CO1A1_HUMAN
ID CO1A1_HUMAN Reviewed; 1464 AA.
AC P02452; O76045; P78441; Q13896; Q13902; Q13903; Q14037; Q14992; Q15176;
AC Q15201; Q16050; Q59F64; Q7KZ30; Q7KZ34; Q8IVI5; Q8N473; Q9UML6; Q9UMM7;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 6.
DT 03-AUG-2022, entry version 251.
DE RecName: Full=Collagen alpha-1(I) chain;
DE AltName: Full=Alpha-1 type I collagen;
DE Flags: Precursor;
GN Name=COL1A1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ALA-1019; LYS-1391 AND SER-1434.
RA Dalgleish R.;
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-1391.
RX PubMed=9443882; DOI=10.1086/301689;
RA Korkko J.M., Ala-Kokko L., De Paepe A., Nuytinck L., Earley J.J.,
RA Prockop D.J.;
RT "Analysis of the COL1A1 and COL1A2 genes by PCR amplification and scanning
RT by conformation-sensitive gel electrophoresis identifies only COL1A1
RT mutations in 15 patients with osteogenesis imperfecta type I:
RT identification of common sequences of null-allele mutations.";
RL Am. J. Hum. Genet. 62:98-110(1998).
RN [3]
RP SEQUENCE REVISION TO 1049.
RA Korkko J.M., Earley J.J., Nuytinck L., DePaepe A., Prockop D.J.,
RA Ala-Kokko L.;
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-1438 AND HIS-1460.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-589.
RX PubMed=2843432; DOI=10.1016/0378-1119(88)90013-3;
RA D'Alessio M., Bernard M.P., Pretorius P.J., de Wet W., Ramirez F.,
RA Pretorious P.J.;
RT "Complete nucleotide sequence of the region encompassing the first twenty-
RT five exons of the human pro alpha 1(I) collagen gene (COL1A1).";
RL Gene 67:105-115(1988).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-472.
RX PubMed=3178743; DOI=10.1042/bj2530919;
RA Tromp G., Kuivaniemi H., Stacey A., Shikata H., Baldwin C.T., Jaenisch R.,
RA Prockup D.J.;
RT "Structure of a full-length cDNA clone for the prepro alpha 1(I) chain of
RT human type I procollagen.";
RL Biochem. J. 253:919-922(1988).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-181.
RX PubMed=6462220; DOI=10.1038/310337a0;
RA Chu M.-L., de Wet W.J., Bernard M.P., Ding J.-F., Morabito M., Myers J.,
RA Williams C., Ramirez F.;
RT "Human pro alpha 1(I) collagen gene structure reveals evolutionary
RT conservation of a pattern of introns and exons.";
RL Nature 310:337-340(1984).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44.
RX PubMed=2822714; DOI=10.1016/s0021-9258(18)48151-3;
RA Rossouw C.M.S., Vergeer W.P., du Plooy S.J., Bernard M.P., Ramirez F.,
RA de Wet W.;
RT "DNA sequences in the first intron of the human pro-alpha 1(I) collagen
RT gene enhance transcription.";
RL J. Biol. Chem. 262:15151-15157(1987).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
RX PubMed=2857713; DOI=10.1016/s0021-9258(18)89556-4;
RA Chu M.-L., de Wet W., Bernard M.P., Ramirez F.;
RT "Fine structural analysis of the human pro-alpha 1 (I) collagen gene.
RT Promoter structure, AluI repeats, and polymorphic transcripts.";
RL J. Biol. Chem. 260:2315-2320(1985).
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
RX PubMed=3480516; DOI=10.1073/pnas.84.24.8869;
RA Bornstein P., McKay J., Morishima J.K., Devarayalu S., Gelinas R.E.;
RT "Regulatory elements in the first intron contribute to transcriptional
RT control of the human alpha 1(I) collagen gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:8869-8873(1987).
RN [12]
RP PROTEIN SEQUENCE OF 33-52.
RX PubMed=2318855; DOI=10.1016/s0021-9258(19)39327-5;
RA Wirtz M.K., Keene D.R., Hori H., Glanville R.W., Steinmann B., Rao V.H.,
RA Hollister D.W.;
RT "In vivo and in vitro noncovalent association of excised alpha 1 (I) amino-
RT terminal propeptides with mutant pN alpha 2(I) collagen chains in native
RT mutant collagen in a case of Ehlers-Danlos syndrome, type VII.";
RL J. Biol. Chem. 265:6312-6317(1990).
RN [13]
RP NUCLEOTIDE SEQUENCE OF 156-183.
RX PubMed=2767050; DOI=10.1002/j.1460-2075.1989.tb03562.x;
RA Weil D., D'Alessio M., Ramirez F., de Wet W., Cole W.G., Chan D.,
RA Bateman J.F.;
RT "A base substitution in the exon of a collagen gene causes alternative
RT splicing and generates a structurally abnormal polypeptide in a patient
RT with Ehlers-Danlos syndrome type VII.";
RL EMBO J. 8:1705-1710(1989).
RN [14]
RP PROTEIN SEQUENCE OF 162-301, ALLYSINE AT LYS-170, AND PYROGLUTAMATE
RP FORMATION AT GLN-162.
RC TISSUE=Skin;
RX PubMed=5529814; DOI=10.1021/bi00826a012;
RA Click E.M., Bornstein P.;
RT "Isolation and characterization of the cyanogen bromide peptides from the
RT alpha 1 and alpha 2 chains of human skin collagen.";
RL Biochemistry 9:4699-4706(1970).
RN [15]
RP PROTEIN SEQUENCE OF 175-187 AND 274-289.
RX PubMed=2169412; DOI=10.1111/j.1432-1033.1990.tb19208.x;
RA Baetge B., Notbohm H., Diebold J., Lehmann H., Bodo M., Deutzmann R.,
RA Muller P.K.;
RT "A critical crosslink region in human-bone-derived collagen type I.
RT Specific cleavage site at residue Leu95.";
RL Eur. J. Biochem. 192:153-159(1990).
RN [16]
RP PROTEIN SEQUENCE OF 263-268, HYDROXYLATION AT LYS-265, AND GLYCOSYLATION AT
RP LYS-265.
RC TISSUE=Skin;
RX PubMed=4319110; DOI=10.1016/s0021-9258(18)62815-7;
RA Morgan P.H., Jacobs H.G., Segrest J.P., Cunningham L.W.;
RT "A comparative study of glycopeptides derived from selected vertebrate
RT collagens. A possible role of the carbohydrate in fibril formation.";
RL J. Biol. Chem. 245:5042-5048(1970).
RN [17]
RP NUCLEOTIDE SEQUENCE OF 281-302; 402-420; 823-842; 924-944; 1026-1045 AND
RP 1143-1162.
RX PubMed=2374517; DOI=10.1016/s0934-8832(11)80178-2;
RA Labhard M.E., Hollister D.W.;
RT "Segmental amplification of the entire helical and telopeptide regions of
RT the cDNA for human alpha 1 (I) collagen.";
RL Matrix 10:124-130(1990).
RN [18]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 425-1464, AND VARIANT ALA-1019.
RX PubMed=6689127; DOI=10.1021/bi00291a023;
RA Bernard M.P., Chu M.-L., Myers J.C., Ramirez F., Eikenberry E.F.,
RA Prockop D.J.;
RT "Nucleotide sequences of complementary deoxyribonucleic acids for the pro
RT alpha 1 chain of human type I procollagen. Statistical evaluation of
RT structures that are conserved during evolution.";
RL Biochemistry 22:5213-5223(1983).
RN [19]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 425-490; 965-1024; 999-1039 AND 1453-1464.
RX PubMed=6183642; DOI=10.1093/nar/10.19.5925;
RA Chu M.-L., Myers J.C., Bernard M.P., Ding J.-F., Ramirez F.;
RT "Cloning and characterization of five overlapping cDNAs specific for the
RT human pro alpha 1(I) collagen chain.";
RL Nucleic Acids Res. 10:5925-5934(1982).
RN [20]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 472-607.
RX PubMed=2981843; DOI=10.1016/s0021-9258(20)71150-6;
RA Chu M.-L., Gargiulo V., Williams C.J., Ramirez F.;
RT "Multiexon deletion in an osteogenesis imperfecta variant with increased
RT type III collagen mRNA.";
RL J. Biol. Chem. 260:691-694(1985).
RN [21]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 488-625.
RX PubMed=3857621; DOI=10.1073/pnas.82.9.2870;
RA Barsh G.S., Roush C.L., Bonadio J., Byers P.H., Gelinas R.E.;
RT "Intron-mediated recombination may cause a deletion in an alpha 1 type I
RT collagen chain in a lethal form of osteogenesis imperfecta.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:2870-2874(1985).
RN [22]
RP NUCLEOTIDE SEQUENCE OF 710-745, AND VARIANT OI2 ARG-728.
RX PubMed=2339700;
RA Wallis G.A., Starman B.J., Zinn A.B., Byers P.H.;
RT "Variable expression of osteogenesis imperfecta in a nuclear family is
RT explained by somatic mosaicism for a lethal point mutation in the alpha
RT 1(I) gene (COL1A1) of type I collagen in a parent.";
RL Am. J. Hum. Genet. 46:1034-1040(1990).
RN [23]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 746-781, AND VARIANT OI3 SER-767.
RX PubMed=7881420; DOI=10.1093/hmg/3.12.2201;
RA Forlino A., Zolezzi F., Valli M., Pignatti P.F., Cetta G., Brunelli P.C.,
RA Mottes M.;
RT "Severe (type III) osteogenesis imperfecta due to glycine substitutions in
RT the central domain of the collagen triple helix.";
RL Hum. Mol. Genet. 3:2201-2206(1994).
RN [24]
RP PROTEIN SEQUENCE OF 1063-1084, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [25]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1179-1464, VARIANTS OI2 HIS-1277; ARG-1388
RP AND 1337-GLU-TYR-1338 DEL, AND VARIANTS THR-1251 AND SER-1434.
RX PubMed=8349697; DOI=10.1016/s0021-9258(17)46833-5;
RA Chessler S.D., Wallis G.A., Byers P.H.;
RT "Mutations in the carboxyl-terminal propeptide of the pro alpha 1(I) chain
RT of type I collagen result in defective chain association and produce lethal
RT osteogenesis imperfecta.";
RL J. Biol. Chem. 268:18218-18225(1993).
RN [26]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1187-1220, AND VARIANT CYS-1195.
RX PubMed=3170557; DOI=10.1016/s0021-9258(18)68076-7;
RA Cohn D.H., Apone S., Eyre D.R., Starman B.J., Andreassen P.,
RA Charbonneau H., Nicholls A.C., Pope F.M., Byers P.H.;
RT "Substitution of cysteine for glycine within the carboxyl-terminal
RT telopeptide of the alpha 1 chain of type I collagen produces mild
RT osteogenesis imperfecta.";
RL J. Biol. Chem. 263:14605-14607(1988).
RN [27]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1229-1454, AND VARIANT LYS-1391.
RC TISSUE=Bone;
RX PubMed=3340531; DOI=10.1093/nar/16.1.349;
RA Maekelae J.K., Raassina M., Virta A., Vuorio E.;
RT "Human pro alpha 1(I) collagen: cDNA sequence for the C-propeptide
RT domain.";
RL Nucleic Acids Res. 16:349-349(1988).
RN [28]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1440-1464.
RX PubMed=2295701; DOI=10.1172/jci114424;
RA Willing M.C., Cohn D.H., Byers P.H.;
RT "Frameshift mutation near the 3' end of the COL1A1 gene of type I collagen
RT predicts an elongated Pro alpha 1(I) chain and results in osteogenesis
RT imperfecta type I.";
RL J. Clin. Invest. 85:282-290(1990).
RN [29]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1454-1464.
RX PubMed=1995349; DOI=10.1016/0014-5793(91)80237-w;
RA Maatta A., Bornstein P., Penttinen R.P.;
RT "Highly conserved sequences in the 3'-untranslated region of the COL1A1
RT gene bind cell-specific nuclear proteins.";
RL FEBS Lett. 279:9-13(1991).
RN [30]
RP REVIEW ON VARIANTS.
RX PubMed=2010058; DOI=10.1096/fasebj.5.7.2010058;
RA Kuivaniemi H., Tromp G., Prockop D.J.;
RT "Mutations in collagen genes: causes of rare and some common diseases in
RT humans.";
RL FASEB J. 5:2052-2060(1991).
RN [31]
RP INVOLVEMENT IN EDSARTH1.
RX PubMed=9295084;
RX DOI=10.1002/(sici)1096-8628(19971003)72:1<94::aid-ajmg20>3.0.co;2-o;
RA Byers P.H., Duvic M., Atkinson M., Robinow M., Smith L.T., Krane S.M.,
RA Greally M.T., Ludman M., Matalon R., Pauker S., Quanbeck D., Schwarze U.;
RT "Ehlers-Danlos syndrome type VIIA and VIIB result from splice-junction
RT mutations or genomic deletions that involve exon 6 in the COL1A1 and COL1A2
RT genes of type I collagen.";
RL Am. J. Med. Genet. 72:94-105(1997).
RN [32]
RP REVIEW ON VARIANTS.
RX PubMed=9101290;
RX DOI=10.1002/(sici)1098-1004(1997)9:4<300::aid-humu2>3.0.co;2-9;
RA Kuivaniemi H., Tromp G., Prockop D.J.;
RT "Mutations in fibrillar collagens (types I, II, III, and XI), fibril-
RT associated collagen (type IX), and network-forming collagen (type X) cause
RT a spectrum of diseases of bone, cartilage, and blood vessels.";
RL Hum. Mutat. 9:300-315(1997).
RN [33]
RP REVIEW ON VARIANTS.
RX PubMed=1895312; DOI=10.1136/jmg.28.7.433;
RA Byers P.H., Wallis G.A., Willing M.C.;
RT "Osteogenesis imperfecta: translation of mutation to phenotype.";
RL J. Med. Genet. 28:433-442(1991).
RN [34]
RP INTERACTION WITH TRAM2.
RX PubMed=14749390; DOI=10.1128/mcb.24.4.1758-1768.2004;
RA Stefanovic B., Stefanovic L., Schnabl B., Bataller R., Brenner D.A.;
RT "TRAM2 protein interacts with endoplasmic reticulum Ca2+ pump Serca2b and
RT is necessary for collagen type I synthesis.";
RL Mol. Cell. Biol. 24:1758-1768(2004).
RN [35]
RP INVOLVEMENT IN EDSARTH1.
RX PubMed=18409203; DOI=10.1002/ajmg.a.32213;
RA Giunta C., Chambaz C., Pedemonte M., Scapolan S., Steinmann B.;
RT "The arthrochalasia type of Ehlers-Danlos syndrome (EDS VIIA and VIIB): the
RT diagnostic value of collagen fibril ultrastructure.";
RL Am. J. Med. Genet. A 146A:1341-1346(2008).
RN [36]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22905912; DOI=10.1021/pr300539b;
RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P.,
RA Mariman E.C., Renes J.;
RT "Resveratrol-induced changes of the human adipocyte secretion profile.";
RL J. Proteome Res. 11:4733-4743(2012).
RN [37]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [38]
RP VARIANT OI2 CYS-1166.
RX PubMed=3016737; DOI=10.1073/pnas.83.16.6045;
RA Cohn D.H., Byers P.H., Steinmann B., Gelinas R.E.;
RT "Lethal osteogenesis imperfecta resulting from a single nucleotide change
RT in one human pro alpha 1(I) collagen allele.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:6045-6047(1986).
RN [39]
RP VARIANT OI2 ARG-569.
RX PubMed=3108247; DOI=10.1016/s0021-9258(18)48196-3;
RA Bateman J.F., Chan D., Walkers I.D., Rogers J.G., Cole W.G.;
RT "Lethal perinatal osteogenesis imperfecta due to the substitution of
RT arginine for glycine at residue 391 of the alpha 1(I) chain of type I
RT collagen.";
RL J. Biol. Chem. 262:7021-7027(1987).
RN [40]
RP VARIANT OI2 CYS-926.
RX PubMed=3667599; DOI=10.1016/s0021-9258(18)47857-x;
RA Vogel B.E., Minor R.R., Freund M., Prockop D.J.;
RT "A point mutation in a type I procollagen gene converts glycine 748 of the
RT alpha 1 chain to cysteine and destabilizes the triple helix in a lethal
RT variant of osteogenesis imperfecta.";
RL J. Biol. Chem. 262:14737-14744(1987).
RN [41]
RP VARIANT OI2 ARG-842.
RX PubMed=3403550; DOI=10.1016/s0021-9258(18)37829-3;
RA Bateman J.F., Lamande S.R., Dahl H.-H.M., Chan D., Cole W.G.;
RT "Substitution of arginine for glycine 664 in the collagen alpha 1(I) chain
RT in lethal perinatal osteogenesis imperfecta. Demonstration of the peptide
RT defect by in vitro expression of the mutant cDNA.";
RL J. Biol. Chem. 263:11627-11630(1988).
RN [42]
RP VARIANT OI1 CYS-1195.
RX PubMed=3244312;
RA Labhard M.E., Wirtz M.K., Pope F.M., Nicholls A.C., Hollister D.W.;
RT "A cysteine for glycine substitution at position 1017 in an alpha 1(I)
RT chain of type I collagen in a patient with mild dominantly inherited
RT osteogenesis imperfecta.";
RL Mol. Biol. Med. 5:197-207(1988).
RN [43]
RP VARIANT OI2 VAL-434.
RX PubMed=2470760; DOI=10.1016/s0021-9258(18)81769-0;
RA Patterson E., Smiley E., Bonadio J.;
RT "RNA sequence analysis of a perinatal lethal osteogenesis imperfecta
RT mutation.";
RL J. Biol. Chem. 264:10083-10087(1989).
RN [44]
RP VARIANT OI4 SER-1010.
RX PubMed=2745420; DOI=10.1016/s0021-9258(18)80150-8;
RA Marini J.C., Grange D.K., Gottesman G.S., Lewis M.B., Koeplin D.A.;
RT "Osteogenesis imperfecta type IV. Detection of a point mutation in one
RT alpha 1(I) collagen allele (COL1A1) by RNA/RNA hybrid analysis.";
RL J. Biol. Chem. 264:11893-11900(1989).
RN [45]
RP VARIANTS OI2 ALA-1106; VAL-1151; ARG-1154 AND VAL-1184.
RX PubMed=2777764; DOI=10.1016/s0021-9258(18)71548-2;
RA Lamande S.R., Dahl H.-H.M., Cole W.G., Bateman J.F.;
RT "Characterization of point mutations in the collagen COL1A1 and COL1A2
RT genes causing lethal perinatal osteogenesis imperfecta.";
RL J. Biol. Chem. 264:15809-15812(1989).
RN [46]
RP VARIANT OI3 SER-1022.
RX PubMed=2511192; DOI=10.1016/s0021-9258(19)47168-8;
RA Pack M., Constantinou C.D., Kalia K., Nielsen K.B., Prockop D.J.;
RT "Substitution of serine for alpha 1(I)-glycine 844 in a severe variant of
RT osteogenesis imperfecta minimally destabilizes the triple helix of type I
RT procollagen. The effects of glycine substitutions on thermal stability are
RT either position of amino acid specific.";
RL J. Biol. Chem. 264:19694-19699(1989).
RN [47]
RP VARIANT OI2 CYS-1082.
RX PubMed=2913053; DOI=10.1172/jci113920;
RA Constantinou C.D., Nielsen K.B., Prockop D.J.;
RT "A lethal variant of osteogenesis imperfecta has a single base mutation
RT that substitutes cysteine for glycine 904 of the alpha 1(I) chain of type I
RT procollagen. The asymptomatic mother has an unidentified mutation producing
RT an overmodified and unstable type I procollagen.";
RL J. Clin. Invest. 83:574-584(1989).
RN [48]
RP VARIANT OI1 CYS-272, VARIANT OI3 CYS-704, AND VARIANT OI2 CYS-896.
RX PubMed=2794057; DOI=10.1172/jci114286;
RA Starman B.J., Eyre D.R., Charbonneau H., Harrylock M., Weis M.A., Weiss L.,
RA Graham J.M. Jr., Byers P.H.;
RT "Osteogenesis imperfecta. The position of substitution for glycine by
RT cysteine in the triple helical domain of the pro alpha 1(I) chains of type
RT I collagen determines the clinical phenotype.";
RL J. Clin. Invest. 84:1206-1214(1989).
RN [49]
RP VARIANT OI2 CYS-422.
RA Fertala A., Westerhausen A., Morris G.M., Rooney J.E., Prockop D.J.;
RT "Two cysteine substitutions in the type I procollagen genes (COL1A1 and
RT COL1A2) that cause lethal osteogenesis imperfecta. The location of glycine
RT substitutions does not in any simple way predict their effects on protein
RT function or phenotype.";
RL Am. J. Hum. Genet. 47:A216-A216(1990).
RN [50]
RP VARIANTS OI2 SER-776 AND SER-809.
RX PubMed=2116413; DOI=10.1016/s0021-9258(18)77447-4;
RA Westerhausen A., Kishi J., Prockop D.J.;
RT "Mutations that substitute serine for glycine alpha 1-598 and glycine alpha
RT 1-631 in type I procollagen. The effects on thermal unfolding of the triple
RT helix are position-specific and demonstrate that the protein unfolds
RT through a series of cooperative blocks.";
RL J. Biol. Chem. 265:13995-14000(1990).
RN [51]
RP VARIANT OI2 ARG-1025.
RX PubMed=2211725; DOI=10.1016/s0021-9258(17)44798-3;
RA Wallis G.A., Starman B.J., Schwartz M.F., Byers P.H.;
RT "Substitution of arginine for glycine at position 847 in the triple-helical
RT domain of the alpha 1 (I) chain of type I collagen produces lethal
RT osteogenesis imperfecta. Molecules that contain one or two abnormal chains
RT differ in stability and secretion.";
RL J. Biol. Chem. 265:18628-18633(1990).
RN [52]
RP VARIANTS OI2 SER-1091; SER-1181; SER-1187 AND VAL-1187.
RA Cohn D.H., Wallis G.A., Zhang X., Byers P.H.;
RT "Serine for glycine substitutions in the alpha1(I) chain of type I
RT collagen: biological plasticity in the Gly-Pro-Hyp clamp at the carboxyl-
RT terminal end of triple helicalH domain.";
RL Matrix 10:236-236(1990).
RN [53]
RP VARIANT OI2 ASP-719.
RX PubMed=2035536;
RA Zhuang J., Constantinou C.D., Ganguly A., Prockop D.J.;
RT "A single base mutation in type I procollagen (COL1A1) that converts
RT glycine alpha 1-541 to aspartate in a lethal variant of osteogenesis
RT imperfecta: detection of the mutation with a carbodiimide reaction of DNA
RT heteroduplexes and direct sequencing of products of the PCR.";
RL Am. J. Hum. Genet. 48:1186-1191(1991).
RN [54]
RP VARIANT OI2 CYS-869.
RX PubMed=1953667; DOI=10.1042/bj2790747;
RA Steinmann B., Westerhausen A., Constantinou C.D., Superti-Furga A.,
RA Prockop D.J.;
RT "Substitution of cysteine for glycine-alpha 1-691 in the pro alpha 1(I)
RT chain of type I procollagen in a proband with lethal osteogenesis
RT imperfecta destabilizes the triple helix at a site C-terminal to the
RT substitution.";
RL Biochem. J. 279:747-752(1991).
RN [55]
RP VARIANT OI2 CYS-926.
RX PubMed=2036375; DOI=10.1021/bi00234a035;
RA Kadler K.E., Torre-Blanco A., Adachi E., Vogel B.E., Hojima Y.,
RA Prockop D.J.;
RT "A type I collagen with substitution of a cysteine for glycine-748 in the
RT alpha 1(I) chain copolymerizes with normal type I collagen and can generate
RT fractallike structures.";
RL Biochemistry 30:5081-5088(1991).
RN [56]
RP VARIANT OI3 ARG-332, AND VARIANT OI2 SER-1181.
RX PubMed=2037280; DOI=10.1007/bf01213088;
RA Pruchno C.J., Cohn D.H., Wallis G.A., Willing M.C., Starman B.J., Zhang X.,
RA Byers P.H.;
RT "Osteogenesis imperfecta due to recurrent point mutations at CpG
RT dinucleotides in the COL1A1 gene of type I collagen.";
RL Hum. Genet. 87:33-40(1991).
RN [57]
RP VARIANT OI4 CYS-356.
RX PubMed=1988452; DOI=10.1016/s0021-9258(18)52374-7;
RA Valli M., Mottes M., Tenni R., Sangalli A., Gomez Lira M., Rossi A.,
RA Antoniazzi F., Cetta G., Pignatti P.F.;
RT "A de novo G to T transversion in a pro-alpha 1 (I) collagen gene for a
RT moderate case of osteogenesis imperfecta. Substitution of cysteine for
RT glycine 178 in the triple helical domain.";
RL J. Biol. Chem. 266:1872-1878(1991).
RN [58]
RP VARIANT OI2 VAL-815.
RX PubMed=1874719; DOI=10.1016/s0021-9258(18)98449-8;
RA Tsuneyoshi T., Westerhausen A., Constantinou C.D., Prockop D.J.;
RT "Substitutions for glycine alpha 1-637 and glycine alpha 2-694 of type I
RT procollagen in lethal osteogenesis imperfecta. The conformational strain on
RT the triple helix introduced by a glycine substitution can be transmitted
RT along the helix.";
RL J. Biol. Chem. 266:15608-15613(1991).
RN [59]
RP VARIANT OI1 ARG-263.
RX PubMed=1718984; DOI=10.1016/s0021-9258(18)54712-8;
RA Deak S.B., Scholz P.M., Amenta P.S., Constantinou C.D., Levi-Minzi S.A.,
RA Gonzalez-Lavin L., MacKenzie J.W.;
RT "The substitution of arginine for glycine 85 of the alpha 1(I) procollagen
RT chain results in mild osteogenesis imperfecta. The mutation provides direct
RT evidence for three discrete domains of cooperative melting of intact type I
RT collagen.";
RL J. Biol. Chem. 266:21827-21832(1991).
RN [60]
RP VARIANT OI2 1046-GLY--PRO-1048 DEL.
RX PubMed=1939261; DOI=10.1016/s0021-9258(18)54581-6;
RA Hawkins J.R., Superti-Furga A., Steinmann B., Dalgleish R.;
RT "A 9-base pair deletion in COL1A1 in a lethal variant of osteogenesis
RT imperfecta.";
RL J. Biol. Chem. 266:22370-22374(1991).
RN [61]
RP VARIANT OI3 CYS-593, AND VARIANT OI4 CYS-593.
RX PubMed=1770532; DOI=10.1136/jmg.28.11.757;
RA Nicholls A.C., Oliver J.E., Renouf D.V., Keston M., Pope F.M.;
RT "Substitution of cysteine for glycine at residue 415 of one allele of the
RT alpha 1(I) chain of type I procollagen in type III/IV osteogenesis
RT imperfecta.";
RL J. Med. Genet. 28:757-764(1991).
RN [62]
RP VARIANT THR-1075.
RX PubMed=1870989; DOI=10.1093/nar/19.15.4302;
RA Sokolov B.P., Constantinou C.D., Tsuneyoshi T., Zhuang J., Prockop D.J.;
RT "G to A polymorphism in exon 45 of the COL1A1 gene.";
RL Nucleic Acids Res. 19:4302-4302(1991).
RN [63]
RP VARIANT OI1 SER-1079.
RX PubMed=1634225; DOI=10.1007/bf00219169;
RA Mottes M., Sangalli A., Valli M., Gomez Lira M., Tenni R., Buttitta P.,
RA Pignatti P.F., Cetta G.;
RT "Mild dominant osteogenesis imperfecta with intrafamilial variability: the
RT cause is a serine for glycine alpha 1(I) 901 substitution in a type-I
RT collagen gene.";
RL Hum. Genet. 89:480-484(1992).
RN [64]
RP VARIANT OI2 VAL-980.
RX PubMed=1511982; DOI=10.1007/bf00221955;
RA Bonaventure J., Cohen-Solal L., Lasselin C., Maroteaux P.;
RT "A dominant mutation in the COL1A1 gene that substitutes glycine for valine
RT causes recurrent lethal osteogenesis imperfecta.";
RL Hum. Genet. 89:640-646(1992).
RN [65]
RP VARIANT OI2 1046-GLY--PRO-1048 DEL.
RX PubMed=1460047; DOI=10.1016/s0021-9258(19)74072-1;
RA Wallis G.A., Kadler K.E., Starman B.J., Byers P.H.;
RT "A tripeptide deletion in the triple-helical domain of the pro alpha 1(I)
RT chain of type I procollagen in a patient with lethal osteogenesis
RT imperfecta does not alter cleavage of the molecule by N-proteinase.";
RL J. Biol. Chem. 267:25529-25534(1992).
RN [66]
RP VARIANT OI1 CYS-221.
RX PubMed=1737847; DOI=10.1172/jci115622;
RA Shapiro J.R., Stover M.L., Burn V.E., McKinstry M.B., Burshell A.L.,
RA Chipman S.D., Rowe D.W.;
RT "An osteopenic nonfracture syndrome with features of mild osteogenesis
RT imperfecta associated with the substitution of a cysteine for glycine at
RT triple helix position 43 in the pro alpha 1(I) chain of type I collagen.";
RL J. Clin. Invest. 89:567-573(1992).
RN [67]
RP VARIANTS OI2 VAL-434; VAL-1151 AND VAL-1184.
RX PubMed=1613761; DOI=10.1136/jmg.29.2.112;
RA Cole W.G., Patterson E., Bonadio J., Campbell P.E., Fortune D.W.;
RT "The clinicopathological features of three babies with osteogenesis
RT imperfecta resulting from the substitution of glycine by valine in the pro
RT alpha 1 (I) chain of type I procollagen.";
RL J. Med. Genet. 29:112-118(1992).
RN [68]
RP VARIANT OI2 CYS-1312.
RX PubMed=8456808; DOI=10.1002/ajmg.1320450216;
RA Bateman J.F., Lamande S.R., Hannagan M., Moeller I., Dahl H.-H.M.,
RA Cole W.G.;
RT "Chemical cleavage method for the detection of RNA base changes: experience
RT in the application to collagen mutations in osteogenesis imperfecta.";
RL Am. J. Med. Genet. 45:233-240(1993).
RN [69]
RP VARIANT OI3 SER-530.
RX PubMed=8456809; DOI=10.1002/ajmg.1320450217;
RA Marini J.C., Lewis M.B., Chen K.J.;
RT "Moderately severe osteogenesis imperfecta associated with substitutions of
RT serine for glycine in the alpha 1(I) chain of type I collagen.";
RL Am. J. Med. Genet. 45:241-245(1993).
RN [70]
RP VARIANT OI4 CYS-353.
RX PubMed=8339541; DOI=10.3109/03008209309061961;
RA Wirtz M.K., Rao V.H., Glanville R.W., Labhard M.E., Pretorius P.J.,
RA de Vries W.N., de Wet W., Hollister D.W.;
RT "A cysteine for glycine substitution at position 175 in an alpha 1 (I)
RT chain of type I collagen produces a clinically heterogeneous form of
RT osteogenesis imperfecta.";
RL Connect. Tissue Res. 29:1-11(1993).
RN [71]
RP VARIANT OI2 ALA-1088.
RX PubMed=7679635; DOI=10.1111/j.1432-1033.1993.tb17565.x;
RA Valli M., Sangalli A., Rossi A., Mottes M., Forlino A., Tenni R.,
RA Pignatti P.F., Cetta G.;
RT "Osteogenesis imperfecta and type-I collagen mutations. A lethal variant
RT caused by a Gly910-->Ala substitution in the alpha 1 (I) chain.";
RL Eur. J. Biochem. 211:415-419(1993).
RN [72]
RP VARIANT OI1 VAL-263.
RX PubMed=8223589; DOI=10.1111/j.1432-1033.1993.tb18220.x;
RA Valli M., Zolezzi F., Mottes M., Antoniazzi F., Stanzial F., Tenni R.,
RA Pignatti P.F., Cetta G.;
RT "Gly85 to Val substitution in pro alpha 1(I) chain causes mild osteogenesis
RT imperfecta and introduces a susceptibility to protease digestion.";
RL Eur. J. Biochem. 217:77-82(1993).
RN [73]
RP VARIANT OI2 VAL-743.
RX PubMed=8100209; DOI=10.1007/bf00217768;
RA Mackay K., Lund A.M., Raghunath M., Steinmann B., Dalgleish R.;
RT "SSCP detection of a Gly565Val substitution in the pro alpha 1(I) collagen
RT chain resulting in osteogenesis imperfecta type II.";
RL Hum. Genet. 91:439-444(1993).
RN [74]
RP VARIANTS OI2 SER-425 AND SER-530, VARIANT OI4 SER-560, VARIANT OI3 SER-719,
RP AND VARIANT ALA-823.
RX PubMed=7691343; DOI=10.1093/hmg/2.8.1155;
RA Mackay K., Byers P.H., Dalgleish R.;
RT "An RT-PCR-SSCP screening strategy for detection of mutations in the gene
RT encoding the alpha 1 chain of type I collagen: application to four patients
RT with osteogenesis imperfecta.";
RL Hum. Mol. Genet. 2:1155-1160(1993).
RN [75]
RP VARIANT OI2 SER-593, AND VARIANT OI3 SER-593.
RX PubMed=8364588; DOI=10.1002/humu.1380020308;
RA Mottes M., Gomez Lira M., Valli M., Scarano G., Lonardo F., Forlino A.,
RA Cetta G., Pignatti P.F.;
RT "Paternal mosaicism for a COL1A1 dominant mutation (alpha 1 Ser-415) causes
RT recurrent osteogenesis imperfecta.";
RL Hum. Mutat. 2:196-204(1993).
RN [76]
RP VARIANT OI4 SER-530.
RX PubMed=8094076; DOI=10.1016/s0021-9258(18)53826-6;
RA Marini J.C., Lewis M.B., Wang Q., Chen K.J., Orrison B.M.;
RT "Serine for glycine substitutions in type I collagen in two cases of type
RT IV osteogenesis imperfecta (OI). Additional evidence for a regional model
RT of OI pathophysiology.";
RL J. Biol. Chem. 268:2667-2673(1993).
RN [77]
RP VARIANTS OI2.
RX PubMed=8349698; DOI=10.1016/s0021-9258(17)46834-7;
RA Chessler S.D., Byers P.H.;
RT "BiP binds type I procollagen pro alpha chains with mutations in the
RT carboxyl-terminal propeptide synthesized by cells from patients with
RT osteogenesis imperfecta.";
RL J. Biol. Chem. 268:18226-18233(1993).
RN [78]
RP VARIANT OI2 ARG-389.
RX PubMed=7520724; DOI=10.1016/8756-3282(94)90295-x;
RA Sztrolovics R., Glorieux F.H., Travers R., van der Rest M., Roughley P.J.;
RT "Osteogenesis imperfecta: comparison of molecular defects with bone
RT histological changes.";
RL Bone 15:321-328(1994).
RN [79]
RP VARIANT OI3 ARG-350.
RX PubMed=8019571; DOI=10.1002/humu.1380030327;
RA Mackay K., de Paepe A., Nuytinck L., Dalgleish R.;
RT "Substitution of glycine-172 by arginine in the alpha 1 chain of type I
RT collagen in a patient with osteogenesis imperfecta, type III.";
RL Hum. Mutat. 3:324-326(1994).
RN [80]
RP VARIANT OI2 CYS-1124.
RX PubMed=7961597; DOI=10.1093/oxfordjournals.jbchem.a124429;
RA Kurosaka D., Hattori S., Hori H., Yamaguchi N., Hasegawa T., Akimoto H.,
RA Nagai Y.;
RT "Substitution of cysteine for glycine-946 in the alpha 1(I) chain of type I
RT procollagen causes lethal osteogenesis imperfecta.";
RL J. Biochem. 115:853-857(1994).
RN [81]
RP VARIANT OI4 SER-1061.
RX PubMed=7982948; DOI=10.1016/s0021-9258(18)43820-3;
RA Lightfoot S.J., Atkinson M.S., Murphy G., Byers P.H., Kadler K.E.;
RT "Substitution of serine for glycine 883 in the triple helix of the pro
RT alpha 1 (I) chain of type I procollagen produces osteogenesis imperfecta
RT type IV and introduces a structural change in the triple helix that does
RT not alter cleavage of the molecule by procollagen N-proteinase.";
RL J. Biol. Chem. 269:30352-30357(1994).
RN [82]
RP VARIANT OI3 ARG-332.
RX PubMed=8669434;
RX DOI=10.1002/(sici)1096-8628(19960111)61:2<111::aid-ajmg1>3.0.co;2-#;
RA Zhuang J., Tromp G., Kuivaniemi H., Castells S., Prockop D.J.;
RT "Substitution of arginine for glycine at position 154 of the alpha 1 chain
RT of type I collagen in a variant of osteogenesis imperfecta: comparison to
RT previous cases with the same mutation.";
RL Am. J. Med. Genet. 61:111-116(1996).
RN [83]
RP VARIANT OI2 SER-839.
RX PubMed=8786074; DOI=10.1007/bf02185764;
RA Nuytinck L., Dalgleish R., Spotila L., Renard J.-P., van Regemorter N.,
RA de Paepe A.;
RT "Substitution of glycine-661 by serine in the alpha1(I) and alpha2(I)
RT chains of type I collagen results in different clinical and biochemical
RT phenotypes.";
RL Hum. Genet. 97:324-329(1996).
RN [84]
RP VARIANT OI3 PRO-1464.
RX PubMed=8723681;
RX DOI=10.1002/(sici)1098-1004(1996)7:4<318::aid-humu5>3.0.co;2-4;
RA Oliver J.E., Thompson E.M., Pope F.M., Nicholls A.C.;
RT "Mutation in the carboxy-terminal propeptide of the Pro alpha 1(I) chain of
RT type I collagen in a child with severe osteogenesis imperfecta (OI type
RT III): possible implications for protein folding.";
RL Hum. Mutat. 7:318-326(1996).
RN [85]
RP INVOLVEMENT IN OSTEOPOROSIS.
RX PubMed=8841196; DOI=10.1038/ng1096-203;
RA Grant S.F.A., Reid D.M., Blake G., Herd R., Fogelman I., Ralston S.H.;
RT "Reduced bone density and osteoporosis associated with a polymorphic Sp1
RT binding site in the collagen type I alpha 1 gene.";
RL Nat. Genet. 14:203-205(1996).
RN [86]
RP VARIANTS OI3 SER-821; SER-1040; SER-1049; SER-1058 AND SER-1076.
RX PubMed=9101304;
RX DOI=10.1002/(sici)1098-1004(1997)9:4<378::aid-humu16>3.0.co;2-#;
RA Lund A.M., Skovby F., Schwartz M.;
RT "Serine for glycine substitutions in the C-terminal third of the alpha 1(I)
RT chain of collagen I in five patients with nonlethal osteogenesis
RT imperfecta.";
RL Hum. Mutat. 9:378-382(1997).
RN [87]
RP VARIANT OI2 VAL-764.
RX PubMed=9143923;
RX DOI=10.1002/(sici)1098-1004(1997)9:5<431::aid-humu9>3.0.co;2-6;
RA Lund A.M., Skovby F., Schwartz M.;
RT "(G586V) substitutions in the alpha 1 and alpha 2 chains of collagen I:
RT effect of alpha-chain stoichiometry on the phenotype of osteogenesis
RT imperfecta?";
RL Hum. Mutat. 9:431-436(1997).
RN [88]
RP VARIANTS OI4 ALA-398; CYS-527 AND CYS-701.
RX PubMed=9600458;
RX DOI=10.1002/(sici)1098-1004(1998)11:5<395::aid-humu7>3.0.co;2-4;
RA Sarafova A.P., Choi H., Forlino A., Gajko A., Cabral W.A., Tosi L.,
RA Reing C.M., Marini J.C.;
RT "Three novel type I collagen mutations in osteogenesis imperfecta type IV
RT probands are associated with discrepancies between electrophoretic
RT migration of osteoblast and fibroblast collagen.";
RL Hum. Mutat. 11:395-403(1998).
RN [89]
RP VARIANTS OI2 SER-656 AND ASP-1172.
RX PubMed=10627137;
RA Mottes M., Gomez Lira M., Zolezzi F., Valli M., Lisi V., Freising P.;
RT "Four new cases of lethal osteogenesis imperfecta due to glycine
RT substitutions in COL1A1 and genes.";
RL Hum. Mutat. 12:71-72(1998).
RN [90]
RP INVOLVEMENT IN INVOLUTIONAL OSTEOPOROSIS.
RX PubMed=9535665; DOI=10.1056/nejm199804093381502;
RA Uitterlinden A.G., Burger H., Huang Q., Yue F., McGuigan F.E.A.,
RA Grant S.F.A., Hofman A., van Leeuwen J.P.T.M., Pols H.A.P., Ralston S.H.;
RT "Relation of alleles of the collagen type Ialpha1 gene to bone density and
RT the risk of osteoporotic fractures in postmenopausal women.";
RL N. Engl. J. Med. 338:1016-1021(1998).
RN [91]
RP VARIANT OI3 SER-866.
RX PubMed=10408781;
RX DOI=10.1002/(sici)1098-1004(1999)13:6<503::aid-humu12>3.0.co;2-i;
RA Lund A.M., Astroem E., Soederhaell S., Schwartz M., Skovby F.;
RT "Osteogenesis imperfecta: mosaicism and refinement of the genotype-
RT phenotype map in OI type III.";
RL Hum. Mutat. 13:503-503(1999).
RN [92]
RP VARIANT EDSCL1 CYS-312.
RX PubMed=10739762; DOI=10.1086/302859;
RA Nuytinck L., Freund M., Lagae L., Pierard G.E., Hermanns-Le T.,
RA De Paepe A.;
RT "Classical Ehlers-Danlos syndrome caused by a mutation in type I
RT collagen.";
RL Am. J. Hum. Genet. 66:1398-1402(2000).
RN [93]
RP DISEASE, AND CHROMOSOMAL TRANSLOCATION WITH PDGFB.
RX PubMed=8988177; DOI=10.1038/ng0197-95;
RA Simon M.-P., Pedeutour F., Sirvent N., Grosgeorge J., Minoletti F.,
RA Coindre J.-M., Terrier-Lacombe M.-J., Mandahl N., Craver R.D., Blin N.,
RA Sozzi G., Turc-Carel C., O'Brien K.P., Kedra D., Fransson I., Guilbaud C.,
RA Dumanski J.P.;
RT "Deregulation of the platelet-derived growth factor B-chain gene via fusion
RT with collagen gene COL1A1 in dermatofibrosarcoma protuberans and giant-cell
RT fibroblastoma.";
RL Nat. Genet. 15:95-98(1997).
RN [94]
RP DISEASE, AND CHROMOSOMAL TRANSLOCATION WITH PDGFB.
RX PubMed=12660034; DOI=10.1016/s0165-4608(02)00844-0;
RA Sandberg A.A., Anderson W.D., Fredenberg C., Hashimoto H.;
RT "Dermatofibrosarcoma protuberans of breast.";
RL Cancer Genet. Cytogenet. 142:56-59(2003).
RN [95]
RP INVOLVEMENT IN OIEDS1, VARIANTS OIEDS1 ASP-191; VAL-203; ARG-212; GLU-254
RP AND GLU-266, AND CHARACTERIZATION OF VARIANTS OIEDS1 ASP-191; VAL-203;
RP ARG-212; GLU-254 AND GLU-266.
RX PubMed=15728585; DOI=10.1074/jbc.m414698200;
RA Cabral W.A., Makareeva E., Colige A., Letocha A.D., Ty J.M., Yeowell H.N.,
RA Pals G., Leikin S., Marini J.C.;
RT "Mutations near amino end of alpha1(I) collagen cause combined osteogenesis
RT imperfecta/Ehlers-Danlos syndrome by interference with N-propeptide
RT processing.";
RL J. Biol. Chem. 280:19259-19269(2005).
RN [96]
RP VARIANT CAFYD CYS-1014.
RX PubMed=15864348; DOI=10.1172/jci200522760;
RA Gensure R.C., Maekitie O., Barclay C., Chan C., Depalma S.R., Bastepe M.,
RA Abuzahra H., Couper R., Mundlos S., Sillence D., Ala-Kokko L.,
RA Seidman J.G., Cole W.G., Jueppner H.;
RT "A novel COL1A1 mutation in infantile cortical hyperostosis (Caffey
RT disease) expands the spectrum of collagen-related disorders.";
RL J. Clin. Invest. 115:1250-1257(2005).
RN [97]
RP VARIANTS OI3 VAL-203 AND SER-821, AND VARIANTS OI4 ARG-257 AND SER-683.
RX PubMed=16879195; DOI=10.1111/j.1399-0004.2006.00646.x;
RA Venturi G., Tedeschi E., Mottes M., Valli M., Camilot M., Viglio S.,
RA Antoniazzi F., Tato L.;
RT "Osteogenesis imperfecta: clinical, biochemical and molecular findings.";
RL Clin. Genet. 70:131-139(2006).
RN [98]
RP VARIANTS OI1/OI3/OI4 ARG-194; ASP-242; ARG-257; SER-722; SER-767; SER-821
RP AND SER-1058.
RX PubMed=16705691; DOI=10.1002/humu.9423;
RA Lee K.S., Song H.R., Cho T.J., Kim H.J., Lee T.M., Jin H.S., Park H.Y.,
RA Kang S., Jung S.C., Koo S.K.;
RT "Mutational spectrum of type I collagen genes in Korean patients with
RT osteogenesis imperfecta.";
RL Hum. Mutat. 27:599-599(2006).
RN [99]
RP VARIANTS OI2 ARG-22; ARG-581; VAL-734 AND ASN-1413, VARIANTS OI4 ARG-197
RP AND CYS-338, VARIANTS OI1 VAL-320; ARG-555; SER-647 AND GLU-1219, AND
RP VARIANTS ALA-205; LYS-288; SER-906 AND HIS-1356.
RX PubMed=16786509; DOI=10.1002/humu.9430;
RA Pollitt R., McMahon R., Nunn J., Bamford R., Afifi A., Bishop N.,
RA Dalton A.;
RT "Mutation analysis of COL1A1 and COL1A2 in patients diagnosed with
RT osteogenesis imperfecta type I-IV.";
RL Hum. Mutat. 27:716-716(2006).
RN [100]
RP VARIANT OI2 ASP-833.
RX PubMed=16566045; DOI=10.1002/pd.1428;
RA Aerts M., Van Holsbeke C., de Ravel T., Devlieger R.;
RT "Prenatal diagnosis of type II osteogenesis imperfecta, describing a new
RT mutation in the COL1A1 gene.";
RL Prenat. Diagn. 26:394-394(2006).
RN [101]
RP VARIANT OI1 ASP-1157.
RX PubMed=16638323;
RA Wang Z., Xu D.L., Chen Z., Hu J.Y., Yang Z., Wang L.T.;
RT "A new mutation in COL1A1 gene in a family with osteogenesis imperfecta.";
RL Zhonghua Yi Xue Za Zhi 86:170-173(2006).
RN [102]
RP VARIANT EDSCL1 CYS-312, AND VARIANTS CYS-574 AND CYS-1093.
RX PubMed=17211858; DOI=10.1002/humu.20455;
RA Malfait F., Symoens S., De Backer J., Hermanns-Le T., Sakalihasan N.,
RA Lapiere C.M., Coucke P., De Paepe A.;
RT "Three arginine to cysteine substitutions in the pro-alpha (I)-collagen
RT chain cause Ehlers-Danlos syndrome with a propensity to arterial rupture in
RT early adulthood.";
RL Hum. Mutat. 28:387-395(2007).
RN [103]
RP VARIANT OIEDS1 CYS-1066, AND INVOLVEMENT IN OIEDS1.
RX PubMed=17206620; DOI=10.1002/humu.20456;
RA Cabral W.A., Makareeva E., Letocha A.D., Scribanu N., Fertala A.,
RA Steplewski A., Keene D.R., Persikov A.V., Leikin S., Marini J.C.;
RT "Y-position cysteine substitution in type I collagen (alpha1(I)
RT R888C/p.R1066C) is associated with osteogenesis imperfecta/Ehlers-Danlos
RT syndrome phenotype.";
RL Hum. Mutat. 28:396-405(2007).
RN [104]
RP VARIANTS OI1 GLU-266 AND SER-287, AND VARIANT OI4 SER-353.
RX PubMed=17875077; DOI=10.1111/j.1442-200x.2007.02422.x;
RA Kataoka K., Ogura E., Hasegawa K., Inoue M., Seino Y., Morishima T.,
RA Tanaka H.;
RT "Mutations in type I collagen genes in Japanese osteogenesis imperfecta
RT patients.";
RL Pediatr. Int. 49:564-569(2007).
RN [105]
RP VARIANTS GLN-1141 AND ILE-1177.
RX PubMed=18272325; DOI=10.1016/j.ygeno.2007.12.008;
RA Chan T.F., Poon A., Basu A., Addleman N.R., Chen J., Phong A., Byers P.H.,
RA Klein T.E., Kwok P.Y.;
RT "Natural variation in four human collagen genes across an ethnically
RT diverse population.";
RL Genomics 91:307-314(2008).
RN [106]
RP VARIANTS OI1 VAL-200 AND PHE-349, VARIANT OI2 SER-866, AND VARIANT OI3
RP SER-1040.
RX PubMed=18670065; DOI=10.1007/bf03195625;
RA Witecka J., Augusciak-Duma A.M., Kruczek A., Szydlo A., Lesiak M.,
RA Krzak M., Pietrzyk J.J., Mannikko M., Sieron A.L.;
RT "Two novel COL1A1 mutations in patients with osteogenesis imperfecta (OI)
RT affect the stability of the collagen type I triple-helix.";
RL J. Appl. Genet. 49:283-295(2008).
RN [107]
RP VARIANTS OI2 THR-146; VAL-288; ASP-353; VAL-368; THR-390; SER-425; ASP-455;
RP VAL-470; VAL-509; ALA-548; ARG-602; ASP-605; ARG-614; ARG-740; SER-809;
RP ARG-824; ARG-845; ARG-848; HIS-855; SER-866; SER-875; SER-884; ASP-896;
RP CYS-947; ASP-977; CYS-1001; VAL-1022; ALA-PRO-GLY-1052 INS; ASP-1055;
RP SER-1094; ASP-1100 AND ASN-1413.
RX PubMed=18996919; DOI=10.1093/hmg/ddn374;
RA Bodian D.L., Chan T.F., Poon A., Schwarze U., Yang K., Byers P.H.,
RA Kwok P.Y., Klein T.E.;
RT "Mutation and polymorphism spectrum in osteogenesis imperfecta type II:
RT implications for genotype-phenotype relationships.";
RL Hum. Mol. Genet. 18:463-471(2009).
RN [108]
RP VARIANT ASN-1219, AND CHARACTERIZATION OF VARIANT ASN-1219.
RX PubMed=21344539; DOI=10.1002/humu.21475;
RA Lindahl K., Barnes A.M., Fratzl-Zelman N., Whyte M.P., Hefferan T.E.,
RA Makareeva E., Brusel M., Yaszemski M.J., Rubin C.J., Kindmark A.,
RA Roschger P., Klaushofer K., McAlister W.H., Mumm S., Leikin S., Kessler E.,
RA Boskey A.L., Ljunggren O., Marini J.C.;
RT "COL1 C-propeptide cleavage site mutations cause high bone mass
RT osteogenesis imperfecta.";
RL Hum. Mutat. 32:598-609(2011).
RN [109]
RP VARIANTS OIEDS1 ASP-188 AND CYS-203, INVOLVEMENT IN OIEDS1, AND
RP CHARACTERIZATION OF VARIANT OIEDS1 ASP-188.
RX PubMed=23692737; DOI=10.1186/1750-1172-8-78;
RA Malfait F., Symoens S., Goemans N., Gyftodimou Y., Holmberg E.,
RA Lopez-Gonzalez V., Mortier G., Nampoothiri S., Petersen M.B., De Paepe A.;
RT "Helical mutations in type I collagen that affect the processing of the
RT amino-propeptide result in an Osteogenesis Imperfecta/Ehlers-Danlos
RT Syndrome overlap syndrome.";
RL Orphanet J. Rare Dis. 8:78-78(2013).
RN [110]
RP VARIANT OI1 GLU-1088.
RX PubMed=24682174; DOI=10.3892/mmr.2014.2084;
RA Xia X.Y., Li W.W., Li N., Wu Q.Y., Cui Y.X., Li X.J.;
RT "A novel mild variant of osteogenesis imperfecta type I caused by a
RT Gly1088Glu mutation in COL1A1.";
RL Mol. Med. Report. 9:2187-2190(2014).
RN [111]
RP VARIANT OI2 CYS-773.
RX PubMed=25958000; DOI=10.1186/s40246-015-0028-0;
RA Maasalu K., Nikopensius T., Koks S., Noukas M., Kals M., Prans E.,
RA Zhytnik L., Metspalu A., Maertson A.;
RT "Whole-exome sequencing identifies de novo mutation in the COL1A1 gene to
RT underlie the severe osteogenesis imperfecta.";
RL Hum. Genomics 9:6-6(2015).
CC -!- FUNCTION: Type I collagen is a member of group I collagen (fibrillar
CC forming collagen).
CC -!- SUBUNIT: Trimers of one alpha 2(I) and two alpha 1(I) chains. Interacts
CC with MRC2 (By similarity). Interacts with TRAM2 (PubMed:14749390).
CC Interacts with MFAP4 in a Ca (2+)-dependent manner (By similarity).
CC {ECO:0000250|UniProtKB:P02453, ECO:0000250|UniProtKB:P02454,
CC ECO:0000269|PubMed:14749390}.
CC -!- INTERACTION:
CC P02452; P08123: COL1A2; NbExp=5; IntAct=EBI-982999, EBI-983038;
CC P02452; P02751: FN1; NbExp=3; IntAct=EBI-982999, EBI-1220319;
CC P02452; Q14145: KEAP1; NbExp=3; IntAct=EBI-982999, EBI-751001;
CC P02452; O01949: AAEL010235; Xeno; NbExp=5; IntAct=EBI-982999, EBI-7685554;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
CC -!- TISSUE SPECIFICITY: Forms the fibrils of tendon, ligaments and bones.
CC In bones the fibrils are mineralized with calcium hydroxyapatite.
CC -!- DOMAIN: The C-terminal propeptide, also known as COLFI domain, have
CC crucial roles in tissue growth and repair by controlling both the
CC intracellular assembly of procollagen molecules and the extracellular
CC assembly of collagen fibrils. It binds a calcium ion which is essential
CC for its function (By similarity). {ECO:0000250}.
CC -!- PTM: Contains mostly 4-hydroxyproline. Proline residues at the third
CC position of the tripeptide repeating unit (G-X-Y) are hydroxylated in
CC some or all of the chains. {ECO:0000269|PubMed:4319110}.
CC -!- PTM: Contains 3-hydroxyproline at a few sites. This modification occurs
CC on the first proline residue in the sequence motif Gly-Pro-Hyp, where
CC Hyp is 4-hydroxyproline. {ECO:0000250|UniProtKB:P11087}.
CC -!- PTM: Lysine residues at the third position of the tripeptide repeating
CC unit (G-X-Y) are 5-hydroxylated in some or all of the chains.
CC {ECO:0000269|PubMed:4319110}.
CC -!- PTM: O-glycosylated on hydroxylated lysine residues. The O-linked
CC glycan consists of a Glc-Gal disaccharide.
CC {ECO:0000269|PubMed:4319110}.
CC -!- DISEASE: Caffey disease (CAFYD) [MIM:114000]: An autosomal dominant
CC disorder characterized by an infantile episode of massive subperiosteal
CC new bone formation that typically involves the diaphyses of the long
CC bones, mandible, and clavicles. The involved bones may also appear
CC inflamed, with painful swelling and systemic fever often accompanying
CC the illness. The bone changes usually begin before 5 months of age and
CC resolve before 2 years of age. {ECO:0000269|PubMed:15864348}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Ehlers-Danlos syndrome, classic type, 1 (EDSCL1) [MIM:130000]:
CC A form of Ehlers-Danlos syndrome, a group of connective tissue
CC disorders characterized by skin hyperextensibility, articular
CC hypermobility, and tissue fragility. The main features of classic
CC Ehlers-Danlos syndrome are joint hypermobility and dislocation, and
CC fragile, bruisable skin. EDSCL1 inheritance is autosomal dominant.
CC {ECO:0000269|PubMed:10739762, ECO:0000269|PubMed:17211858}. Note=The
CC disease may be caused by variants affecting the gene represented in
CC this entry.
CC -!- DISEASE: Ehlers-Danlos syndrome, arthrochalasia type, 1 (EDSARTH1)
CC [MIM:130060]: A form of Ehlers-Danlos syndrome, a connective tissue
CC disorder characterized by hyperextensible skin, atrophic cutaneous
CC scars due to tissue fragility and joint hyperlaxity. EDSARTH1 is an
CC autosomal dominant form characterized by frequent congenital hip
CC dislocation and extreme joint laxity with recurrent joint subluxations
CC and minimal skin involvement. {ECO:0000269|PubMed:18409203,
CC ECO:0000269|PubMed:9295084}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Osteogenesis imperfecta 1 (OI1) [MIM:166200]: An autosomal
CC dominant form of osteogenesis imperfecta, a connective tissue disorder
CC characterized by low bone mass, bone fragility and susceptibility to
CC fractures after minimal trauma. Disease severity ranges from very mild
CC forms without fractures to intrauterine fractures and perinatal
CC lethality. Extraskeletal manifestations, which affect a variable number
CC of patients, are dentinogenesis imperfecta, hearing loss, and blue
CC sclerae. OI1 is a non-deforming form with normal height or mild short
CC stature, and no dentinogenesis imperfecta. {ECO:0000269|PubMed:1634225,
CC ECO:0000269|PubMed:16638323, ECO:0000269|PubMed:16705691,
CC ECO:0000269|PubMed:16786509, ECO:0000269|PubMed:1718984,
CC ECO:0000269|PubMed:1737847, ECO:0000269|PubMed:17875077,
CC ECO:0000269|PubMed:18670065, ECO:0000269|PubMed:24682174,
CC ECO:0000269|PubMed:2794057, ECO:0000269|PubMed:3244312,
CC ECO:0000269|PubMed:8223589}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Osteogenesis imperfecta 2 (OI2) [MIM:166210]: An autosomal
CC dominant form of osteogenesis imperfecta, a connective tissue disorder
CC characterized by low bone mass, bone fragility and susceptibility to
CC fractures after minimal trauma. Disease severity ranges from very mild
CC forms without fractures to intrauterine fractures and perinatal
CC lethality. Extraskeletal manifestations, which affect a variable number
CC of patients, are dentinogenesis imperfecta, hearing loss, and blue
CC sclerae. OI2 is characterized by bone fragility, with many perinatal
CC fractures, severe bowing of long bones, undermineralization, and death
CC in the perinatal period due to respiratory insufficiency.
CC {ECO:0000269|PubMed:10627137, ECO:0000269|PubMed:1460047,
CC ECO:0000269|PubMed:1511982, ECO:0000269|PubMed:1613761,
CC ECO:0000269|PubMed:16566045, ECO:0000269|PubMed:16786509,
CC ECO:0000269|PubMed:18670065, ECO:0000269|PubMed:1874719,
CC ECO:0000269|PubMed:18996919, ECO:0000269|PubMed:1939261,
CC ECO:0000269|PubMed:1953667, ECO:0000269|PubMed:2035536,
CC ECO:0000269|PubMed:2036375, ECO:0000269|PubMed:2037280,
CC ECO:0000269|PubMed:2116413, ECO:0000269|PubMed:2211725,
CC ECO:0000269|PubMed:2339700, ECO:0000269|PubMed:2470760,
CC ECO:0000269|PubMed:25958000, ECO:0000269|PubMed:2777764,
CC ECO:0000269|PubMed:2794057, ECO:0000269|PubMed:2913053,
CC ECO:0000269|PubMed:3016737, ECO:0000269|PubMed:3108247,
CC ECO:0000269|PubMed:3403550, ECO:0000269|PubMed:3667599,
CC ECO:0000269|PubMed:7520724, ECO:0000269|PubMed:7679635,
CC ECO:0000269|PubMed:7691343, ECO:0000269|PubMed:7961597,
CC ECO:0000269|PubMed:8100209, ECO:0000269|PubMed:8349697,
CC ECO:0000269|PubMed:8349698, ECO:0000269|PubMed:8364588,
CC ECO:0000269|PubMed:8456808, ECO:0000269|PubMed:8786074,
CC ECO:0000269|PubMed:9143923, ECO:0000269|Ref.49, ECO:0000269|Ref.52}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- DISEASE: Osteogenesis imperfecta 3 (OI3) [MIM:259420]: An autosomal
CC dominant form of osteogenesis imperfecta, a connective tissue disorder
CC characterized by low bone mass, bone fragility and susceptibility to
CC fractures after minimal trauma. Disease severity ranges from very mild
CC forms without fractures to intrauterine fractures and perinatal
CC lethality. Extraskeletal manifestations, which affect a variable number
CC of patients, are dentinogenesis imperfecta, hearing loss, and blue
CC sclerae. OI3 is characterized by progressively deforming bones, very
CC short stature, a triangular face, severe scoliosis, grayish sclera and
CC dentinogenesis imperfecta. {ECO:0000269|PubMed:10408781,
CC ECO:0000269|PubMed:16879195, ECO:0000269|PubMed:1770532,
CC ECO:0000269|PubMed:18670065, ECO:0000269|PubMed:2037280,
CC ECO:0000269|PubMed:2511192, ECO:0000269|PubMed:2794057,
CC ECO:0000269|PubMed:7691343, ECO:0000269|PubMed:7881420,
CC ECO:0000269|PubMed:8019571, ECO:0000269|PubMed:8364588,
CC ECO:0000269|PubMed:8456809, ECO:0000269|PubMed:8669434,
CC ECO:0000269|PubMed:8723681, ECO:0000269|PubMed:9101304}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Osteogenesis imperfecta 4 (OI4) [MIM:166220]: An autosomal
CC dominant form of osteogenesis imperfecta, a connective tissue disorder
CC characterized by low bone mass, bone fragility and susceptibility to
CC fractures after minimal trauma. Disease severity ranges from very mild
CC forms without fractures to intrauterine fractures and perinatal
CC lethality. Extraskeletal manifestations, which affect a variable number
CC of patients, are dentinogenesis imperfecta, hearing loss, and blue
CC sclerae. OI4 is characterized by moderately short stature, mild to
CC moderate scoliosis, grayish or white sclera and dentinogenesis
CC imperfecta. {ECO:0000269|PubMed:16786509, ECO:0000269|PubMed:16879195,
CC ECO:0000269|PubMed:1770532, ECO:0000269|PubMed:17875077,
CC ECO:0000269|PubMed:1988452, ECO:0000269|PubMed:2745420,
CC ECO:0000269|PubMed:7691343, ECO:0000269|PubMed:7982948,
CC ECO:0000269|PubMed:8094076, ECO:0000269|PubMed:8339541,
CC ECO:0000269|PubMed:9600458}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Combined osteogenesis imperfecta and Ehlers-Danlos syndrome 1
CC (OIEDS1) [MIM:619115]: An autosomal dominant connective tissue disorder
CC characterized by osteopenia, bone fragility, long bone fractures, blue
CC sclerae, joint hyperextensibility, soft and hyperextensible skin,
CC abnormal wound healing, easy bruising, and vascular fragility.
CC {ECO:0000269|PubMed:15728585, ECO:0000269|PubMed:17206620,
CC ECO:0000269|PubMed:23692737}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Osteoporosis (OSTEOP) [MIM:166710]: A systemic skeletal
CC disorder characterized by decreased bone mass and deterioration of bone
CC microarchitecture without alteration in the composition of bone. The
CC result is fragile bones and an increased risk of fractures, even after
CC minimal trauma. Osteoporosis is a chronic condition of multifactorial
CC etiology and is usually clinically silent until a fracture occurs.
CC {ECO:0000269|PubMed:8841196, ECO:0000269|PubMed:9535665}. Note=Disease
CC susceptibility is associated with variants affecting the gene
CC represented in this entry.
CC -!- DISEASE: Note=A chromosomal aberration involving COL1A1 is found in
CC dermatofibrosarcoma protuberans. Translocation t(17;22)(q22;q13) with
CC PDGF.
CC -!- SIMILARITY: Belongs to the fibrillar collagen family.
CC {ECO:0000255|PROSITE-ProRule:PRU00793}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92834.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Osteogenesis imperfecta variant database;
CC Note=Collagen type I alpha 1 (COL1A1);
CC URL="http://oi.gene.le.ac.uk/home.php?select_db=COL1A1";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/COL1A1ID186.html";
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Type-I collagen entry;
CC URL="https://en.wikipedia.org/wiki/Type-I_collagen";
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DR EMBL; Z74615; CAA98968.1; -; mRNA.
DR EMBL; AF017178; AAB94054.3; -; Genomic_DNA.
DR EMBL; AB209597; BAD92834.1; ALT_INIT; mRNA.
DR EMBL; BC036531; AAH36531.1; -; mRNA.
DR EMBL; M20789; AAB59373.1; -; Genomic_DNA.
DR EMBL; M36546; AAA60150.1; -; mRNA.
DR EMBL; X07884; CAA30731.1; -; mRNA.
DR EMBL; X00820; CAA25394.1; -; Genomic_DNA.
DR EMBL; J02829; AAA51993.1; -; Genomic_DNA.
DR EMBL; M10627; AAA51992.1; -; Genomic_DNA.
DR EMBL; J03559; AAA52052.1; -; Genomic_DNA.
DR EMBL; K01228; AAA51995.1; -; mRNA.
DR EMBL; J00110; AAA52289.1; -; mRNA.
DR EMBL; J00111; AAA52290.1; -; mRNA.
DR EMBL; J00112; AAA52291.1; -; mRNA.
DR EMBL; J00113; AAN86574.1; -; mRNA.
DR EMBL; K03179; AAA51847.1; -; Genomic_DNA.
DR EMBL; M11162; AAA75386.1; -; Genomic_DNA.
DR EMBL; L47667; AAB59576.1; -; Genomic_DNA.
DR EMBL; S64596; AAB27856.1; -; mRNA.
DR EMBL; M23213; AAB59363.1; -; Genomic_DNA.
DR EMBL; X06269; CAA29605.1; -; mRNA.
DR EMBL; M32798; AAA52049.1; -; mRNA.
DR EMBL; M55998; AAA52036.1; -; Genomic_DNA.
DR CCDS; CCDS11561.1; -.
DR PIR; I60114; CGHU1S.
DR RefSeq; NP_000079.2; NM_000088.3.
DR PDB; 1Q7D; X-ray; 1.80 A; A/B/C=680-685.
DR PDB; 2LLP; NMR; -; A/B/C=949-965.
DR PDB; 3EJH; X-ray; 2.10 A; E/F=956-977.
DR PDB; 3GXE; X-ray; 2.60 A; E/F=254-275.
DR PDB; 5CTD; X-ray; 1.60 A; A=572-583, C=554-583.
DR PDB; 5CTI; X-ray; 1.90 A; A=572-583, C=565-583, C=893-904.
DR PDB; 5CVA; X-ray; 2.10 A; B/C/E/F=554-583, B/E=593-629.
DR PDB; 5CVB; X-ray; 2.25 A; A/D=572-583, B/C/E/F=554-583, B/E=593-606.
DR PDB; 5K31; X-ray; 2.20 A; A/B/C/D/E/F=1219-1464.
DR PDB; 5OU8; X-ray; 2.50 A; C/D/E=1178-1192.
DR PDB; 5OU9; X-ray; 2.50 A; C/D/E=1172-1192.
DR PDB; 7E7B; EM; 2.60 A; A/B/C=1156-1462.
DR PDB; 7E7D; EM; 3.20 A; A/B/C=1156-1462.
DR PDBsum; 1Q7D; -.
DR PDBsum; 2LLP; -.
DR PDBsum; 3EJH; -.
DR PDBsum; 3GXE; -.
DR PDBsum; 5CTD; -.
DR PDBsum; 5CTI; -.
DR PDBsum; 5CVA; -.
DR PDBsum; 5CVB; -.
DR PDBsum; 5K31; -.
DR PDBsum; 5OU8; -.
DR PDBsum; 5OU9; -.
DR PDBsum; 7E7B; -.
DR PDBsum; 7E7D; -.
DR AlphaFoldDB; P02452; -.
DR SMR; P02452; -.
DR BioGRID; 107674; 116.
DR ComplexPortal; CPX-1650; Collagen type I trimer.
DR ComplexPortal; CPX-4108; Collagen type I homotrimer.
DR CORUM; P02452; -.
DR DIP; DIP-36077N; -.
DR IntAct; P02452; 87.
DR MINT; P02452; -.
DR STRING; 9606.ENSP00000225964; -.
DR ChEMBL; CHEMBL2364188; -.
DR DrugBank; DB11338; Clove oil.
DR DrugBank; DB00048; Collagenase clostridium histolyticum.
DR DrugBank; DB04866; Halofuginone.
DR DrugBank; DB13133; Von Willebrand factor human.
DR DrugBank; DB12872; Vonicog alfa.
DR GlyConnect; 1125; 7 N-Linked glycans (1 site).
DR GlyGen; P02452; 6 sites, 7 N-linked glycans (1 site), 1 O-linked glycan (3 sites).
DR iPTMnet; P02452; -.
DR MetOSite; P02452; -.
DR PhosphoSitePlus; P02452; -.
DR BioMuta; COL1A1; -.
DR DMDM; 296439504; -.
DR DOSAC-COBS-2DPAGE; P02452; -.
DR EPD; P02452; -.
DR jPOST; P02452; -.
DR MassIVE; P02452; -.
DR MaxQB; P02452; -.
DR PaxDb; P02452; -.
DR PeptideAtlas; P02452; -.
DR PRIDE; P02452; -.
DR ProteomicsDB; 51518; -.
DR ABCD; P02452; 3 sequenced antibodies.
DR Antibodypedia; 1980; 911 antibodies from 41 providers.
DR DNASU; 1277; -.
DR Ensembl; ENST00000225964.10; ENSP00000225964.6; ENSG00000108821.14.
DR GeneID; 1277; -.
DR KEGG; hsa:1277; -.
DR MANE-Select; ENST00000225964.10; ENSP00000225964.6; NM_000088.4; NP_000079.2.
DR UCSC; uc002iqm.4; human.
DR CTD; 1277; -.
DR DisGeNET; 1277; -.
DR GeneCards; COL1A1; -.
DR GeneReviews; COL1A1; -.
DR HGNC; HGNC:2197; COL1A1.
DR HPA; ENSG00000108821; Tissue enhanced (cervix, gallbladder).
DR MalaCards; COL1A1; -.
DR MIM; 114000; phenotype.
DR MIM; 120150; gene.
DR MIM; 130000; phenotype.
DR MIM; 130060; phenotype.
DR MIM; 166200; phenotype.
DR MIM; 166210; phenotype.
DR MIM; 166220; phenotype.
DR MIM; 166710; phenotype.
DR MIM; 259420; phenotype.
DR MIM; 607907; phenotype.
DR MIM; 619115; phenotype.
DR neXtProt; NX_P02452; -.
DR OpenTargets; ENSG00000108821; -.
DR Orphanet; 1899; Arthrochalasia Ehlers-Danlos syndrome.
DR Orphanet; 1310; Caffey disease.
DR Orphanet; 287; Classical Ehlers-Danlos syndrome.
DR Orphanet; 31112; Dermatofibrosarcoma protuberans.
DR Orphanet; 230857; Ehlers-Danlos/osteogenesis imperfecta syndrome.
DR Orphanet; 314029; High bone mass osteogenesis imperfecta.
DR Orphanet; 216796; Osteogenesis imperfecta type 1.
DR Orphanet; 216804; Osteogenesis imperfecta type 2.
DR Orphanet; 216812; Osteogenesis imperfecta type 3.
DR Orphanet; 216820; Osteogenesis imperfecta type 4.
DR PharmGKB; PA35041; -.
DR VEuPathDB; HostDB:ENSG00000108821; -.
DR eggNOG; KOG3544; Eukaryota.
DR GeneTree; ENSGT00940000156584; -.
DR HOGENOM; CLU_001074_2_3_1; -.
DR InParanoid; P02452; -.
DR OrthoDB; 337699at2759; -.
DR PhylomeDB; P02452; -.
DR TreeFam; TF344135; -.
DR PathwayCommons; P02452; -.
DR Reactome; R-HSA-114604; GPVI-mediated activation cascade.
DR Reactome; R-HSA-1442490; Collagen degradation.
DR Reactome; R-HSA-1474244; Extracellular matrix organization.
DR Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
DR Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures.
DR Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
DR Reactome; R-HSA-216083; Integrin cell surface interactions.
DR Reactome; R-HSA-2214320; Anchoring fibril formation.
DR Reactome; R-HSA-2243919; Crosslinking of collagen fibrils.
DR Reactome; R-HSA-3000170; Syndecan interactions.
DR Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions.
DR Reactome; R-HSA-3000178; ECM proteoglycans.
DR Reactome; R-HSA-3000480; Scavenging by Class A Receptors.
DR Reactome; R-HSA-430116; GP1b-IX-V activation signalling.
DR Reactome; R-HSA-75892; Platelet Adhesion to exposed collagen.
DR Reactome; R-HSA-76009; Platelet Aggregation (Plug Formation).
DR Reactome; R-HSA-8874081; MET activates PTK2 signaling.
DR Reactome; R-HSA-8940973; RUNX2 regulates osteoblast differentiation.
DR Reactome; R-HSA-8948216; Collagen chain trimerization.
DR SignaLink; P02452; -.
DR SIGNOR; P02452; -.
DR BioGRID-ORCS; 1277; 12 hits in 1073 CRISPR screens.
DR ChiTaRS; COL1A1; human.
DR EvolutionaryTrace; P02452; -.
DR GeneWiki; Collagen,_type_I,_alpha_1; -.
DR GenomeRNAi; 1277; -.
DR Pharos; P02452; Tbio.
DR PRO; PR:P02452; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P02452; protein.
DR Bgee; ENSG00000108821; Expressed in stromal cell of endometrium and 218 other tissues.
DR ExpressionAtlas; P02452; baseline and differential.
DR Genevisible; P02452; HS.
DR GO; GO:0005584; C:collagen type I trimer; IDA:CAFA.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IMP:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0030141; C:secretory granule; IEA:Ensembl.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; HDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048407; F:platelet-derived growth factor binding; IDA:MGI.
DR GO; GO:0002020; F:protease binding; IPI:CAFA.
DR GO; GO:0001568; P:blood vessel development; IMP:UniProtKB.
DR GO; GO:0060346; P:bone trabecula formation; IEA:Ensembl.
DR GO; GO:0060351; P:cartilage development involved in endochondral bone morphogenesis; IEA:Ensembl.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEA:Ensembl.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEA:Ensembl.
DR GO; GO:1902618; P:cellular response to fluoride; IEA:Ensembl.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0071306; P:cellular response to vitamin E; IEA:Ensembl.
DR GO; GO:0032964; P:collagen biosynthetic process; IMP:UniProtKB.
DR GO; GO:0030199; P:collagen fibril organization; IMP:UniProtKB.
DR GO; GO:0038063; P:collagen-activated tyrosine kinase receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0048706; P:embryonic skeletal system development; IMP:UniProtKB.
DR GO; GO:0001958; P:endochondral ossification; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0060325; P:face morphogenesis; IEA:Ensembl.
DR GO; GO:0001957; P:intramembranous ossification; IEA:Ensembl.
DR GO; GO:0010812; P:negative regulation of cell-substrate adhesion; IEA:Ensembl.
DR GO; GO:0001503; P:ossification; IBA:GO_Central.
DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IDA:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0034504; P:protein localization to nucleus; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:Ensembl.
DR GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
DR GO; GO:0031960; P:response to corticosteroid; IEA:Ensembl.
DR GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
DR GO; GO:0055093; P:response to hyperoxia; IEA:Ensembl.
DR GO; GO:0009612; P:response to mechanical stimulus; IBA:GO_Central.
DR GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0007605; P:sensory perception of sound; IMP:UniProtKB.
DR GO; GO:0001501; P:skeletal system development; IMP:UniProtKB.
DR GO; GO:0043588; P:skin development; IBA:GO_Central.
DR GO; GO:0043589; P:skin morphogenesis; IMP:UniProtKB.
DR GO; GO:0044691; P:tooth eruption; IEA:Ensembl.
DR GO; GO:0034505; P:tooth mineralization; IMP:UniProtKB.
DR GO; GO:0007601; P:visual perception; IMP:UniProtKB.
DR GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR000885; Fib_collagen_C.
DR InterPro; IPR001007; VWF_dom.
DR Pfam; PF01410; COLFI; 1.
DR Pfam; PF01391; Collagen; 12.
DR Pfam; PF00093; VWC; 1.
DR SMART; SM00038; COLFI; 1.
DR SMART; SM00214; VWC; 1.
DR PROSITE; PS51461; NC1_FIB; 1.
DR PROSITE; PS01208; VWFC_1; 1.
DR PROSITE; PS50184; VWFC_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Chromosomal rearrangement; Collagen;
KW Direct protein sequencing; Disease variant; Disulfide bond; Dwarfism;
KW Ehlers-Danlos syndrome; Extracellular matrix; Glycoprotein; Hydroxylation;
KW Metal-binding; Osteogenesis imperfecta; Phosphoprotein;
KW Pyrrolidone carboxylic acid; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..22
FT PROPEP 23..161
FT /note="N-terminal propeptide"
FT /evidence="ECO:0000269|PubMed:5529814"
FT /id="PRO_0000005719"
FT CHAIN 162..1218
FT /note="Collagen alpha-1(I) chain"
FT /id="PRO_0000005720"
FT PROPEP 1219..1464
FT /note="C-terminal propeptide"
FT /id="PRO_0000005721"
FT DOMAIN 38..96
FT /note="VWFC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00220"
FT DOMAIN 1229..1464
FT /note="Fibrillar collagen NC1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT REGION 98..1214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 162..178
FT /note="Nonhelical region (N-terminal)"
FT REGION 179..1192
FT /note="Triple-helical region"
FT REGION 1193..1218
FT /note="Nonhelical region (C-terminal)"
FT MOTIF 745..747
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT MOTIF 1093..1095
FT /note="Cell attachment site"
FT /evidence="ECO:0000255"
FT COMPBIAS 122..156
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..226
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..433
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..572
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..902
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1176..1195
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1277
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1279
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1280
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1282
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 1285
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT SITE 161..162
FT /note="Cleavage; by procollagen N-endopeptidase"
FT SITE 953..954
FT /note="Cleavage; by collagenase"
FT /evidence="ECO:0000250"
FT SITE 1218..1219
FT /note="Cleavage; by procollagen C-endopeptidase"
FT MOD_RES 162
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:5529814"
FT MOD_RES 170
FT /note="Allysine"
FT /evidence="ECO:0000269|PubMed:5529814"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02454"
FT MOD_RES 190
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 193
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 196
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 205
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 208
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 211
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 226
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 241
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 247
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 256
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 262
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 265
FT /note="5-hydroxylysine; alternate"
FT /evidence="ECO:0000269|PubMed:4319110"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02454"
FT MOD_RES 289
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 292
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 298
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 307
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 313
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 334
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 343
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 346
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 373
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 376
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 388
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 394
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 403
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 409
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 412
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 427
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 430
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 436
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 439
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 451
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 460
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 475
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 481
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 490
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 496
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 505
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 514
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 523
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 529
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 535
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 544
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 547
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 556
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 565
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 571
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 583
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 592
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 601
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 604
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 622
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 640
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 646
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 652
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 658
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 664
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 670
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 682
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 691
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 703
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 715
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 718
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 724
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 730
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 739
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 751
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 757
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 772
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 778
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 787
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P02454"
FT MOD_RES 799
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 805
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 808
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 817
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 823
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 841
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 850
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 859
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 862
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 871
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 877
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 885
FT /note="3-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P11087"
FT MOD_RES 886
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P11087"
FT MOD_RES 895
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P11087"
FT MOD_RES 898
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P11087"
FT MOD_RES 919
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 928
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 937
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 946
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 964
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 973
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 976
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 982
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 997
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 1003
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 1009
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 1018
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 1024
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 1033
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 1045
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 1048
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 1051
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 1096
FT /note="5-hydroxylysine"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 1108
FT /note="5-hydroxylysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 1120
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 1123
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 1126
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 1144
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT MOD_RES 1159
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P11087"
FT MOD_RES 1164
FT /note="3-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P11087"
FT MOD_RES 1165
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P11087"
FT MOD_RES 1179
FT /note="3-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P11087"
FT MOD_RES 1180
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P11087"
FT MOD_RES 1182
FT /note="3-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P11087"
FT MOD_RES 1183
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P11087"
FT MOD_RES 1185
FT /note="3-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P11087"
FT MOD_RES 1186
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P11087"
FT MOD_RES 1189
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P11087"
FT MOD_RES 1192
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250|UniProtKB:P11087"
FT MOD_RES 1208
FT /note="Allysine"
FT /evidence="ECO:0000250|UniProtKB:P02453"
FT CARBOHYD 265
FT /note="O-linked (Gal...) hydroxylysine; alternate"
FT /evidence="ECO:0000269|PubMed:4319110"
FT CARBOHYD 1108
FT /note="O-linked (Gal...) hydroxylysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P02457"
FT CARBOHYD 1365
FT /note="N-linked (GlcNAc...) asparagine"
FT DISULFID 1259..1291
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1265
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1282
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1299..1462
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT DISULFID 1370..1415
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00793"
FT VARIANT 22
FT /note="G -> R (in OI2; dbSNP:rs72667007)"
FT /evidence="ECO:0000269|PubMed:16786509"
FT /id="VAR_063290"
FT VARIANT 146
FT /note="P -> T (in OI2; rare variant; unknown pathological
FT significance; dbSNP:rs756846639)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_063291"
FT VARIANT 188
FT /note="G -> D (in OIEDS1; decreased N-terminal propeptide
FT processing; dbSNP:rs1114167408)"
FT /evidence="ECO:0000269|PubMed:23692737"
FT /id="VAR_085148"
FT VARIANT 191
FT /note="G -> D (in OIEDS1; severely decreased cleavage of N-
FT terminal propeptide; affects collagen fibril organization;
FT collagen dermal fibrils in patients have smaller diameters
FT than in age-matched controls; dbSNP:rs67828806)"
FT /evidence="ECO:0000269|PubMed:15728585"
FT /id="VAR_085149"
FT VARIANT 194
FT /note="G -> R (in OI1; dbSNP:rs72667024)"
FT /evidence="ECO:0000269|PubMed:16705691"
FT /id="VAR_063292"
FT VARIANT 197
FT /note="G -> C (in dbSNP:rs8179178)"
FT /id="VAR_001642"
FT VARIANT 197
FT /note="G -> R (in OI4)"
FT /evidence="ECO:0000269|PubMed:16786509"
FT /id="VAR_063293"
FT VARIANT 200
FT /note="G -> V (in OI1; patient diagnosed with OI1/OI4;
FT dbSNP:rs72667029)"
FT /evidence="ECO:0000269|PubMed:18670065"
FT /id="VAR_063294"
FT VARIANT 203
FT /note="G -> C (in OIEDS1)"
FT /evidence="ECO:0000269|PubMed:23692737"
FT /id="VAR_085150"
FT VARIANT 203
FT /note="G -> V (in OI3 and OIEDS1; small decrease of N-
FT terminal propeptide; affects collagen fibril organization;
FT collagen dermal fibrils in patients have smaller diameters
FT than in age-matched controls; dbSNP:rs72667031)"
FT /evidence="ECO:0000269|PubMed:15728585,
FT ECO:0000269|PubMed:16879195"
FT /id="VAR_063295"
FT VARIANT 205
FT /note="P -> A (in dbSNP:rs72667032)"
FT /evidence="ECO:0000269|PubMed:16786509"
FT /id="VAR_001643"
FT VARIANT 212
FT /note="G -> R (in OIEDS1; small decrease of N-terminal
FT propeptide; affects collagen fibril organization; collagen
FT dermal fibrils in patients have smaller diameters than in
FT age-matched controls; dbSNP:rs72667034)"
FT /evidence="ECO:0000269|PubMed:15728585"
FT /id="VAR_085151"
FT VARIANT 221
FT /note="G -> C (in OI1; mild form; dbSNP:rs72667037)"
FT /evidence="ECO:0000269|PubMed:1737847"
FT /id="VAR_001644"
FT VARIANT 224
FT /note="G -> C (in OI1; mild phenotype; dbSNP:rs72667038)"
FT /id="VAR_001645"
FT VARIANT 242
FT /note="G -> D (in OI; dbSNP:rs72645315)"
FT /evidence="ECO:0000269|PubMed:16705691"
FT /id="VAR_063296"
FT VARIANT 254
FT /note="G -> E (in OIEDS1; affects collagen fibril
FT organization; collagen dermal fibrils in patients have
FT smaller diameters than in age-matched controls;
FT dbSNP:rs72645320)"
FT /evidence="ECO:0000269|PubMed:15728585"
FT /id="VAR_085152"
FT VARIANT 257
FT /note="G -> R (in OI4; dbSNP:rs72645321)"
FT /evidence="ECO:0000269|PubMed:16705691,
FT ECO:0000269|PubMed:16879195"
FT /id="VAR_063297"
FT VARIANT 263
FT /note="G -> R (in OI1; mild form; dbSNP:rs72645323)"
FT /evidence="ECO:0000269|PubMed:1718984"
FT /id="VAR_001646"
FT VARIANT 263
FT /note="G -> V (in OI1; mild form; dbSNP:rs72645324)"
FT /evidence="ECO:0000269|PubMed:8223589"
FT /id="VAR_001647"
FT VARIANT 266
FT /note="G -> E (in OI1 and OIEDS1; affects collagen fibril
FT organization; collagen dermal fibrils in patients have
FT smaller diameters than in age-matched controls;
FT dbSNP:rs72645325)"
FT /evidence="ECO:0000269|PubMed:15728585,
FT ECO:0000269|PubMed:17875077"
FT /id="VAR_063298"
FT VARIANT 272
FT /note="G -> C (in OI1; dbSNP:rs72645331)"
FT /evidence="ECO:0000269|PubMed:2794057"
FT /id="VAR_001648"
FT VARIANT 275
FT /note="G -> D (in OI2; dbSNP:rs72645333)"
FT /id="VAR_001649"
FT VARIANT 287
FT /note="G -> S (in OI1; dbSNP:rs72645340)"
FT /evidence="ECO:0000269|PubMed:17875077"
FT /id="VAR_063299"
FT VARIANT 288
FT /note="E -> K (in OI1; the patient also has mutation Glu-
FT 1219; unknown pathological significance; dbSNP:rs72645341)"
FT /evidence="ECO:0000269|PubMed:16786509"
FT /id="VAR_063300"
FT VARIANT 288
FT /note="E -> V (in OI2; rare variant; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_063301"
FT VARIANT 312
FT /note="R -> C (in EDSCL1; dbSNP:rs72645347)"
FT /evidence="ECO:0000269|PubMed:10739762,
FT ECO:0000269|PubMed:17211858"
FT /id="VAR_013579"
FT VARIANT 320
FT /note="G -> V (in OI1; dbSNP:rs72645353)"
FT /evidence="ECO:0000269|PubMed:16786509"
FT /id="VAR_063302"
FT VARIANT 332
FT /note="G -> R (in OI3; mild to moderate form;
FT dbSNP:rs72645357)"
FT /evidence="ECO:0000269|PubMed:2037280,
FT ECO:0000269|PubMed:8669434"
FT /id="VAR_001650"
FT VARIANT 338
FT /note="G -> C (in OI4; dbSNP:rs66664580)"
FT /evidence="ECO:0000269|PubMed:16786509"
FT /id="VAR_063303"
FT VARIANT 349
FT /note="V -> F (in OI1; dbSNP:rs72645362)"
FT /evidence="ECO:0000269|PubMed:18670065"
FT /id="VAR_063304"
FT VARIANT 350
FT /note="G -> R (in OI3; dbSNP:rs72645363)"
FT /evidence="ECO:0000269|PubMed:8019571"
FT /id="VAR_001651"
FT VARIANT 353
FT /note="G -> C (in OI4; dbSNP:rs66721653)"
FT /evidence="ECO:0000269|PubMed:8339541"
FT /id="VAR_001652"
FT VARIANT 353
FT /note="G -> D (in OI2)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_063305"
FT VARIANT 353
FT /note="G -> S (in OI4; dbSNP:rs66721653)"
FT /evidence="ECO:0000269|PubMed:17875077"
FT /id="VAR_063306"
FT VARIANT 356
FT /note="G -> C (in OI4; mild form; dbSNP:rs72645365)"
FT /evidence="ECO:0000269|PubMed:1988452"
FT /id="VAR_001653"
FT VARIANT 368
FT /note="G -> V (in OI2)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_063307"
FT VARIANT 383
FT /note="G -> C (in OI4; dbSNP:rs67182491)"
FT /id="VAR_001654"
FT VARIANT 389
FT /note="G -> C (in OI; moderate form; dbSNP:rs66548636)"
FT /id="VAR_001655"
FT VARIANT 389
FT /note="G -> R (in OI2; dbSNP:rs66548636)"
FT /evidence="ECO:0000269|PubMed:7520724"
FT /id="VAR_001656"
FT VARIANT 390
FT /note="A -> T (in OI2; rare variant; unknown pathological
FT significance; dbSNP:rs116794104)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_063308"
FT VARIANT 398
FT /note="G -> A (in OI4; dbSNP:rs66501246)"
FT /evidence="ECO:0000269|PubMed:9600458"
FT /id="VAR_001657"
FT VARIANT 398
FT /note="G -> D (in OI2; dbSNP:rs66501246)"
FT /id="VAR_001658"
FT VARIANT 401
FT /note="G -> C (in OI4; dbSNP:rs72648322)"
FT /id="VAR_001659"
FT VARIANT 404
FT /note="G -> C (in OI; moderate form; dbSNP:rs66893386)"
FT /id="VAR_001660"
FT VARIANT 422
FT /note="G -> C (in OI2; dbSNP:rs72648328)"
FT /evidence="ECO:0000269|Ref.49"
FT /id="VAR_001661"
FT VARIANT 425
FT /note="G -> S (in OI2; lethal form; dbSNP:rs72648330)"
FT /evidence="ECO:0000269|PubMed:18996919,
FT ECO:0000269|PubMed:7691343"
FT /id="VAR_001662"
FT VARIANT 434
FT /note="G -> V (in OI2; dbSNP:rs72648333)"
FT /evidence="ECO:0000269|PubMed:1613761,
FT ECO:0000269|PubMed:2470760"
FT /id="VAR_001663"
FT VARIANT 455
FT /note="G -> D (in OI2)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_063309"
FT VARIANT 470
FT /note="G -> V (in OI2)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_063310"
FT VARIANT 476
FT /note="G -> R (in OI2; dbSNP:rs57377812)"
FT /id="VAR_001664"
FT VARIANT 509
FT /note="G -> V (in OI2)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_063311"
FT VARIANT 527
FT /note="G -> C (in OI4; dbSNP:rs72648353)"
FT /evidence="ECO:0000269|PubMed:9600458"
FT /id="VAR_001665"
FT VARIANT 530
FT /note="G -> S (in OI2, OI3 and OI4; mild to lethal form;
FT dbSNP:rs67682641)"
FT /evidence="ECO:0000269|PubMed:7691343,
FT ECO:0000269|PubMed:8094076, ECO:0000269|PubMed:8456809"
FT /id="VAR_001666"
FT VARIANT 533
FT /note="G -> D (in OI2; dbSNP:rs72648356)"
FT /id="VAR_001667"
FT VARIANT 548
FT /note="G -> A (in OI2)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_063312"
FT VARIANT 555
FT /note="P -> R (in OI1; dbSNP:rs72648359)"
FT /evidence="ECO:0000269|PubMed:16786509"
FT /id="VAR_063313"
FT VARIANT 560
FT /note="G -> C (in OI4; dbSNP:rs67507747)"
FT /id="VAR_001669"
FT VARIANT 560
FT /note="G -> R (in OI2; dbSNP:rs67507747)"
FT /id="VAR_001670"
FT VARIANT 560
FT /note="G -> S (in OI4; dbSNP:rs67507747)"
FT /evidence="ECO:0000269|PubMed:7691343"
FT /id="VAR_001668"
FT VARIANT 564
FT /note="R -> H (in dbSNP:rs1800211)"
FT /id="VAR_001671"
FT VARIANT 569
FT /note="G -> R (in OI2; dbSNP:rs72648363)"
FT /evidence="ECO:0000269|PubMed:3108247"
FT /id="VAR_001672"
FT VARIANT 574
FT /note="R -> C (found in a patient with isolated osteopenia
FT and vascular rupture; unknown pathological significance;
FT dbSNP:rs72648365)"
FT /evidence="ECO:0000269|PubMed:17211858"
FT /id="VAR_063314"
FT VARIANT 581
FT /note="G -> R (in OI2; dbSNP:rs72648366)"
FT /evidence="ECO:0000269|PubMed:16786509"
FT /id="VAR_063315"
FT VARIANT 593
FT /note="G -> C (in OI3 and OI4; dbSNP:rs66527965)"
FT /evidence="ECO:0000269|PubMed:1770532"
FT /id="VAR_001673"
FT VARIANT 593
FT /note="G -> S (in OI2 and OI3; moderate to lethal form;
FT dbSNP:rs66527965)"
FT /evidence="ECO:0000269|PubMed:8364588"
FT /id="VAR_001674"
FT VARIANT 602
FT /note="G -> R (in OI2; dbSNP:rs72651615)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_063316"
FT VARIANT 605
FT /note="G -> D (in OI2)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_063317"
FT VARIANT 614
FT /note="G -> R (in OI2)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_063318"
FT VARIANT 647
FT /note="G -> S (in OI1; dbSNP:rs72651627)"
FT /evidence="ECO:0000269|PubMed:16786509"
FT /id="VAR_063319"
FT VARIANT 656
FT /note="G -> S (in OI2; dbSNP:rs72651629)"
FT /evidence="ECO:0000269|PubMed:10627137"
FT /id="VAR_001676"
FT VARIANT 683
FT /note="G -> S (in OI4; dbSNP:rs72651636)"
FT /evidence="ECO:0000269|PubMed:16879195"
FT /id="VAR_063320"
FT VARIANT 701
FT /note="G -> C (in OI4; dbSNP:rs68114505)"
FT /evidence="ECO:0000269|PubMed:9600458"
FT /id="VAR_001677"
FT VARIANT 704
FT /note="G -> C (in OI3; dbSNP:rs67368147)"
FT /evidence="ECO:0000269|PubMed:2794057"
FT /id="VAR_001678"
FT VARIANT 719
FT /note="G -> D (in OI2; dbSNP:rs72651646)"
FT /evidence="ECO:0000269|PubMed:2035536"
FT /id="VAR_001679"
FT VARIANT 719
FT /note="G -> S (in OI3; dbSNP:rs72651645)"
FT /evidence="ECO:0000269|PubMed:7691343"
FT /id="VAR_001680"
FT VARIANT 722
FT /note="G -> S (in OI1; dbSNP:rs72651647)"
FT /evidence="ECO:0000269|PubMed:16705691"
FT /id="VAR_063321"
FT VARIANT 728
FT /note="G -> R (in OI2; dbSNP:rs72651648)"
FT /evidence="ECO:0000269|PubMed:2339700"
FT /id="VAR_001681"
FT VARIANT 734
FT /note="G -> V (in OI2; dbSNP:rs72651649)"
FT /evidence="ECO:0000269|PubMed:16786509"
FT /id="VAR_063322"
FT VARIANT 737
FT /note="G -> D (in OI2; dbSNP:rs72651651)"
FT /id="VAR_001682"
FT VARIANT 740
FT /note="G -> R (in OI2)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_063323"
FT VARIANT 743
FT /note="G -> S (in OI2; dbSNP:rs72651652)"
FT /id="VAR_001683"
FT VARIANT 743
FT /note="G -> V (in OI2; dbSNP:rs72651653)"
FT /evidence="ECO:0000269|PubMed:8100209"
FT /id="VAR_001684"
FT VARIANT 764
FT /note="G -> V (in OI2; dbSNP:rs72651657)"
FT /evidence="ECO:0000269|PubMed:9143923"
FT /id="VAR_001685"
FT VARIANT 767
FT /note="G -> S (in OI3; severe; dbSNP:rs72651658)"
FT /evidence="ECO:0000269|PubMed:16705691,
FT ECO:0000269|PubMed:7881420"
FT /id="VAR_001686"
FT VARIANT 773
FT /note="G -> C (in OI2; de novo mutation)"
FT /evidence="ECO:0000269|PubMed:25958000"
FT /id="VAR_074158"
FT VARIANT 776
FT /note="G -> S (in OI2; dbSNP:rs72651660)"
FT /evidence="ECO:0000269|PubMed:2116413"
FT /id="VAR_001687"
FT VARIANT 809
FT /note="G -> S (in OI2; dbSNP:rs72651663)"
FT /evidence="ECO:0000269|PubMed:18996919,
FT ECO:0000269|PubMed:2116413"
FT /id="VAR_001688"
FT VARIANT 815
FT /note="G -> V (in OI2; dbSNP:rs66929517)"
FT /evidence="ECO:0000269|PubMed:1874719"
FT /id="VAR_001689"
FT VARIANT 821
FT /note="G -> S (in OI3; dbSNP:rs67693970)"
FT /evidence="ECO:0000269|PubMed:16705691,
FT ECO:0000269|PubMed:16879195, ECO:0000269|PubMed:9101304"
FT /id="VAR_001690"
FT VARIANT 823
FT /note="P -> A (in dbSNP:rs1800214)"
FT /evidence="ECO:0000269|PubMed:7691343"
FT /id="VAR_001691"
FT VARIANT 824
FT /note="G -> R (in OI2)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_063324"
FT VARIANT 833
FT /note="G -> D (in OI2; dbSNP:rs67067133)"
FT /evidence="ECO:0000269|PubMed:16566045"
FT /id="VAR_063325"
FT VARIANT 839
FT /note="G -> S (in OI2; mild to moderate form;
FT dbSNP:rs72653131)"
FT /evidence="ECO:0000269|PubMed:8786074"
FT /id="VAR_001692"
FT VARIANT 842
FT /note="G -> R (in OI2; dbSNP:rs72653134)"
FT /evidence="ECO:0000269|PubMed:3403550"
FT /id="VAR_001693"
FT VARIANT 845
FT /note="G -> R (in OI2; dbSNP:rs72653136)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_001694"
FT VARIANT 848
FT /note="G -> R (in OI2)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_063342"
FT VARIANT 851
FT /note="G -> D (in OI2; dbSNP:rs72653137)"
FT /id="VAR_001695"
FT VARIANT 855
FT /note="N -> H (in OI2; rare variant; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_063326"
FT VARIANT 866
FT /note="G -> S (in OI3 and OI2; dbSNP:rs67445413)"
FT /evidence="ECO:0000269|PubMed:10408781,
FT ECO:0000269|PubMed:18670065, ECO:0000269|PubMed:18996919"
FT /id="VAR_008118"
FT VARIANT 869
FT /note="G -> C (in OI2; dbSNP:rs72653143)"
FT /evidence="ECO:0000269|PubMed:1953667"
FT /id="VAR_001696"
FT VARIANT 875
FT /note="G -> S (in OI2; dbSNP:rs72653145)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_063327"
FT VARIANT 884
FT /note="G -> S (in OI2 and OI3; extremely severe form;
FT dbSNP:rs1567755602)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_001697"
FT VARIANT 896
FT /note="G -> C (in OI2; dbSNP:rs72653152)"
FT /evidence="ECO:0000269|PubMed:2794057"
FT /id="VAR_001698"
FT VARIANT 896
FT /note="G -> D (in OI2)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_063328"
FT VARIANT 906
FT /note="G -> S (found in a patient with mild osteogenesis
FT imperfecta; uncertain pathological significance;
FT dbSNP:rs145446512)"
FT /evidence="ECO:0000269|PubMed:16786509"
FT /id="VAR_063329"
FT VARIANT 926
FT /note="G -> C (in OI2; dbSNP:rs72653154)"
FT /evidence="ECO:0000269|PubMed:2036375,
FT ECO:0000269|PubMed:3667599"
FT /id="VAR_001699"
FT VARIANT 947
FT /note="G -> C (in OI2; dbSNP:rs72653159)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_063330"
FT VARIANT 977
FT /note="G -> D (in OI2)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_063331"
FT VARIANT 980
FT /note="G -> V (in OI2; dbSNP:rs72653166)"
FT /evidence="ECO:0000269|PubMed:1511982"
FT /id="VAR_001700"
FT VARIANT 1001
FT /note="G -> C (in OI2; dbSNP:rs72653167)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_063332"
FT VARIANT 1010
FT /note="G -> S (in OI4; dbSNP:rs72653169)"
FT /evidence="ECO:0000269|PubMed:2745420"
FT /id="VAR_001701"
FT VARIANT 1014
FT /note="R -> C (in CAFYD; dbSNP:rs72653170)"
FT /evidence="ECO:0000269|PubMed:15864348"
FT /id="VAR_033097"
FT VARIANT 1019
FT /note="G -> A (in dbSNP:rs1135348)"
FT /evidence="ECO:0000269|PubMed:6689127, ECO:0000269|Ref.1"
FT /id="VAR_030013"
FT VARIANT 1022
FT /note="G -> S (in OI3; severe form; dbSNP:rs66523073)"
FT /evidence="ECO:0000269|PubMed:2511192"
FT /id="VAR_001702"
FT VARIANT 1022
FT /note="G -> V (in OI2; dbSNP:rs67771061)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_001703"
FT VARIANT 1025
FT /note="G -> R (in OI2; dbSNP:rs72653172)"
FT /evidence="ECO:0000269|PubMed:2211725"
FT /id="VAR_001704"
FT VARIANT 1040
FT /note="G -> S (in OI2 and OI3; moderate to lethal form;
FT dbSNP:rs72653178)"
FT /evidence="ECO:0000269|PubMed:18670065,
FT ECO:0000269|PubMed:9101304"
FT /id="VAR_001705"
FT VARIANT 1043
FT /note="G -> S (in OI2)"
FT /id="VAR_001706"
FT VARIANT 1046..1048
FT /note="Missing (in OI2)"
FT /evidence="ECO:0000269|PubMed:1460047,
FT ECO:0000269|PubMed:1939261"
FT /id="VAR_001707"
FT VARIANT 1049
FT /note="G -> S (in OI3; dbSNP:rs67641695)"
FT /evidence="ECO:0000269|PubMed:9101304"
FT /id="VAR_001708"
FT VARIANT 1052
FT /note="G -> GAPG (in OI2)"
FT /id="VAR_063333"
FT VARIANT 1055
FT /note="G -> D (in OI2)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_063334"
FT VARIANT 1058
FT /note="G -> S (in OI3 and OI4; mild form;
FT dbSNP:rs72654795)"
FT /evidence="ECO:0000269|PubMed:16705691,
FT ECO:0000269|PubMed:9101304"
FT /id="VAR_001709"
FT VARIANT 1061
FT /note="G -> D (in OI2; dbSNP:rs72654797)"
FT /id="VAR_001710"
FT VARIANT 1061
FT /note="G -> S (in OI4; dbSNP:rs72654796)"
FT /evidence="ECO:0000269|PubMed:7982948"
FT /id="VAR_001711"
FT VARIANT 1066
FT /note="R -> C (in OIEDS1; affects dimer formation, helix
FT stability and organization of collagen fibrils;
FT dbSNP:rs72654799)"
FT /evidence="ECO:0000269|PubMed:17206620"
FT /id="VAR_063335"
FT VARIANT 1075
FT /note="A -> T (in dbSNP:rs1800215)"
FT /evidence="ECO:0000269|PubMed:1870989"
FT /id="VAR_001712"
FT VARIANT 1076
FT /note="G -> S (in OI3; severe form; dbSNP:rs67394386)"
FT /evidence="ECO:0000269|PubMed:9101304"
FT /id="VAR_001713"
FT VARIANT 1079
FT /note="G -> S (in OI1 and OI2; mild to moderate form;
FT dbSNP:rs72654802)"
FT /evidence="ECO:0000269|PubMed:1634225"
FT /id="VAR_001714"
FT VARIANT 1082
FT /note="G -> C (in OI2; dbSNP:rs72656303)"
FT /evidence="ECO:0000269|PubMed:2913053"
FT /id="VAR_001715"
FT VARIANT 1088
FT /note="G -> A (in OI2; dbSNP:rs72656305)"
FT /evidence="ECO:0000269|PubMed:7679635"
FT /id="VAR_001716"
FT VARIANT 1088
FT /note="G -> E (in OI1; de novo mutation; unknown
FT pathological significance)"
FT /evidence="ECO:0000269|PubMed:24682174"
FT /id="VAR_074159"
FT VARIANT 1091
FT /note="G -> S (in OI2; dbSNP:rs72656306)"
FT /evidence="ECO:0000269|Ref.52"
FT /id="VAR_001717"
FT VARIANT 1093
FT /note="R -> C (found in a patient with isolated osteopenia
FT and vascular rupture; unknown pathological significance;
FT dbSNP:rs72656307)"
FT /evidence="ECO:0000269|PubMed:17211858"
FT /id="VAR_063336"
FT VARIANT 1094
FT /note="G -> S (in OI2)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_063337"
FT VARIANT 1100
FT /note="G -> D (in OI2; dbSNP:rs72656308)"
FT /evidence="ECO:0000269|PubMed:18996919"
FT /id="VAR_001718"
FT VARIANT 1106
FT /note="G -> A (in OI2; dbSNP:rs72656311)"
FT /evidence="ECO:0000269|PubMed:2777764"
FT /id="VAR_001719"
FT VARIANT 1124
FT /note="G -> C (in OI2; dbSNP:rs72656312)"
FT /evidence="ECO:0000269|PubMed:7961597"
FT /id="VAR_001720"
FT VARIANT 1141
FT /note="R -> Q (in dbSNP:rs41316713)"
FT /evidence="ECO:0000269|PubMed:18272325"
FT /id="VAR_033778"
FT VARIANT 1142
FT /note="G -> S (in OI2; dbSNP:rs72656317)"
FT /id="VAR_001721"
FT VARIANT 1151
FT /note="G -> S (in OI3; dbSNP:rs72656320)"
FT /id="VAR_001722"
FT VARIANT 1151
FT /note="G -> V (in OI2; dbSNP:rs72656321)"
FT /evidence="ECO:0000269|PubMed:1613761,
FT ECO:0000269|PubMed:2777764"
FT /id="VAR_001723"
FT VARIANT 1154
FT /note="G -> R (in OI2; dbSNP:rs72656322)"
FT /evidence="ECO:0000269|PubMed:2777764"
FT /id="VAR_001724"
FT VARIANT 1157
FT /note="G -> D (in OI1; dbSNP:rs72656323)"
FT /evidence="ECO:0000269|PubMed:16638323"
FT /id="VAR_063338"
FT VARIANT 1166
FT /note="G -> C (in OI2; dbSNP:rs72656324)"
FT /evidence="ECO:0000269|PubMed:3016737"
FT /id="VAR_001725"
FT VARIANT 1172
FT /note="G -> D (in OI2; dbSNP:rs72656325)"
FT /evidence="ECO:0000269|PubMed:10627137"
FT /id="VAR_001726"
FT VARIANT 1177
FT /note="V -> I (in dbSNP:rs41316719)"
FT /evidence="ECO:0000269|PubMed:18272325"
FT /id="VAR_033779"
FT VARIANT 1181
FT /note="G -> S (in OI2; dbSNP:rs72656330)"
FT /evidence="ECO:0000269|PubMed:2037280, ECO:0000269|Ref.52"
FT /id="VAR_001727"
FT VARIANT 1184
FT /note="G -> V (in OI2; dbSNP:rs72656331)"
FT /evidence="ECO:0000269|PubMed:1613761,
FT ECO:0000269|PubMed:2777764"
FT /id="VAR_001728"
FT VARIANT 1187
FT /note="G -> S (in OI2 and OI3; extremely severe form;
FT dbSNP:rs72656332)"
FT /evidence="ECO:0000269|Ref.52"
FT /id="VAR_001729"
FT VARIANT 1187
FT /note="G -> V (in OI2; dbSNP:rs66948146)"
FT /evidence="ECO:0000269|Ref.52"
FT /id="VAR_001730"
FT VARIANT 1195
FT /note="G -> C (in OI1; mild form; dbSNP:rs72656334)"
FT /evidence="ECO:0000269|PubMed:3170557,
FT ECO:0000269|PubMed:3244312"
FT /id="VAR_001731"
FT VARIANT 1219
FT /note="D -> E (in OI1; dbSNP:rs72656339)"
FT /evidence="ECO:0000269|PubMed:16786509"
FT /id="VAR_063339"
FT VARIANT 1219
FT /note="D -> N (found in a patient with mild osteogenesis
FT imperfecta associated with increased bone mineral density;
FT results in defective type I procollagen processing;
FT incorporation of the immature procollagen into the matrix
FT leads to increased bone matrix mineralization and altered
FT collagen fibril structure; dbSNP:rs72656338)"
FT /evidence="ECO:0000269|PubMed:21344539"
FT /id="VAR_066385"
FT VARIANT 1251
FT /note="S -> T (in dbSNP:rs3205325)"
FT /evidence="ECO:0000269|PubMed:8349697"
FT /id="VAR_030014"
FT VARIANT 1277
FT /note="D -> H (in OI2; impaired pro-alpha chain
FT association; dbSNP:rs72656342)"
FT /evidence="ECO:0000269|PubMed:8349697"
FT /id="VAR_001732"
FT VARIANT 1312
FT /note="W -> C (in OI2; dbSNP:rs72656343)"
FT /evidence="ECO:0000269|PubMed:8456808"
FT /id="VAR_001733"
FT VARIANT 1337..1338
FT /note="Missing (in OI2; impaired pro-alpha chain
FT association)"
FT /evidence="ECO:0000269|PubMed:8349697"
FT /id="VAR_001734"
FT VARIANT 1356
FT /note="R -> H (in dbSNP:rs149820303)"
FT /evidence="ECO:0000269|PubMed:16786509"
FT /id="VAR_063340"
FT VARIANT 1388
FT /note="L -> R (in OI2; impaired pro-alpha chain
FT association; dbSNP:rs72656348)"
FT /evidence="ECO:0000269|PubMed:8349697"
FT /id="VAR_001735"
FT VARIANT 1391
FT /note="Q -> K (in dbSNP:rs2586486)"
FT /evidence="ECO:0000269|PubMed:3340531,
FT ECO:0000269|PubMed:9443882, ECO:0000269|Ref.1"
FT /id="VAR_030015"
FT VARIANT 1413
FT /note="D -> N (in OI2; dbSNP:rs72656349)"
FT /evidence="ECO:0000269|PubMed:16786509,
FT ECO:0000269|PubMed:18996919"
FT /id="VAR_063341"
FT VARIANT 1430
FT /note="K -> N (in dbSNP:rs1059454)"
FT /id="VAR_033780"
FT VARIANT 1431
FT /note="T -> P (in dbSNP:rs1059454)"
FT /id="VAR_033781"
FT VARIANT 1434
FT /note="T -> S (in dbSNP:rs1800220)"
FT /evidence="ECO:0000269|PubMed:8349697, ECO:0000269|Ref.1"
FT /id="VAR_001736"
FT VARIANT 1438
FT /note="P -> R (in dbSNP:rs17857117)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_030016"
FT VARIANT 1460
FT /note="P -> H (in dbSNP:rs17853657)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_030017"
FT VARIANT 1464
FT /note="L -> P (in OI3; dbSNP:rs72656353)"
FT /evidence="ECO:0000269|PubMed:8723681"
FT /id="VAR_001737"
FT CONFLICT 59
FT /note="R -> Q (in Ref. 8; CAA25394)"
FT /evidence="ECO:0000305"
FT CONFLICT 112..114
FT /note="Missing (in Ref. 2; AAB94054)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="E -> P (in Ref. 15; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="R -> L (in Ref. 6; AAB59373)"
FT /evidence="ECO:0000305"
FT CONFLICT 484
FT /note="P -> L (in Ref. 19; AAA52289)"
FT /evidence="ECO:0000305"
FT CONFLICT 595
FT /note="A -> R (in Ref. 20; AAA51847)"
FT /evidence="ECO:0000305"
FT CONFLICT 721
FT /note="Q -> E (in Ref. 22; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 738
FT /note="L -> E (in Ref. 22; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 975..976
FT /note="LP -> PL (in Ref. 19; AAA52291)"
FT /evidence="ECO:0000305"
FT CONFLICT 1081
FT /note="V -> A (in Ref. 18; AAA51995)"
FT /evidence="ECO:0000305"
FT CONFLICT 1329
FT /note="S -> T (in Ref. 25; AAB27856)"
FT /evidence="ECO:0000305"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:3GXE"
FT STRAND 966..968
FT /evidence="ECO:0007829|PDB:3EJH"
FT HELIX 1227..1246
FT /evidence="ECO:0007829|PDB:5K31"
FT STRAND 1251..1254
FT /evidence="ECO:0007829|PDB:5K31"
FT HELIX 1259..1265
FT /evidence="ECO:0007829|PDB:5K31"
FT STRAND 1271..1276
FT /evidence="ECO:0007829|PDB:5K31"
FT HELIX 1283..1285
FT /evidence="ECO:0007829|PDB:5K31"
FT STRAND 1287..1292
FT /evidence="ECO:0007829|PDB:5K31"
FT TURN 1293..1296
FT /evidence="ECO:0007829|PDB:5K31"
FT STRAND 1297..1300
FT /evidence="ECO:0007829|PDB:5K31"
FT STRAND 1306..1310
FT /evidence="ECO:0007829|PDB:5K31"
FT HELIX 1326..1329
FT /evidence="ECO:0007829|PDB:5K31"
FT HELIX 1345..1357
FT /evidence="ECO:0007829|PDB:5K31"
FT STRAND 1362..1372
FT /evidence="ECO:0007829|PDB:5K31"
FT TURN 1379..1382
FT /evidence="ECO:0007829|PDB:5K31"
FT STRAND 1389..1391
FT /evidence="ECO:0007829|PDB:5K31"
FT STRAND 1397..1403
FT /evidence="ECO:0007829|PDB:5K31"
FT STRAND 1409..1413
FT /evidence="ECO:0007829|PDB:5K31"
FT STRAND 1420..1432
FT /evidence="ECO:0007829|PDB:5K31"
FT HELIX 1434..1436
FT /evidence="ECO:0007829|PDB:5K31"
FT STRAND 1441..1443
FT /evidence="ECO:0007829|PDB:5K31"
FT STRAND 1453..1463
FT /evidence="ECO:0007829|PDB:5K31"
SQ SEQUENCE 1464 AA; 138911 MW; B0581DAD2809DDE8 CRC64;
MFSFVDLRLL LLLAATALLT HGQEEGQVEG QDEDIPPITC VQNGLRYHDR DVWKPEPCRI
CVCDNGKVLC DDVICDETKN CPGAEVPEGE CCPVCPDGSE SPTDQETTGV EGPKGDTGPR
GPRGPAGPPG RDGIPGQPGL PGPPGPPGPP GPPGLGGNFA PQLSYGYDEK STGGISVPGP
MGPSGPRGLP GPPGAPGPQG FQGPPGEPGE PGASGPMGPR GPPGPPGKNG DDGEAGKPGR
PGERGPPGPQ GARGLPGTAG LPGMKGHRGF SGLDGAKGDA GPAGPKGEPG SPGENGAPGQ
MGPRGLPGER GRPGAPGPAG ARGNDGATGA AGPPGPTGPA GPPGFPGAVG AKGEAGPQGP
RGSEGPQGVR GEPGPPGPAG AAGPAGNPGA DGQPGAKGAN GAPGIAGAPG FPGARGPSGP
QGPGGPPGPK GNSGEPGAPG SKGDTGAKGE PGPVGVQGPP GPAGEEGKRG ARGEPGPTGL
PGPPGERGGP GSRGFPGADG VAGPKGPAGE RGSPGPAGPK GSPGEAGRPG EAGLPGAKGL
TGSPGSPGPD GKTGPPGPAG QDGRPGPPGP PGARGQAGVM GFPGPKGAAG EPGKAGERGV
PGPPGAVGPA GKDGEAGAQG PPGPAGPAGE RGEQGPAGSP GFQGLPGPAG PPGEAGKPGE
QGVPGDLGAP GPSGARGERG FPGERGVQGP PGPAGPRGAN GAPGNDGAKG DAGAPGAPGS
QGAPGLQGMP GERGAAGLPG PKGDRGDAGP KGADGSPGKD GVRGLTGPIG PPGPAGAPGD
KGESGPSGPA GPTGARGAPG DRGEPGPPGP AGFAGPPGAD GQPGAKGEPG DAGAKGDAGP
PGPAGPAGPP GPIGNVGAPG AKGARGSAGP PGATGFPGAA GRVGPPGPSG NAGPPGPPGP
AGKEGGKGPR GETGPAGRPG EVGPPGPPGP AGEKGSPGAD GPAGAPGTPG PQGIAGQRGV
VGLPGQRGER GFPGLPGPSG EPGKQGPSGA SGERGPPGPM GPPGLAGPPG ESGREGAPGA
EGSPGRDGSP GAKGDRGETG PAGPPGAPGA PGAPGPVGPA GKSGDRGETG PAGPAGPVGP
VGARGPAGPQ GPRGDKGETG EQGDRGIKGH RGFSGLQGPP GPPGSPGEQG PSGASGPAGP
RGPPGSAGAP GKDGLNGLPG PIGPPGPRGR TGDAGPVGPP GPPGPPGPPG PPSAGFDFSF
LPQPPQEKAH DGGRYYRADD ANVVRDRDLE VDTTLKSLSQ QIENIRSPEG SRKNPARTCR
DLKMCHSDWK SGEYWIDPNQ GCNLDAIKVF CNMETGETCV YPTQPSVAQK NWYISKNPKD
KRHVWFGESM TDGFQFEYGG QGSDPADVAI QLTFLRLMST EASQNITYHC KNSVAYMDQQ
TGNLKKALLL QGSNEIEIRA EGNSRFTYSV TVDGCTSHTG AWGKTVIEYK TTKTSRLPII
DVAPLDVGAP DQEFGFDVGP VCFL
