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P02458 (CO2A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 178. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Collagen alpha-1(II) chain
Alternative name(s):
Alpha-1 type II collagen

Cleaved into the following 2 chains:

  1. Collagen alpha-1(II) chain
  2. Chondrocalcin
Gene names
Name:COL2A1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1487 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Subunit structure

Homotrimers of alpha 1(II) chains.

Subcellular location

Secretedextracellular spaceextracellular matrix By similarity.

Tissue specificity

Isoform 2 is highly expressed in juvenile chondrocyte and low in fetal chondrocyte. Ref.11

Domain

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.

Post-translational modification

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.

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.

Involvement in disease

Spondyloepiphyseal dysplasia congenital type (SEDC) [MIM:183900]: Disorder characterized by disproportionate short stature and pleiotropic involvement of the skeletal and ocular systems.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.22 Ref.23 Ref.42 Ref.43 Ref.46 Ref.48 Ref.56 Ref.59

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.38 Ref.50 Ref.65

Achondrogenesis 2 (ACG2) [MIM:200610]: A disease characterized by the absence of ossification in the vertebral column, sacrum and pubic bones.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.33 Ref.47 Ref.48 Ref.49 Ref.57 Ref.58 Ref.69

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.70

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.45 Ref.52

Primary avascular necrosis of femoral head (ANFH) [MIM:608805]: Causes disability that often requires surgical intervention. Most cases are sporadic, but families in which there is an autosomal dominant inheritance of the disease have been identified. It has been estimated that 300,000 to 600,000 people in the United States have ANFH. Approximately 15,000 new cases of this common and disabling disorder are reported annually. The age at the onset is earlier than that for osteoarthritis. The diagnosis is typically made when patients are between the ages of 30 and 60 years. The clinical manifestations, such as pain on exertion, a limping gait, and a discrepancy in leg length, cause considerable disability. Moreover, nearly 10 percent of the 500,000 total-hip arthroplasties performed each year in the United States involve patients with ANFH. As a result, this disease creates a substantial socioeconomic cost as well as a burden for patients and their families.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.67

Osteoarthritis with mild chondrodysplasia (OACD) [MIM:604864]: Osteoarthritis is a common disease that produces joint pain and stiffness together with radiologic evidence of progressive degeneration of joint cartilage.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.34 Ref.35 Ref.39 Ref.48

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.58 Ref.63 Ref.64

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.53

Spondyloperipheral dysplasia (SPD) [MIM:271700]: SPD patients manifest short stature, midface hypoplasia, sensorineural hearing loss, spondyloepiphyseal dysplasia, platyspondyly and brachydactyly.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Stickler syndrome 1 (STL1) [MIM:108300]: An autosomal dominant form of Stickler syndrome, an inherited disorder that associates ocular signs with more or less complete forms of Pierre Robin sequence, bone disorders and sensorineural deafness. Ocular disorders may include juvenile cataract, myopia, strabismus, vitreoretinal or chorioretinal degeneration, retinal detachment, and chronic uveitis. Robin sequence includes an opening in the roof of the mouth (a cleft palate), a large tongue (macroglossia), and a small lower jaw (micrognathia). Bones are affected by slight platyspondylisis and large, often defective epiphyses. Juvenile joint laxity is followed by early signs of arthrosis. The degree of hearing loss varies among affected individuals and may become more severe over time. Syndrome expressivity is variable.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.37 Ref.44 Ref.55 Ref.68 Ref.73 Ref.75

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.37 Ref.68 Ref.73

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.55 Ref.66

Czech dysplasia (CZECHD) [MIM:609162]: A skeletal dysplasia characterized by early-onset, progressive pseudorheumatoid arthritis, platyspondyly, and short third and fourth toes.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.41 Ref.48 Ref.71 Ref.74

Sequence similarities

Belongs to the fibrillar collagen family.

Contains 1 fibrillar collagen NC1 domain.

Contains 1 VWFC domain.

Sequence caution

The sequence AAH07252.1 differs from that shown. Reason: Frameshift at position 1198.

Ontologies

Keywords
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCataract
Deafness
Disease mutation
Dwarfism
Stickler syndrome
   DomainCollagen
Repeat
Signal
   LigandCalcium
Metal-binding
   PTMDisulfide bond
Glycoprotein
Hydroxylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processaxon guidance

Traceable author statement. Source: Reactome

cartilage condensation

Inferred from electronic annotation. Source: Ensembl

cartilage development

Traceable author statement Ref.50. Source: BHF-UCL

cartilage development involved in endochondral bone morphogenesis

Inferred from electronic annotation. Source: Ensembl

cellular response to BMP stimulus

Inferred from electronic annotation. Source: Ensembl

central nervous system development

Inferred from electronic annotation. Source: Ensembl

chondrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

collagen catabolic process

Traceable author statement. Source: Reactome

collagen fibril organization

Inferred from mutant phenotype Ref.20. Source: BHF-UCL

embryonic skeletal joint morphogenesis

Inferred from mutant phenotype Ref.68. Source: BHF-UCL

endochondral ossification

Inferred from electronic annotation. Source: Ensembl

extracellular matrix disassembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

heart morphogenesis

Inferred from electronic annotation. Source: Ensembl

inner ear morphogenesis

Inferred from electronic annotation. Source: Ensembl

limb bud formation

Inferred from electronic annotation. Source: Ensembl

negative regulation of extrinsic apoptotic signaling pathway in absence of ligand

Inferred from electronic annotation. Source: Ensembl

notochord development

Inferred from electronic annotation. Source: Ensembl

otic vesicle development

Inferred from electronic annotation. Source: Ensembl

palate development

Inferred from electronic annotation. Source: Ensembl

proteoglycan metabolic process

Inferred from electronic annotation. Source: Ensembl

regulation of gene expression

Inferred from electronic annotation. Source: Ensembl

sensory perception of sound

Inferred from mutant phenotype Ref.68. Source: BHF-UCL

skeletal system development

Inferred from mutant phenotype Ref.20. Source: BHF-UCL

tissue homeostasis

Inferred from electronic annotation. Source: Ensembl

visual perception

Inferred from mutant phenotype PubMed 10486316. Source: UniProtKB

   Cellular_componentbasement membrane

Inferred from electronic annotation. Source: Ensembl

collagen type II

Inferred from direct assay Ref.13. Source: BHF-UCL

endoplasmic reticulum lumen

Traceable author statement. Source: Reactome

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionextracellular matrix structural constituent conferring tensile strength

Inferred by curator Ref.13. Source: BHF-UCL

identical protein binding

Non-traceable author statement Ref.1. Source: BHF-UCL

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

platelet-derived growth factor binding

Inferred from direct assay PubMed 8900172. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 2 (identifier: P02458-2)

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.
Isoform 1 (identifier: P02458-1)

The sequence of this isoform differs from the canonical sequence as follows:
     29-98: QEAGSCVQDGQRYNDKDVWKPEPCRICVCDTGTVLCDDIICEDVKDCLSPEIPFGECCPICPTDLATASG → R
Isoform 3 (identifier: P02458-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1219: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Propeptide26 – 181156N-terminal propeptide
PRO_0000005729
Chain182 – 12411060Collagen alpha-1(II) chain
PRO_0000005730
Chain1242 – 1487246Chondrocalcin
PRO_0000005731

Regions

Domain32 – 9059VWFC
Domain1253 – 1487235Fibrillar collagen NC1
Region201 – 12141014Triple-helical region
Region1215 – 124127Nonhelical region (C-terminal)

Sites

Metal binding13011Calcium By similarity
Metal binding13031Calcium By similarity
Metal binding13041Calcium; via carbonyl oxygen By similarity
Metal binding13061Calcium; via carbonyl oxygen By similarity
Metal binding13091Calcium By similarity
Site181 – 1822Cleavage; by procollagen N-endopeptidase By similarity
Site1241 – 12422Cleavage; by procollagen C-endopeptidase By similarity

Amino acid modifications

Modified residue19015-hydroxylysine By similarity
Modified residue28715-hydroxylysine By similarity
Modified residue29915-hydroxylysine By similarity
Modified residue30815-hydroxylysine By similarity
Modified residue37415-hydroxylysine By similarity
Modified residue60815-hydroxylysine By similarity
Modified residue62015-hydroxylysine By similarity
Modified residue67013-hydroxyproline By similarity
Modified residue90713-hydroxyproline By similarity
Modified residue113015-hydroxylysine By similarity
Modified residue114413-hydroxyproline By similarity
Modified residue118613-hydroxyproline By similarity
Modified residue120113-hydroxyproline By similarity
Modified residue120713-hydroxyproline By similarity
Modified residue121313-hydroxyproline By similarity
Glycosylation1901O-linked (Gal...) By similarity
Glycosylation2871O-linked (Gal...) By similarity
Glycosylation2991O-linked (Gal...) By similarity
Glycosylation3081O-linked (Gal...) By similarity
Glycosylation3741O-linked (Gal...) By similarity
Glycosylation6081O-linked (Gal...) By similarity
Glycosylation6201O-linked (Gal...) By similarity
Glycosylation11301O-linked (Gal...) By similarity
Glycosylation13881N-linked (GlcNAc...)
Disulfide bond1283 ↔ 1315 By similarity
Disulfide bond1289Interchain (with C-1306) By similarity
Disulfide bond1306Interchain (with C-1289) By similarity
Disulfide bond1323 ↔ 1485 By similarity
Disulfide bond1393 ↔ 1438 By similarity

Natural variations

Alternative sequence1 – 12191219Missing in isoform 3.
VSP_022365
Alternative sequence29 – 9870QEAGS…ATASG → R in isoform 1.
VSP_022366
Natural variant91T → S. Ref.1 Ref.2 Ref.6 Ref.7 Ref.8 Ref.72
Corresponds to variant rs3803183 [ dbSNP | Ensembl ].
VAR_017638
Natural variant571C → Y in STL1O. Ref.73
VAR_063891
Natural variant1421E → D. Ref.72
Corresponds to variant rs34392760 [ dbSNP | Ensembl ].
VAR_033782
Natural variant1581P → L. Ref.1
Corresponds to variant rs1050861 [ dbSNP | Ensembl ].
VAR_019836
Natural variant2401G → D in STL1. Ref.75
VAR_063892
Natural variant2671G → D in STL1O. Ref.37
VAR_001738
Natural variant2701G → R in STL1. Ref.75
VAR_063893
Natural variant2751R → C in CZECHD. Ref.41 Ref.48 Ref.71 Ref.74
VAR_001739
Natural variant2821G → D in STL1. Ref.75
VAR_063894
Natural variant302 – 3087Missing in STL1.
VAR_001740
Natural variant3031G → D in KD; abnormal allele expressed in the cartilage. Ref.45
VAR_001741
Natural variant3181G → R in DRRD. Ref.66
VAR_023925
Natural variant3541G → R in spondylometaphyseal dysplasia; congenital type. Ref.40
VAR_001742
Natural variant3751G → R in SEDC.
VAR_001743
Natural variant4471G → S in SEDC. Ref.46
VAR_001744
Natural variant4531G → A in STL1. Ref.75
VAR_063895
Natural variant4531G → D in ACG2. Ref.57
VAR_017639
Natural variant4531G → V in ACG2. Ref.57
VAR_017640
Natural variant4921G → V in SEMDSTWK. Ref.50
VAR_001745
Natural variant5011G → R in STL1. Ref.75
VAR_063896
Natural variant5041G → C in SEMDSTWK. Ref.50
VAR_001746
Natural variant5101G → D in ACG2.
VAR_001747
Natural variant5131G → S in ACG2. Ref.58
VAR_024819
Natural variant5161G → D in ACGA2. Ref.61
VAR_023926
Natural variant5471D → V in ACG2. Ref.69
VAR_063897
Natural variant5651R → C in STL1. Ref.55
VAR_023927
Natural variant6381T → I. Ref.72
Corresponds to variant rs41263847 [ dbSNP | Ensembl ].
VAR_033783
Natural variant6671L → F in DRRD. Ref.55 Ref.66
VAR_023928
Natural variant7171G → S in ANFH. Ref.67
VAR_023929
Natural variant7171G → V in ACG2. Ref.58
VAR_024820
Natural variant7191R → C in OACD; also in mild spondyloepiphyseal dysplasia and precocious osteoarthritis. Ref.34 Ref.35 Ref.39 Ref.48 Ref.54
VAR_001748
Natural variant7711G → A in ACG2. Ref.58
VAR_024821
Natural variant7711G → D in ACG2. Ref.57
VAR_017641
Natural variant7741G → S in SEDC and hypochondrogenesis; lethal. Ref.36
VAR_001749
Natural variant7801G → R in ACG2. Ref.57
VAR_017642
Natural variant7951G → R in ACG2. Ref.57
VAR_017643
Natural variant8041G → A in hypochondrogenesis.
VAR_001751
Natural variant8551G → S in SEDC.
VAR_023930
Natural variant8911G → R in ACG2 and SEDC. Ref.47 Ref.48
VAR_001752
Natural variant8941G → E in ACG2. Ref.57
VAR_017644
Natural variant8971G → V in SEMDSTWK. Ref.38
VAR_023931
Natural variant9041R → C in EDMMD and STL1. Ref.53 Ref.75
VAR_017645
Natural variant9091G → C in SEMDSTWK. Ref.38 Ref.50
VAR_001753
Natural variant9481G → D in ACG2. Ref.57
VAR_017646
Natural variant9691G → S in ACG2. Ref.49
VAR_001754
Natural variant9811G → S in ACG2. Ref.57
VAR_017647
Natural variant9891R → C in SEDC. Ref.42
VAR_001755
Natural variant9921R → G in SEMDSTWK. Ref.65
VAR_023932
Natural variant10051G → S in hypochondrogenesis.
VAR_001756
Natural variant1017 – 10226Missing in hypochondrogenesis.
VAR_017648
Natural variant10171G → V in ACG2.
VAR_001757
Natural variant10511A → T. Ref.72
Corresponds to variant rs41272041 [ dbSNP | Ensembl ].
VAR_033784
Natural variant10531G → E in hypochondrogenesis; lethal. Ref.20
VAR_001758
Natural variant10651G → V in ACG2. Ref.57
VAR_017649
Natural variant11101G → C in ACG2. Ref.58
VAR_001759
Natural variant11131G → C in hypochondrogenesis. Ref.51
VAR_001760
Natural variant11191G → R in ACG2. Ref.57
VAR_017650
Natural variant11431G → S in ACG2. Ref.33 Ref.58
VAR_001761
Natural variant11581G → A in STL1. Ref.75
VAR_063898
Natural variant1164 – 119936Missing in SEDC.
VAR_001762
Natural variant11701G → S in ANFH and in LCPD. Ref.67 Ref.70
VAR_023933
Natural variant11731G → R in SEDC. Ref.56
VAR_017651
Natural variant11761G → S in SEDC. Ref.48
VAR_001763
Natural variant11761G → V Mutation found in a patient with features of multiple epiphyseal dysplasia; features overlap with SEDC. Ref.76
VAR_066836
Natural variant11791G → R Mutation found in a patient with features of multiple epiphyseal dysplasia; features overlap with SEDC. Ref.76
VAR_066837
Natural variant11841I → IGPSGKDGANGIPGPI in SEDC.
VAR_019837
Natural variant11881G → R in ACG2. Ref.48
VAR_001764
Natural variant11971G → S in SEDC. Ref.43
VAR_001765
Natural variant1207 – 12126Missing in KD.
VAR_001766
Natural variant13051G → D in vitreoretinopathy; with phalangeal epiphyseal dysplasia. Ref.60
VAR_023934
Natural variant13311V → I. Ref.57 Ref.72
Corresponds to variant rs12721427 [ dbSNP | Ensembl ].
VAR_017652
Natural variant13901T → N in PLSD-T; phenotype previously considered as achondrogenesis-hypochondrogenesis type 2. Ref.58 Ref.64
VAR_024822
Natural variant13911Y → C in PLSD-T. Ref.63
VAR_023935
Natural variant14051G → S. Ref.72
Corresponds to variant rs2070739 [ dbSNP | Ensembl ].
VAR_033785
Natural variant14391T → M in SEDC. Ref.59
VAR_017105
Natural variant14481T → P in PLSD-T. Ref.64
VAR_024823
Natural variant14691D → H in PLSD-T. Ref.64
VAR_024824
Natural variant14841Missing in PLSD-T. Ref.64
VAR_024825
Natural variant14851C → G in PLSD-T. Ref.64
VAR_024826

Experimental info

Sequence conflict4411G → D in CAA34488. Ref.1
Sequence conflict4571E → K in CAA34488. Ref.1
Sequence conflict4811A → P in AAB60370. Ref.15
Sequence conflict6411A → E in CAA34488. Ref.1
Sequence conflict6411A → E in CAA32030. Ref.16
Sequence conflict6771G → A in CAA32030. Ref.16
Sequence conflict7841G → A in CAA32030. Ref.16
Sequence conflict832 – 8354PAGF → TSGI in CAA34488. Ref.1
Sequence conflict10061K → Q in CAA34488. Ref.1
Sequence conflict10061K → Q in CAA32030. Ref.16
Sequence conflict10371E → Q in CAA34683. Ref.6
Sequence conflict10571D → N in AAD15287. Ref.17
Sequence conflict10571D → N in CAA26223. Ref.17
Sequence conflict10571D → N in AAA51997. Ref.19
Sequence conflict10691A → T in CAA34683. Ref.6
Sequence conflict10691A → T in AAD15287. Ref.17
Sequence conflict10691A → T in CAA26223. Ref.17
Sequence conflict10691A → T in AAA51997. Ref.19
Sequence conflict12431Q → E in CAA29604. Ref.24
Sequence conflict12471G → N in CAA29604. Ref.24
Sequence conflict12711S → T in AAA52038. Ref.21
Sequence conflict12741G → A in AAA52038. Ref.21
Sequence conflict13331K → R in M12048. Ref.28
Sequence conflict13501G → A in M12048. Ref.28
Sequence conflict13721N → D in CAA26223. Ref.17
Sequence conflict13831T → A in CAA26223. Ref.17
Sequence conflict14001L → M in CAA26223. Ref.17

Secondary structure

......... 1487
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: A8312503825BF0BB

FASTA1,487141,785
        10         20         30         40         50         60 
MIRLGAPQTL VLLTLLVAAV LRCQGQDVQE AGSCVQDGQR YNDKDVWKPE PCRICVCDTG 

        70         80         90        100        110        120 
TVLCDDIICE DVKDCLSPEI PFGECCPICP TDLATASGQP GPKGQKGEPG DIKDIVGPKG 

       130        140        150        160        170        180 
PPGPQGPAGE QGPRGDRGDK GEKGAPGPRG RDGEPGTPGN PGPPGPPGPP GPPGLGGNFA 

       190        200        210        220        230        240 
AQMAGGFDEK AGGAQLGVMQ GPMGPMGPRG PPGPAGAPGP QGFQGNPGEP GEPGVSGPMG 

       250        260        270        280        290        300 
PRGPPGPPGK PGDDGEAGKP GKAGERGPPG PQGARGFPGT PGLPGVKGHR GYPGLDGAKG 

       310        320        330        340        350        360 
EAGAPGVKGE SGSPGENGSP GPMGPRGLPG ERGRTGPAGA AGARGNDGQP GPAGPPGPVG 

       370        380        390        400        410        420 
PAGGPGFPGA PGAKGEAGPT GARGPEGAQG PRGEPGTPGS PGPAGASGNP GTDGIPGAKG 

       430        440        450        460        470        480 
SAGAPGIAGA PGFPGPRGPP GPQGATGPLG PKGQTGEPGI AGFKGEQGPK GEPGPAGPQG 

       490        500        510        520        530        540 
APGPAGEEGK RGARGEPGGV GPIGPPGERG APGNRGFPGQ DGLAGPKGAP GERGPSGLAG 

       550        560        570        580        590        600 
PKGANGDPGR PGEPGLPGAR GLTGRPGDAG PQGKVGPSGA PGEDGRPGPP GPQGARGQPG 

       610        620        630        640        650        660 
VMGFPGPKGA NGEPGKAGEK GLPGAPGLRG LPGKDGETGA AGPPGPAGPA GERGEQGAPG 

       670        680        690        700        710        720 
PSGFQGLPGP PGPPGEGGKP GDQGVPGEAG APGLVGPRGE RGFPGERGSP GAQGLQGPRG 

       730        740        750        760        770        780 
LPGTPGTDGP KGASGPAGPP GAQGPPGLQG MPGERGAAGI AGPKGDRGDV GEKGPEGAPG 

       790        800        810        820        830        840 
KDGGRGLTGP IGPPGPAGAN GEKGEVGPPG PAGSAGARGA PGERGETGPP GPAGFAGPPG 

       850        860        870        880        890        900 
ADGQPGAKGE QGEAGQKGDA GAPGPQGPSG APGPQGPTGV TGPKGARGAQ GPPGATGFPG 

       910        920        930        940        950        960 
AAGRVGPPGS NGNPGPPGPP GPSGKDGPKG ARGDSGPPGR AGEPGLQGPA GPPGEKGEPG 

       970        980        990       1000       1010       1020 
DDGPSGAEGP PGPQGLAGQR GIVGLPGQRG ERGFPGLPGP SGEPGKQGAP GASGDRGPPG 

      1030       1040       1050       1060       1070       1080 
PVGPPGLTGP AGEPGREGSP GADGPPGRDG AAGVKGDRGE TGAVGAPGAP GPPGSPGPAG 

      1090       1100       1110       1120       1130       1140 
PTGKQGDRGE AGAQGPMGPS GPAGARGIQG PQGPRGDKGE AGEPGERGLK GHRGFTGLQG 

      1150       1160       1170       1180       1190       1200 
LPGPPGPSGD QGASGPAGPS GPRGPPGPVG PSGKDGANGI PGPIGPPGPR GRSGETGPAG 

      1210       1220       1230       1240       1250       1260 
PPGNPGPPGP PGPPGPGIDM SAFAGLGPRE KGPDPLQYMR ADQAAGGLRQ HDAEVDATLK 

      1270       1280       1290       1300       1310       1320 
SLNNQIESIR SPEGSRKNPA RTCRDLKLCH PEWKSGDYWI DPNQGCTLDA MKVFCNMETG 

      1330       1340       1350       1360       1370       1380 
ETCVYPNPAN VPKKNWWSSK SKEKKHIWFG ETINGGFHFS YGDDNLAPNT ANVQMTFLRL 

      1390       1400       1410       1420       1430       1440 
LSTEGSQNIT YHCKNSIAYL DEAAGNLKKA LLIQGSNDVE IRAEGNSRFT YTALKDGCTK 

      1450       1460       1470       1480 
HTGKWGKTVI EYRSQKTSRL PIIDIAPMDI GGPEQEFGVD IGPVCFL 

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Isoform 1 [UniParc].

Checksum: 1A9E7505AEC4168A
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FASTA1,418134,389
Isoform 3 [UniParc].

Checksum: E8337954D719ACBF
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FASTA26829,781

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the full length cDNA encoding for human type II procollagen."
Su M.W., Lee B., Ramirez F., Machado M.A., Horton W.A.
Nucleic Acids Res. 17:9473-9473(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS SER-9 AND LEU-158.
[2]"Conservation of the sizes of 53 introns and over 100 intronic sequences for the binding of common transcription factors in the human and mouse genes for type II procollagen (COL2A1)."
Ala-Kokko L., Kvist A.-P., Metsaranta M., Kivirikko K.I., de Crombrugghe B., Prockop D.J., Vuorio E.
Biochem. J. 308:923-929(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), VARIANT SER-9.
Tissue: Blood.
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[4]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1109-1487 (ISOFORMS 1/2).
Tissue: Embryonic stem cell and Muscle.
[6]"Structure of cDNA clones coding for human type II procollagen. The alpha 1(II) chain is more similar to the alpha 1(I) chain than two other alpha chains of fibrillar collagens."
Baldwin C.T., Reginato A.M., Smith C., Jimenez S.A., Prockop D.J.
Biochem. J. 262:521-528(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-1229 (ISOFORM 1), VARIANT SER-9.
[7]"Organization of the exons coding for pro alpha 1(II) collagen N-propeptide confirms a distinct evolutionary history of this domain of the fibrillar collagen genes."
Su M.W., Benson-Chanda V., Vissing H., Ramirez F.
Genomics 4:438-441(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-236 (ISOFORM 1), VARIANT SER-9.
[8]"The human type II procollagen gene: identification of an additional protein-coding domain and location of potential regulatory sequences in the promoter and first intron."
Ryan M.C., Sieraski M., Sandell L.J.
Genomics 8:41-48(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-103 (ISOFORM 2), VARIANT SER-9.
[9]"Promoter region of the human pro-alpha 1(II)-collagen gene."
Nunez A.M., Kohno K., Martin G.R., Yamada Y.
Gene 44:11-16(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28 (ISOFORMS 1/2).
[10]"Structural analysis of the regulatory elements of the type-II procollagen gene. Conservation of promoter and first intron sequences between human and mouse."
Vikkula M., Metsaranta M., Syvaenen A.-C., Ala-Kokko L., Vuorio E., Peltonen L.
Biochem. J. 285:287-294(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28 (ISOFORMS 1/2).
[11]"Differential expression of a cysteine-rich domain in the amino-terminal propeptide of type II (cartilage) procollagen by alternative splicing of mRNA."
Ryan M.C., Sandell L.J.
J. Biol. Chem. 265:10334-10339(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 27-103 (ISOFORM 2), TISSUE SPECIFICITY.
[12]"Genomic organization of the human procollagen alpha 1(II) collagen gene."
Huang M.C., Seyer J.M., Thompson J.P., Spinella D.G., Cheah K.S., Kang A.H.
Eur. J. Biochem. 195:593-600(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 99-341 (ISOFORMS 1/2).
Tissue: Fetal sternum.
[13]"Collagen type IX from human cartilage: a structural profile of intermolecular cross-linking sites."
Diab M., Wu J.J., Eyre D.R.
Biochem. J. 314:327-332(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 188-195 AND 1224-1236.
[14]"Immunohistochemical and biochemical analyses of 20,000-25,000-year-old fossil cartilage."
Franc S., Marzin E., Boutillon M.-M., Lafont R., Lechene de la Porte P., Herbage D.
Eur. J. Biochem. 234:125-131(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 243-261; 575-590 AND 756-779.
[15]"An RNA-splicing mutation (G+5IVS20) in the type II collagen gene (COL2A1) in a family with spondyloepiphyseal dysplasia congenita."
Tiller G.E., Weis M.A., Polumbo P.A., Gruber H.E., Rimoin D.L., Cohn D.H., Eyre D.R.
Am. J. Hum. Genet. 56:388-395(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 440-509 (ISOFORMS 1/2).
[16]Ramirez F.
Submitted (DEC-1988) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 501-1214 (ISOFORMS 1/2).
[17]"Isolation and partial characterization of the entire human pro alpha 1(II) collagen gene."
Sangiorgi F.O., Benson-Chanda V., de Wet W.J., Sobel M.E., Tsipouras P., Ramirez F.
Nucleic Acids Res. 13:2207-2225(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 541-578; 784-803; 1056-1109 AND 1200-1487 (ISOFORMS 1/2).
[18]"Structural analyses of the polymorphic area in type II collagen gene."
Vikkula M., Peltonen L.
FEBS Lett. 250:171-174(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 630-785 (ISOFORMS 1/2).
[19]"Identification and characterization of the human type II collagen gene (COL2A1)."
Cheah K.S.E., Stoker N.G., Griffin J.R., Grosveld F.G., Solomon E.
Proc. Natl. Acad. Sci. U.S.A. 82:2555-2559(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1032-1487 (ISOFORMS 1/2).
[20]"An amino acid substitution (Gly853-->Glu) in the collagen alpha 1(II) chain produces hypochondrogenesis."
Bogaert R., Tiller G.E., Wies M.A., Gruber H.E., Rimoin D.L., Cohn D.H., Eyre D.R.
J. Biol. Chem. 267:22522-22526(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1038-1055 (ISOFORMS 1/2), VARIANT HYPOCHONDROGENESIS GLU-1053.
[21]"Low basal transcription of genes for tissue-specific collagens by fibroblasts and lymphoblastoid cells. Application to the characterization of a glycine 997 to serine substitution in alpha 1(II) collagen chains of a patient with spondyloepiphyseal dysplasia."
Chan D., Cole W.G.
J. Biol. Chem. 266:12487-12494(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1082-1288 (ISOFORMS 1/2).
[22]"Identification of the molecular defect in a family with spondyloepiphyseal dysplasia."
Lee B., Vissing H., Ramirez F., Rogers D., Rimoin D.L.
Science 244:978-980(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1146-1199 (ISOFORMS 1/2), VARIANT SEDC 1164-GLY--TYR-1399 DEL.
[23]"Tandem duplication within a type II collagen gene (COL2A1) exon in an individual with spondyloepiphyseal dysplasia."
Tiller G.E., Rimoin D.L., Murray L.W., Cohn D.H.
Proc. Natl. Acad. Sci. U.S.A. 87:3889-3893(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 1164-1199 (ISOFORMS 1/2), VARIANT SEDC GLY-PRO-SER-GLY-LYS-ASP-GLY-ALA-ASN-GLY-ILE-PRO-GLY-PRO-ILE-1184 INS.
[24]"Determination of the single polyadenylation site of the human pro alpha 1(II) collagen gene."
Elima K., Vuorio T., Vuorio E.
Nucleic Acids Res. 15:9499-9504(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1175-1487 (ISOFORMS 1/2).
[25]"Construction and identification of a cDNA clone for human type II procollagen mRNA."
Elima K., Maekelae J.K., Vuorio T., Kauppinen S., Knowles J., Vuorio E.
Biochem. J. 229:183-188(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1189-1467 (ISOFORMS 1/2).
[26]"Chondrocalcin is identical with the C-propeptide of type II procollagen."
Van der Rest M., Rosenberg L.C., Olsen B.R., Poole A.R.
Biochem. J. 237:923-925(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1242-1265; 1295-1305 AND 1395-1408.
[27]"Isolation and characterization of genomic clones corresponding to the human type II procollagen gene."
Strom C.M., Upholt W.B.
Nucleic Acids Res. 12:1025-1038(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1245-1295 (ISOFORMS 1/2/3).
[28]"Isolation and partial characterization of genomic clones coding for a human pro-alpha 1 (II) collagen chain and demonstration of restriction fragment length polymorphism at the 3' end of the gene."
Nunez A.M., Francomano C., Young M.F., Martin G.R., Yamada Y.
Biochemistry 24:6343-6348(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1296-1358 (ISOFORMS 1/2/3).
[29]"X-ray crystal structure of HLA-DR4 (DRA*0101, DRB1*0401) complexed with a peptide from human collagen II."
Dessen A., Lawrence C.M., Cupo S., Zaller D.M., Wiley D.C.
Immunity 7:473-481(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1238-1247.
[30]"Solution structure and dynamics of a prototypical chordin-like cysteine-rich repeat (von Willebrand Factor type C module) from collagen IIA."
O'Leary J.M., Hamilton J.M., Deane C.M., Valeyev N.V., Sandell L.J., Downing A.K.
J. Biol. Chem. 279:53857-53866(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 25-162 (ISOFORM 2), DISULFIDE BONDS.
[31]"Mutations in collagen genes: causes of rare and some common diseases in humans."
Kuivaniemi H., Tromp G., Prockop D.J.
FASEB J. 5:2052-2060(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[32]"Mutations in fibrillar collagens (types I, II, III, and XI), fibril-associated collagen (type IX), and network-forming collagen (type X) cause a spectrum of diseases of bone, cartilage, and blood vessels."
Kuivaniemi H., Tromp G., Prockop D.J.
Hum. Mutat. 9:300-315(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[33]"Glycine to serine substitution in the triple helical domain of pro-alpha 1 (II) collagen results in a lethal perinatal form of short-limbed dwarfism."
Vissing H., D'Alessio M., Lee B., Ramirez F., Godfrey M., Hollister D.W.
J. Biol. Chem. 264:18265-18267(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ACG2 SER-1143.
[34]"Single base mutation in the type II procollagen gene (COL2A1) as a cause of primary osteoarthritis associated with a mild chondrodysplasia."
Ala-Kokko L., Baldwin C.T., Moskowitz R.W., Prockop D.J.
Proc. Natl. Acad. Sci. U.S.A. 87:6565-6568(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OACD CYS-719.
[35]"Cartilage expression of a type II collagen mutation in an inherited form of osteoarthritis associated with a mild chondrodysplasia."
Eyre D.R., Weis M.A., Moskowitz R.W.
J. Clin. Invest. 87:357-361(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OACD CYS-719.
[36]"Characterization of a type II collagen gene (COL2A1) mutation identified in cultured chondrocytes from human hypochondrogenesis."
Horton W.A., Machado M.A., Ellard J., Campbell D., Bartley J., Ramirez F., Vitale E., Lee B.
Proc. Natl. Acad. Sci. U.S.A. 89:4583-4587(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HYPOCHONDROGENESIS SER-774.
[37]"Mutation in type II procollagen (COL2A1) that substitutes aspartate for glycine alpha 1-67 and that causes cataracts and retinal detachment: evidence for molecular heterogeneity in the Wagner syndrome and the Stickler syndrome (arthro-ophthalmopathy)."
Koerkkoe J., Ritvaniemi P., Haataja L., Kaeaeriaeinen H., Kivirikko K.I., Prockop D.J., Ala-Kokko L.
Am. J. Hum. Genet. 53:55-61(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT STL1O ASP-267.
[38]"A dominant mutation in the type II collagen gene (COL2A1) produces spondyloepimetaphyseal dysplasia (SEMD), Strudwick type."
Tiller G.E., Weis M.A., Lachman R.S., Cohn D.H., Rimoin D.L., Eyre D.R.
Am. J. Hum. Genet. 53:A209-A209(1993)
Cited for: VARIANTS SEMDSTWK VAL-897 AND CYS-909.
[39]"Human cartilage from late stage familial osteoarthritis transcribes type II collagen mRNA encoding a cysteine in position 519."
Holderbaum D., Malemud C.J., Moskowitz R.W., Haqqi T.M.
Biochem. Biophys. Res. Commun. 192:1169-1174(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT OACD CYS-719.
[40]"A mutation in the amino-terminal end of the triple helix of type II collagen causing severe osteochondrodysplasia."
Vikkula M., Ritvaniemi P., Vuorio A.F., Kaitila I., Ala-Kokko L., Peltonen L.
Genomics 16:282-285(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPONDYLOMETAPHYSEAL DYSPLASIA ARG-354.
[41]"Spondyloepiphyseal dysplasia and precocious osteoarthritis in a family with an Arg75-->Cys mutation in the procollagen type II gene (COL2A1)."
Williams C.J., Considine E.L., Knowlton R.G., Reginato A., Neumann G., Harrison D., Buxton P., Jimenez S.A., Prockop D.J.
Hum. Genet. 92:499-505(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CZECHD CYS-275.
[42]"Characterization of an arginine 789 to cysteine substitution in alpha 1 (II) collagen chains of a patient with spondyloepiphyseal dysplasia."
Chan D., Taylor T.K.F., Cole W.G.
J. Biol. Chem. 268:15238-15245(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SEDC CYS-989.
[43]"The clinical features of spondyloepiphyseal dysplasia congenita resulting from the substitution of glycine 997 by serine in the alpha 1(II) chain of type II collagen."
Cole W.G., Hall R.K., Rogers J.G.
J. Med. Genet. 30:27-35(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SEDC SER-1197.
[44]"Expression, in cartilage, of a 7-amino-acid deletion in type II collagen from two unrelated individuals with Kniest dysplasia."
Bogaert R., Wilkin D.J., Wilcox W.R., Lachman R.S., Rimoin D.L., Cohn D.H., Eyre D.R.
Am. J. Hum. Genet. 55:1128-1136(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT STL1 302-ALA--LYS-308 DEL.
[45]"A single amino acid substitution (G103D) in the type II collagen triple helix produces Kniest dysplasia."
Wilkin D.J., Bogaert R., Lachman R.S., Rimoin D.L., Eyres D.R., Cohn D.H.
Hum. Mol. Genet. 3:1999-2003(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT KD ASP-303.
[46]"A single base mutation in the type II procollagen gene (COL2A1) that converts glycine alpha 1-247 to serine in a family with late-onset spondyloepiphyseal dysplasia."
Ritvaniemi P., Sokolov B.P., Williams C.J., Considine W., Yurgenev L., Meerson E.M., Ala-Kokko L., Prockop D.J.
Hum. Mutat. 3:261-267(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SEDC SER-447.
[47]"A radiographic, morphologic, biochemical and molecular analysis of a case of achondrogenesis type II resulting from substitution for a glycine residue (Gly691-->Arg) in the type II collagen trimer."
Mortier G.R., Wilkin D.J., Wilcox W.R., Rimoin D.L., Lachman R.S., Eyre D.R., Cohn D.H.
Hum. Mol. Genet. 4:285-288(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ACG2 ARG-891.
[48]"Three new point mutations in type II procollagen (COL2A1) and identification of a fourth family with the COL2A1 Arg519-->Cys base substitution using conformation sensitive gel electrophoresis."
Williams C.J., Rock M., Considine E.L., McCarron S., Gow P., Ladda R., McLain D., Michels V.M., Murphy W., Prockop D.J., Ganguly A.
Hum. Mol. Genet. 4:309-312(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CZECHD CYS-275, VARIANT SEDC SER-1176, VARIANT OACD CYS-719, VARIANT HYPOCHONDROGENESIS ARG-891, VARIANT ACG2 ARG-1188.
[49]"A COL2A1 mutation in achondrogenesis type II results in the replacement of type II collagen by type I and III collagens in cartilage."
Chan D., Cole W.G., Chow C.W., Mundlos S., Bateman J.F.
J. Biol. Chem. 270:1747-1753(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ACG2 SER-969.
[50]"Dominant mutations in the type II collagen gene, COL2A1, produce spondyloepimetaphyseal dysplasia, Strudwick type."
Tiller G.E., Polumbo P.A., Weis M.A., Bogaert R., Lachman R.S., Cohn D.H., Rimoin D.L., Eyre D.R.
Nat. Genet. 11:87-89(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SEMDSTWK VAL-492; CYS-504 AND CYS-909.
[51]"An alpha 1(II) Gly913 to Cys substitution prevents the matrix incorporation of type II collagen which is replaced with type I and III collagens in cartilage from a patient with hypochondrogenesis."
Mundlos S., Chan D., McGill J., Bateman J.F.
Am. J. Med. Genet. 63:129-136(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HYPOCHONDROGENESIS CYS-1113.
[52]"The deletion of six amino acids at the C-terminus of the alpha 1 (II) chain causes overmodification of type II and type XI collagen: further evidence for the association between small deletions in COL2A1 and Kniest dysplasia."
Winterpacht A., Superti-Furga A., Schwarze U., Stoess H., Steinmann B., Spranger J., Zabel B.
J. Med. Genet. 33:649-654(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT KD 1207-PRO--GLY-1212 DEL.
[53]"Stickler-like syndrome due to a dominant negative mutation in the COL2A1 gene."
Ballo R., Beighton P.H., Ramesar R.S.
Am. J. Med. Genet. 80:6-11(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EDMMD CYS-904.
[54]"Five families with arginine 519-cysteine mutation in COL2A1: evidence for three distinct founders."
Bleasel J.F., Holderbaum D., Brancolini V., Moskowitz R.W., Considine E.L., Prockop D.J., Devoto M., Williams C.J.
Hum. Mutat. 12:172-176(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SPONDYLOEPIPHYSEAL DYSPLASIA CYS-719.
[55]"Variation in the vitreous phenotype of Stickler syndrome can be caused by different amino acid substitutions in the X position of the type II collagen Gly-X-Y triple helix."
Richards A.J., Baguley D.M., Yates J.R.W., Lane C., Nicol M., Harper P.S., Scott J.D., Snead M.P.
Am. J. Hum. Genet. 67:1083-1094(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT STL1 CYS-565, VARIANT DRRD PHE-667.
[56]"Boy with syndactylies, macrocephaly, and severe skeletal dysplasia: not a new syndrome, but two dominant mutations (GLI3 E543X and COL2A1 G973R) in the same individual."
Sobetzko D., Eich G., Kalff-Suske M., Grzeschik K.-H., Superti-Furga A.
Am. J. Med. Genet. 90:239-242(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SEDC ARG-1173.
[57]"Widely distributed mutations in the COL2A1 gene produce achondrogenesis type II/hypochondrogenesis."
Koerkkoe J., Cohn D.H., Ala-Kokko L., Krakow D., Prockop D.J.
Am. J. Med. Genet. 92:95-100(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ACG2 VAL-453; ASP-453; ASP-771; ARG-780; ARG-795; GLU-894; ASP-948; SER-981; VAL-1065 AND ARG-1119, VARIANT HYPOCHONDROGENESIS 1017-GLY--VAL-1022 DEL, VARIANT ILE-1331.
[58]"Report of five novel and one recurrent COL2A1 mutations with analysis of genotype-phenotype correlation in patients with a lethal type II collagen disorder."
Mortier G.R., Weis M., Nuytinck L., King L.M., Wilkin D.J., De Paepe A., Lachman R.S., Rimoin D.L., Eyre D.R., Cohn D.H.
J. Med. Genet. 37:263-271(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ACG2 SER-513; VAL-717; ALA-771; CYS-1110 AND SER-1143, VARIANT PLSD-T ASN-1390.
[59]"Double heterozygosity for pseudoachondroplasia and spondyloepiphyseal dysplasia congenita."
Unger S., Koerkkoe J., Krakow D., Lachman R.S., Rimoin D.L., Cohn D.H.
Am. J. Med. Genet. 104:140-146(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SEDC MET-1439.
[60]"Vitreoretinopathy with phalangeal epiphyseal dysplasia, a type II collagenopathy resulting from a novel mutation in the C-propeptide region of the molecule."
Richards A.J., Morgan J., Bearcroft P.W.P., Pickering E., Owen M.J., Holmans P., Williams N., Tysoe C., Pope F.M., Snead M.P., Hughes H.
J. Med. Genet. 39:661-665(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT VITREORETINOPATHY ASP-1305.
[61]"Recurrence of achondrogenesis type II within the same family: evidence for germline mosaicism."
Faivre L., Le Merrer M., Douvier S., Laurent N., Thauvin-Robinet C., Rousseau T., Vereecke I., Sagot P., Delezoide A.-L., Coucke P., Mortier G.
Am. J. Med. Genet. A 126:308-312(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ACGA2 ASP-516.
[62]"Spondyloperipheral dysplasia is caused by truncating mutations in the C-propeptide of COL2A1."
Zankl A., Zabel B., Hilbert K., Wildhardt G., Cuenot S., Xavier B., Ha-Vinh R., Bonafe L., Spranger J., Superti-Furga A.
Am. J. Med. Genet. A 129:144-148(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN SPONDYLOPERIPHERAL DYSPLASIA.
[63]"Identification of COL2A1 mutations in platyspondylic skeletal dysplasia, Torrance type."
Nishimura G., Nakashima E., Mabuchi A., Shimamoto K., Shimamoto T., Shimao Y., Nagai T., Yamaguchi T., Kosaki R., Ohashi H., Makita Y., Ikegawa S.
J. Med. Genet. 41:75-79(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PLSD-T CYS-1391.
[64]"Dominant negative mutations in the C-propeptide of COL2A1 cause platyspondylic lethal skeletal dysplasia, torrance type, and define a novel subfamily within the type 2 collagenopathies."
Zankl A., Neumann L., Ignatius J., Nikkels P., Schrander-Stumpel C., Mortier G., Omran H., Wright M., Hilbert K., Bonafe L., Spranger J., Zabel B., Superti-Furga A.
Am. J. Med. Genet. A 133:61-67(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PLSD-T PRO-1448; HIS-1469; VAL-1484 DEL AND GLY-1485, DISCUSSION OF VARIANT ASN-1390.
[65]"Novel amino acid substitution in the Y-position of collagen type II causes spondyloepimetaphyseal dysplasia congenita."
Sulko J., Czarny-Ratajczak M., Wozniak A., Latos-Bielenska A., Kozlowski K.
Am. J. Med. Genet. A 137:292-297(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SEMDSTWK GLY-992.
[66]"A novel mutation of COL2A1 resulting in dominantly inherited rhegmatogenous retinal detachment."
Richards A.J., Meredith S., Poulson A., Bearcroft P., Crossland G., Baguley D.M., Scott J.D., Snead M.P.
Invest. Ophthalmol. Vis. Sci. 46:663-668(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS DRRD ARG-318 AND PHE-667.
[67]"Type II collagen gene variants and inherited osteonecrosis of the femoral head."
Liu Y.-F., Chen W.-M., Lin Y.-F., Yang R.-C., Lin M.-W., Li L.-H., Chang Y.-H., Jou Y.-S., Lin P.-Y., Su J.-S., Huang S.-F., Hsiao K.-J., Fann C.S.J., Hwang H.-W., Chen Y.-T., Tsai S.-F.
N. Engl. J. Med. 352:2294-2301(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ANFH SER-717 AND SER-1170.
[68]"High efficiency of mutation detection in type 1 stickler syndrome using a two-stage approach: vitreoretinal assessment coupled with exon sequencing for screening COL2A1."
Richards A.J., Laidlaw M., Whittaker J., Treacy B., Rai H., Bearcroft P., Baguley D.M., Poulson A., Ang A., Scott J.D., Snead M.P.
Hum. Mutat. 27:696-704(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN STL1O.
[69]"A familial case of achondrogenesis type II caused by a dominant COL2A1 mutation and 'patchy' expression in the mosaic father."
Forzano F., Lituania M., Viassolo A., Superti-Furga V., Wildhardt G., Zabel B., Faravelli F.
Am. J. Med. Genet. A 143:2815-2820(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ACG2 VAL-547.
[70]"A recurrent mutation in type II collagen gene causes Legg-Calve-Perthes disease in a Japanese family."
Miyamoto Y., Matsuda T., Kitoh H., Haga N., Ohashi H., Nishimura G., Ikegawa S.
Hum. Genet. 121:625-629(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LCPD SER-1170.
[71]"Czech dysplasia: report of a large family and further delineation of the phenotype."
Tzschach A., Tinschert S., Kaminsky E., Lusga E., Mundlos S., Graul-Neumann L.M.
Am. J. Med. Genet. A 146:1859-1864(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CZECHD CYS-275.
[72]"Natural variation in four human collagen genes across an ethnically diverse population."
Chan T.F., Poon A., Basu A., Addleman N.R., Chen J., Phong A., Byers P.H., Klein T.E., Kwok P.Y.
Genomics 91:307-314(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SER-9; ASP-142; ILE-638; THR-1051; ILE-1331 AND SER-1405.
[73]"Missense and nonsense mutations in the alternatively-spliced exon 2 of COL2A1 cause the ocular variant of Stickler syndrome."
McAlinden A., Majava M., Bishop P.N., Perveen R., Black G.C.M., Pierpont M.E., Ala-Kokko L., Maennikkoe M.
Hum. Mutat. 29:83-90(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT STL1O TYR-57.
[74]"Czech dysplasia occurring in a Japanese family."
Matsui Y., Michigami T., Tachikawa K., Yamazaki M., Kawabata H., Nishimura G.
Am. J. Med. Genet. A 149:2285-2289(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CZECHD CYS-275.
[75]"Stickler syndrome and the vitreous phenotype: mutations in COL2A1 and COL11A1."
Richards A.J., McNinch A., Martin H., Oakhill K., Rai H., Waller S., Treacy B., Whittaker J., Meredith S., Poulson A., Snead M.P.
Hum. Mutat. 31:E1461-E1471(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS STL1 ASP-240; ARG-270; ASP-282; ALA-453; ARG-501; CYS-904 AND ALA-1158.
[76]"Pseudoachondroplasia and multiple epiphyseal dysplasia: A 7-year comprehensive analysis of the known disease genes identify novel and recurrent mutations and provides an accurate assessment of their relative contribution."
Jackson G.C., Mittaz-Crettol L., Taylor J.A., Mortier G.R., Spranger J., Zabel B., Le Merrer M., Cormier-Daire V., Hall C.M., Offiah A., Wright M.J., Savarirayan R., Nishimura G., Ramsden S.C., Elles R., Bonafe L., Superti-Furga A., Unger S., Zankl A., Briggs M.D.
Hum. Mutat. 33:144-157(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS VAL-1176 AND ARG-1179.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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 expand/collapse EMBL AC list , 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 expand/collapse EMBL AC list , 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.
PIRCGHU6C. A38513.
RefSeqNP_001835.3. NM_001844.4.
NP_149162.2. NM_033150.2.
UniGeneHs.408182.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1U5MNMR-A29-94[»]
2FSEX-ray3.10E/F461-474[»]
2SEBX-ray2.50E1238-1247[»]
DisProtDP00274.
ProteinModelPortalP02458.
SMRP02458. Positions 27-97, 1271-1487.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107677. 15 interactions.
IntActP02458. 3 interactions.
MINTMINT-6796075.

Chemistry

ChEMBLCHEMBL2364188.
DrugBankDB00048. Collagenase.

PTM databases

PhosphoSiteP02458.

Polymorphism databases

DMDM124056489.

Proteomic databases

PaxDbP02458.
PRIDEP02458.

Protocols and materials databases

DNASU1280.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000337299; ENSP00000338213; ENSG00000139219. [P02458-1]
ENST00000380518; ENSP00000369889; ENSG00000139219. [P02458-2]
GeneID1280.
KEGGhsa:1280.
UCSCuc001rqt.3. human. [P02458-3]
uc001rqu.3. human. [P02458-2]
uc001rqv.3. human. [P02458-1]

Organism-specific databases

CTD1280.
GeneCardsGC12M048266.
HGNCHGNC:2200. COL2A1.
HPACAB002214.
HPA045939.
MIM108300. 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.
neXtProtNX_P02458.
Orphanet93296. Achondrogenesis type 2.
209867. Autosomal dominant rhegmatogenous retinal detachment.
137678. Czech dysplasia, metatarsal type.
86820. Familial avascular necrosis of femoral head.
93297. Hypochondrogenesis.
485. Kniest dysplasia.
2380. Legg-Calve-Perthes disease.
93279. Mild spondyloepiphyseal dysplasia due to COL2A1 mutation with early-onset osteoarthritis.
166011. Multiple epiphyseal dysplasia, Beighton type.
1427. Otospondylomegaepiphyseal dysplasia.
85166. Platyspondylic dysplasia, Torrance type.
93346. Spondyloepimetaphyseal dysplasia congenita, Strudwick type.
94068. Spondyloepiphyseal dysplasia congenita.
93315. Spondylometaphyseal dysplasia, 'corner fracture' type.
93316. Spondylometaphyseal dysplasia, Schmidt type.
1856. Spondyloperipheral dysplasia - short ulna.
90653. Stickler syndrome type 1.
PharmGKBPA26715.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOVERGENHBG004933.
KOK06236.
OMAPLQYMRA.
OrthoDBEOG7TJ3HH.
PhylomeDBP02458.
TreeFamTF344135.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_118779. Extracellular matrix organization.

Gene expression databases

BgeeP02458.
GenevestigatorP02458.

Family and domain databases

InterProIPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_C.
[Graphical view]
PfamPF01410. COLFI. 1 hit.
PF01391. Collagen. 9 hits.
PF00093. VWC. 1 hit.
[Graphical view]
ProDomPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00038. COLFI. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
PROSITEPS51461. NC1_FIB. 1 hit.
PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCOL2A1. human.
EvolutionaryTraceP02458.
GeneWikiCollagen,_type_II,_alpha_1.
GenomeRNAi1280.
NextBio5171.
PMAP-CutDBP02458.
PROP02458.
SOURCESearch...

Entry information

Entry nameCO2A1_HUMAN
AccessionPrimary (citable) accession number: P02458
Secondary accession number(s): A6NGA0 expand/collapse secondary AC list , Q12985, Q14009, Q14044, Q14045, Q14046, Q14047, Q14056, Q14058, Q16672, Q1JQ82, Q2V4X7, Q6LBY1, Q6LBY2, Q6LBY3, Q96IT5, Q99227, Q9UE38, Q9UE39, Q9UE40, Q9UE41, Q9UE42, Q9UE43
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 178 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM