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UniProtKB - P02458 (CO2A1_HUMAN)

Entry version 245 (23 Feb 2022)
Sequence version 3 (23 Jan 2007)
Previous versions | rss
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi1301CalciumBy similarity1
Metal bindingi1303CalciumBy similarity1
Metal bindingi1304Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1306Calcium; via carbonyl oxygenBy similarity1
Metal bindingi1309CalciumBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

LigandCalcium, Metal-binding

Enzyme and pathway databases

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		P02458

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-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
R-HSA-8948216, Collagen chain trimerization

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...SignaLinki		P02458

SIGNOR Signaling Network Open Resource

More...SIGNORi		P02458

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Collagen alpha-1(II) chainCurated
Alternative name(s):
Alpha-1 type II collagenCurated
Cleaved into the following 2 chains:
Collagen alpha-1(II) chainCurated
Chondrocalcin1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:COL2A1Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 12

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:2200, COL2A1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		120140, gene+phenotype

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P02458

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000139219

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Extracellular matrix, Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Spondyloepiphyseal dysplasia congenital type (SEDC)8 Publications
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionDisorder characterized by disproportionate short stature and pleiotropic involvement of the skeletal and ocular systems.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>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 dbSNP:rs121912867EnsemblClinVar.1
Natural variantiVAR_023930855G → S in SEDC. Corresponds to variant dbSNP:rs1193507525Ensembl.1
Natural variantiVAR_001752891G → R in ACG2 and SEDC. 2 PublicationsCorresponds to variant dbSNP:rs121912879EnsemblClinVar.1
Natural variantiVAR_001755989R → C in SEDC. 1 PublicationCorresponds to variant dbSNP:rs121912874EnsemblClinVar.1
Natural variantiVAR_0017621164 – 1199Missing in SEDC. Add BLAST36
Natural variantiVAR_0176511173G → R in SEDC. 1 PublicationCorresponds to variant dbSNP:rs121912883EnsemblClinVar.1
Natural variantiVAR_0017631176G → S in SEDC. 1 Publication1
Natural variantiVAR_0198371184I → IGPSGKDGANGIPGPI in SEDC. 1 Publication1
Natural variantiVAR_0017651197G → S in SEDC. 1 PublicationCorresponds to variant dbSNP:rs121912870EnsemblClinVar.1
Natural variantiVAR_0171051439T → M in SEDC. 1 PublicationCorresponds to variant dbSNP:rs121912886EnsemblClinVar.1
Spondyloepiphyseal dysplasia, Stanescu type (SEDSTN)1 Publication
The disease is caused by variants 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.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_075729207G → R in SEDSTN. 1 PublicationCorresponds to variant dbSNP:rs869312907EnsemblClinVar.1
Spondyloepimetaphyseal dysplasia, Strudwick type (SEMDSTWK)3 Publications
The disease is caused by variants 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.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_001745492G → V in SEMDSTWK. 1 PublicationCorresponds to variant dbSNP:rs121912881EnsemblClinVar.1
Natural variantiVAR_001746504G → C in SEMDSTWK. 1 PublicationCorresponds to variant dbSNP:rs121912880EnsemblClinVar.1
Natural variantiVAR_023931897G → V in SEMDSTWK. 1 Publication1
Natural variantiVAR_001753909G → C in SEMDSTWK. 2 PublicationsCorresponds to variant dbSNP:rs121912875EnsemblClinVar.1
Natural variantiVAR_023932992R → G in SEMDSTWK. 1 PublicationCorresponds to variant dbSNP:rs121912895EnsemblClinVar.1
Achondrogenesis 2 (ACG2)8 Publications
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant disease characterized by the absence of ossification in the vertebral column, sacrum and pubic bones.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_017639453G → D in ACG2. 1 PublicationCorresponds to variant dbSNP:rs794727339EnsemblClinVar.1
Natural variantiVAR_017640453G → V in ACG2. 1 Publication1
Natural variantiVAR_001747510G → D in ACG2. 1
Natural variantiVAR_024819513G → S in ACG2. 1 PublicationCorresponds to variant dbSNP:rs1555167156EnsemblClinVar.1
Natural variantiVAR_023926516G → D in ACG2. 1 PublicationCorresponds to variant dbSNP:rs121912888EnsemblClinVar.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 dbSNP:rs121912879EnsemblClinVar.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 dbSNP:rs121912878EnsemblClinVar.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 variants 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.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0239331170G → S in ANFH1 and LCPD. 2 PublicationsCorresponds to variant dbSNP:rs121912891EnsemblClinVar.1
Kniest dysplasia (KD)2 Publications
The disease is caused by variants 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.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_001741303G → D in KD; abnormal allele expressed in the cartilage. 1 PublicationCorresponds to variant dbSNP:rs121912877EnsemblClinVar.1
Natural variantiVAR_0017661207 – 1212Missing in KD. 1 Publication6
Avascular necrosis of femoral head, primary, 1 (ANFH1)2 Publications
The disease is caused by variants 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. ANFH1 inheritance is autosomal dominant.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_023929717G → S in ANFH1. 1 PublicationCorresponds to variant dbSNP:rs387906558EnsemblClinVar.1
Natural variantiVAR_0239331170G → S in ANFH1 and LCPD. 2 PublicationsCorresponds to variant dbSNP:rs121912891EnsemblClinVar.1
Natural variantiVAR_0757301383T → M in ANFH1. 1 PublicationCorresponds to variant dbSNP:rs138498898EnsemblClinVar.1
Osteoarthritis with mild chondrodysplasia (OSCDP)4 Publications
The disease is caused by variants 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.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_001748719R → C in OSCDP; also in mild spondyloepiphyseal dysplasia and precocious osteoarthritis. 5 PublicationsCorresponds to variant dbSNP:rs121912865EnsemblClinVar.1
Platyspondylic lethal skeletal dysplasia Torrance type (PLSD-T)3 Publications
The disease is caused by variants 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.
Related information in OMIM
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 dbSNP:rs121912889EnsemblClinVar.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 variants 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.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_017645904R → C in EDMMD and STL1. 2 PublicationsCorresponds to variant dbSNP:rs121912882EnsemblClinVar.1
Spondyloperipheral dysplasia (SPD)1 Publication
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionSPD patients manifest short stature, midface hypoplasia, sensorineural hearing loss, spondyloepiphyseal dysplasia, platyspondyly and brachydactyly.
Related information in OMIM
Stickler syndrome 1 (STL1)3 Publications
The disease is caused by variants 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.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_063892240G → D in STL1. 1 PublicationCorresponds to variant dbSNP:rs1592232040EnsemblClinVar.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 dbSNP:rs794727339EnsemblClinVar.1
Natural variantiVAR_063896501G → R in STL1. 1 Publication1
Natural variantiVAR_023927565R → C in STL1. 1 PublicationCorresponds to variant dbSNP:rs121912884EnsemblClinVar.1
Natural variantiVAR_017645904R → C in EDMMD and STL1. 2 PublicationsCorresponds to variant dbSNP:rs121912882EnsemblClinVar.1
Natural variantiVAR_0638981158G → A in STL1. 1 Publication1
Stickler syndrome 1 non-syndromic ocular (STL1O)3 Publications
The disease is caused by variants 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.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06389157C → Y in STL1O. 1 PublicationCorresponds to variant dbSNP:rs121912898EnsemblClinVar.1
Natural variantiVAR_001738267G → D in STL1O. 1 PublicationCorresponds to variant dbSNP:rs121912872EnsemblClinVar.1
Rhegmatogenous retinal detachment autosomal dominant (DRRD)2 Publications
The disease is caused by variants 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.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_023925318G → R in DRRD. 1 PublicationCorresponds to variant dbSNP:rs121912894EnsemblClinVar.1
Natural variantiVAR_023928667L → F in DRRD. 2 PublicationsCorresponds to variant dbSNP:rs121912885EnsemblClinVar.1
Czech dysplasia (CZECHD)4 Publications
The disease is caused by variants 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.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_001739275R → C in CZECHD. 4 PublicationsCorresponds to variant dbSNP:rs121912876EnsemblClinVar.1
Vitreoretinopathy with phalangeal epiphyseal dysplasia (VPED)1 Publication
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant disorder characterized by rhegmatogenous retinal detachment, premature arthropathy, and development of phalangeal epiphyseal dysplasia resulting in brachydactyly.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0239341305G → D in VPED. 1 PublicationCorresponds to variant dbSNP:rs121912887EnsemblClinVar.1

Keywords - Diseasei

Cataract, Deafness, Disease variant, Dwarfism, Stickler syndrome

Organism-specific databases

DisGeNET

More...DisGeNETi		1280

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

More...GeneReviewsi		COL2A1

MalaCards human disease database

More...MalaCardsi		COL2A1
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
619248, phenotype

Open Targets

More...OpenTargetsi		ENSG00000139219

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		93296, Achondrogenesis type 2
166100, Autosomal dominant otospondylomegaepiphyseal dysplasia
209867, Autosomal dominant rhegmatogenous retinal detachment
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
137678, Spondyloepiphyseal dysplasia with metatarsal shortening
459051, Spondyloepiphyseal dysplasia, Stanescu type
93315, Spondylometaphyseal dysplasia, 'corner fracture' type
93316, Spondylometaphyseal dysplasia, Schmidt type
1856, Spondyloperipheral dysplasia-short ulna syndrome
90653, Stickler syndrome type 1

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA26715

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P02458, Tbio

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2364188

Drug and drug target database

More...DrugBanki		DB00048, Collagenase clostridium histolyticum

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		COL2A1

Domain mapping of disease mutations (DMDM)

More...DMDMi		124056489

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 25Sequence analysisAdd BLAST25
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_000000572926 – 181N-terminal propeptideAdd BLAST156
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000005730182 – 1241Collagen alpha-1(II) chainAdd BLAST1060
ChainiPRO_00000057311242 – 1487ChondrocalcinAdd BLAST246

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1905-hydroxylysineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi190O-linked (Gal...) hydroxylysineBy similarity1
Modified residuei2875-hydroxylysineBy similarity1
Glycosylationi287O-linked (Gal...) hydroxylysineBy similarity1
Modified residuei2995-hydroxylysineBy similarity1
Glycosylationi299O-linked (Gal...) hydroxylysineBy similarity1
Modified residuei3085-hydroxylysineBy similarity1
Glycosylationi308O-linked (Gal...) hydroxylysineBy similarity1
Modified residuei3745-hydroxylysineBy similarity1
Glycosylationi374O-linked (Gal...) hydroxylysineBy similarity1
Modified residuei6085-hydroxylysineBy similarity1
Glycosylationi608O-linked (Gal...) hydroxylysineBy similarity1
Modified residuei6205-hydroxylysineBy similarity1
Glycosylationi620O-linked (Gal...) hydroxylysineBy similarity1
Modified residuei6594-hydroxyprolineBy similarity1
Modified residuei6684-hydroxyprolineBy similarity1
Modified residuei6703-hydroxyprolineBy similarity1
Modified residuei6714-hydroxyprolineBy similarity1
Modified residuei6744-hydroxyprolineBy similarity1
Modified residuei9073-hydroxyprolineBy similarity1
Modified residuei9084-hydroxyprolineBy similarity1
Modified residuei9144-hydroxyprolineBy similarity1
Modified residuei9204-hydroxyprolineBy similarity1
Modified residuei11305-hydroxylysineBy similarity1
Glycosylationi1130O-linked (Gal...) hydroxylysineBy similarity1
Modified residuei11443-hydroxyprolineBy similarity1
Modified residuei11814-hydroxyprolineBy similarity1
Modified residuei11863-hydroxyprolineBy similarity1
Modified residuei11874-hydroxyprolineBy similarity1
Modified residuei12013-hydroxyprolineBy similarity1
Modified residuei12024-hydroxyprolineBy similarity1
Modified residuei12054-hydroxyprolineBy similarity1
Modified residuei12073-hydroxyprolineBy similarity1
Modified residuei12084-hydroxyprolineBy similarity1
Modified residuei12114-hydroxyprolineBy similarity1
Modified residuei12133-hydroxyprolineBy similarity1
Modified residuei12144-hydroxyprolineBy similarity1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>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...) asparagine1
Disulfide bondi1393 ↔ 1438PROSITE-ProRule annotation

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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.
Contains mostly 4-hydroxyproline. Prolines at the third position of the tripeptide repeating unit (G-X-P) are 4-hydroxylated in some or all of the chains.By similarity
Contains 3-hydroxyproline at a few sites. This modification occurs on the first proline residue in the sequence motif Gly-Pro-Hyp, where Hyp is 4-hydroxyproline.By similarity
Lysine residues at the third position of the tripeptide repeating unit (G-X-Y) are 5-hydroxylated in some or all of the chains.By similarity
O-glycosylated on hydroxylated lysine residues. The O-linked glycan consists of a Glc-Gal disaccharide.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei181 – 182Cleavage; by procollagen N-endopeptidaseBy similarity2
Sitei1241 – 1242Cleavage; by procollagen C-endopeptidaseBy similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P02458

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P02458

MaxQB - The MaxQuant DataBase

More...MaxQBi		P02458

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P02458

PeptideAtlas

More...PeptideAtlasi		P02458

PRoteomics IDEntifications database

More...PRIDEi		P02458

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		51519 [P02458-2]
51520 [P02458-1]
51521 [P02458-3]

PTM databases

GlyConnect protein glycosylation platform

More...GlyConnecti		1126, 1 N-Linked glycan (1 site)

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		P02458, 9 sites, 1 N-linked glycan (1 site)

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P02458

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P02458

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000139219, Expressed in tibia and 115 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P02458, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000139219, Group enriched (epididymis, pituitary gland, retina, stomach)

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotrimers of alpha 1(II) chains.

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		107677, 36 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-1713, Collagen type II trimer
CPX-1750, Collagen type XI trimer variant 1

Protein interaction database and analysis system

More...IntActi		P02458, 27 interactors

Molecular INTeraction database

More...MINTi		P02458

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000369889

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P02458, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

11487
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P02458

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P02458

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini32 – 90VWFCPROSITE-ProRule annotationAdd BLAST59
Domaini1253 – 1487Fibrillar collagen NC1PROSITE-ProRule annotationAdd BLAST235

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni97 – 1237DisorderedSequence analysisAdd BLAST1141
Regioni201 – 1214Triple-helical regionAdd BLAST1014
Regioni1215 – 1241Nonhelical region (C-terminal)Add BLAST27

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi133 – 149Basic and acidic residuesSequence analysisAdd BLAST17
Compositional biasi157 – 174Pro residuesSequence analysisAdd BLAST18
Compositional biasi237 – 251Pro residuesSequence analysisAdd BLAST15
Compositional biasi351 – 365Pro residuesSequence analysisAdd BLAST15
Compositional biasi432 – 446Pro residuesSequence analysisAdd BLAST15
Compositional biasi910 – 924Pro residuesSequence analysisAdd BLAST15
Compositional biasi1200 – 1217Pro residuesSequence analysisAdd BLAST18

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the fibrillar collagen family.PROSITE-ProRule annotation

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3544, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000155224

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_001074_2_3_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P02458

Identification of Orthologs from Complete Genome Data

More...OMAi		WGKTMIE

Database of Orthologous Groups

More...OrthoDBi		337699at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P02458

TreeFam database of animal gene trees

More...TreeFami		TF344135

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR008160, Collagen
IPR000885, Fib_collagen_C
IPR001007, VWF_dom

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01410, COLFI, 1 hit
PF01391, Collagen, 6 hits
PF00093, VWC, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00038, COLFI, 1 hit
SM00214, VWC, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51461, NC1_FIB, 1 hit
PS01208, VWFC_1, 1 hit
PS50184, VWFC_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 2 (identifier: P02458-2) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <p><strong>What is the canonical sequence?</strong><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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.

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

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAH07252 differs from that shown. Reason: Frameshift.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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 → S6 PublicationsCorresponds to variant dbSNP:rs3803183EnsemblClinVar.1
Natural variantiVAR_06389157C → Y in STL1O. 1 PublicationCorresponds to variant dbSNP:rs121912898EnsemblClinVar.1
Natural variantiVAR_033782142E → D1 PublicationCorresponds to variant dbSNP:rs34392760EnsemblClinVar.1
Natural variantiVAR_019836158P → L1 PublicationCorresponds to variant dbSNP:rs1050861Ensembl.1
Natural variantiVAR_075729207G → R in SEDSTN. 1 PublicationCorresponds to variant dbSNP:rs869312907EnsemblClinVar.1
Natural variantiVAR_063892240G → D in STL1. 1 PublicationCorresponds to variant dbSNP:rs1592232040EnsemblClinVar.1
Natural variantiVAR_001738267G → D in STL1O. 1 PublicationCorresponds to variant dbSNP:rs121912872EnsemblClinVar.1
Natural variantiVAR_063893270G → R in STL1. 1 Publication1
Natural variantiVAR_001739275R → C in CZECHD. 4 PublicationsCorresponds to variant dbSNP:rs121912876EnsemblClinVar.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 dbSNP:rs121912877EnsemblClinVar.1
Natural variantiVAR_023925318G → R in DRRD. 1 PublicationCorresponds to variant dbSNP:rs121912894EnsemblClinVar.1
Natural variantiVAR_001742354G → R in spondylometaphyseal dysplasia; congenital type. 1 PublicationCorresponds to variant dbSNP:rs121912871EnsemblClinVar.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 dbSNP:rs794727339EnsemblClinVar.1
Natural variantiVAR_017639453G → D in ACG2. 1 PublicationCorresponds to variant dbSNP:rs794727339EnsemblClinVar.1
Natural variantiVAR_017640453G → V in ACG2. 1 Publication1
Natural variantiVAR_001745492G → V in SEMDSTWK. 1 PublicationCorresponds to variant dbSNP:rs121912881EnsemblClinVar.1
Natural variantiVAR_063896501G → R in STL1. 1 Publication1
Natural variantiVAR_001746504G → C in SEMDSTWK. 1 PublicationCorresponds to variant dbSNP:rs121912880EnsemblClinVar.1
Natural variantiVAR_001747510G → D in ACG2. 1
Natural variantiVAR_024819513G → S in ACG2. 1 PublicationCorresponds to variant dbSNP:rs1555167156EnsemblClinVar.1
Natural variantiVAR_023926516G → D in ACG2. 1 PublicationCorresponds to variant dbSNP:rs121912888EnsemblClinVar.1
Natural variantiVAR_063897547D → V in ACG2. 1 Publication1
Natural variantiVAR_023927565R → C in STL1. 1 PublicationCorresponds to variant dbSNP:rs121912884EnsemblClinVar.1
Natural variantiVAR_033783638T → I1 PublicationCorresponds to variant dbSNP:rs41263847EnsemblClinVar.1
Natural variantiVAR_023928667L → F in DRRD. 2 PublicationsCorresponds to variant dbSNP:rs121912885EnsemblClinVar.1
Natural variantiVAR_023929717G → S in ANFH1. 1 PublicationCorresponds to variant dbSNP:rs387906558EnsemblClinVar.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 dbSNP:rs121912865EnsemblClinVar.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 dbSNP:rs121912867EnsemblClinVar.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. Corresponds to variant dbSNP:rs1193507525Ensembl.1
Natural variantiVAR_001752891G → R in ACG2 and SEDC. 2 PublicationsCorresponds to variant dbSNP:rs121912879EnsemblClinVar.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 dbSNP:rs121912882EnsemblClinVar.1
Natural variantiVAR_001753909G → C in SEMDSTWK. 2 PublicationsCorresponds to variant dbSNP:rs121912875EnsemblClinVar.1
Natural variantiVAR_017646948G → D in ACG2. 1 Publication1
Natural variantiVAR_001754969G → S in ACG2. 1 PublicationCorresponds to variant dbSNP:rs121912878EnsemblClinVar.1
Natural variantiVAR_017647981G → S in ACG2. 1 Publication1
Natural variantiVAR_001755989R → C in SEDC. 1 PublicationCorresponds to variant dbSNP:rs121912874EnsemblClinVar.1
Natural variantiVAR_023932992R → G in SEMDSTWK. 1 PublicationCorresponds to variant dbSNP:rs121912895EnsemblClinVar.1
Natural variantiVAR_0017561005G → S in hypochondrogenesis. Corresponds to variant dbSNP:rs753342774EnsemblClinVar.1
Natural variantiVAR_0176481017 – 1022Missing in hypochondrogenesis. 1 Publication6
Natural variantiVAR_0017571017G → V in ACG2. 1
Natural variantiVAR_0337841051A → T1 PublicationCorresponds to variant dbSNP:rs41272041EnsemblClinVar.1
Natural variantiVAR_0017581053G → E in hypochondrogenesis; lethal. 1 PublicationCorresponds to variant dbSNP:rs121912868EnsemblClinVar.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 ANFH1 and LCPD. 2 PublicationsCorresponds to variant dbSNP:rs121912891EnsemblClinVar.1
Natural variantiVAR_0176511173G → R in SEDC. 1 PublicationCorresponds to variant dbSNP:rs121912883EnsemblClinVar.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 dbSNP:rs121912870EnsemblClinVar.1
Natural variantiVAR_0017661207 – 1212Missing in KD. 1 Publication6
Natural variantiVAR_0239341305G → D in VPED. 1 PublicationCorresponds to variant dbSNP:rs121912887EnsemblClinVar.1
Natural variantiVAR_0176521331V → I2 PublicationsCorresponds to variant dbSNP:rs12721427EnsemblClinVar.1
Natural variantiVAR_0757301383T → M in ANFH1. 1 PublicationCorresponds to variant dbSNP:rs138498898EnsemblClinVar.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 dbSNP:rs121912889EnsemblClinVar.1
Natural variantiVAR_0337851405G → S1 PublicationCorresponds to variant dbSNP:rs2070739EnsemblClinVar.1
Natural variantiVAR_0171051439T → M in SEDC. 1 PublicationCorresponds to variant dbSNP:rs121912886EnsemblClinVar.1
Natural variantiVAR_0248231448T → P in PLSD-T. 1 Publication1
Natural variantiVAR_0797481459R → C1 PublicationCorresponds to variant dbSNP:rs148838496EnsemblClinVar.1
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
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...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 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 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.

The Consensus CDS (CCDS) project

More...CCDSi		CCDS41778.1 [P02458-2]
CCDS8759.1 [P02458-1]

Protein sequence database of the Protein Information Resource

More...PIRi		A38513, CGHU6C

NCBI Reference Sequences

More...RefSeqi		NP_001835.3, NM_001844.4 [P02458-2]
NP_149162.2, NM_033150.2 [P02458-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000337299; ENSP00000338213; ENSG00000139219 [P02458-1]
ENST00000380518; ENSP00000369889; ENSG00000139219

Database of genes from NCBI RefSeq genomes

More...GeneIDi		1280

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:1280

Matched Annotation from NCBI and EMBL-EBI (MANE) - Phase one

More...MANE-Selecti		ENST00000380518.8; ENSP00000369889.3; NM_001844.5; NP_001835.3

UCSC genome browser

More...UCSCi		uc001rqu.4, human [P02458-2]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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 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 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]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1U5MNMR-A29-97[»]
2FSEX-ray3.10E/F461-474[»]
2SEBX-ray2.50E1238-1247[»]
5NIRX-ray1.74A/B29-98[»]
5OCXX-ray1.75A484-498[»]
5OCYX-ray2.60C1120-1134[»]
6BINX-ray2.50C1237-1249[»]
6NIXX-ray2.10C459-473[»]
SMRiP02458
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi107677, 36 interactors
ComplexPortaliCPX-1713, Collagen type II trimer
CPX-1750, Collagen type XI trimer variant 1
IntActiP02458, 27 interactors
MINTiP02458
STRINGi9606.ENSP00000369889

Chemistry databases

ChEMBLiCHEMBL2364188
DrugBankiDB00048, Collagenase clostridium histolyticum

PTM databases

GlyConnecti1126, 1 N-Linked glycan (1 site)
GlyGeniP02458, 9 sites, 1 N-linked glycan (1 site)
iPTMnetiP02458
PhosphoSitePlusiP02458

Genetic variation databases

BioMutaiCOL2A1
DMDMi124056489

Proteomic databases

jPOSTiP02458
MassIVEiP02458
MaxQBiP02458
PaxDbiP02458
PeptideAtlasiP02458
PRIDEiP02458
ProteomicsDBi51519 [P02458-2]
51520 [P02458-1]
51521 [P02458-3]

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...ABCDi		P02458, 25 sequenced antibodies

Antibodypedia a portal for validated antibodies

More...Antibodypediai		3697, 789 antibodies from 41 providers

The DNASU plasmid repository

More...DNASUi		1280

Genome annotation databases

EnsembliENST00000337299; ENSP00000338213; ENSG00000139219 [P02458-1]
ENST00000380518; ENSP00000369889; ENSG00000139219
GeneIDi1280
KEGGihsa:1280
MANE-SelectiENST00000380518.8; ENSP00000369889.3; NM_001844.5; NP_001835.3
UCSCiuc001rqu.4, human [P02458-2]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		1280
DisGeNETi1280

GeneCards: human genes, protein and diseases

More...GeneCardsi		COL2A1
GeneReviewsiCOL2A1
HGNCiHGNC:2200, COL2A1
HPAiENSG00000139219, Group enriched (epididymis, pituitary gland, retina, stomach)
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
619248, phenotype
neXtProtiNX_P02458
OpenTargetsiENSG00000139219
Orphaneti93296, Achondrogenesis type 2
166100, Autosomal dominant otospondylomegaepiphyseal dysplasia
209867, Autosomal dominant rhegmatogenous retinal detachment
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
137678, Spondyloepiphyseal dysplasia with metatarsal shortening
459051, Spondyloepiphyseal dysplasia, Stanescu type
93315, Spondylometaphyseal dysplasia, 'corner fracture' type
93316, Spondylometaphyseal dysplasia, Schmidt type
1856, Spondyloperipheral dysplasia-short ulna syndrome
90653, Stickler syndrome type 1
PharmGKBiPA26715
VEuPathDBiHostDB:ENSG00000139219

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG3544, Eukaryota
GeneTreeiENSGT00940000155224
HOGENOMiCLU_001074_2_3_1
InParanoidiP02458
OMAiWGKTMIE
OrthoDBi337699at2759
PhylomeDBiP02458
TreeFamiTF344135

Enzyme and pathway databases

PathwayCommonsiP02458
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
R-HSA-8948216, Collagen chain trimerization
SignaLinkiP02458
SIGNORiP02458

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		1280, 11 hits in 1040 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		COL2A1, human
EvolutionaryTraceiP02458

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Collagen,_type_II,_alpha_1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		1280
PharosiP02458, Tbio

Protein Ontology

More...PROi		PR:P02458
RNActiP02458, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000139219, Expressed in tibia and 115 other tissues
GenevisibleiP02458, HS

Family and domain databases

InterProiView protein in InterPro
IPR008160, Collagen
IPR000885, Fib_collagen_C
IPR001007, VWF_dom
PfamiView protein in Pfam
PF01410, COLFI, 1 hit
PF01391, Collagen, 6 hits
PF00093, VWC, 1 hit
SMARTiView protein in SMART
SM00038, COLFI, 1 hit
SM00214, VWC, 1 hit
PROSITEiView protein in PROSITE
PS51461, NC1_FIB, 1 hit
PS01208, VWFC_1, 1 hit
PS50184, VWFC_2, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCO2A1_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>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
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: February 23, 2022
This is version 245 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, 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 genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  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
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