conflicti641A → E in CAA32030 (Ref. 16) Curated1
Sequence conflicti677G → A in CAA32030 (Ref. 16) Curated1
Sequence conflicti784G → A in CAA32030 (Ref. 16) Curated1
Sequence conflicti832 – 835PAGF → TSGI in CAA34488 (PubMed:2587267).Curated4
Sequence conflicti1006K → Q in CAA34488 (PubMed:2587267).Curated1
Sequence conflicti1006K → Q in CAA32030 (Ref. 16) Curated1
Sequence conflicti1037E → Q in CAA34683 (PubMed:2803268).Curated1
Sequence conflicti1057D → N in AAD15287 (PubMed:2987845).Curated1
Sequence conflicti1057D → N in CAA26223 (PubMed:2987845).Curated1
Sequence conflicti1057D → N in AAA51997 (PubMed:3857598).Curated1
Sequence conflicti1069A → T in CAA34683 (PubMed:2803268).Curated1
Sequence conflicti1069A → T in AAD15287 (PubMed:2987845).Curated1
Sequence conflicti1069A → T in CAA26223 (PubMed:2987845).Curated1
Sequence conflicti1069A → T in AAA51997 (PubMed:3857598).Curated1
Sequence conflicti1243Q → E in CAA29604 (PubMed:2825137).Curated1
Sequence conflicti1247G → N in CAA29604 (PubMed:2825137).Curated1
Sequence conflicti1271S → T in AAA52038 (PubMed:1905723).Curated1
Sequence conflicti1274G → A in AAA52038 (PubMed:1905723).Curated1
Sequence conflicti1333K → R in M12048 (PubMed:3002437).Curated1
Sequence conflicti1350G → A in M12048 (PubMed:3002437).Curated1
Sequence conflicti1372N → D in CAA26223 (PubMed:2987845).Curated1
Sequence conflicti1383T → A in CAA26223 (PubMed:2987845).Curated1
Sequence conflicti1400L → M in CAA26223 (PubMed:2987845).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0176389T → S.6 PublicationsCorresponds to variant rs3803183dbSNPEnsembl.1
Natural variantiVAR_06389157C → Y in STL1O. 1 PublicationCorresponds to variant rs121912898dbSNPEnsembl.1
Natural variantiVAR_033782142E → D.1 PublicationCorresponds to variant rs34392760dbSNPEnsembl.1
Natural variantiVAR_019836158P → L.1 PublicationCorresponds to variant rs1050861dbSNPEnsembl.1
Natural variantiVAR_075729207G → R in SEDSTN. 1 Publication1
Natural variantiVAR_063892240G → D in STL1. 1 Publication1
Natural variantiVAR_001738267G → D in STL1O. 1 PublicationCorresponds to variant rs121912872dbSNPEnsembl.1
Natural variantiVAR_063893270G → R in STL1. 1 Publication1
Natural variantiVAR_001739275R → C in CZECHD. 4 PublicationsCorresponds to variant rs121912876dbSNPEnsembl.1
Natural variantiVAR_063894282G → D in STL1. 1 Publication1
Natural variantiVAR_001740302 – 308Missing in STL1. 1 Publication7
Natural variantiVAR_001741303G → D in KD; abnormal allele expressed in the cartilage. 1 PublicationCorresponds to variant rs121912877dbSNPEnsembl.1
Natural variantiVAR_023925318G → R in DRRD. 1 PublicationCorresponds to variant rs121912894dbSNPEnsembl.1
Natural variantiVAR_001742354G → R in spondylometaphyseal dysplasia; congenital type. 1 PublicationCorresponds to variant rs121912871dbSNPEnsembl.1
Natural variantiVAR_001743375G → R in SEDC. 1
Natural variantiVAR_001744447G → S in SEDC. 1 Publication1
Natural variantiVAR_063895453G → A in STL1. 1 PublicationCorresponds to variant rs794727339dbSNPEnsembl.1
Natural variantiVAR_017639453G → D in ACG2. 1 Publication1
Natural variantiVAR_017640453G → V in ACG2. 1 Publication1
Natural variantiVAR_001745492G → V in SEMDSTWK. 1 PublicationCorresponds to variant rs121912881dbSNPEnsembl.1
Natural variantiVAR_063896501G → R in STL1. 1 Publication1
Natural variantiVAR_001746504G → C in SEMDSTWK. 1 PublicationCorresponds to variant rs121912880dbSNPEnsembl.1
Natural variantiVAR_001747510G → D in ACG2. 1
Natural variantiVAR_024819513G → S in ACG2. 1 Publication1
Natural variantiVAR_023926516G → D in ACG2. 1 PublicationCorresponds to variant rs121912888dbSNPEnsembl.1
Natural variantiVAR_063897547D → V in ACG2. 1 Publication1
Natural variantiVAR_023927565R → C in STL1. 1 PublicationCorresponds to variant rs121912884dbSNPEnsembl.1
Natural variantiVAR_033783638T → I.1 PublicationCorresponds to variant rs41263847dbSNPEnsembl.1
Natural variantiVAR_023928667L → F in DRRD. 2 PublicationsCorresponds to variant rs121912885dbSNPEnsembl.1
Natural variantiVAR_023929717G → S in ANFH. 1 PublicationCorresponds to variant rs387906558dbSNPEnsembl.1
Natural variantiVAR_024820717G → V in ACG2. 1 Publication1
Natural variantiVAR_001748719R → C in OSCDP; also in mild spondyloepiphyseal dysplasia and precocious osteoarthritis. 5 PublicationsCorresponds to variant rs121912865dbSNPEnsembl.1
Natural variantiVAR_024821771G → A in ACG2. 1 Publication1
Natural variantiVAR_017641771G → D in ACG2. 1 Publication1
Natural variantiVAR_001749774G → S in SEDC and hypochondrogenesis; lethal. 1 PublicationCorresponds to variant rs121912867dbSNPEnsembl.1
Natural variantiVAR_017642780G → R in ACG2. 1 Publication1
Natural variantiVAR_017643795G → R in ACG2. 1 Publication1
Natural variantiVAR_001751804G → A in hypochondrogenesis. 1
Natural variantiVAR_023930855G → S in SEDC. 1
Natural variantiVAR_001752891G → R in ACG2 and SEDC. 2 PublicationsCorresponds to variant rs121912879dbSNPEnsembl.1
Natural variantiVAR_017644894G → E in ACG2. 1 Publication1
Natural variantiVAR_023931897G → V in SEMDSTWK. 1 Publication1
Natural variantiVAR_017645904R → C in EDMMD and STL1. 2 PublicationsCorresponds to variant rs121912882dbSNPEnsembl.1
Natural variantiVAR_001753909G → C in SEMDSTWK. 2 PublicationsCorresponds to variant rs121912875dbSNPEnsembl.1
Natural variantiVAR_017646948G → D in ACG2. 1 Publication1
Natural variantiVAR_001754969G → S in ACG2. 1 PublicationCorresponds to variant rs121912878dbSNPEnsembl.1
Natural variantiVAR_017647981G → S in ACG2. 1 Publication1
Natural variantiVAR_001755989R → C in SEDC. 1 PublicationCorresponds to variant rs121912874dbSNPEnsembl.1
Natural variantiVAR_023932992R → G in SEMDSTWK. 1 PublicationCorresponds to variant rs121912895dbSNPEnsembl.1
Natural variantiVAR_0017561005G → S in hypochondrogenesis. Corresponds to variant rs753342774dbSNPEnsembl.1
Natural variantiVAR_0176481017 – 1022Missing in hypochondrogenesis. 1 Publication6
Natural variantiVAR_0017571017G → V in ACG2. 1
Natural variantiVAR_0337841051A → T.1 PublicationCorresponds to variant rs41272041dbSNPEnsembl.1
Natural variantiVAR_0017581053G → E in hypochondrogenesis; lethal. 1 PublicationCorresponds to variant rs121912868dbSNPEnsembl.1
Natural variantiVAR_0176491065G → V in ACG2. 1 Publication1
Natural variantiVAR_0017591110G → C in ACG2. 1 Publication1
Natural variantiVAR_0017601113G → C in hypochondrogenesis. 1 Publication1
Natural variantiVAR_0176501119G → R in ACG2. 1 Publication1
Natural variantiVAR_0017611143G → S in ACG2. 2 Publications1
Natural variantiVAR_0638981158G → A in STL1. 1 Publication1
Natural variantiVAR_0017621164 – 1199Missing in SEDC. Add BLAST36
Natural variantiVAR_0239331170G → S in ANFH and in LCPD. 2 PublicationsCorresponds to variant rs121912891dbSNPEnsembl.1
Natural variantiVAR_0176511173G → R in SEDC. 1 PublicationCorresponds to variant rs121912883dbSNPEnsembl.1
Natural variantiVAR_0017631176G → S in SEDC. 1 Publication1
Natural variantiVAR_0668361176G → V Mutation found in a patient with features of multiple epiphyseal dysplasia; features overlap with SEDC. 1 Publication1
Natural variantiVAR_0668371179G → R Mutation found in a patient with features of multiple epiphyseal dysplasia; features overlap with SEDC. 1 Publication1
Natural variantiVAR_0198371184I → IGPSGKDGANGIPGPI in SEDC. 1 Publication1
Natural variantiVAR_0017641188G → R in ACG2. 1 Publication1
Natural variantiVAR_0017651197G → S in SEDC. 1 PublicationCorresponds to variant rs121912870dbSNPEnsembl.1
Natural variantiVAR_0017661207 – 1212Missing in KD. 1 Publication6
Natural variantiVAR_0239341305G → D in vitreoretinopathy; with phalangeal epiphyseal dysplasia. 1 PublicationCorresponds to variant rs121912887dbSNPEnsembl.1
Natural variantiVAR_0176521331V → I.2 PublicationsCorresponds to variant rs12721427dbSNPEnsembl.1
Natural variantiVAR_0757301383T → M in ANFH. 1 PublicationCorresponds to variant rs138498898dbSNPEnsembl.1
Natural variantiVAR_0248221390T → N in PLSD-T; phenotype previously considered as achondrogenesis-hypochondrogenesis type 2. 2 Publications1
Natural variantiVAR_0239351391Y → C in PLSD-T. 1 PublicationCorresponds to variant rs121912889dbSNPEnsembl.1
Natural variantiVAR_0337851405G → S.1 PublicationCorresponds to variant rs2070739dbSNPEnsembl.1
Natural variantiVAR_0171051439T → M in SEDC. 1 PublicationCorresponds to variant rs121912886dbSNPEnsembl.1
Natural variantiVAR_0248231448T → P in PLSD-T. 1 Publication1
Natural variantiVAR_0248241469D → H in PLSD-T. 1 Publication1
Natural variantiVAR_0248251484Missing in PLSD-T. 1 Publication1
Natural variantiVAR_0248261485C → G in PLSD-T. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0223651 – 1219Missing in isoform 3. 1 PublicationAdd BLAST1219
Alternative sequenceiVSP_02236629 – 98QEAGS…ATASG → R in isoform 1. 2 PublicationsAdd BLAST70

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1U5MNMR-A29-97[»]
2FSEX-ray3.10E/F461-474[»]
2SEBX-ray2.50E1238-1247[»]
DisProtiDP00274.
ProteinModelPortaliP02458.
SMRiP02458.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107677. 24 interactors.
IntActiP02458. 4 interactors.
MINTiMINT-6796075.
STRINGi9606.ENSP00000369889.

Chemistry databases

ChEMBLiCHEMBL2364188.
DrugBankiDB00048. Collagenase clostridium histolyticum.

PTM databases

iPTMnetiP02458.
PhosphoSitePlusiP02458.

Polymorphism and mutation databases

BioMutaiCOL2A1.
DMDMi124056489.

Proteomic databases

EPDiP02458.
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.
DisGeNETi1280.
GeneCardsiCOL2A1.
GeneReviewsiCOL2A1.
HGNCiHGNC:2200. COL2A1.
HPAiCAB002214.
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.
OpenTargetsiENSG00000139219.
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.
OMAiLQDGCTK.
OrthoDBiEOG091G03LV.
PhylomeDBiP02458.
TreeFamiTF344135.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000139219-MONOMER.
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.
R-HSA-8874081. MET activates PTK2 signaling.
SIGNORiP02458.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000139219.
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...

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: November 30, 2016
This is version 206 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.