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UniProtKB/Swiss-Prot P08123 (CO1A2_HUMAN)
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January 19, 2010.
Version 126.
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Collagen alpha-2(I) chain Alternative name(s): Alpha-2 type I collagen | ||
| Gene names |
| ||
| Organism | Homo sapiens (Human) [Complete proteome] | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 1366 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Type I collagen is a member of group I collagen (fibrillar forming collagen). |
| Subunit structure | Trimers of one alpha 2(I) and two alpha 1(I) chains. |
| Subcellular location | Secreted › extracellular space › extracellular matrix By similarity. |
| Tissue specificity | Forms the fibrils of tendon, ligaments and bones. In bones the fibrils are mineralized with calcium hydroxyapatite. |
| Post-translational modification | Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. |
| Involvement in disease | Defects in COL1A2 are the cause of Ehlers-Danlos syndrome type 7B (EDS7B) [MIM:130060]. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS7B is marked by bilateral congenital hip dislocation, hyperlaxity of the joints, and recurrent partial dislocations. Ref.8 Ref.9 Ref.28 Defects in COL1A2 are a cause of osteogenesis imperfecta type I (OI-I) [MIM:166200]. OI-I is a dominantly inherited serious newborn disease characterized by bone fragility, normal stature, little or no deformity, blue sclerae and hearing loss in 50% of families. Dentinogenesis imperfecta is rare and may distinguish a subset of OI type I (formation of dentine). Ref.12 Ref.18 Ref.19 Ref.22 Ref.29 Ref.30 Ref.31 Ref.32 Ref.34 Ref.35 Ref.36 Ref.37 Ref.40 Ref.41 Ref.42 Ref.43 Ref.45 Ref.46 Ref.47 Ref.48 Ref.49 Ref.50 Ref.51 Ref.52 Ref.53 Ref.55 Ref.56 Ref.57 Defects in COL1A2 are a cause of osteogenesis imperfecta type II (OI-II) [MIM:166210]; also known as osteogenesis imperfecta congenita (OIC) or lethal perinatal. OI-II is a serious newborn disease that diffusely affects bone. Infants are born with multiple fractures, which lead to shortening of the extremities. The skull is soft, and resembles a 'bag of bones' when palpated, the sclera are abnormally thin and may appear blue, and some infants also have a hearing loss. Infants born alive often die suddenly during the first few days or weeks of life, but a few survive as deformed dwarfs. Mental development is normal unless head trauma with CNS injury occurs. There is no effective treatment. Defects in COL1A2 are the cause of cardiac valvular form of autosomal recessive Ehlers-Danlos syndrome (cardiac valvular EDS) [MIM:225320]; also known as arthrochalasis type Ehlers-Danlos syndrome. In addition to joint laxity, skin hyperextensibility and friability, and abnormal scar formation, individuals with this form of EDS appear to be at increased risk for cardiac valvular dysfunction. Defects in COL1A2 are a cause of osteogenesis imperfecta type III (OI-III) [MIM:259420]. OI-III usually presents with moderate deformity at birth, progressively deforming bones, and sclerae variable in color. Dentinogenesis imperfecta and hearing loss are common. Stature is very short. Defects in COL1A2 are a cause of osteogenesis imperfecta type IV (OI-IV) [MIM:166220]; also known as osteogenesis imperfecta with normal sclerae. OI-IV presents with moderate to mild deformity and variable short stature. Dentinogenesis imperfecta is common and hearing loss occurs in some. A chromosomal aberration involving COL1A2 may be a cause of lipoblastomas, which are benign tumors resulting from transformation of adipocytes, usually diagnosed in children. Translocation t(7;8)(p22;q13) with PLAG1. |
| Sequence similarities | Belongs to the fibrillar collagen family. Contains 1 fibrillar collagen NC1 domain. |
Ontologies
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| Q5YB85 | 1 | EBI-983038,EBI-982988 | From a different organism. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 24 | 24 | Potential | ||||||
| Propeptide | 25 – 79 | 55 | N-terminal propeptide | PRO_0000005804 | |||||
| Chain | 80 – 1102 | 1023 | Collagen alpha-2(I) chain | PRO_0000005805 | |||||
| Propeptide | 1103 – 1366 | 264 | C-terminal propeptide | PRO_0000005806 | |||||
Regions | |||||||||
| Domain | 1133 – 1366 | 234 | Fibrillar collagen NC1 | ||||||
Amino acid modifications | |||||||||
| Modified residue | 80 | 1 | Pyrrolidone carboxylic acid By similarity | ||||||
| Modified residue | 84 | 1 | Allysine | ||||||
| Modified residue | 420 | 1 | Hydroxyproline | ||||||
| Modified residue | 441 | 1 | Hydroxyproline | ||||||
| Modified residue | 444 | 1 | Hydroxyproline | ||||||
| Glycosylation | 1267 | 1 | N-linked (GlcNAc...) Potential | ||||||
Natural variations | |||||||||
| Natural variant | 59 | 1 | T → P: dbSNP rs1800221. Ref.6 | VAR_030116 | |||||
| Natural variant | 76 – 93 | 18 | Missing in EDS7B. | VAR_001851 | |||||
| Natural variant | 181 – 198 | 18 | Missing in OI-IV. | VAR_030117 | |||||
| Natural variant | 211 | 1 | G → D in OI-I. Ref.54 | VAR_001852 | |||||
| Natural variant | 249 | 1 | I → N: dbSNP rs1800228. Ref.1 | VAR_001853 | |||||
| Natural variant | 270 | 1 | V → I: dbSNP rs368468. Ref.3 | VAR_030118 | |||||
| Natural variant | 276 | 1 | A → T: dbSNP rs1800231. Ref.1 | VAR_001854 | |||||
| Natural variant | 328 | 1 | G → S in OI-III. Ref.51 | VAR_001855 | |||||
| Natural variant | 331 | 1 | G → D in OI-III. Ref.57 | VAR_008119 | |||||
| Natural variant | 334 | 1 | G → C in OI-II. | VAR_001856 | |||||
| Natural variant | 337 | 1 | G → C in OI-III. Ref.57 | VAR_001857 | |||||
| Natural variant | 337 | 1 | G → S in OI-I. Ref.54 | VAR_001858 | |||||
| Natural variant | 344 | 1 | L → V: dbSNP rs16868573. | VAR_055677 | |||||
| Natural variant | 345 | 1 | Missing in OI-III. | VAR_001859 | |||||
| Natural variant | 349 | 1 | G → C in OI-III. Ref.33 Ref.38 | VAR_001860 | |||||
| Natural variant | 409 | 1 | G → V in OI-II. Ref.56 | VAR_001861 | |||||
| Natural variant | 433 | 1 | G → E in OI-II. Ref.42 | VAR_001862 | |||||
| Natural variant | 460 | 1 | G → S in OI-III. Ref.54 | VAR_001863 | |||||
| Natural variant | 483 | 1 | A → V: dbSNP rs414408. Ref.1 Ref.3 | VAR_030119 | |||||
| Natural variant | 511 | 1 | G → D in OI-II. | VAR_001864 | |||||
| Natural variant | 517 | 1 | G → R in OI-III. Ref.45 | VAR_001865 | |||||
| Natural variant | 528 | 1 | N → S: dbSNP rs41317144. | VAR_033040 | |||||
| Natural variant | 547 | 1 | G → R in OI-II. Ref.36 | VAR_001866 | |||||
| Natural variant | 549 | 1 | A → P: dbSNP rs42524. Ref.13 Ref.39 | VAR_001867 | |||||
| Natural variant | 562 | 1 | G → C in OI-II. | VAR_001868 | |||||
| Natural variant | 564 | 1 | A → T: dbSNP rs41317153. | VAR_033041 | |||||
| Natural variant | 586 | 1 | G → R in OI-II. | VAR_001869 | |||||
| Natural variant | 592 | 1 | G → S in OI-II. Ref.46 | VAR_001870 | |||||
| Natural variant | 634 | 1 | G → V in OI-IV. Ref.41 | VAR_001871 | |||||
| Natural variant | 637 | 1 | G → D in OI-II. | VAR_001872 | |||||
| Natural variant | 640 | 1 | G → S in OI-II. | VAR_001873 | |||||
| Natural variant | 670 | 1 | G → D in OI-II. Ref.37 | VAR_001874 | |||||
| Natural variant | 676 – 855 | 180 | Missing in OI-II. | VAR_030120 | |||||
| Natural variant | 676 | 1 | G → V in OI-III and OI-IV. Ref.19 Ref.32 | VAR_001875 | |||||
| Natural variant | 678 | 1 | P → H: dbSNP rs409108. Ref.1 Ref.3 Ref.2 Ref.5 Ref.17 | VAR_030121 | |||||
| Natural variant | 708 | 1 | R → Q in Marfan syndrome. | VAR_001876 | |||||
| Natural variant | 715 | 1 | G → D in OI-II. | VAR_001877 | |||||
| Natural variant | 730 | 1 | G → C in OI-II. Ref.49 | VAR_001878 | |||||
| Natural variant | 736 | 1 | G → C in OI-I; mild. Ref.33 Ref.38 | VAR_001879 | |||||
| Natural variant | 743 | 1 | A → G: dbSNP rs408535. Ref.1 Ref.3 Ref.5 | VAR_001880 | |||||
| Natural variant | 751 | 1 | G → S in OI-IV. Ref.35 | VAR_001881 | |||||
| Natural variant | 754 | 1 | G → R in OI-II. | VAR_001882 | |||||
| Natural variant | 766 | 1 | G → V in OI-IV. Ref.44 | VAR_001883 | |||||
| Natural variant | 778 | 1 | G → S in OI-II. Ref.50 | VAR_001884 | |||||
| Natural variant | 784 | 1 | G → R in OI-II. Ref.34 | VAR_001885 | |||||
| Natural variant | 787 | 1 | G → C in OI-II. Ref.56 | VAR_001886 | |||||
| Natural variant | 790 | 1 | G → D in OI-II. Ref.48 | VAR_001887 | |||||
| Natural variant | 796 | 1 | G → S in OI-II. Ref.44 | VAR_001888 | |||||
| Natural variant | 822 | 1 | R → H: dbSNP rs1800240. Ref.54 | VAR_001889 | |||||
| Natural variant | 835 | 1 | G → S in OI-I. Ref.54 | VAR_001890 | |||||
| Natural variant | 877 | 1 | G → C in OI-II. Ref.31 | VAR_001891 | |||||
| Natural variant | 892 | 1 | G → D in OI-III and OI-IV. Ref.53 | VAR_001892 | |||||
| Natural variant | 895 | 1 | G → D in OI-II. | VAR_001893 | |||||
| Natural variant | 949 | 1 | G → S in OI-III; moderate. Ref.47 | VAR_001894 | |||||
| Natural variant | 955 | 1 | G → S in OI-II. Ref.30 | VAR_001895 | |||||
| Natural variant | 973 | 1 | G → V in OI-III. Ref.57 | VAR_008120 | |||||
| Natural variant | 997 | 1 | G → D in OI-II. Ref.29 | VAR_001896 | |||||
| Natural variant | 1012 | 1 | G → S in OI-IV; moderate. Ref.43 | VAR_001897 | |||||
| Natural variant | 1022 | 1 | L → F: dbSNP rs392609. Ref.1 Ref.3 Ref.17 | VAR_001898 | |||||
| Natural variant | 1066 | 1 | G → D in OI-II. | VAR_001899 | |||||
| Natural variant | 1078 | 1 | G → C in OI-II. | VAR_001900 | |||||
| Natural variant | 1096 | 1 | G → A in OI-III. Ref.52 | VAR_001901 | |||||
| Natural variant | 1101 | 1 | P → L | VAR_001903 | |||||
| Natural variant | 1102 | 1 | G → R in OI-IV. Ref.22 | VAR_001902 | |||||
| Natural variant | 1148 | 1 | T → P in OI-III. dbSNP rs1800250. Ref.55 | VAR_001904 | |||||
| Natural variant | 1189 | 1 | D → E: dbSNP rs422361. Ref.1 Ref.3 Ref.17 | VAR_001905 | |||||
| Natural variant | 1198 | 1 | S → P: dbSNP rs384487. Ref.1 Ref.3 Ref.17 | VAR_001906 | |||||
| Natural variant | 1354 | 1 | Q → H: dbSNP rs418570. Ref.1 Ref.3 Ref.2 Ref.17 Ref.20 Ref.23 Ref.24 | VAR_030122 | |||||
Experimental info | |||||||||
| Sequence conflict | 55 | 1 | E → G in CAA26320. Ref.6 | ||||||
| Sequence conflict | 333 | 1 | V → P in AAB59374. Ref.1 | ||||||
| Sequence conflict | 338 | 1 | A → T in AAB59374. Ref.1 | ||||||
| Sequence conflict | 549 | 1 | A → D in CAA68709. Ref.5 | ||||||
| Sequence conflict | 828 | 1 | V → A in CAA23761. Ref.17 | ||||||
| Sequence conflict | 831 | 1 | T → P in CAA23761. Ref.17 | ||||||
| Sequence conflict | 837 | 1 | V → P in CAA23761. Ref.17 | ||||||
| Sequence conflict | 980 | 1 | E → V in AAA51996. Ref.21 | ||||||
| Sequence conflict | 1098 | 1 | P → L in CAA23761. Ref.17 | ||||||
| Sequence conflict | 1122 – 1125 | 4 | Missing in CAA23761. Ref.17 | ||||||
| Sequence conflict | 1338 | 1 | R → A in AAA51887. Ref.23 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Organization of the human pro-alpha 2(I) collagen gene." de Wet W.J., Bernard M.P., Benson-Chanda V., Chu M.-L., Dickson L.A., Weil D., Ramirez F. J. Biol. Chem. 262:16032-16036(1987) [PubMed: 2824475] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ASN-249; THR-276; VAL-483; HIS-678; GLY-743; PHE-1022; GLU-1189; PRO-1198 AND HIS-1354. |
| [2] | "The human type I collagen mutation database." Dalgleish R. Nucleic Acids Res. 25:181-187(1997) [PubMed: 9016532] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], REVIEW ON OI VARIANTS, VARIANTS HIS-678 AND HIS-1354. |
| [3] | "Analysis of the COL1A1 and COL1A2 genes by PCR amplification and scanning by conformation-sensitive gel electrophoresis identifies only COL1A1 mutations in 15 patients with osteogenesis imperfecta type I: identification of common sequences of null-allele mutations." Korkko J.M., Ala-Kokko L., De Paepe A., Nuytinck L., Earley J.J., Prockop D.J. Am. J. Hum. Genet. 62:98-110(1998) [PubMed: 9443882] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ILE-270; VAL-483; HIS-678; GLY-743; PHE-1022; GLU-1189; PRO-1198 AND HIS-1354. |
| [4] | "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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Skin and Uterus. |
| [5] | "Structure of a full-length cDNA clone for the prepro alpha 2(I) chain of human type I procollagen. Comparison with the chicken gene confirms unusual patterns of gene conservation." Kuivaniemi H., Tromp G., Chu M.-L., Prockop D.J. Biochem. J. 252:633-640(1988) [PubMed: 3421913] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-765, VARIANTS HIS-678 AND GLY-743. Tissue: Placenta. |
| [6] | "Analysis of the promoter region and the N-propeptide domain of the human pro alpha 2(I) collagen gene." Dickson L.A., de Wet W., Di Liberto M., Weil D., Ramirez F. Nucleic Acids Res. 13:3427-3438(1985) [PubMed: 4011429] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-93, VARIANT PRO-59. |
| [7] | "Fine structural analysis of the unique 5' region of the human COL1A2 gene containing two regions of dinucleotide repeats adjacent to the transcriptional start site." Akai J., Kimura A., Arai K., Uehara K., Hata R. Connect. Tissue Res. 30:1-6(1998) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32. |
| [8] | "Structural and functional characterization of a splicing mutation in the pro-alpha 2(I) collagen gene of an Ehlers-Danlos type VII patient." Weil D., D'Alessio M., Ramirez F., Eyre D.R. J. Biol. Chem. 265:16007-16011(1990) [PubMed: 2394758] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-93, VARIANT EDS7B 76-ASN--MET-93 DEL. |
| [9] | "Ehlers Danlos syndrome type VIIB. Incomplete cleavage of abnormal type I procollagen by N-proteinase in vitro results in the formation of copolymers of collagen and partially cleaved pNcollagen that are near circular in cross-section." Watson R.B., Wallis G.A., Holmes D.F., Viljoen D., Byers P.H., Kadler K.E. J. Biol. Chem. 267:9093-9100(1992) [PubMed: 1577745] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-93, VARIANT EDS7B 76-ASN--MET-93 DEL. |
| [10] | "Isolation and characterization of the cyanogen bromide peptides from the alpha 1 and alpha 2 chains of human skin collagen." Click E.M., Bornstein P. Biochemistry 9:4699-4706(1970) [PubMed: 5529814] [Abstract] Cited for: PROTEIN SEQUENCE OF 80-96. Tissue: Skin. |
| [11] | "A 19-base pair deletion in the pro-alpha 2(I) gene of type I procollagen that causes in-frame RNA splicing from exon 10 to exon 12 in a proband with atypical osteogenesis imperfecta and in his asymptomatic mother." Kuivaniemi H., Sabol C., Tromp G., Sippola-Thiele M., Prockop D.J. J. Biol. Chem. 263:11407-11413(1988) [PubMed: 3403536] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 145-198. |
| [12] | "Expression of mutant alpha (I)-procollagen in osteoblast and fibroblast cultures from a proband with osteogenesis imperfecta type IV." Chipman S.D., Shapiro J.R., McKinstry M.B., Stover M.L., Branson P., Rowe D.W. J. Bone Miner. Res. 7:793-805(1992) [PubMed: 1642148] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 163-213, VARIANT OI-IV 181-GLY--LYS-198 DEL. |
| [13] | Kalicki J., Wamsley P., Gibson A. Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 181-1366, VARIANT PRO-549. |
| [14] | "Comparative sequence studies on alpha2-CB2 from calf, human, rabbit and pig-skin collagen." Fietzek P.P., Furthmayr H., Kuehn K. Eur. J. Biochem. 47:257-261(1974) [PubMed: 4412529] [Abstract] Cited for: PROTEIN SEQUENCE OF 417-447. Tissue: Skin. |
| [15] | "Single base mutation in the pro alpha 2(I) collagen gene that causes efficient splicing of RNA from exon 27 to exon 29 and synthesis of a shortened but in-frame pro alpha 2(I) chain." Tromp G., Prockop D.J. Proc. Natl. Acad. Sci. U.S.A. 85:5254-5258(1988) [PubMed: 2839839] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 520-573. |
| [16] | "Isolation and characterization of a human pro alpha 2(I) collagen gene segment." Tajima S., Ting J.P., Pinnell S.R., Kaufman R.E. J. Invest. Dermatol. 82:265-269(1984) [PubMed: 6321602] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 622-657. |
| [17] | "Structure of a cDNA for the pro alpha 2 chain of human type I procollagen. Comparison with chick cDNA for pro alpha 2(I) identifies structurally conserved features of the protein and the gene." Bernard M.P., Myers J.C., Chu M.-L., Ramirez F., Eikenberry E.F., Prockop D.J. Biochemistry 22:1139-1145(1983) [PubMed: 6687691] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 623-1366, VARIANTS HIS-678; PHE-1022; GLU-1189; PRO-1198 AND HIS-1354. |
| [18] | "Defective folding and stable association with protein disulfide isomerase/prolyl hydroxylase of type I procollagen with a deletion in the pro alpha 2(I) chain that preserves the Gly-X-Y repeat pattern." Chessler S.D., Byers P.H. J. Biol. Chem. 267:7751-7757(1992) [PubMed: 1339453] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 631-864, VARIANT OI-II 676-GLY--ALA-855 DEL. |
| [19] | "Severe (type III) osteogenesis imperfecta due to glycine substitutions in the central domain of the collagen triple helix." Forlino A., Zolezzi F., Valli M., Pignatti P.F., Cetta G., Brunelli P.C., Mottes M. Hum. Mol. Genet. 3:2201-2206(1994) [PubMed: 7881420] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 663-746, VARIANT OI-III VAL-676. |
| [20] | "Growth-dependent modulation of type I collagen production and mRNA levels in cultured human skin fibroblasts." Maekelae J.K., Vuorio T., Vuorio E. Biochim. Biophys. Acta 1049:171-176(1990) [PubMed: 2364107] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 960-1356, VARIANT HIS-1354. Tissue: Skin. |
| [21] | "Cloning a cDNA for the pro-alpha 2 chain of human type I collagen." Myers J.C., Chu M.-L., Faro S.H., Clark W.J., Prockop D.J., Ramirez F. Proc. Natl. Acad. Sci. U.S.A. 78:3516-3520(1981) [PubMed: 6267597] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 964-1019. |
| [22] | "Arginine for glycine substitution in the triple-helical domain of the products of one alpha 2(I) collagen allele (COL1A2) produces the osteogenesis imperfecta type IV phenotype." Wenstrup R.J., Cohn D.H., Cohen T., Byers P.H. J. Biol. Chem. 263:7734-7740(1988) [PubMed: 2897363] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1090-1107, VARIANT OI-IV ARG-1102. |
| [23] | "Analysis of the 3' end of the human pro-alpha 2(I) collagen gene. Utilization of multiple polyadenylation sites in cultured fibroblasts." Myers J.C., Dickson L.A., de Wet W.J., Bernard M.P., Chu M.-L., Di Liberto M., Pepe G., Sangiorgi F.O., Ramirez F. J. Biol. Chem. 258:10128-10135(1983) [PubMed: 6309769] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1319-1366, VARIANT HIS-1354. |
| [24] | "Osteogenesis imperfecta: cloning of a pro-alpha 2(I) collagen gene with a frameshift mutation." Pihlajaniemi T., Dickson L.A., Pope F.M., Korhonen V.R., Nicholls A., Prockop D.J., Myers J.C. J. Biol. Chem. 259:12941-12944(1984) [PubMed: 6092353] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1319-1366, VARIANT HIS-1354. Tissue: Skin. |
| [25] | "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: 2010058] [Abstract] Cited for: REVIEW ON VARIANTS. |
| [26] | "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: 9101290] [Abstract] Cited for: REVIEW ON VARIANTS. |
| [27] | "Osteogenesis imperfecta: translation of mutation to phenotype." Byers P.H., Wallis G.A., Willing M.C. J. Med. Genet. 28:433-442(1991) [PubMed: 1895312] [Abstract] Cited for: REVIEW ON OI VARIANTS. |
| [28] | "Ehlers-Danlos syndrome type VIIB. Deletion of 18 amino acids comprising the N-telopeptide region of a pro-alpha 2(I) chain." Wirtz M.K., Glanville R.W., Steinmann B., Rao V.H., Hollister D.W. J. Biol. Chem. 262:16376-16385(1987) [PubMed: 3680255] [Abstract] Cited for: VARIANT EDS7B 76-ASN--MET-93 DEL. |
| [29] | "A single base mutation that converts glycine 907 of the alpha 2(I) chain of type I procollagen to aspartate in a lethal variant of osteogenesis imperfecta. The single amino acid substitution near the carboxyl terminus destabilizes the whole triple helix." Baldwin C.T., Constantinou C., Dumars K.W., Prockop D.J. J. Biol. Chem. 264:3002-3006(1989) [PubMed: 2914942] [Abstract] Cited for: VARIANT OI-II ASP-997. |
| [30] | "Characterization of point mutations in the collagen COL1A1 and COL1A2 genes causing lethal perinatal osteogenesis imperfecta." Lamande S.R., Dahl H.-H.M., Cole W.G., Bateman J.F. J. Biol. Chem. 264:15809-15812(1989) [PubMed: 2777764] [Abstract] Cited for: VARIANT OI-II SER-955. |
| [31] | "Two cysteine substitutions in the type I procollagen genes (COL1A1 and COL1A2) that cause lethal osteogenesis imperfecta. The location of glycine substitutions does not in any simple way predict their effets on protein function or phenotype." Fertala A., Westerhausen A., Morris G.M., Rooney J.E., Prockop D.J. Am. J. Hum. Genet. 47:A216-A216(1990) Cited for: VARIANT OI-II CYS-877. |
| [32] | "Characterization of a type I collagen alpha 2(I) glycine-586 to valine substitution in osteogenesis imperfecta type IV. Detection of the mutation and prenatal diagnosis by a chemical cleavage method." Bateman J.F., Hannagan M., Chan D., Cole W.G. Biochem. J. 276:765-770(1991) [PubMed: 2064612] [Abstract] Cited for: VARIANT OI-IV VAL-676. |
| [33] | "The effects of different cysteine for glycine substitutions within alpha 2(I) chains. Evidence of distinct structural domains within the type I collagen triple helix." Wenstrup R.J., Shrago-Howe A.W., Lever L.W., Phillips C.L., Byers P.H., Cohn D.H. J. Biol. Chem. 266:2590-2594(1991) [PubMed: 1990009] [Abstract] Cited for: VARIANTS OI CYS-349 AND CYS-736. |
| [34] | "Substitutions for glycine alpha 1-637 and glycine alpha 2-694 of type I procollagen in lethal osteogenesis imperfecta. The conformational strain on the triple helix introduced by a glycine substitution can be transmitted along the helix." Tsuneyoshi T., Westerhausen A., Constantinou C.D., Prockop D.J. J. Biol. Chem. 266:15608-15613(1991) [PubMed: 1874719] [Abstract] Cited for: VARIANT OI-II ARG-784. |
| [35] | "Mutation in a gene for type I procollagen (COL1A2) in a woman with postmenopausal osteoporosis: evidence for phenotypic and genotypic overlap with mild osteogenesis imperfecta." Spotila L.D., Constantinou C.D., Sereda L., Ganguly A., Riggs B.L., Prockop D.J. Proc. Natl. Acad. Sci. U.S.A. 88:5423-5427(1991) [PubMed: 2052622] [Abstract] Cited for: VARIANT OI-IV SER-751. |
| [36] | "Lethal perinatal osteogenesis imperfecta due to a type I collagen alpha 2(I) Gly to Arg substitution detected by chemical cleavage of an mRNA:cDNA sequence mismatch." Bateman J.F., Moeller I., Hannagan M., Chan D., Cole W.G. Hum. Mutat. 1:55-62(1992) [PubMed: 1284475] [Abstract] Cited for: VARIANT OI-II ARG-547. |
| [37] | "Incorporation of type I collagen molecules that contain a mutant alpha 2(I) chain (Gly580-->Asp) into bone matrix in a lethal case of osteogenesis imperfecta." Niyibizi C., Bonadio J., Byers P.H., Eyre D.R. J. Biol. Chem. 267:23108-23112(1992) [PubMed: 1385413] [Abstract] Cited for: VARIANT OI-II ASP-670. |
| [38] | "Mutations in the COL1A2 gene of type I collagen that result in nonlethal forms of osteogenesis imperfecta." Wenstrup R.J., Lever L.W., Phillips C.L., Quarles L.D. Am. J. Med. Genet. 45:228-232(1993) [PubMed: 8456807] [Abstract] Cited for: VARIANTS OI CYS-349 AND CYS-736. |
| [39] | "Chemical cleavage method for the detection of RNA base changes: experience in the application to collagen mutations in osteogenesis imperfecta." Bateman J.F., Lamande S.R., Hannagan M., Moeller I., Dahl H.-H.M., Cole W.G. Am. J. Med. Genet. 45:233-240(1993) [PubMed: 8456808] [Abstract] Cited for: VARIANT PRO-549. |
| [40] | "A single amino acid deletion in the alpha 2(I) chain of type I collagen produces osteogenesis imperfecta type III." Molyneux K., Starman B.J., Byers P.H., Dalgleish R. Hum. Genet. 90:621-628(1993) [PubMed: 8444468] [Abstract] Cited for: VARIANT OI-III VAL-345 DEL. |
| [41] | "Identification of type I collagen gene (COL1A2) mutations in nonlethal osteogenesis imperfecta." Sztrolovics R., Glorieux F.H., van der Rest M., Roughley P.J. Hum. Mol. Genet. 2:1319-1321(1993) [PubMed: 8401517] [Abstract] Cited for: VARIANT OI-IV VAL-634. |
| [42] | "A novel glycine to glutamic acid substitution at position 343 in the alpha 2 chain of type I collagen in an individual with lethal osteogenesis imperfecta." Rose N.J., Mackay K., Byers P.H., Dalgleish R. Hum. Mol. Genet. 2:2175-2177(1993) [PubMed: 7906591] [Abstract] Cited for: VARIANT OI-II GLU-433. |
| [43] | "Serine for glycine substitutions in type I collagen in two cases of type IV osteogenesis imperfecta (OI). Additional evidence for a regional model of OI pathophysiology." Marini J.C., Lewis M.B., Wang Q., Chen K.J., Orrison B.M. J. Biol. Chem. 268:2667-2673(1993) [PubMed: 8094076] [Abstract] Cited for: VARIANT OI-IV SER-1012. |
| [44] | "Two additional cases of osteogenesis imperfecta with substitutions for glycine in the alpha 2(I) collagen chain. A regional model relating mutation location with phenotype." Wang Q., Orrison B.M., Marini J.C. J. Biol. Chem. 268:25162-25167(1993) [PubMed: 7693712] [Abstract] Cited for: VARIANTS OI VAL-766 AND SER-796. |
| [45] | "Osteogenesis imperfecta: comparison of molecular defects with bone histological changes." Sztrolovics R., Glorieux F.H., Travers R., van der Rest M., Roughley P.J. Bone 15:321-328(1994) [PubMed: 7520724] [Abstract] Cited for: VARIANT OI-III ARG-517. |
| [46] | "Three unrelated individuals with perinatally lethal osteogenesis imperfecta resulting from identical Gly502Ser substitutions in the alpha 2-chain of type I collagen." Rose N.J., Mackay K., de Paepe A., Steinmann B., Punnett H.H., Dalgleish R. Hum. Genet. 94:497-503(1994) [PubMed: 7959683] [Abstract] Cited for: VARIANT OI-II SER-592. |
| [47] | "A Gly859Ser substitution in the triple helical domain of the alpha 2 chain of type I collagen resulting in osteogenesis imperfecta type III in two unrelated individuals." Rose N.J., Mackay K., Byers P.H., Dalgleish R. Hum. Mutat. 3:391-394(1994) [PubMed: 8081394] [Abstract] Cited for: VARIANT OI-III SER-949. |
| [48] | "Substitution of an aspartic acid for glycine 700 in the alpha 2(I) chain of type I collagen in a recurrent lethal type II osteogenesis imperfecta dramatically affects the mineralization of bone." Cohen-Solal L., Zylberberg L., Sangalli A., Gomez Lira M., Mottes M. J. Biol. Chem. 269:14751-14758(1994) [PubMed: 8182080] [Abstract] Cited for: VARIANT OI-II ASP-790. |
| [49] | "Determination of a new collagen type I alpha 2 gene point mutation which causes a Gly640 Cys substitution in osteogenesis imperfecta and prenatal diagnosis by DNA hybridisation." Gomez Lira M., Sangalli A., Pignatti P.F., Digilio M.C., Giannotti A., Carnevale E., Mottes M. J. Med. Genet. 31:965-968(1994) [PubMed: 7891382] [Abstract] Cited for: VARIANT OI-II CYS-730. |
| [50] | "Genetic counselling on brittle grounds: recurring osteogenesis imperfecta due to parental mosaicism for a dominant mutation." Raghunath M., Mackay K., Dalgleish R., Steinmann B. Eur. J. Pediatr. 154:123-129(1995) [PubMed: 7720740] [Abstract] Cited for: VARIANT OI-III SER-778. |
| [51] | "A Gly238Ser substitution in the alpha 2 chain of type I collagen results in osteogenesis imperfecta type III." Rose N.J., Mackay K., Byers P.H., Dalgleish R. Hum. Genet. 95:215-218(1995) [PubMed: 7860070] [Abstract] Cited for: VARIANT OI-III SER-328. |
| [52] | "A novel G1006A substitution in the alpha 2(I) chain of type I collagen produces osteogenesis imperfecta type III." Lu J., Costa T., Cole W.G. Hum. Mutat. 5:175-178(1995) [PubMed: 7749416] [Abstract] Cited for: VARIANT OI-III ALA-1096. |
| [53] | "Gly802Asp substitution in the pro alpha 2(I) collagen chain in a family with recurrent osteogenesis imperfecta due to paternal mosaicism." Lund A.M., Schwartz M., Raghunath M., Steinmann B., Skovby F. Eur. J. Hum. Genet. 4:39-45(1996) [PubMed: 8800927] [Abstract] Cited for: VARIANT OI-III/IV ASP-892. |
| [54] | "Direct sequencing of PCR products derived from cDNAs for the pro alpha 1 and pro alpha 2 chains of type I procollagen as a screening method to detect mutations in patients with osteogenesis imperfecta." Zhuang J., Tromp G., Kuivaniemi H., Castells S., Bugge M., Prockop D.J. Hum. Mutat. 7:89-99(1996) [PubMed: 8829649] [Abstract] Cited for: VARIANTS OI ASP-211; SER-337; SER-460 AND SER-835, VARIANT HIS-822. |
| [55] | "Mutation in the carboxy-terminal propeptide of the Pro alpha 1(I) chain of type I collagen in a child with severe osteogenesis imperfecta (OI type III): possible implications for protein folding." Oliver J.E., Thompson E.M., Pope F.M., Nicholls A.C. Hum. Mutat. 7:318-326(1996) [PubMed: 8723681] [Abstract] Cited for: VARIANT OI-III PRO-1148. |
| [56] | "Four new cases of lethal osteogenesis imperfecta due to glycine substitutions in COL1A1 and genes." Mottes M., Gomez Lira M., Zolezzi F., Valli M., Lisi V., Freising P. Hum. Mutat. 12:71-72(1998) [PubMed: 10627137] [Abstract] Cited for: VARIANTS OI-II VAL-409 AND CYS-787. |
| [57] | "Osteogenesis imperfecta: mosaicism and refinement of the genotype-phenotype map in OI type III." Lund A.M., Astroem E., Soederhaell S., Schwartz M., Skovby F. Hum. Mutat. 13:503-503(1999) [PubMed: 10408781] [Abstract] Cited for: VARIANTS OI-III ASP-331; CYS-337 AND VAL-973. |
| [58] | "PLAG1 fusion oncogenes in lipoblastoma." Hibbard M.K., Kozakewich H.P., Dal Cin P., Sciot R., Tan X., Xiao S., Fletcher J.A. Cancer Res. 60:4869-4872(2000) [PubMed: 10987300] [Abstract] Cited for: CHROMOSOMAL REARRANGEMENT WITH PLAG1. |
| [59] | "Rare autosomal recessive cardiac valvular form of Ehlers-Danlos syndrome results from mutations in the COL1A2 gene that activate the nonsense-mediated RNA decay pathway." Schwarze U., Hata R., McKusick V.A., Shinkai H., Hoyme H.E., Pyeritz R.E., Byers P.H. Am. J. Hum. Genet. 74:917-930(2004) [PubMed: 15077201] [Abstract] Cited for: INVOLVEMENT IN CARDIAC VALVULAR EDS. |
| [60] | "Total absence of the alpha2(I) chain of collagen type I causes a rare form of Ehlers-Danlos syndrome with hypermobility and propensity to cardiac valvular problems." Malfait F., Symoens S., Coucke P., Nunes L., De Almeida S., De Paepe A. J. Med. Genet. 43:E36-E36(2006) [PubMed: 16816023] [Abstract] Cited for: INVOLVEMENT IN CARDIAC VALVULAR EDS. |
| + | Additional computationally mapped references. |
Web resources
| Atlas of Genetics and Cytogenetics in Oncology and Haematology |
| COL1A2 Collagen type I alpha-2 chain mutations |
| GeneReviews |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | J03464 mRNA. Translation: AAB59374.1. Z74616 mRNA. Translation: CAA98969.1. AF004877 Genomic DNA. Translation: AAB93981.1. BC042586 mRNA. Translation: AAH42586.1. BC054498 mRNA. Translation: AAH54498.1. Y00724 mRNA. Translation: CAA68709.1. X02488 mRNA. Translation: CAA26320.1. AB004317 Genomic DNA. Translation: BAA25383.1. M35391 Genomic DNA. Translation: AAA60041.1. S98904 Genomic DNA. Translation: AAB22126.1. M21671 Genomic DNA. Translation: AAA59994.1. S41099 mRNA. Translation: AAB22761.1. AC002528 Genomic DNA. Translation: AAB69977.1. M21353 Genomic DNA. Translation: AAA52053.1. M28985 Genomic DNA. Translation: AAA60356.1. V00503 mRNA. Translation: CAA23761.1. S96821 mRNA. Translation: AAB22020.2. L47668 mRNA. Translation: AAB59577.1. X55525 mRNA. Translation: CAA39142.1. J00114 mRNA. Translation: AAA51996.1. M22816 mRNA. Translation: AAA51844.1. M22817 Genomic DNA. Translation: AAA51846.1. K01078 Genomic DNA. Translation: AAA51887.1. K02568 Genomic DNA. Translation: AAA51850.1. |
| IPI | IPI00304962. |
| PIR | CGHU2S. A28500. |
| RefSeq | NP_000080.2. |
| UniGene | Hs.489142 |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P08123. 2 interactions. |
| STRING | P08123. |
PTM databases | |
| PhosphoSite | P08123. |
Proteomic databases | |
| PRIDE | P08123. |
Genome annotation databases | |
| Ensembl | ENST00000297268; ENSP00000297268; ENSG00000164692; Homo sapiens. [Genome view] |
| GeneID | 1278. |
| KEGG | hsa:1278. |
| UCSC | uc003ung.1. human. |
Organism-specific databases | |
| CTD | 1278. |
| GeneCards | GC07P093861. |
| H-InvDB | HIX0006854. |
| HGNC | HGNC:2198. COL1A2. |
| MIM | 120160. gene. 130060. phenotype. 166200. phenotype. 166210. phenotype. 166220. phenotype. 225320. phenotype. 259420. phenotype. |
| Orphanet | 1899. Ehlers-Danlos syndrome, type 7. 558. Marfan syndrome. 666. Osteogenesis imperfecta. |
| PharmGKB | PA35042. |
| GenAtlas | Search... |
Phylogenomic databases | |
| HOVERGEN | P08123. |
Enzyme and pathway databases | |
| Pathway_Interaction_DB | endothelinpathway. Endothelins. il4_2pathway. IL4-mediated signaling events. smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling. lymphangiogenesis_pathway. VEGFR3 signaling in lymphatic endothelium. |
| Reactome | REACT_13552. Integrin cell surface interactions. REACT_16888. Signaling by PDGF. REACT_18266. Axon guidance. REACT_604. Hemostasis. REACT_6900. Signaling in Immune system. |
Gene expression databases | |
| ArrayExpress | P08123. |
| Bgee | P08123. |
| Genevestigator | P08123. |
| GermOnline | ENSG00000164692. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR008160. Collagen. IPR000885. Fib_collagen_C. [Graphical view] |
| Pfam | PF01410. COLFI. 1 hit. PF01391. Collagen. 8 hits. [Graphical view] |
| ProDom | PD002078. Fib_collagen_C. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| SMART | SM00038. COLFI. 1 hit. [Graphical view] |
| PROSITE | PS51461. NC1_FIB. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| DrugBank | DB00048. Collagenase. |
| NextBio | 5165. |
| SOURCE | Search... |
Entry information
| Entry name | CO1A2_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P08123 Secondary accession number(s): P02464  Q9UPH0 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| Disclaimer | Any 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
| Human chromosome 7 Human chromosome 7: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |
