COL2A1
entrez
1280
canonical
uniprot
P02458
canonical
ensembl
ENSG00000139219
resolver
ensp
ENSP00000338213
resolver
ensp
ENSP00000369889
resolver
genesymbol
COL2A1
resolver
hgnc
HGNC:2200
resolver
uniprot
A6NGA0
resolver
uniprot
Q12985
resolver
uniprot
Q14009
resolver
uniprot
Q14044
resolver
uniprot
Q14045
resolver
uniprot
Q14046
resolver
uniprot
Q14047
resolver
uniprot
Q14056
resolver
uniprot
Q14058
resolver
uniprot
Q16672
resolver
uniprot
Q1JQ82
resolver
uniprot
Q2V4X7
resolver
uniprot
Q6LBY1
resolver
uniprot
Q6LBY2
resolver
uniprot
Q6LBY3
resolver
uniprot
Q96IT5
resolver
uniprot
Q99227
resolver
uniprot
Q9UE38
resolver
uniprot
Q9UE39
resolver
uniprot
Q9UE40
resolver
uniprot
Q9UE41
resolver
uniprot
Q9UE42
resolver
uniprot
Q9UE43
resolver
uniprot_entry
CO2A1_HUMAN
resolver
uniprot_sec
A6NGA0
resolver
uniprot_sec
Q12985
resolver
uniprot_sec
Q14009
resolver
uniprot_sec
Q14044
resolver
uniprot_sec
Q14045
resolver
uniprot_sec
Q14046
resolver
uniprot_sec
Q14047
resolver
uniprot_sec
Q14056
resolver
uniprot_sec
Q14058
resolver
uniprot_sec
Q16672
resolver
uniprot_sec
Q1JQ82
resolver
uniprot_sec
Q2V4X7
resolver
uniprot_sec
Q6LBY1
resolver
uniprot_sec
Q6LBY2
resolver
uniprot_sec
Q6LBY3
resolver
uniprot_sec
Q96IT5
resolver
uniprot_sec
Q99227
resolver
uniprot_sec
Q9UE38
resolver
uniprot_sec
Q9UE39
resolver
uniprot_sec
Q9UE40
resolver
uniprot_sec
Q9UE41
resolver
uniprot_sec
Q9UE42
resolver
uniprot_sec
Q9UE43
resolver
amino_acid_sequence
MIRLGAPQTLVLLTLLVAAVLRCQGQDVQEAGSCVQDGQRYNDKDVWKPEPCRICVCDTGTVLCDDIICEDVKDCLSPEIPFGECCPICPTDLATASGQPGPKGQKGEPGDIKDIVGPKGPPGPQGPAGEQGPRGDRGDKGEKGAPGPRGRDGEPGTPGNPGPPGPPGPPGPPGLGGNFAAQMAGGFDEKAGGAQLGVMQGPMGPMGPRGPPGPAGAPGPQGFQGNPGEPGEPGVSGPMGPRGPPGPPGKPGDDGEAGKPGKAGERGPPGPQGARGFPGTPGLPGVKGHRGYPGLDGAKGEAGAPGVKGESGSPGENGSPGPMGPRGLPGERGRTGPAGAAGARGNDGQPGPAGPPGPVGPAGGPGFPGAPGAKGEAGPTGARGPEGAQGPRGEPGTPGSPGPAGASGNPGTDGIPGAKGSAGAPGIAGAPGFPGPRGPPGPQGATGPLGPKGQTGEPGIAGFKGEQGPKGEPGPAGPQGAPGPAGEEGKRGARGEPGGVGPIGPPGERGAPGNRGFPGQDGLAGPKGAPGERGPSGLAGPKGANGDPGRPGEPGLPGARGLTGRPGDAGPQGKVGPSGAPGEDGRPGPPGPQGARGQPGVMGFPGPKGANGEPGKAGEKGLPGAPGLRGLPGKDGETGAAGPPGPAGPAGERGEQGAPGPSGFQGLPGPPGPPGEGGKPGDQGVPGEAGAPGLVGPRGERGFPGERGSPGAQGLQGPRGLPGTPGTDGPKGASGPAGPPGAQGPPGLQGMPGERGAAGIAGPKGDRGDVGEKGPEGAPGKDGGRGLTGPIGPPGPAGANGEKGEVGPPGPAGSAGARGAPGERGETGPPGPAGFAGPPGADGQPGAKGEQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPGAAGRVGPPGSNGNPGPPGPPGPSGKDGPKGARGDSGPPGRAGEPGLQGPAGPPGEKGEPGDDGPSGAEGPPGPQGLAGQRGIVGLPGQRGERGFPGLPGPSGEPGKQGAPGASGDRGPPGPVGPPGLTGPAGEPGREGSPGADGPPGRDGAAGVKGDRGETGAVGAPGAPGPPGSPGPAGPTGKQGDRGEAGAQGPMGPSGPAGARGIQGPQGPRGDKGEAGEPGERGLKGHRGFTGLQGLPGPPGPSGDQGASGPAGPSGPRGPPGPVGPSGKDGANGIPGPIGPPGPRGRSGETGPAGPPGNPGPPGPPGPPGPGIDMSAFAGLGPREKGPDPLQYMRADQAAGGLRQHDAEVDATLKSLNNQIESIRSPEGSRKNPARTCRDLKLCHPEWKSGDYWIDPNQGCTLDAMKVFCNMETGETCVYPNPANVPKKNWWSSKSKEKKHIWFGETINGGFHFSYGDDNLAPNTANVQMTFLRLLSTEGSQNITYHCKNSIAYLDEAAGNLKKALLIQGSNDVEIRAEGNSRFTYTALKDGCTKHTGKWGKTVIEYRSQKTSRLPIIDIAPMDIGGPEQEFGVDIGPVCFL
uniprot
proteins
disease_involvement
DISEASE: Spondyloepiphyseal dysplasia congenital type (SEDC) [MIM:183900]: Disorder characterized by disproportionate short stature and pleiotropic involvement of the skeletal and ocular systems. {ECO:0000269|PubMed:10678662, ECO:0000269|PubMed:11746045, ECO:0000269|PubMed:2339128, ECO:0000269|PubMed:2543071, ECO:0000269|PubMed:7757086, ECO:0000269|PubMed:8019561, ECO:0000269|PubMed:8325895, ECO:0000269|PubMed:8423604}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Spondyloepiphyseal dysplasia, Stanescu type (SEDSTN) [MIM:616583]: An 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. {ECO:0000269|PubMed:26183434}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Spondyloepimetaphyseal dysplasia, Strudwick type (SEMDSTWK) [MIM:184250]: A bone disease characterized by disproportionate short stature from birth, with a very short trunk and shortened limbs, and skeletal abnormalities including lordosis, scoliosis, flattened vertebrae, pectus carinatum, coxa vara, clubfoot, and abnormal epiphyses or metaphyses. A distinctive radiographic feature is irregular sclerotic changes, described as dappled in the metaphyses of the long bones. {ECO:0000269|PubMed:16088915, ECO:0000269|PubMed:7550321, ECO:0000269|Ref.40}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Achondrogenesis 2 (ACG2) [MIM:200610]: An autosomal dominant disease characterized by the absence of ossification in the vertebral column, sacrum and pubic bones. {ECO:0000269|PubMed:10745044, ECO:0000269|PubMed:10797431, ECO:0000269|PubMed:15054848, ECO:0000269|PubMed:17994563, ECO:0000269|PubMed:2572591, ECO:0000269|PubMed:7741714, ECO:0000269|PubMed:7757081, ECO:0000269|PubMed:7757086, ECO:0000269|PubMed:7829510, ECO:0000269|PubMed:9101290}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Legg-Calve-Perthes disease (LCPD) [MIM:150600]: Characterized by loss of circulation to the femoral head, resulting in avascular necrosis in a growing child. Clinical pictures of the disease vary, depending on the phase of disease progression through ischemia, revascularization, fracture and collapse, and repair and remodeling of the bone. {ECO:0000269|PubMed:17394019}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Kniest dysplasia (KD) [MIM:156550]: Moderately severe chondrodysplasia phenotype that results from mutations in the COL2A1 gene. Characteristics of the disorder include a short trunk and extremities, mid-face hypoplasia, cleft palate, myopia, retinal detachment, and hearing loss. {ECO:0000269|PubMed:7874117, ECO:0000269|PubMed:8863156}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Avascular necrosis of femoral head, primary, 1 (ANFH1) [MIM:608805]: A 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. {ECO:0000269|PubMed:15930420, ECO:0000269|PubMed:21671384}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Osteoarthritis with mild chondrodysplasia (OSCDP) [MIM:604864]: Osteoarthritis is a common disease that produces joint pain and stiffness together with radiologic evidence of progressive degeneration of joint cartilage. {ECO:0000269|PubMed:1975693, ECO:0000269|PubMed:1985108, ECO:0000269|PubMed:7757086, ECO:0000269|PubMed:8507190}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Platyspondylic lethal skeletal dysplasia Torrance type (PLSD-T) [MIM:151210]: Platyspondylic lethal skeletal dysplasias (PLSDs) are a heterogeneous group of chondrodysplasias characterized by severe platyspondyly and limb shortening. PLSD-T is characterized by varying platyspondyly, short ribs with anterior cupping, hypoplasia of the lower ilia with broad ischial and pubic bones, and shortening of the tubular bones with splayed and cupped metaphyses. Histology of the growth plate typically shows focal hypercellularity with slightly enlarged chondrocytes in the resting cartilage and relatively well-preserved columnar formation and ossification at the chondro-osseous junction. PLSD-T is generally a perinatally lethal disease, but a few long-term survivors have been reported. {ECO:0000269|PubMed:10745044, ECO:0000269|PubMed:14729840, ECO:0000269|PubMed:15643621}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Multiple epiphyseal dysplasia with myopia and conductive deafness (EDMMD) [MIM:132450]: A generalized skeletal dysplasia associated with significant morbidity. Joint pain, joint deformity, waddling gait, and short stature are the main clinical signs and symptoms. EDMMD is an autosomal dominant disorder characterized by epiphyseal dysplasia associated with progressive myopia, retinal thinning, crenated cataracts, conductive deafness. {ECO:0000269|PubMed:9800905}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Spondyloperipheral dysplasia (SPD) [MIM:271700]: SPD patients manifest short stature, midface hypoplasia, sensorineural hearing loss, spondyloepiphyseal dysplasia, platyspondyly and brachydactyly. {ECO:0000269|PubMed:15316962}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Stickler syndrome 1 (STL1) [MIM:108300]: An autosomal dominant form of Stickler syndrome, an inherited disorder that associates ocular signs with more or less complete forms of Pierre Robin sequence, bone disorders and sensorineural deafness. Ocular disorders may include juvenile cataract, myopia, strabismus, vitreoretinal or chorioretinal degeneration, retinal detachment, and chronic uveitis. 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. {ECO:0000269|PubMed:11007540, ECO:0000269|PubMed:20513134, ECO:0000269|PubMed:7977371}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Stickler syndrome 1 non-syndromic ocular (STL1O) [MIM:609508]: An autosomal dominant form of Stickler syndrome characterized by the ocular signs typically seen in Stickler syndrome type 1 such as cataract, myopia, retinal detachment. Systemic features of premature osteoarthritis, cleft palate, hearing impairment, and craniofacial abnormalities are either absent or very mild. {ECO:0000269|PubMed:16752401, ECO:0000269|PubMed:17721977, ECO:0000269|PubMed:8317498}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Rhegmatogenous retinal detachment autosomal dominant (DRRD) [MIM:609508]: A eye disease that most frequently results from a break or tear in the retina that allows fluid from the vitreous humor to enter the potential space beneath the retina. It is often associated with pathologic myopia and in most cases leads to visual impairment or blindness if untreated. {ECO:0000269|PubMed:11007540, ECO:0000269|PubMed:15671297}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Czech dysplasia (CZECHD) [MIM:609162]: A skeletal dysplasia characterized by early-onset, progressive pseudorheumatoid arthritis, platyspondyly, and short third and fourth toes. {ECO:0000269|PubMed:18553548, ECO:0000269|PubMed:19764028, ECO:0000269|PubMed:7757086, ECO:0000269|PubMed:8244341}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Vitreoretinopathy with phalangeal epiphyseal dysplasia (VPED) [MIM:619248]: An autosomal dominant disorder characterized by rhegmatogenous retinal detachment, premature arthropathy, and development of phalangeal epiphyseal dysplasia resulting in brachydactyly. {ECO:0000269|PubMed:12205109}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Spondylometaphyseal dysplasia, Algerian type (SMDALG) [MIM:184253]: A form of spondylometaphyseal dysplasia, a group of short stature disorders distinguished by abnormalities in the vertebrae and the metaphyses of the tubular bones. SMDALG is an autosomal dominant form characterized by short trunk and severe genu valgum. Myopia may be a syndromic component. SMDALG radiological hallmarks include moderate platyspondyly, particularly with dorsal vertebral flattening, short ilia with narrow greater sciatic notches and generalized metaphyseal dysplasia of the long bones. The metaphyseal changes are most conspicuous in the hip and knee, and are associated with coxa vara and severe genu valgum. The short tubular bones are mildly affected. The epiphyses of the tubular bones are said to be normal. {ECO:0000269|PubMed:23653587, ECO:0000269|PubMed:38162154}. Note=The disease may be caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: 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.
uniprot
proteins
mass_dalton
141785
uniprot
proteins
post_translational_modification
PTM: 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.; PTM: 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. {ECO:0000250|UniProtKB:P05539}.; PTM: 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. {ECO:0000250|UniProtKB:P05539}.; PTM: Lysine residues at the third position of the tripeptide repeating unit (G-X-Y) are 5-hydroxylated in some or all of the chains. {ECO:0000250|UniProtKB:P05539}.; PTM: O-glycosylated on hydroxylated lysine residues. The O-linked glycan consists of a Glc-Gal disaccharide. {ECO:0000250|UniProtKB:P05539}.
uniprot
proteins
protein_family
Fibrillar collagen family
uniprot
proteins
pubmed
10678662
uniprot
proteins
pubmed
10745044
uniprot
proteins
pubmed
10797431
uniprot
proteins
pubmed
11007540
uniprot
proteins
pubmed
11746045
uniprot
proteins
pubmed
12205109
uniprot
proteins
pubmed
1374906
uniprot
proteins
pubmed
1429602
uniprot
proteins
pubmed
14729840
uniprot
proteins
pubmed
15054848
uniprot
proteins
pubmed
15316962
uniprot
proteins
pubmed
15466413
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15643621
uniprot
proteins
pubmed
15671297
uniprot
proteins
pubmed
15930420
uniprot
proteins
pubmed
16088915
uniprot
proteins
pubmed
1637314
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
16752401
uniprot
proteins
pubmed
17394019
uniprot
proteins
pubmed
17721977
uniprot
proteins
pubmed
17994563
uniprot
proteins
pubmed
18272325
uniprot
proteins
pubmed
18553548
uniprot
proteins
pubmed
1905723
uniprot
proteins
pubmed
1975693
uniprot
proteins
pubmed
19764028
uniprot
proteins
pubmed
1985108
uniprot
proteins
pubmed
1999183
uniprot
proteins
pubmed
2010058
uniprot
proteins
pubmed
20513134
uniprot
proteins
pubmed
2081599
uniprot
proteins
pubmed
21671384
uniprot
proteins
pubmed
21922596
uniprot
proteins
pubmed
2339128
uniprot
proteins
pubmed
2355003
uniprot
proteins
pubmed
23653587
uniprot
proteins
pubmed
2543071
uniprot
proteins
pubmed
2572591
uniprot
proteins
pubmed
2587267
uniprot
proteins
pubmed
26183434
uniprot
proteins
pubmed
2714801
uniprot
proteins
pubmed
2753125
uniprot
proteins
pubmed
2803268
uniprot
proteins
pubmed
2825137
uniprot
proteins
pubmed
28887846
uniprot
proteins
pubmed
2987845
uniprot
proteins
pubmed
3002437
uniprot
proteins
pubmed
3021582
uniprot
proteins
pubmed
3800925
uniprot
proteins
pubmed
38162154
uniprot
proteins
pubmed
3840017
uniprot
proteins
pubmed
3857598
uniprot
proteins
pubmed
6320112
uniprot
proteins
pubmed
7550321
uniprot
proteins
pubmed
7741714
uniprot
proteins
pubmed
7757081
uniprot
proteins
pubmed
7757086
uniprot
proteins
pubmed
7829510
uniprot
proteins
pubmed
7847372
uniprot
proteins
pubmed
7874117
uniprot
proteins
pubmed
7977371
uniprot
proteins
pubmed
8019561
uniprot
proteins
pubmed
8244341
uniprot
proteins
pubmed
8317498
uniprot
proteins
pubmed
8325895
uniprot
proteins
pubmed
8423604
uniprot
proteins
pubmed
8486375
uniprot
proteins
pubmed
8507190
uniprot
proteins
pubmed
8529631
uniprot
proteins
pubmed
8660302
uniprot
proteins
pubmed
8723098
uniprot
proteins
pubmed
8863156
uniprot
proteins
pubmed
8948452
uniprot
proteins
pubmed
9101290
uniprot
proteins
pubmed
9354468
uniprot
proteins
pubmed
9711874
uniprot
proteins
pubmed
9800905
uniprot
proteins
sequence_length
1487
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
uniprot
proteins