Collagen alpha-1(II) chain

Details

Name
Collagen alpha-1(II) chain
Synonyms
  • Alpha-1 type II collagen
Gene Name
COL2A1
Organism
Humans
Amino acid sequence
>lcl|BSEQ0004198|Collagen alpha-1(II) chain
MIRLGAPQTLVLLTLLVAAVLRCQGQDVQEAGSCVQDGQRYNDKDVWKPEPCRICVCDTG
TVLCDDIICEDVKDCLSPEIPFGECCPICPTDLATASGQPGPKGQKGEPGDIKDIVGPKG
PPGPQGPAGEQGPRGDRGDKGEKGAPGPRGRDGEPGTPGNPGPPGPPGPPGPPGLGGNFA
AQMAGGFDEKAGGAQLGVMQGPMGPMGPRGPPGPAGAPGPQGFQGNPGEPGEPGVSGPMG
PRGPPGPPGKPGDDGEAGKPGKAGERGPPGPQGARGFPGTPGLPGVKGHRGYPGLDGAKG
EAGAPGVKGESGSPGENGSPGPMGPRGLPGERGRTGPAGAAGARGNDGQPGPAGPPGPVG
PAGGPGFPGAPGAKGEAGPTGARGPEGAQGPRGEPGTPGSPGPAGASGNPGTDGIPGAKG
SAGAPGIAGAPGFPGPRGPPGPQGATGPLGPKGQTGEPGIAGFKGEQGPKGEPGPAGPQG
APGPAGEEGKRGARGEPGGVGPIGPPGERGAPGNRGFPGQDGLAGPKGAPGERGPSGLAG
PKGANGDPGRPGEPGLPGARGLTGRPGDAGPQGKVGPSGAPGEDGRPGPPGPQGARGQPG
VMGFPGPKGANGEPGKAGEKGLPGAPGLRGLPGKDGETGAAGPPGPAGPAGERGEQGAPG
PSGFQGLPGPPGPPGEGGKPGDQGVPGEAGAPGLVGPRGERGFPGERGSPGAQGLQGPRG
LPGTPGTDGPKGASGPAGPPGAQGPPGLQGMPGERGAAGIAGPKGDRGDVGEKGPEGAPG
KDGGRGLTGPIGPPGPAGANGEKGEVGPPGPAGSAGARGAPGERGETGPPGPAGFAGPPG
ADGQPGAKGEQGEAGQKGDAGAPGPQGPSGAPGPQGPTGVTGPKGARGAQGPPGATGFPG
AAGRVGPPGSNGNPGPPGPPGPSGKDGPKGARGDSGPPGRAGEPGLQGPAGPPGEKGEPG
DDGPSGAEGPPGPQGLAGQRGIVGLPGQRGERGFPGLPGPSGEPGKQGAPGASGDRGPPG
PVGPPGLTGPAGEPGREGSPGADGPPGRDGAAGVKGDRGETGAVGAPGAPGPPGSPGPAG
PTGKQGDRGEAGAQGPMGPSGPAGARGIQGPQGPRGDKGEAGEPGERGLKGHRGFTGLQG
LPGPPGPSGDQGASGPAGPSGPRGPPGPVGPSGKDGANGIPGPIGPPGPRGRSGETGPAG
PPGNPGPPGPPGPPGPGIDMSAFAGLGPREKGPDPLQYMRADQAAGGLRQHDAEVDATLK
SLNNQIESIRSPEGSRKNPARTCRDLKLCHPEWKSGDYWIDPNQGCTLDAMKVFCNMETG
ETCVYPNPANVPKKNWWSSKSKEKKHIWFGETINGGFHFSYGDDNLAPNTANVQMTFLRL
LSTEGSQNITYHCKNSIAYLDEAAGNLKKALLIQGSNDVEIRAEGNSRFTYTALKDGCTK
HTGKWGKTVIEYRSQKTSRLPIIDIAPMDIGGPEQEFGVDIGPVCFL
Number of residues
1487
Molecular Weight
141785.08
Theoretical pI
6.89
GO Classification
Functions
extracellular matrix structural constituent conferring tensile strength / identical protein binding / metal ion binding / platelet-derived growth factor binding
Processes
axon guidance / cartilage condensation / cartilage development / cartilage development involved in endochondral bone morphogenesis / cellular response to BMP stimulus / central nervous system development / chondrocyte differentiation / collagen catabolic process / collagen fibril organization / embryonic skeletal joint morphogenesis / endochondral ossification / extracellular matrix disassembly / extracellular matrix organization / heart morphogenesis / inner ear morphogenesis / limb bud formation / negative regulation of extrinsic apoptotic signaling pathway in absence of ligand / notochord development / otic vesicle development / palate development / proteoglycan metabolic process / regulation of gene expression / regulation of immune response / sensory perception of sound / skeletal system development / tissue homeostasis / visual perception
Components
basement membrane / collagen type II trimer / endoplasmic reticulum lumen / extracellular matrix / extracellular region / extracellular space
General Function
Platelet-derived growth factor binding
Specific 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.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Secreted
Gene sequence
>lcl|BSEQ0019241|Collagen alpha-1(II) chain (COL2A1)
ATGATTCGCCTCGGGGCTCCCCAGACGCTGGTGCTGCTGACGCTGCTCGTCGCCGCTGTC
CTTCGGTGTCAGGGCCAGGATGTCCAGGAGGCTGGCAGCTGTGTGCAGGATGGGCAGAGG
TATAATGATAAGGATGTGTGGAAGCCGGAGCCCTGCCGGATCTGTGTCTGTGACACTGGG
ACTGTCCTCTGCGACGACATAATCTGTGAAGACGTGAAAGACTGCCTCAGCCCTGAGATC
CCCTTCGGAGAGTGCTGCCCCATCTGCCCAACTGACCTCGCCACTGCCAGTGGGCAACCA
GGACCAAAGGGACAGAAAGGAGAACCTGGAGACATCAAGGATATTGTAGGACCCAAAGGA
CCTCCTGGGCCTCAGGGACCTGCAGGGGAACAAGGACCCAGAGGGGATCGTGGTGACAAA
GGTGAAAAAGGTGCCCCTGGACCTCGTGGCAGAGATGGAGAACCTGGGACCCCTGGAAAT
CCTGGCCCCCCTGGTCCTCCCGGCCCCCCTGGTCCCCCTGGTCTTGGTGGAAACTTTGCT
GCCCAGATGGCTGGAGGATTTGATGAAAAGGCTGGTGGCGCCCAGTTGGGAGTAATGCAA
GGACCAATGGGCCCCATGGGACCTCGAGGACCTCCAGGCCCTGCAGGTGCTCCTGGGCCT
CAAGGATTTCAAGGCAATCCTGGTGAACCTGGTGAACCTGGTGTCTCTGGTCCCATGGGT
CCCCGTGGTCCTCCTGGTCCCCCTGGAAAGCCTGGTGATGATGGTGAAGCTGGAAAACCT
GGAAAAGCTGGTGAAAGGGGTCCGCCTGGTCCTCAGGGTGCTCGTGGTTTCCCAGGAACC
CCAGGCCTTCCTGGTGTCAAAGGTCACAGAGGTTATCCAGGCCTGGACGGTGCTAAGGGA
GAGGCGGGTGCTCCTGGTGTGAAGGGTGAGAGTGGTTCCCCGGGTGAGAACGGATCTCCG
GGCCCAATGGGTCCTCGTGGCCTGCCTGGTGAAAGAGGACGGACTGGCCCTGCTGGCGCT
GCGGGTGCCCGAGGCAACGATGGTCAGCCAGGCCCCGCAGGGCCTCCGGGTCCTGTCGGT
CCTGCTGGTGGTCCTGGCTTCCCTGGTGCTCCTGGAGCCAAGGGTGAAGCCGGCCCCACT
GGTGCCCGTGGTCCTGAAGGTGCTCAAGGTCCTCGCGGTGAACCTGGTACTCCTGGGTCC
CCTGGGCCTGCTGGTGCCTCCGGTAACCCTGGAACAGATGGAATTCCTGGAGCCAAAGGA
TCTGCTGGTGCTCCTGGCATTGCTGGTGCTCCTGGCTTCCCTGGGCCACGGGGCCCTCCT
GGCCCTCAAGGTGCAACTGGTCCTCTGGGCCCGAAAGGTCAGACGGGTGAACCTGGTATT
GCTGGCTTCAAAGGTGAACAAGGCCCCAAGGGAGAACCTGGCCCTGCTGGCCCCCAGGGA
GCCCCTGGACCCGCTGGTGAAGAAGGCAAGAGAGGTGCCCGTGGAGAGCCTGGTGGCGTT
GGGCCCATCGGTCCCCCTGGAGAAAGAGGTGCTCCCGGCAACCGCGGTTTCCCAGGTCAA
GATGGTCTGGCAGGTCCCAAGGGAGCCCCTGGAGAGCGAGGGCCCAGTGGTCTTGCTGGC
CCCAAGGGAGCCAACGGTGACCCTGGCCGTCCTGGAGAACCTGGCCTTCCTGGAGCCCGG
GGTCTCACTGGCCGCCCTGGTGATGCTGGTCCTCAAGGCAAAGTTGGCCCTTCTGGAGCC
CCTGGTGAAGATGGTCGTCCTGGACCTCCAGGTCCTCAGGGGGCTCGTGGGCAGCCTGGT
GTCATGGGTTTCCCTGGCCCCAAAGGTGCCAACGGTGAGCCTGGCAAAGCTGGTGAGAAG
GGACTGCCTGGTGCTCCTGGTCTGAGGGGTCTTCCTGGCAAAGATGGTGAGACAGGTGCT
GCAGGACCCCCTGGCCCTGCTGGACCTGCTGGTGAACGAGGCGAGCAGGGTGCTCCTGGG
CCATCTGGGTTCCAGGGACTTCCTGGCCCTCCTGGTCCCCCAGGTGAAGGTGGAAAACCA
GGTGACCAGGGTGTTCCCGGTGAAGCTGGAGCCCCTGGCCTCGTGGGTCCCAGGGGTGAA
CGAGGTTTCCCAGGTGAACGTGGCTCTCCCGGTGCCCAGGGCCTCCAGGGTCCCCGTGGC
CTCCCCGGCACTCCTGGCACTGATGGTCCCAAAGGTGCATCTGGCCCAGCAGGCCCCCCT
GGGGCTCAGGGCCCTCCAGGTCTTCAGGGAATGCCTGGCGAGAGGGGAGCAGCTGGTATC
GCTGGGCCCAAAGGCGACAGGGGTGACGTTGGTGAGAAAGGCCCTGAGGGAGCCCCTGGA
AAGGATGGTGGACGAGGCCTGACAGGTCCCATTGGCCCCCCTGGCCCAGCTGGTGCTAAT
GGCGAGAAGGGAGAAGTTGGACCTCCTGGTCCTGCAGGAAGTGCTGGTGCTCGTGGCGCT
CCGGGTGAACGTGGAGAGACTGGGCCCCCCGGACCAGCGGGATTTGCTGGGCCTCCTGGT
GCTGATGGCCAGCCTGGGGCCAAGGGTGAGCAAGGAGAGGCCGGCCAGAAAGGCGATGCT
GGTGCCCCTGGTCCTCAGGGCCCCTCTGGAGCACCTGGGCCTCAGGGTCCTACTGGAGTG
ACTGGTCCTAAAGGAGCCCGAGGTGCCCAAGGCCCCCCGGGAGCCACTGGATTCCCTGGA
GCTGCTGGCCGCGTTGGACCCCCAGGCTCCAATGGCAACCCTGGACCCCCTGGTCCCCCT
GGTCCTTCTGGAAAAGATGGTCCCAAAGGTGCTCGAGGAGACAGCGGCCCCCCTGGCCGA
GCTGGTGAACCCGGCCTCCAAGGTCCTGCTGGACCCCCTGGCGAGAAGGGAGAGCCTGGA
GATGACGGTCCCTCTGGTGCCGAAGGTCCACCAGGTCCCCAGGGTCTGGCTGGTCAGAGA
GGCATCGTCGGTCTGCCTGGGCAACGTGGTGAGAGAGGATTCCCTGGCTTGCCTGGCCCG
TCGGGTGAGCCCGGCAAGCAGGGTGCTCCTGGAGCATCTGGAGACAGAGGTCCTCCTGGC
CCCGTGGGTCCTCCTGGCCTGACGGGTCCTGCAGGTGAACCTGGACGAGAGGGAAGCCCC
GGTGCTGATGGCCCCCCTGGCAGAGATGGCGCTGCTGGAGTCAAGGGTGATCGTGGTGAG
ACTGGTGCTGTGGGAGCTCCTGGAGCCCCTGGGCCCCCTGGCTCCCCTGGCCCCGCTGGT
CCAACTGGCAAGCAAGGAGACAGAGGAGAAGCTGGTGCACAAGGCCCCATGGGACCCTCA
GGACCAGCTGGAGCCCGGGGAATCCAGGGTCCTCAAGGCCCCAGAGGTGACAAAGGAGAG
GCTGGAGAGCCTGGCGAGAGAGGCCTGAAGGGACACCGTGGCTTCACTGGTCTGCAGGGT
CTGCCCGGCCCTCCTGGTCCTTCTGGAGACCAAGGTGCTTCTGGTCCTGCTGGTCCTTCT
GGCCCTAGAGGTCCTCCTGGCCCCGTCGGTCCCTCTGGCAAAGATGGTGCTAATGGAATC
CCTGGCCCCATTGGGCCTCCTGGTCCCCGTGGACGATCAGGCGAAACCGGCCCTGCTGGT
CCTCCTGGAAATCCTGGACCCCCTGGTCCTCCAGGTCCCCCTGGCCCTGGCATCGACATG
TCCGCCTTTGCTGGCTTAGGCCCGAGAGAGAAGGGCCCCGACCCCCTGCAGTACATGCGG
GCCGACCAGGCAGCCGGTGGCCTGAGACAGCATGACGCCGAGGTGGATGCCACACTCAAG
TCCCTCAACAACCAGATTGAGAGCATCCGCAGCCCCGAGGGCTCCCGCAAGAACCCTGCT
CGCACCTGCAGAGACCTGAAACTCTGCCACCCTGAGTGGAAGAGTGGAGACTACTGGATT
GACCCCAACCAAGGCTGCACCTTGGACGCCATGAAGGTTTTCTGCAACATGGAGACTGGC
GAGACTTGCGTCTACCCCAATCCAGCAAACGTTCCCAAGAAGAACTGGTGGAGCAGCAAG
AGCAAGGAGAAGAAACACATCTGGTTTGGAGAAACCATCAATGGTGGCTTCCATTTCAGC
TATGGAGATGACAATCTGGCTCCCAACACTGCCAACGTCCAGATGACCTTCCTACGCCTG
CTGTCCACGGAAGGCTCCCAGAACATCACCTACCACTGCAAGAACAGCATTGCCTATCTG
GACGAAGCAGCTGGCAACCTCAAGAAGGCCCTGCTCATCCAGGGCTCCAATGACGTGGAG
ATCCGGGCAGAGGGCAATAGCAGGTTCACGTACACTGCCCTGAAGGATGGCTGCACGAAA
CATACCGGTAAGTGGGGCAAGACTGTTATCGAGTACCGGTCACAGAAGACCTCACGCCTC
CCCATCATTGACATTGCACCCATGGACATAGGAGGGCCCGAGCAGGAATTCGGTGTGGAC
ATAGGGCCGGTCTGCTTCTTGTAA
Chromosome Location
12
Locus
12q13.11-q13.2
External Identifiers
ResourceLink
UniProtKB IDP02458
UniProtKB Entry NameCO2A1_HUMAN
GenBank Protein ID29516
GenBank Gene IDX16468
GenAtlas IDCOL2A1
HGNC IDHGNC:2200
General References
  1. Su MW, Lee B, Ramirez F, Machado M, Horton W: Nucleotide sequence of the full length cDNA encoding for human type II procollagen. Nucleic Acids Res. 1989 Nov 25;17(22):9473. [Article]
  2. Ala-Kokko L, Kvist AP, Metsaranta M, Kivirikko KI, de Crombrugghe B, Prockop DJ, Vuorio E: 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). Biochem J. 1995 Jun 15;308 ( Pt 3):923-9. [Article]
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  5. Baldwin CT, Reginato AM, Smith C, Jimenez SA, Prockop DJ: 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. Biochem J. 1989 Sep 1;262(2):521-8. [Article]
  6. Su MW, Benson-Chanda V, Vissing H, Ramirez F: 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. Genomics. 1989 Apr;4(3):438-41. [Article]
  7. Ryan MC, Sieraski M, Sandell LJ: 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. Genomics. 1990 Sep;8(1):41-8. [Article]
  8. Nunez AM, Kohno K, Martin GR, Yamada Y: Promoter region of the human pro-alpha 1(II)-collagen gene. Gene. 1986;44(1):11-6. [Article]
  9. Vikkula M, Metsaranta M, Syvanen AC, Ala-Kokko L, Vuorio E, Peltonen L: Structural analysis of the regulatory elements of the type-II procollagen gene. Conservation of promoter and first intron sequences between human and mouse. Biochem J. 1992 Jul 1;285 ( Pt 1):287-94. [Article]
  10. Ryan MC, Sandell LJ: Differential expression of a cysteine-rich domain in the amino-terminal propeptide of type II (cartilage) procollagen by alternative splicing of mRNA. J Biol Chem. 1990 Jun 25;265(18):10334-9. [Article]
  11. Huang MC, Seyer JM, Thompson JP, Spinella DG, Cheah KS, Kang AH: Genomic organization of the human procollagen alpha 1(II) collagen gene. Eur J Biochem. 1991 Feb 14;195(3):593-600. [Article]
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  14. Tiller GE, Weis MA, Polumbo PA, Gruber HE, Rimoin DL, Cohn DH, Eyre DR: An RNA-splicing mutation (G+5IVS20) in the type II collagen gene (COL2A1) in a family with spondyloepiphyseal dysplasia congenita. Am J Hum Genet. 1995 Feb;56(2):388-95. [Article]
  15. Sangiorgi FO, Benson-Chanda V, de Wet WJ, Sobel ME, Tsipouras P, Ramirez F: Isolation and partial characterization of the entire human pro alpha 1(II) collagen gene. Nucleic Acids Res. 1985 Apr 11;13(7):2207-25. [Article]
  16. Vikkula M, Peltonen L: Structural analyses of the polymorphic area in type II collagen gene. FEBS Lett. 1989 Jul 3;250(2):171-4. [Article]
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  18. Bogaert R, Tiller GE, Weis MA, Gruber HE, Rimoin DL, Cohn DH, Eyre DR: An amino acid substitution (Gly853-->Glu) in the collagen alpha 1(II) chain produces hypochondrogenesis. J Biol Chem. 1992 Nov 5;267(31):22522-6. [Article]
  19. Chan D, Cole WG: 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. J Biol Chem. 1991 Jul 5;266(19):12487-94. [Article]
  20. Lee B, Vissing H, Ramirez F, Rogers D, Rimoin D: Identification of the molecular defect in a family with spondyloepiphyseal dysplasia. Science. 1989 May 26;244(4907):978-80. [Article]
  21. Tiller GE, Rimoin DL, Murray LW, Cohn DH: Tandem duplication within a type II collagen gene (COL2A1) exon in an individual with spondyloepiphyseal dysplasia. Proc Natl Acad Sci U S A. 1990 May;87(10):3889-93. [Article]
  22. Elima K, Vuorio T, Vuorio E: Determination of the single polyadenylation site of the human pro alpha 1(II) collagen gene. Nucleic Acids Res. 1987 Nov 25;15(22):9499-504. [Article]
  23. Elima K, Makela JK, Vuorio T, Kauppinen S, Knowles J, Vuorio E: Construction and identification of a cDNA clone for human type II procollagen mRNA. Biochem J. 1985 Jul 1;229(1):183-8. [Article]
  24. Van der Rest M, Rosenberg LC, Olsen BR, Poole AR: Chondrocalcin is identical with the C-propeptide of type II procollagen. Biochem J. 1986 Aug 1;237(3):923-5. [Article]
  25. Strom CM, Upholt WB: Isolation and characterization of genomic clones corresponding to the human type II procollagen gene. Nucleic Acids Res. 1984 Jan 25;12(2):1025-38. [Article]
  26. Nunez AM, Francomano C, Young MF, Martin GR, Yamada Y: 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. Biochemistry. 1985 Nov 5;24(23):6343-8. [Article]
  27. Dessen A, Lawrence CM, Cupo S, Zaller DM, Wiley DC: X-ray crystal structure of HLA-DR4 (DRA*0101, DRB1*0401) complexed with a peptide from human collagen II. Immunity. 1997 Oct;7(4):473-81. [Article]
  28. O'Leary JM, Hamilton JM, Deane CM, Valeyev NV, Sandell LJ, Downing AK: Solution structure and dynamics of a prototypical chordin-like cysteine-rich repeat (von Willebrand Factor type C module) from collagen IIA. J Biol Chem. 2004 Dec 17;279(51):53857-66. Epub 2004 Oct 1. [Article]
  29. Kuivaniemi H, Tromp G, Prockop DJ: Mutations in collagen genes: causes of rare and some common diseases in humans. FASEB J. 1991 Apr;5(7):2052-60. [Article]
  30. Kuivaniemi H, Tromp G, Prockop DJ: 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. Hum Mutat. 1997;9(4):300-15. [Article]
  31. Vissing H, D'Alessio M, Lee B, Ramirez F, Godfrey M, Hollister DW: 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. J Biol Chem. 1989 Nov 5;264(31):18265-7. [Article]
  32. Ala-Kokko L, Baldwin CT, Moskowitz RW, Prockop DJ: Single base mutation in the type II procollagen gene (COL2A1) as a cause of primary osteoarthritis associated with a mild chondrodysplasia. Proc Natl Acad Sci U S A. 1990 Sep;87(17):6565-8. [Article]
  33. Eyre DR, Weis MA, Moskowitz RW: Cartilage expression of a type II collagen mutation in an inherited form of osteoarthritis associated with a mild chondrodysplasia. J Clin Invest. 1991 Jan;87(1):357-61. [Article]
  34. Horton WA, Machado MA, Ellard J, Campbell D, Bartley J, Ramirez F, Vitale E, Lee B: Characterization of a type II collagen gene (COL2A1) mutation identified in cultured chondrocytes from human hypochondrogenesis. Proc Natl Acad Sci U S A. 1992 May 15;89(10):4583-7. [Article]
  35. Korkko J, Ritvaniemi P, Haataja L, Kaariainen H, Kivirikko KI, Prockop DJ, Ala-Kokko L: 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) Am J Hum Genet. 1993 Jul;53(1):55-61. [Article]
  36. Holderbaum D, Malemud CJ, Moskowitz RW, Haqqi TM: Human cartilage from late stage familial osteoarthritis transcribes type II collagen mRNA encoding a cysteine in position 519. Biochem Biophys Res Commun. 1993 May 14;192(3):1169-74. [Article]
  37. Vikkula M, Ritvaniemi P, Vuorio AF, Kaitila I, Ala-Kokko L, Peltonen L: A mutation in the amino-terminal end of the triple helix of type II collagen causing severe osteochondrodysplasia. Genomics. 1993 Apr;16(1):282-5. [Article]
  38. Williams CJ, Considine EL, Knowlton RG, Reginato A, Neumann G, Harrison D, Buxton P, Jimenez S, Prockop DJ: Spondyloepiphyseal dysplasia and precocious osteoarthritis in a family with an Arg75-->Cys mutation in the procollagen type II gene (COL2A1). Hum Genet. 1993 Nov;92(5):499-505. [Article]
  39. Chan D, Taylor TK, Cole WG: Characterization of an arginine 789 to cysteine substitution in alpha 1 (II) collagen chains of a patient with spondyloepiphyseal dysplasia. J Biol Chem. 1993 Jul 15;268(20):15238-45. [Article]
  40. Cole WG, Hall RK, Rogers JG: 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. J Med Genet. 1993 Jan;30(1):27-35. [Article]
  41. Bogaert R, Wilkin D, Wilcox WR, Lachman R, Rimoin D, Cohn DH, Eyre DR: Expression, in cartilage, of a 7-amino-acid deletion in type II collagen from two unrelated individuals with Kniest dysplasia. Am J Hum Genet. 1994 Dec;55(6):1128-36. [Article]
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Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00048Collagenase clostridium histolyticumapproved, investigationalyesbinderDetails