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Collagen alpha-1(I) chain (Alpha-1 type I collagen)

 CO1A1_HUMAN             Reviewed;        1464 AA.
P02452; O76045; P78441; Q13896; Q13902; Q13903; Q14037; Q14992;
Q15176; Q15201; Q16050; Q59F64; Q7KZ30; Q7KZ34; Q8IVI5; Q8N473;
Q9UML6; Q9UMM7;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 5.
22-NOV-2017, entry version 221.
RecName: Full=Collagen alpha-1(I) chain;
AltName: Full=Alpha-1 type I collagen;
Flags: Precursor;
Name=COL1A1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ALA-1019; ALA-1075; LYS-1391
AND SER-1434.
Dalgleish R.;
Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-1075 AND LYS-1391.
PubMed=9443882; DOI=10.1086/301689;
Korkko J.M., Ala-Kokko L., De Paepe A., Nuytinck L., Earley J.J.,
Prockop D.J.;
"Analysis of the COL1A1 and COL1A2 genes by PCR amplification and
scanning by conformation-sensitive gel electrophoresis identifies only
COL1A1 mutations in 15 patients with osteogenesis imperfecta type I:
identification of common sequences of null-allele mutations.";
Am. J. Hum. Genet. 62:98-110(1998).
[3]
SEQUENCE REVISION TO 1049.
Korkko J.M., Earley J.J., Nuytinck L., DePaepe A., Prockop D.J.,
Ala-Kokko L.;
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-1075.
TISSUE=Spleen;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ALA-1075;
ARG-1438 AND HIS-1460.
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-589.
PubMed=2843432; DOI=10.1016/0378-1119(88)90013-3;
D'Alessio M., Bernard M.P., Pretorius P.J., de Wet W., Ramirez F.,
Pretorious P.J.;
"Complete nucleotide sequence of the region encompassing the first
twenty-five exons of the human pro alpha 1(I) collagen gene
(COL1A1).";
Gene 67:105-115(1988).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-472.
PubMed=3178743; DOI=10.1042/bj2530919;
Tromp G., Kuivaniemi H., Stacey A., Shikata H., Baldwin C.T.,
Jaenisch R., Prockup D.J.;
"Structure of a full-length cDNA clone for the prepro alpha 1(I) chain
of human type I procollagen.";
Biochem. J. 253:919-922(1988).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-181.
PubMed=6462220; DOI=10.1038/310337a0;
Chu M.-L., de Wet W.J., Bernard M.P., Ding J.-F., Morabito M.,
Myers J., Williams C., Ramirez F.;
"Human pro alpha 1(I) collagen gene structure reveals evolutionary
conservation of a pattern of introns and exons.";
Nature 310:337-340(1984).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44.
PubMed=2822714;
Rossouw C.M.S., Vergeer W.P., du Plooy S.J., Bernard M.P., Ramirez F.,
de Wet W.;
"DNA sequences in the first intron of the human pro-alpha 1(I)
collagen gene enhance transcription.";
J. Biol. Chem. 262:15151-15157(1987).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
PubMed=2857713;
Chu M.-L., de Wet W., Bernard M.P., Ramirez F.;
"Fine structural analysis of the human pro-alpha 1 (I) collagen gene.
Promoter structure, AluI repeats, and polymorphic transcripts.";
J. Biol. Chem. 260:2315-2320(1985).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
PubMed=3480516; DOI=10.1073/pnas.84.24.8869;
Bornstein P., McKay J., Morishima J.K., Devarayalu S., Gelinas R.E.;
"Regulatory elements in the first intron contribute to transcriptional
control of the human alpha 1(I) collagen gene.";
Proc. Natl. Acad. Sci. U.S.A. 84:8869-8873(1987).
[12]
PROTEIN SEQUENCE OF 33-52.
PubMed=2318855;
Wirtz M.K., Keene D.R., Hori H., Glanville R.W., Steinmann B.,
Rao V.H., Hollister D.W.;
"In vivo and in vitro noncovalent association of excised alpha 1 (I)
amino-terminal propeptides with mutant pN alpha 2(I) collagen chains
in native mutant collagen in a case of Ehlers-Danlos syndrome, type
VII.";
J. Biol. Chem. 265:6312-6317(1990).
[13]
NUCLEOTIDE SEQUENCE OF 156-183.
PubMed=2767050;
Weil D., D'Alessio M., Ramirez F., de Wet W., Cole W.G., Chan D.,
Bateman J.F.;
"A base substitution in the exon of a collagen gene causes alternative
splicing and generates a structurally abnormal polypeptide in a
patient with Ehlers-Danlos syndrome type VII.";
EMBO J. 8:1705-1710(1989).
[14]
PROTEIN SEQUENCE OF 162-301, ALLYSINE AT LYS-170, AND PYROGLUTAMATE
FORMATION AT GLN-162.
TISSUE=Skin;
PubMed=5529814; DOI=10.1021/bi00826a012;
Click E.M., Bornstein P.;
"Isolation and characterization of the cyanogen bromide peptides from
the alpha 1 and alpha 2 chains of human skin collagen.";
Biochemistry 9:4699-4706(1970).
[15]
PROTEIN SEQUENCE OF 175-187 AND 274-289.
PubMed=2169412; DOI=10.1111/j.1432-1033.1990.tb19208.x;
Baetge B., Notbohm H., Diebold J., Lehmann H., Bodo M., Deutzmann R.,
Muller P.K.;
"A critical crosslink region in human-bone-derived collagen type I.
Specific cleavage site at residue Leu95.";
Eur. J. Biochem. 192:153-159(1990).
[16]
PROTEIN SEQUENCE OF 263-268, HYDROXYLATION AT LYS-265, AND
GLYCOSYLATION AT LYS-265.
TISSUE=Skin;
PubMed=4319110;
Morgan P.H., Jacobs H.G., Segrest J.P., Cunningham L.W.;
"A comparative study of glycopeptides derived from selected vertebrate
collagens. A possible role of the carbohydrate in fibril formation.";
J. Biol. Chem. 245:5042-5048(1970).
[17]
NUCLEOTIDE SEQUENCE OF 281-302; 402-420; 823-842; 924-944; 1026-1045
AND 1143-1162.
PubMed=2374517;
Labhard M.E., Hollister D.W.;
"Segmental amplification of the entire helical and telopeptide regions
of the cDNA for human alpha 1 (I) collagen.";
Matrix 10:124-130(1990).
[18]
NUCLEOTIDE SEQUENCE [MRNA] OF 425-1464, AND VARIANTS ALA-1019 AND
ALA-1075.
PubMed=6689127; DOI=10.1021/bi00291a023;
Bernard M.P., Chu M.-L., Myers J.C., Ramirez F., Eikenberry E.F.,
Prockop D.J.;
"Nucleotide sequences of complementary deoxyribonucleic acids for the
pro alpha 1 chain of human type I procollagen. Statistical evaluation
of structures that are conserved during evolution.";
Biochemistry 22:5213-5223(1983).
[19]
NUCLEOTIDE SEQUENCE [MRNA] OF 425-490; 965-1024; 999-1039 AND
1453-1464.
PubMed=6183642; DOI=10.1093/nar/10.19.5925;
Chu M.-L., Myers J.C., Bernard M.P., Ding J.-F., Ramirez F.;
"Cloning and characterization of five overlapping cDNAs specific for
the human pro alpha 1(I) collagen chain.";
Nucleic Acids Res. 10:5925-5934(1982).
[20]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 472-607.
PubMed=2981843;
Chu M.-L., Gargiulo V., Williams C.J., Ramirez F.;
"Multiexon deletion in an osteogenesis imperfecta variant with
increased type III collagen mRNA.";
J. Biol. Chem. 260:691-694(1985).
[21]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 488-625.
PubMed=3857621; DOI=10.1073/pnas.82.9.2870;
Barsh G.S., Roush C.L., Bonadio J., Byers P.H., Gelinas R.E.;
"Intron-mediated recombination may cause a deletion in an alpha 1 type
I collagen chain in a lethal form of osteogenesis imperfecta.";
Proc. Natl. Acad. Sci. U.S.A. 82:2870-2874(1985).
[22]
NUCLEOTIDE SEQUENCE OF 710-745, AND VARIANT OI2 ARG-728.
PubMed=2339700;
Wallis G.A., Starman B.J., Zinn A.B., Byers P.H.;
"Variable expression of osteogenesis imperfecta in a nuclear family is
explained by somatic mosaicism for a lethal point mutation in the
alpha 1(I) gene (COL1A1) of type I collagen in a parent.";
Am. J. Hum. Genet. 46:1034-1040(1990).
[23]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 746-781, AND VARIANT OI3 SER-767.
PubMed=7881420; DOI=10.1093/hmg/3.12.2201;
Forlino A., Zolezzi F., Valli M., Pignatti P.F., Cetta G.,
Brunelli P.C., Mottes M.;
"Severe (type III) osteogenesis imperfecta due to glycine
substitutions in the central domain of the collagen triple helix.";
Hum. Mol. Genet. 3:2201-2206(1994).
[24]
PROTEIN SEQUENCE OF 1063-1084, IDENTIFICATION BY MASS SPECTROMETRY,
AND VARIANT ALA-1075.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[25]
NUCLEOTIDE SEQUENCE [MRNA] OF 1179-1464, VARIANTS OI2 HIS-1277;
ARG-1388 AND 1337-GLU-TYR-1338 DEL, AND VARIANTS THR-1251 AND
SER-1434.
PubMed=8349697;
Chessler S.D., Wallis G.A., Byers P.H.;
"Mutations in the carboxyl-terminal propeptide of the pro alpha 1(I)
chain of type I collagen result in defective chain association and
produce lethal osteogenesis imperfecta.";
J. Biol. Chem. 268:18218-18225(1993).
[26]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1187-1220, AND VARIANT CYS-1195.
PubMed=3170557;
Cohn D.H., Apone S., Eyre D.R., Starman B.J., Andreassen P.,
Charbonneau H., Nicholls A.C., Pope F.M., Byers P.H.;
"Substitution of cysteine for glycine within the carboxyl-terminal
telopeptide of the alpha 1 chain of type I collagen produces mild
osteogenesis imperfecta.";
J. Biol. Chem. 263:14605-14607(1988).
[27]
NUCLEOTIDE SEQUENCE [MRNA] OF 1229-1454, AND VARIANT LYS-1391.
TISSUE=Bone;
PubMed=3340531; DOI=10.1093/nar/16.1.349;
Maekelae J.K., Raassina M., Virta A., Vuorio E.;
"Human pro alpha 1(I) collagen: cDNA sequence for the C-propeptide
domain.";
Nucleic Acids Res. 16:349-349(1988).
[28]
NUCLEOTIDE SEQUENCE [MRNA] OF 1440-1464.
PubMed=2295701; DOI=10.1172/JCI114424;
Willing M.C., Cohn D.H., Byers P.H.;
"Frameshift mutation near the 3' end of the COL1A1 gene of type I
collagen predicts an elongated Pro alpha 1(I) chain and results in
osteogenesis imperfecta type I.";
J. Clin. Invest. 85:282-290(1990).
[29]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1454-1464, AND VARIANT ALA-1075.
PubMed=1995349; DOI=10.1016/0014-5793(91)80237-W;
Maatta A., Bornstein P., Penttinen R.P.;
"Highly conserved sequences in the 3'-untranslated region of the
COL1A1 gene bind cell-specific nuclear proteins.";
FEBS Lett. 279:9-13(1991).
[30]
REVIEW ON VARIANTS.
PubMed=2010058;
Kuivaniemi H., Tromp G., Prockop D.J.;
"Mutations in collagen genes: causes of rare and some common diseases
in humans.";
FASEB J. 5:2052-2060(1991).
[31]
REVIEW ON VARIANTS.
PubMed=9101290;
DOI=10.1002/(SICI)1098-1004(1997)9:4<300::AID-HUMU2>3.0.CO;2-9;
Kuivaniemi H., Tromp G., Prockop D.J.;
"Mutations in fibrillar collagens (types I, II, III, and XI), fibril-
associated collagen (type IX), and network-forming collagen (type X)
cause a spectrum of diseases of bone, cartilage, and blood vessels.";
Hum. Mutat. 9:300-315(1997).
[32]
REVIEW ON VARIANTS.
PubMed=1895312; DOI=10.1136/jmg.28.7.433;
Byers P.H., Wallis G.A., Willing M.C.;
"Osteogenesis imperfecta: translation of mutation to phenotype.";
J. Med. Genet. 28:433-442(1991).
[33]
INTERACTION WITH TRAM2.
PubMed=14749390; DOI=10.1128/MCB.24.4.1758-1768.2004;
Stefanovic B., Stefanovic L., Schnabl B., Bataller R., Brenner D.A.;
"TRAM2 protein interacts with endoplasmic reticulum Ca2+ pump Serca2b
and is necessary for collagen type I synthesis.";
Mol. Cell. Biol. 24:1758-1768(2004).
[34]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22905912; DOI=10.1021/pr300539b;
Rosenow A., Noben J.P., Jocken J., Kallendrusch S.,
Fischer-Posovszky P., Mariman E.C., Renes J.;
"Resveratrol-induced changes of the human adipocyte secretion
profile.";
J. Proteome Res. 11:4733-4743(2012).
[35]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[36]
VARIANT OI2 CYS-1166.
PubMed=3016737; DOI=10.1073/pnas.83.16.6045;
Cohn D.H., Byers P.H., Steinmann B., Gelinas R.E.;
"Lethal osteogenesis imperfecta resulting from a single nucleotide
change in one human pro alpha 1(I) collagen allele.";
Proc. Natl. Acad. Sci. U.S.A. 83:6045-6047(1986).
[37]
VARIANT OI2 ARG-569.
PubMed=3108247;
Bateman J.F., Chan D., Walkers I.D., Rogers J.G., Cole W.G.;
"Lethal perinatal osteogenesis imperfecta due to the substitution of
arginine for glycine at residue 391 of the alpha 1(I) chain of type I
collagen.";
J. Biol. Chem. 262:7021-7027(1987).
[38]
VARIANT OI2 CYS-926.
PubMed=3667599;
Vogel B.E., Minor R.R., Freund M., Prockop D.J.;
"A point mutation in a type I procollagen gene converts glycine 748 of
the alpha 1 chain to cysteine and destabilizes the triple helix in a
lethal variant of osteogenesis imperfecta.";
J. Biol. Chem. 262:14737-14744(1987).
[39]
VARIANT OI2 ARG-842.
PubMed=3403550;
Bateman J.F., Lamande S.R., Dahl H.-H.M., Chan D., Cole W.G.;
"Substitution of arginine for glycine 664 in the collagen alpha 1(I)
chain in lethal perinatal osteogenesis imperfecta. Demonstration of
the peptide defect by in vitro expression of the mutant cDNA.";
J. Biol. Chem. 263:11627-11630(1988).
[40]
VARIANT OI1 CYS-1195.
PubMed=3244312;
Labhard M.E., Wirtz M.K., Pope F.M., Nicholls A.C., Hollister D.W.;
"A cysteine for glycine substitution at position 1017 in an alpha 1(I)
chain of type I collagen in a patient with mild dominantly inherited
osteogenesis imperfecta.";
Mol. Biol. Med. 5:197-207(1988).
[41]
VARIANT OI2 VAL-434.
PubMed=2470760;
Patterson E., Smiley E., Bonadio J.;
"RNA sequence analysis of a perinatal lethal osteogenesis imperfecta
mutation.";
J. Biol. Chem. 264:10083-10087(1989).
[42]
VARIANT OI4 SER-1010.
PubMed=2745420;
Marini J.C., Grange D.K., Gottesman G.S., Lewis M.B., Koeplin D.A.;
"Osteogenesis imperfecta type IV. Detection of a point mutation in one
alpha 1(I) collagen allele (COL1A1) by RNA/RNA hybrid analysis.";
J. Biol. Chem. 264:11893-11900(1989).
[43]
VARIANTS OI2 ALA-1106; VAL-1151; ARG-1154 AND VAL-1184.
PubMed=2777764;
Lamande S.R., Dahl H.-H.M., Cole W.G., Bateman J.F.;
"Characterization of point mutations in the collagen COL1A1 and COL1A2
genes causing lethal perinatal osteogenesis imperfecta.";
J. Biol. Chem. 264:15809-15812(1989).
[44]
VARIANT OI3 SER-1022.
PubMed=2511192;
Pack M., Constantinou C.D., Kalia K., Nielsen K.B., Prockop D.J.;
"Substitution of serine for alpha 1(I)-glycine 844 in a severe variant
of osteogenesis imperfecta minimally destabilizes the triple helix of
type I procollagen. The effects of glycine substitutions on thermal
stability are either position of amino acid specific.";
J. Biol. Chem. 264:19694-19699(1989).
[45]
VARIANT OI2 CYS-1082.
PubMed=2913053; DOI=10.1172/JCI113920;
Constantinou C.D., Nielsen K.B., Prockop D.J.;
"A lethal variant of osteogenesis imperfecta has a single base
mutation that substitutes cysteine for glycine 904 of the alpha 1(I)
chain of type I procollagen. The asymptomatic mother has an
unidentified mutation producing an overmodified and unstable type I
procollagen.";
J. Clin. Invest. 83:574-584(1989).
[46]
VARIANT OI1 CYS-272, VARIANT OI3 CYS-704, AND VARIANT OI2 CYS-896.
PubMed=2794057; DOI=10.1172/JCI114286;
Starman B.J., Eyre D.R., Charbonneau H., Harrylock M., Weis M.A.,
Weiss L., Graham J.M. Jr., Byers P.H.;
"Osteogenesis imperfecta. The position of substitution for glycine by
cysteine in the triple helical domain of the pro alpha 1(I) chains of
type I collagen determines the clinical phenotype.";
J. Clin. Invest. 84:1206-1214(1989).
[47]
VARIANT OI2 CYS-422.
Fertala A., Westerhausen A., Morris G.M., Rooney J.E., Prockop D.J.;
"Two cysteine substitutions in the type I procollagen genes (COL1A1
and COL1A2) that cause lethal osteogenesis imperfecta. The location of
glycine substitutions does not in any simple way predict their effects
on protein function or phenotype.";
Am. J. Hum. Genet. 47:A216-A216(1990).
[48]
VARIANTS OI2 SER-776 AND SER-809.
PubMed=2116413;
Westerhausen A., Kishi J., Prockop D.J.;
"Mutations that substitute serine for glycine alpha 1-598 and glycine
alpha 1-631 in type I procollagen. The effects on thermal unfolding of
the triple helix are position-specific and demonstrate that the
protein unfolds through a series of cooperative blocks.";
J. Biol. Chem. 265:13995-14000(1990).
[49]
VARIANT OI2 ARG-1025.
PubMed=2211725;
Wallis G.A., Starman B.J., Schwartz M.F., Byers P.H.;
"Substitution of arginine for glycine at position 847 in the triple-
helical domain of the alpha 1 (I) chain of type I collagen produces
lethal osteogenesis imperfecta. Molecules that contain one or two
abnormal chains differ in stability and secretion.";
J. Biol. Chem. 265:18628-18633(1990).
[50]
VARIANTS OI2 SER-1091; SER-1181; SER-1187 AND VAL-1187.
Cohn D.H., Wallis G.A., Zhang X., Byers P.H.;
"Serine for glycine substitutions in the alpha1(I) chain of type I
collagen: biological plasticity in the Gly-Pro-Hyp clamp at the
carboxyl-terminal end of triple helicalH domain.";
Matrix 10:236-236(1990).
[51]
VARIANT OI2 ASP-719.
PubMed=2035536;
Zhuang J., Constantinou C.D., Ganguly A., Prockop D.J.;
"A single base mutation in type I procollagen (COL1A1) that converts
glycine alpha 1-541 to aspartate in a lethal variant of osteogenesis
imperfecta: detection of the mutation with a carbodiimide reaction of
DNA heteroduplexes and direct sequencing of products of the PCR.";
Am. J. Hum. Genet. 48:1186-1191(1991).
[52]
VARIANT OI2 CYS-869.
PubMed=1953667; DOI=10.1042/bj2790747;
Steinmann B., Westerhausen A., Constantinou C.D., Superti-Furga A.,
Prockop D.J.;
"Substitution of cysteine for glycine-alpha 1-691 in the pro alpha
1(I) chain of type I procollagen in a proband with lethal osteogenesis
imperfecta destabilizes the triple helix at a site C-terminal to the
substitution.";
Biochem. J. 279:747-752(1991).
[53]
VARIANT OI2 CYS-926.
PubMed=2036375; DOI=10.1021/bi00234a035;
Kadler K.E., Torre-Blanco A., Adachi E., Vogel B.E., Hojima Y.,
Prockop D.J.;
"A type I collagen with substitution of a cysteine for glycine-748 in
the alpha 1(I) chain copolymerizes with normal type I collagen and can
generate fractallike structures.";
Biochemistry 30:5081-5088(1991).
[54]
VARIANT OI3 ARG-332, AND VARIANT OI2 SER-1181.
PubMed=2037280; DOI=10.1007/BF01213088;
Pruchno C.J., Cohn D.H., Wallis G.A., Willing M.C., Starman B.J.,
Zhang X., Byers P.H.;
"Osteogenesis imperfecta due to recurrent point mutations at CpG
dinucleotides in the COL1A1 gene of type I collagen.";
Hum. Genet. 87:33-40(1991).
[55]
VARIANT OI4 CYS-356.
PubMed=1988452;
Valli M., Mottes M., Tenni R., Sangalli A., Gomez Lira M., Rossi A.,
Antoniazzi F., Cetta G., Pignatti P.F.;
"A de novo G to T transversion in a pro-alpha 1 (I) collagen gene for
a moderate case of osteogenesis imperfecta. Substitution of cysteine
for glycine 178 in the triple helical domain.";
J. Biol. Chem. 266:1872-1878(1991).
[56]
VARIANT OI2 VAL-815.
PubMed=1874719;
Tsuneyoshi T., Westerhausen A., Constantinou C.D., Prockop D.J.;
"Substitutions for glycine alpha 1-637 and glycine alpha 2-694 of type
I procollagen in lethal osteogenesis imperfecta. The conformational
strain on the triple helix introduced by a glycine substitution can be
transmitted along the helix.";
J. Biol. Chem. 266:15608-15613(1991).
[57]
VARIANT OI1 ARG-263.
PubMed=1718984;
Deak S.B., Scholz P.M., Amenta P.S., Constantinou C.D.,
Levi-Minzi S.A., Gonzalez-Lavin L., MacKenzie J.W.;
"The substitution of arginine for glycine 85 of the alpha 1(I)
procollagen chain results in mild osteogenesis imperfecta. The
mutation provides direct evidence for three discrete domains of
cooperative melting of intact type I collagen.";
J. Biol. Chem. 266:21827-21832(1991).
[58]
VARIANT OI2 1046-GLY--PRO-1048 DEL.
PubMed=1939261;
Hawkins J.R., Superti-Furga A., Steinmann B., Dalgleish R.;
"A 9-base pair deletion in COL1A1 in a lethal variant of osteogenesis
imperfecta.";
J. Biol. Chem. 266:22370-22374(1991).
[59]
VARIANT OI3 CYS-593, AND VARIANT OI4 CYS-593.
PubMed=1770532; DOI=10.1136/jmg.28.11.757;
Nicholls A.C., Oliver J.E., Renouf D.V., Keston M., Pope F.M.;
"Substitution of cysteine for glycine at residue 415 of one allele of
the alpha 1(I) chain of type I procollagen in type III/IV osteogenesis
imperfecta.";
J. Med. Genet. 28:757-764(1991).
[60]
VARIANT ALA-1075.
PubMed=1870989; DOI=10.1093/nar/19.15.4302;
Sokolov B.P., Constantinou C.D., Tsuneyoshi T., Zhuang J.,
Prockop D.J.;
"G to A polymorphism in exon 45 of the COL1A1 gene.";
Nucleic Acids Res. 19:4302-4302(1991).
[61]
VARIANT OI1 SER-1079.
PubMed=1634225; DOI=10.1007/BF00219169;
Mottes M., Sangalli A., Valli M., Gomez Lira M., Tenni R.,
Buttitta P., Pignatti P.F., Cetta G.;
"Mild dominant osteogenesis imperfecta with intrafamilial variability:
the cause is a serine for glycine alpha 1(I) 901 substitution in a
type-I collagen gene.";
Hum. Genet. 89:480-484(1992).
[62]
VARIANT OI2 VAL-980.
PubMed=1511982; DOI=10.1007/BF00221955;
Bonaventure J., Cohen-Solal L., Lasselin C., Maroteaux P.;
"A dominant mutation in the COL1A1 gene that substitutes glycine for
valine causes recurrent lethal osteogenesis imperfecta.";
Hum. Genet. 89:640-646(1992).
[63]
VARIANT OI2 1046-GLY--PRO-1048 DEL.
PubMed=1460047;
Wallis G.A., Kadler K.E., Starman B.J., Byers P.H.;
"A tripeptide deletion in the triple-helical domain of the pro alpha
1(I) chain of type I procollagen in a patient with lethal osteogenesis
imperfecta does not alter cleavage of the molecule by N-proteinase.";
J. Biol. Chem. 267:25529-25534(1992).
[64]
VARIANT OI1 CYS-221.
PubMed=1737847; DOI=10.1172/JCI115622;
Shapiro J.R., Stover M.L., Burn V.E., McKinstry M.B., Burshell A.L.,
Chipman S.D., Rowe D.W.;
"An osteopenic nonfracture syndrome with features of mild osteogenesis
imperfecta associated with the substitution of a cysteine for glycine
at triple helix position 43 in the pro alpha 1(I) chain of type I
collagen.";
J. Clin. Invest. 89:567-573(1992).
[65]
VARIANTS OI2 VAL-434; VAL-1151 AND VAL-1184.
PubMed=1613761; DOI=10.1136/jmg.29.2.112;
Cole W.G., Patterson E., Bonadio J., Campbell P.E., Fortune D.W.;
"The clinicopathological features of three babies with osteogenesis
imperfecta resulting from the substitution of glycine by valine in the
pro alpha 1 (I) chain of type I procollagen.";
J. Med. Genet. 29:112-118(1992).
[66]
VARIANT OI2 CYS-1312.
PubMed=8456808; DOI=10.1002/ajmg.1320450216;
Bateman J.F., Lamande S.R., Hannagan M., Moeller I., Dahl H.-H.M.,
Cole W.G.;
"Chemical cleavage method for the detection of RNA base changes:
experience in the application to collagen mutations in osteogenesis
imperfecta.";
Am. J. Med. Genet. 45:233-240(1993).
[67]
VARIANT OI3 SER-530.
PubMed=8456809; DOI=10.1002/ajmg.1320450217;
Marini J.C., Lewis M.B., Chen K.J.;
"Moderately severe osteogenesis imperfecta associated with
substitutions of serine for glycine in the alpha 1(I) chain of type I
collagen.";
Am. J. Med. Genet. 45:241-245(1993).
[68]
VARIANT OI4 CYS-353.
PubMed=8339541; DOI=10.3109/03008209309061961;
Wirtz M.K., Rao V.H., Glanville R.W., Labhard M.E., Pretorius P.J.,
de Vries W.N., de Wet W., Hollister D.W.;
"A cysteine for glycine substitution at position 175 in an alpha 1 (I)
chain of type I collagen produces a clinically heterogeneous form of
osteogenesis imperfecta.";
Connect. Tissue Res. 29:1-11(1993).
[69]
VARIANT OI2 ALA-1088.
PubMed=7679635; DOI=10.1111/j.1432-1033.1993.tb17565.x;
Valli M., Sangalli A., Rossi A., Mottes M., Forlino A., Tenni R.,
Pignatti P.F., Cetta G.;
"Osteogenesis imperfecta and type-I collagen mutations. A lethal
variant caused by a Gly910-->Ala substitution in the alpha 1 (I)
chain.";
Eur. J. Biochem. 211:415-419(1993).
[70]
VARIANT OI1 VAL-263.
PubMed=8223589; DOI=10.1111/j.1432-1033.1993.tb18220.x;
Valli M., Zolezzi F., Mottes M., Antoniazzi F., Stanzial F., Tenni R.,
Pignatti P.F., Cetta G.;
"Gly85 to Val substitution in pro alpha 1(I) chain causes mild
osteogenesis imperfecta and introduces a susceptibility to protease
digestion.";
Eur. J. Biochem. 217:77-82(1993).
[71]
VARIANT OI2 VAL-743.
PubMed=8100209; DOI=10.1007/BF00217768;
Mackay K., Lund A.M., Raghunath M., Steinmann B., Dalgleish R.;
"SSCP detection of a Gly565Val substitution in the pro alpha 1(I)
collagen chain resulting in osteogenesis imperfecta type II.";
Hum. Genet. 91:439-444(1993).
[72]
VARIANTS OI2 SER-425 AND SER-530, VARIANT OI4 SER-560, VARIANT OI3
SER-719, AND VARIANT ALA-823.
PubMed=7691343; DOI=10.1093/hmg/2.8.1155;
Mackay K., Byers P.H., Dalgleish R.;
"An RT-PCR-SSCP screening strategy for detection of mutations in the
gene encoding the alpha 1 chain of type I collagen: application to
four patients with osteogenesis imperfecta.";
Hum. Mol. Genet. 2:1155-1160(1993).
[73]
VARIANT OI2 SER-593, AND VARIANT OI3 SER-593.
PubMed=8364588; DOI=10.1002/humu.1380020308;
Mottes M., Gomez Lira M., Valli M., Scarano G., Lonardo F.,
Forlino A., Cetta G., Pignatti P.F.;
"Paternal mosaicism for a COL1A1 dominant mutation (alpha 1 Ser-415)
causes recurrent osteogenesis imperfecta.";
Hum. Mutat. 2:196-204(1993).
[74]
VARIANT OI4 SER-530.
PubMed=8094076;
Marini J.C., Lewis M.B., Wang Q., Chen K.J., Orrison B.M.;
"Serine for glycine substitutions in type I collagen in two cases of
type IV osteogenesis imperfecta (OI). Additional evidence for a
regional model of OI pathophysiology.";
J. Biol. Chem. 268:2667-2673(1993).
[75]
VARIANTS OI2.
PubMed=8349698;
Chessler S.D., Byers P.H.;
"BiP binds type I procollagen pro alpha chains with mutations in the
carboxyl-terminal propeptide synthesized by cells from patients with
osteogenesis imperfecta.";
J. Biol. Chem. 268:18226-18233(1993).
[76]
VARIANT OI2 ARG-389.
PubMed=7520724; DOI=10.1016/8756-3282(94)90295-X;
Sztrolovics R., Glorieux F.H., Travers R., van der Rest M.,
Roughley P.J.;
"Osteogenesis imperfecta: comparison of molecular defects with bone
histological changes.";
Bone 15:321-328(1994).
[77]
VARIANT OI3 ARG-350.
PubMed=8019571; DOI=10.1002/humu.1380030327;
Mackay K., de Paepe A., Nuytinck L., Dalgleish R.;
"Substitution of glycine-172 by arginine in the alpha 1 chain of type
I collagen in a patient with osteogenesis imperfecta, type III.";
Hum. Mutat. 3:324-326(1994).
[78]
VARIANT OI2 CYS-1124.
PubMed=7961597; DOI=10.1093/oxfordjournals.jbchem.a124429;
Kurosaka D., Hattori S., Hori H., Yamaguchi N., Hasegawa T.,
Akimoto H., Nagai Y.;
"Substitution of cysteine for glycine-946 in the alpha 1(I) chain of
type I procollagen causes lethal osteogenesis imperfecta.";
J. Biochem. 115:853-857(1994).
[79]
VARIANT OI4 SER-1061.
PubMed=7982948;
Lightfoot S.J., Atkinson M.S., Murphy G., Byers P.H., Kadler K.E.;
"Substitution of serine for glycine 883 in the triple helix of the pro
alpha 1 (I) chain of type I procollagen produces osteogenesis
imperfecta type IV and introduces a structural change in the triple
helix that does not alter cleavage of the molecule by procollagen N-
proteinase.";
J. Biol. Chem. 269:30352-30357(1994).
[80]
VARIANT OI3 ARG-332.
PubMed=8669434;
DOI=10.1002/(SICI)1096-8628(19960111)61:2<111::AID-AJMG1>3.0.CO;2-#;
Zhuang J., Tromp G., Kuivaniemi H., Castells S., Prockop D.J.;
"Substitution of arginine for glycine at position 154 of the alpha 1
chain of type I collagen in a variant of osteogenesis imperfecta:
comparison to previous cases with the same mutation.";
Am. J. Med. Genet. 61:111-116(1996).
[81]
VARIANT OI2 SER-839.
PubMed=8786074; DOI=10.1007/BF02185764;
Nuytinck L., Dalgleish R., Spotila L., Renard J.-P.,
van Regemorter N., de Paepe A.;
"Substitution of glycine-661 by serine in the alpha1(I) and alpha2(I)
chains of type I collagen results in different clinical and
biochemical phenotypes.";
Hum. Genet. 97:324-329(1996).
[82]
VARIANT OI3 PRO-1464.
PubMed=8723681;
DOI=10.1002/(SICI)1098-1004(1996)7:4<318::AID-HUMU5>3.0.CO;2-4;
Oliver J.E., Thompson E.M., Pope F.M., Nicholls A.C.;
"Mutation in the carboxy-terminal propeptide of the Pro alpha 1(I)
chain of type I collagen in a child with severe osteogenesis
imperfecta (OI type III): possible implications for protein folding.";
Hum. Mutat. 7:318-326(1996).
[83]
INVOLVEMENT IN OSTEOPOROSIS.
PubMed=8841196; DOI=10.1038/ng1096-203;
Grant S.F.A., Reid D.M., Blake G., Herd R., Fogelman I., Ralston S.H.;
"Reduced bone density and osteoporosis associated with a polymorphic
Sp1 binding site in the collagen type I alpha 1 gene.";
Nat. Genet. 14:203-205(1996).
[84]
VARIANTS OI3 SER-821; SER-1040; SER-1049; SER-1058 AND SER-1076.
PubMed=9101304;
DOI=10.1002/(SICI)1098-1004(1997)9:4<378::AID-HUMU16>3.3.CO;2-5;
Lund A.M., Skovby F., Schwartz M.;
"Serine for glycine substitutions in the C-terminal third of the alpha
1(I) chain of collagen I in five patients with nonlethal osteogenesis
imperfecta.";
Hum. Mutat. 9:378-382(1997).
[85]
VARIANT OI2 VAL-764.
PubMed=9143923;
DOI=10.1002/(SICI)1098-1004(1997)9:5<431::AID-HUMU9>3.0.CO;2-6;
Lund A.M., Skovby F., Schwartz M.;
"(G586V) substitutions in the alpha 1 and alpha 2 chains of collagen
I: effect of alpha-chain stoichiometry on the phenotype of
osteogenesis imperfecta?";
Hum. Mutat. 9:431-436(1997).
[86]
VARIANTS OI4 ALA-398; CYS-527 AND CYS-701.
PubMed=9600458;
DOI=10.1002/(SICI)1098-1004(1998)11:5<395::AID-HUMU7>3.0.CO;2-4;
Sarafova A.P., Choi H., Forlino A., Gajko A., Cabral W.A., Tosi L.,
Reing C.M., Marini J.C.;
"Three novel type I collagen mutations in osteogenesis imperfecta type
IV probands are associated with discrepancies between electrophoretic
migration of osteoblast and fibroblast collagen.";
Hum. Mutat. 11:395-403(1998).
[87]
VARIANTS OI2 SER-656 AND ASP-1172.
PubMed=10627137;
DOI=10.1002/(SICI)1098-1004(1998)12:1<71::AID-HUMU16>3.0.CO;2-4;
Mottes M., Gomez Lira M., Zolezzi F., Valli M., Lisi V., Freising P.;
"Four new cases of lethal osteogenesis imperfecta due to glycine
substitutions in COL1A1 and genes.";
Hum. Mutat. 12:71-72(1998).
[88]
INVOLVEMENT IN INVOLUTIONAL OSTEOPOROSIS.
PubMed=9535665; DOI=10.1056/NEJM199804093381502;
Uitterlinden A.G., Burger H., Huang Q., Yue F., McGuigan F.E.A.,
Grant S.F.A., Hofman A., van Leeuwen J.P.T.M., Pols H.A.P.,
Ralston S.H.;
"Relation of alleles of the collagen type Ialpha1 gene to bone density
and the risk of osteoporotic fractures in postmenopausal women.";
N. Engl. J. Med. 338:1016-1021(1998).
[89]
VARIANT OI3 SER-866.
PubMed=10408781;
DOI=10.1002/(SICI)1098-1004(1999)13:6<503::AID-HUMU11>3.0.CO;2-L;
Lund A.M., Astroem E., Soederhaell S., Schwartz M., Skovby F.;
"Osteogenesis imperfecta: mosaicism and refinement of the genotype-
phenotype map in OI type III.";
Hum. Mutat. 13:503-503(1999).
[90]
VARIANT EDS CYS-312.
PubMed=10739762; DOI=10.1086/302859;
Nuytinck L., Freund M., Lagae L., Pierard G.E., Hermanns-Le T.,
De Paepe A.;
"Classical Ehlers-Danlos syndrome caused by a mutation in type I
collagen.";
Am. J. Hum. Genet. 66:1398-1402(2000).
[91]
DISEASE, AND CHROMOSOMAL TRANSLOCATION WITH PDGFB.
PubMed=8988177; DOI=10.1038/ng0197-95;
Simon M.-P., Pedeutour F., Sirvent N., Grosgeorge J., Minoletti F.,
Coindre J.-M., Terrier-Lacombe M.-J., Mandahl N., Craver R.D.,
Blin N., Sozzi G., Turc-Carel C., O'Brien K.P., Kedra D., Fransson I.,
Guilbaud C., Dumanski J.P.;
"Deregulation of the platelet-derived growth factor B-chain gene via
fusion with collagen gene COL1A1 in dermatofibrosarcoma protuberans
and giant-cell fibroblastoma.";
Nat. Genet. 15:95-98(1997).
[92]
DISEASE, AND CHROMOSOMAL TRANSLOCATION WITH PDGFB.
PubMed=12660034; DOI=10.1016/S0165-4608(02)00844-0;
Sandberg A.A., Anderson W.D., Fredenberg C., Hashimoto H.;
"Dermatofibrosarcoma protuberans of breast.";
Cancer Genet. Cytogenet. 142:56-59(2003).
[93]
VARIANT CAFFD CYS-1014.
PubMed=15864348; DOI=10.1172/JCI22760;
Gensure R.C., Maekitie O., Barclay C., Chan C., Depalma S.R.,
Bastepe M., Abuzahra H., Couper R., Mundlos S., Sillence D.,
Ala-Kokko L., Seidman J.G., Cole W.G., Jueppner H.;
"A novel COL1A1 mutation in infantile cortical hyperostosis (Caffey
disease) expands the spectrum of collagen-related disorders.";
J. Clin. Invest. 115:1250-1257(2005).
[94]
VARIANTS OI3 VAL-203 AND SER-821, AND VARIANTS OI4 ARG-257 AND
SER-683.
PubMed=16879195; DOI=10.1111/j.1399-0004.2006.00646.x;
Venturi G., Tedeschi E., Mottes M., Valli M., Camilot M., Viglio S.,
Antoniazzi F., Tato L.;
"Osteogenesis imperfecta: clinical, biochemical and molecular
findings.";
Clin. Genet. 70:131-139(2006).
[95]
VARIANTS OI1/OI3/OI4 ARG-194; ASP-242; ARG-257; SER-722; SER-767;
SER-821 AND SER-1058.
PubMed=16705691; DOI=10.1002/humu.9423;
Lee K.S., Song H.R., Cho T.J., Kim H.J., Lee T.M., Jin H.S.,
Park H.Y., Kang S., Jung S.C., Koo S.K.;
"Mutational spectrum of type I collagen genes in Korean patients with
osteogenesis imperfecta.";
Hum. Mutat. 27:599-599(2006).
[96]
VARIANTS OI2 ARG-22; ARG-581; VAL-734 AND ASN-1413, VARIANTS OI4
ARG-197 AND CYS-338, VARIANTS OI1 VAL-320; ARG-555; SER-647 AND
GLU-1219, AND VARIANTS ALA-205; LYS-288; SER-906 AND HIS-1356.
PubMed=16786509; DOI=10.1002/humu.9430;
Pollitt R., McMahon R., Nunn J., Bamford R., Afifi A., Bishop N.,
Dalton A.;
"Mutation analysis of COL1A1 and COL1A2 in patients diagnosed with
osteogenesis imperfecta type I-IV.";
Hum. Mutat. 27:716-716(2006).
[97]
VARIANT OI2 ASP-833.
PubMed=16566045; DOI=10.1002/pd.1428;
Aerts M., Van Holsbeke C., de Ravel T., Devlieger R.;
"Prenatal diagnosis of type II osteogenesis imperfecta, describing a
new mutation in the COL1A1 gene.";
Prenat. Diagn. 26:394-394(2006).
[98]
VARIANT OI1 ASP-1157.
PubMed=16638323;
Wang Z., Xu D.L., Chen Z., Hu J.Y., Yang Z., Wang L.T.;
"A new mutation in COL1A1 gene in a family with osteogenesis
imperfecta.";
Zhonghua Yi Xue Za Zhi 86:170-173(2006).
[99]
VARIANT EDS CYS-312, AND VARIANTS CYS-574 AND CYS-1093.
PubMed=17211858; DOI=10.1002/humu.20455;
Malfait F., Symoens S., De Backer J., Hermanns-Le T., Sakalihasan N.,
Lapiere C.M., Coucke P., De Paepe A.;
"Three arginine to cysteine substitutions in the pro-alpha (I)-
collagen chain cause Ehlers-Danlos syndrome with a propensity to
arterial rupture in early adulthood.";
Hum. Mutat. 28:387-395(2007).
[100]
VARIANT CYS-1066.
PubMed=17206620; DOI=10.1002/humu.20456;
Cabral W.A., Makareeva E., Letocha A.D., Scribanu N., Fertala A.,
Steplewski A., Keene D.R., Persikov A.V., Leikin S., Marini J.C.;
"Y-position cysteine substitution in type I collagen (alpha1(I)
R888C/p.R1066C) is associated with osteogenesis imperfecta/Ehlers-
Danlos syndrome phenotype.";
Hum. Mutat. 28:396-405(2007).
[101]
VARIANTS OI1 GLU-266 AND SER-287, AND VARIANT OI4 SER-353.
PubMed=17875077; DOI=10.1111/j.1442-200X.2007.02422.x;
Kataoka K., Ogura E., Hasegawa K., Inoue M., Seino Y., Morishima T.,
Tanaka H.;
"Mutations in type I collagen genes in Japanese osteogenesis
imperfecta patients.";
Pediatr. Int. 49:564-569(2007).
[102]
VARIANTS ALA-1075; GLN-1141 AND ILE-1177.
PubMed=18272325; DOI=10.1016/j.ygeno.2007.12.008;
Chan T.F., Poon A., Basu A., Addleman N.R., Chen J., Phong A.,
Byers P.H., Klein T.E., Kwok P.Y.;
"Natural variation in four human collagen genes across an ethnically
diverse population.";
Genomics 91:307-314(2008).
[103]
VARIANTS OI1 VAL-200 AND PHE-349, VARIANT OI2 SER-866, AND VARIANT OI3
SER-1040.
PubMed=18670065; DOI=10.1007/BF03195625;
Witecka J., Augusciak-Duma A.M., Kruczek A., Szydlo A., Lesiak M.,
Krzak M., Pietrzyk J.J., Mannikko M., Sieron A.L.;
"Two novel COL1A1 mutations in patients with osteogenesis imperfecta
(OI) affect the stability of the collagen type I triple-helix.";
J. Appl. Genet. 49:283-295(2008).
[104]
VARIANTS OI2 THR-146; VAL-288; ASP-353; VAL-368; THR-390; SER-425;
ASP-455; VAL-470; VAL-509; ALA-548; ARG-602; ASP-605; ARG-614;
ARG-740; SER-809; ARG-824; ARG-845; ARG-848; HIS-855; SER-866;
SER-875; SER-884; ASP-896; CYS-947; ASP-977; CYS-1001; VAL-1022;
ALA-PRO-GLY-1052 INS; ASP-1055; SER-1094; ASP-1100 AND ASN-1413, AND
VARIANT ALA-1075.
PubMed=18996919; DOI=10.1093/hmg/ddn374;
Bodian D.L., Chan T.F., Poon A., Schwarze U., Yang K., Byers P.H.,
Kwok P.Y., Klein T.E.;
"Mutation and polymorphism spectrum in osteogenesis imperfecta type
II: implications for genotype-phenotype relationships.";
Hum. Mol. Genet. 18:463-471(2009).
[105]
VARIANT ASN-1219, AND CHARACTERIZATION OF VARIANT ASN-1219.
PubMed=21344539; DOI=10.1002/humu.21475;
Lindahl K., Barnes A.M., Fratzl-Zelman N., Whyte M.P., Hefferan T.E.,
Makareeva E., Brusel M., Yaszemski M.J., Rubin C.J., Kindmark A.,
Roschger P., Klaushofer K., McAlister W.H., Mumm S., Leikin S.,
Kessler E., Boskey A.L., Ljunggren O., Marini J.C.;
"COL1 C-propeptide cleavage site mutations cause high bone mass
osteogenesis imperfecta.";
Hum. Mutat. 32:598-609(2011).
[106]
VARIANT OI1 GLU-1088.
PubMed=24682174; DOI=10.3892/mmr.2014.2084;
Xia X.Y., Li W.W., Li N., Wu Q.Y., Cui Y.X., Li X.J.;
"A novel mild variant of osteogenesis imperfecta type I caused by a
Gly1088Glu mutation in COL1A1.";
Mol. Med. Report. 9:2187-2190(2014).
[107]
VARIANT OI2 CYS-773.
PubMed=25958000; DOI=10.1186/s40246-015-0028-0;
Maasalu K., Nikopensius T., Koks S., Noukas M., Kals M., Prans E.,
Zhytnik L., Metspalu A., Maertson A.;
"Whole-exome sequencing identifies de novo mutation in the COL1A1 gene
to underlie the severe osteogenesis imperfecta.";
Hum. Genomics 9:6-6(2015).
-!- FUNCTION: Type I collagen is a member of group I collagen
(fibrillar forming collagen).
-!- SUBUNIT: Trimers of one alpha 2(I) and two alpha 1(I) chains.
Interacts with MRC2 (By similarity). Interacts with TRAM2
(PubMed:14749390). Interacts with MFAP4 in a Ca (2+)-dependent
manner (By similarity). {ECO:0000250|UniProtKB:P02453,
ECO:0000250|UniProtKB:P02454, ECO:0000269|PubMed:14749390}.
-!- INTERACTION:
O01949:AAEL010235 (xeno); NbExp=5; IntAct=EBI-982999, EBI-7685554;
P02751:FN1; NbExp=2; IntAct=EBI-982999, EBI-1220319;
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000255|PROSITE-ProRule:PRU00793}.
-!- TISSUE SPECIFICITY: Forms the fibrils of tendon, ligaments and
bones. In bones the fibrils are mineralized with calcium
hydroxyapatite.
-!- DOMAIN: The C-terminal propeptide, also known as COLFI domain,
have crucial roles in tissue growth and repair by controlling both
the intracellular assembly of procollagen molecules and the
extracellular assembly of collagen fibrils. It binds a calcium ion
which is essential for its function (By similarity).
{ECO:0000250}.
-!- PTM: Contains mostly 4-hydroxyproline. Proline residues at the
third position of the tripeptide repeating unit (G-X-Y) are
hydroxylated in some or all of the chains.
{ECO:0000269|PubMed:4319110}.
-!- PTM: Contains 3-hydroxyproline at a few sites. This modification
occurs on the first proline residue in the sequence motif Gly-Pro-
Hyp, where Hyp is 4-hydroxyproline.
{ECO:0000250|UniProtKB:P11087}.
-!- PTM: Lysine residues at the third position of the tripeptide
repeating unit (G-X-Y) are 5-hydroxylated in some or all of the
chains. {ECO:0000269|PubMed:4319110}.
-!- PTM: O-glycosylated on hydroxylated lysine residues. The O-linked
glycan consists of a Glc-Gal disaccharide.
{ECO:0000269|PubMed:4319110}.
-!- DISEASE: Caffey disease (CAFFD) [MIM:114000]: Characterized by an
infantile episode of massive subperiosteal new bone formation that
typically involves the diaphyses of the long bones, mandible, and
clavicles. The involved bones may also appear inflamed, with
painful swelling and systemic fever often accompanying the
illness. The bone changes usually begin before 5 months of age and
resolve before 2 years of age. {ECO:0000269|PubMed:15864348}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Ehlers-Danlos syndrome, classic type (EDS) [MIM:130000]:
A connective tissue disorder characterized by hyperextensible
skin, atrophic cutaneous scars due to tissue fragility and joint
hyperlaxity. {ECO:0000269|PubMed:10739762,
ECO:0000269|PubMed:17211858}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Ehlers-Danlos syndrome 7A (EDS7A) [MIM:130060]: A
connective tissue disorder characterized by hyperextensible skin,
atrophic cutaneous scars due to tissue fragility and joint
hyperlaxity. Marked by bilateral congenital hip dislocation,
hyperlaxity of the joints, and recurrent partial dislocations.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Osteogenesis imperfecta 1 (OI1) [MIM:166200]: An
autosomal dominant form of osteogenesis imperfecta, a connective
tissue disorder characterized by low bone mass, bone fragility and
susceptibility to fractures after minimal trauma. Disease severity
ranges from very mild forms without fractures to intrauterine
fractures and perinatal lethality. Extraskeletal manifestations,
which affect a variable number of patients, are dentinogenesis
imperfecta, hearing loss, and blue sclerae. OI1 is a non-deforming
form with normal height or mild short stature, and no
dentinogenesis imperfecta. {ECO:0000269|PubMed:1634225,
ECO:0000269|PubMed:16638323, ECO:0000269|PubMed:16705691,
ECO:0000269|PubMed:16786509, ECO:0000269|PubMed:1718984,
ECO:0000269|PubMed:1737847, ECO:0000269|PubMed:17875077,
ECO:0000269|PubMed:18670065, ECO:0000269|PubMed:24682174,
ECO:0000269|PubMed:2794057, ECO:0000269|PubMed:3244312,
ECO:0000269|PubMed:8223589}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Osteogenesis imperfecta 2 (OI2) [MIM:166210]: An
autosomal dominant form of osteogenesis imperfecta, a connective
tissue disorder characterized by low bone mass, bone fragility and
susceptibility to fractures after minimal trauma. Disease severity
ranges from very mild forms without fractures to intrauterine
fractures and perinatal lethality. Extraskeletal manifestations,
which affect a variable number of patients, are dentinogenesis
imperfecta, hearing loss, and blue sclerae. OI2 is characterized
by bone fragility, with many perinatal fractures, severe bowing of
long bones, undermineralization, and death in the perinatal period
due to respiratory insufficiency. {ECO:0000269|PubMed:10627137,
ECO:0000269|PubMed:1460047, ECO:0000269|PubMed:1511982,
ECO:0000269|PubMed:1613761, ECO:0000269|PubMed:16566045,
ECO:0000269|PubMed:16786509, ECO:0000269|PubMed:18670065,
ECO:0000269|PubMed:1874719, ECO:0000269|PubMed:18996919,
ECO:0000269|PubMed:1939261, ECO:0000269|PubMed:1953667,
ECO:0000269|PubMed:2035536, ECO:0000269|PubMed:2036375,
ECO:0000269|PubMed:2037280, ECO:0000269|PubMed:2116413,
ECO:0000269|PubMed:2211725, ECO:0000269|PubMed:2339700,
ECO:0000269|PubMed:2470760, ECO:0000269|PubMed:25958000,
ECO:0000269|PubMed:2777764, ECO:0000269|PubMed:2794057,
ECO:0000269|PubMed:2913053, ECO:0000269|PubMed:3016737,
ECO:0000269|PubMed:3108247, ECO:0000269|PubMed:3403550,
ECO:0000269|PubMed:3667599, ECO:0000269|PubMed:7520724,
ECO:0000269|PubMed:7679635, ECO:0000269|PubMed:7691343,
ECO:0000269|PubMed:7961597, ECO:0000269|PubMed:8100209,
ECO:0000269|PubMed:8349697, ECO:0000269|PubMed:8349698,
ECO:0000269|PubMed:8364588, ECO:0000269|PubMed:8456808,
ECO:0000269|PubMed:8786074, ECO:0000269|PubMed:9143923,
ECO:0000269|Ref.47, ECO:0000269|Ref.50}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- DISEASE: Osteogenesis imperfecta 3 (OI3) [MIM:259420]: An
autosomal dominant form of osteogenesis imperfecta, a connective
tissue disorder characterized by low bone mass, bone fragility and
susceptibility to fractures after minimal trauma. Disease severity
ranges from very mild forms without fractures to intrauterine
fractures and perinatal lethality. Extraskeletal manifestations,
which affect a variable number of patients, are dentinogenesis
imperfecta, hearing loss, and blue sclerae. OI3 is characterized
by progressively deforming bones, very short stature, a triangular
face, severe scoliosis, grayish sclera and dentinogenesis
imperfecta. {ECO:0000269|PubMed:10408781,
ECO:0000269|PubMed:16879195, ECO:0000269|PubMed:1770532,
ECO:0000269|PubMed:18670065, ECO:0000269|PubMed:2037280,
ECO:0000269|PubMed:2511192, ECO:0000269|PubMed:2794057,
ECO:0000269|PubMed:7691343, ECO:0000269|PubMed:7881420,
ECO:0000269|PubMed:8019571, ECO:0000269|PubMed:8364588,
ECO:0000269|PubMed:8456809, ECO:0000269|PubMed:8669434,
ECO:0000269|PubMed:8723681, ECO:0000269|PubMed:9101304}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Osteogenesis imperfecta 4 (OI4) [MIM:166220]: An
autosomal dominant form of osteogenesis imperfecta, a connective
tissue disorder characterized by low bone mass, bone fragility and
susceptibility to fractures after minimal trauma. Disease severity
ranges from very mild forms without fractures to intrauterine
fractures and perinatal lethality. Extraskeletal manifestations,
which affect a variable number of patients, are dentinogenesis
imperfecta, hearing loss, and blue sclerae. OI4 is characterized
by moderately short stature, mild to moderate scoliosis, grayish
or white sclera and dentinogenesis imperfecta.
{ECO:0000269|PubMed:16786509, ECO:0000269|PubMed:16879195,
ECO:0000269|PubMed:1770532, ECO:0000269|PubMed:17875077,
ECO:0000269|PubMed:1988452, ECO:0000269|PubMed:2745420,
ECO:0000269|PubMed:7691343, ECO:0000269|PubMed:7982948,
ECO:0000269|PubMed:8094076, ECO:0000269|PubMed:8339541,
ECO:0000269|PubMed:9600458}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Osteoporosis (OSTEOP) [MIM:166710]: A systemic skeletal
disorder characterized by decreased bone mass and deterioration of
bone microarchitecture without alteration in the composition of
bone. The result is fragile bones and an increased risk of
fractures, even after minimal trauma. Osteoporosis is a chronic
condition of multifactorial etiology and is usually clinically
silent until a fracture occurs. {ECO:0000269|PubMed:8841196,
ECO:0000269|PubMed:9535665}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- DISEASE: Note=A chromosomal aberration involving COL1A1 is found
in dermatofibrosarcoma protuberans. Translocation
t(17;22)(q22;q13) with PDGF.
-!- SIMILARITY: Belongs to the fibrillar collagen family.
{ECO:0000255|PROSITE-ProRule:PRU00793}.
-!- SEQUENCE CAUTION:
Sequence=BAD92834.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Osteogenesis imperfecta variant database;
Note=Collagen type I alpha 1 (COL1A1);
URL="http://oi.gene.le.ac.uk/home.php?select_db=COL1A1";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/COL1A1ID186.html";
-!- WEB RESOURCE: Name=Wikipedia; Note=Type-I collagen entry;
URL="https://en.wikipedia.org/wiki/Type-I_collagen";
-----------------------------------------------------------------------
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EMBL; Z74615; CAA98968.1; -; mRNA.
EMBL; AF017178; AAB94054.3; -; Genomic_DNA.
EMBL; AB209597; BAD92834.1; ALT_INIT; mRNA.
EMBL; BC036531; AAH36531.1; -; mRNA.
EMBL; M20789; AAB59373.1; -; Genomic_DNA.
EMBL; M36546; AAA60150.1; -; mRNA.
EMBL; X07884; CAA30731.1; -; mRNA.
EMBL; X00820; CAA25394.1; -; Genomic_DNA.
EMBL; J02829; AAA51993.1; -; Genomic_DNA.
EMBL; M10627; AAA51992.1; -; Genomic_DNA.
EMBL; J03559; AAA52052.1; -; Genomic_DNA.
EMBL; K01228; AAA51995.1; -; mRNA.
EMBL; J00110; AAA52289.1; -; mRNA.
EMBL; J00111; AAA52290.1; -; mRNA.
EMBL; J00112; AAA52291.1; -; mRNA.
EMBL; J00113; AAN86574.1; -; mRNA.
EMBL; K03179; AAA51847.1; -; Genomic_DNA.
EMBL; M11162; AAA75386.1; -; Genomic_DNA.
EMBL; L47667; AAB59576.1; -; Genomic_DNA.
EMBL; S64596; AAB27856.1; -; mRNA.
EMBL; M23213; AAB59363.1; -; Genomic_DNA.
EMBL; X06269; CAA29605.1; -; mRNA.
EMBL; M32798; AAA52049.1; -; mRNA.
EMBL; M55998; AAA52036.1; -; Genomic_DNA.
CCDS; CCDS11561.1; -.
PIR; I60114; CGHU1S.
RefSeq; NP_000079.2; NM_000088.3.
UniGene; Hs.172928; -.
UniGene; Hs.681002; -.
PDB; 1Q7D; X-ray; 1.80 A; A/B/C=677-685.
PDB; 2LLP; NMR; -; A/B/C=949-965.
PDB; 3EJH; X-ray; 2.10 A; E/F=956-977.
PDB; 3GXE; X-ray; 2.60 A; E/F=254-275.
PDB; 5CTD; X-ray; 1.60 A; A=572-583, C=554-583.
PDB; 5CTI; X-ray; 1.90 A; A=572-583, C=554-583, C=611-665.
PDB; 5CVA; X-ray; 2.10 A; B/C/E/F=554-583, B/E=593-629.
PDB; 5CVB; X-ray; 2.25 A; A/D=572-583, B/C/E/F=554-583, B/E=593-606.
PDB; 5K31; X-ray; 2.20 A; A/B/C/D/E/F=1219-1464.
PDBsum; 1Q7D; -.
PDBsum; 2LLP; -.
PDBsum; 3EJH; -.
PDBsum; 3GXE; -.
PDBsum; 5CTD; -.
PDBsum; 5CTI; -.
PDBsum; 5CVA; -.
PDBsum; 5CVB; -.
PDBsum; 5K31; -.
ProteinModelPortal; P02452; -.
SMR; P02452; -.
BioGrid; 107674; 53.
CORUM; P02452; -.
DIP; DIP-36077N; -.
IntAct; P02452; 20.
STRING; 9606.ENSP00000225964; -.
ChEMBL; CHEMBL2364188; -.
DrugBank; DB00048; Collagenase clostridium histolyticum.
DrugBank; DB04866; Halofuginone.
iPTMnet; P02452; -.
PhosphoSitePlus; P02452; -.
BioMuta; COL1A1; -.
DMDM; 296439504; -.
DOSAC-COBS-2DPAGE; P02452; -.
EPD; P02452; -.
MaxQB; P02452; -.
PaxDb; P02452; -.
PeptideAtlas; P02452; -.
PRIDE; P02452; -.
DNASU; 1277; -.
Ensembl; ENST00000225964; ENSP00000225964; ENSG00000108821.
GeneID; 1277; -.
KEGG; hsa:1277; -.
UCSC; uc002iqm.4; human.
CTD; 1277; -.
DisGeNET; 1277; -.
EuPathDB; HostDB:ENSG00000108821.13; -.
GeneCards; COL1A1; -.
GeneReviews; COL1A1; -.
HGNC; HGNC:2197; COL1A1.
HPA; HPA008405; -.
HPA; HPA011795; -.
MalaCards; COL1A1; -.
MIM; 114000; phenotype.
MIM; 120150; gene.
MIM; 130000; phenotype.
MIM; 130060; phenotype.
MIM; 166200; phenotype.
MIM; 166210; phenotype.
MIM; 166220; phenotype.
MIM; 166710; phenotype.
MIM; 259420; phenotype.
MIM; 607907; phenotype.
neXtProt; NX_P02452; -.
Orphanet; 1310; Caffey disease.
Orphanet; 31112; Dermatofibrosarcoma protuberans.
Orphanet; 90309; Ehlers-Danlos syndrome type 1.
Orphanet; 99875; Ehlers-Danlos syndrome type 7A.
Orphanet; 230845; Ehlers-Danlos syndrome, vascular-like type.
Orphanet; 230857; Ehlers-Danlos/osteogenesis imperfecta syndrome.
Orphanet; 314029; High bone mass osteogenesis imperfecta.
Orphanet; 216796; Osteogenesis imperfecta type 1.
Orphanet; 216804; Osteogenesis imperfecta type 2.
Orphanet; 216812; Osteogenesis imperfecta type 3.
Orphanet; 216820; Osteogenesis imperfecta type 4.
PharmGKB; PA35041; -.
eggNOG; KOG3544; Eukaryota.
eggNOG; ENOG410XNMM; LUCA.
HOVERGEN; HBG004933; -.
InParanoid; P02452; -.
KO; K06236; -.
OrthoDB; EOG091G03LV; -.
PhylomeDB; P02452; -.
TreeFam; TF344135; -.
Reactome; R-HSA-114604; GPVI-mediated activation cascade.
Reactome; R-HSA-1442490; Collagen degradation.
Reactome; R-HSA-1474244; Extracellular matrix organization.
Reactome; R-HSA-1650814; Collagen biosynthesis and modifying enzymes.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-HSA-2022090; Assembly of collagen fibrils and other multimeric structures.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
Reactome; R-HSA-216083; Integrin cell surface interactions.
Reactome; R-HSA-2214320; Anchoring fibril formation.
Reactome; R-HSA-2243919; Crosslinking of collagen fibrils.
Reactome; R-HSA-3000170; Syndecan interactions.
Reactome; R-HSA-3000171; Non-integrin membrane-ECM interactions.
Reactome; R-HSA-3000178; ECM proteoglycans.
Reactome; R-HSA-3000480; Scavenging by Class A Receptors.
Reactome; R-HSA-430116; GP1b-IX-V activation signalling.
Reactome; R-HSA-75892; Platelet Adhesion to exposed collagen.
Reactome; R-HSA-76009; Platelet Aggregation (Plug Formation).
Reactome; R-HSA-8874081; MET activates PTK2 signaling.
Reactome; R-HSA-8940973; RUNX2 regulates osteoblast differentiation.
Reactome; R-HSA-8948216; Collagen chain trimerization.
SIGNOR; P02452; -.
ChiTaRS; COL1A1; human.
EvolutionaryTrace; P02452; -.
GeneWiki; Collagen,_type_I,_alpha_1; -.
GenomeRNAi; 1277; -.
PMAP-CutDB; P02452; -.
PRO; PR:P02452; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000108821; -.
ExpressionAtlas; P02452; baseline and differential.
Genevisible; P02452; HS.
GO; GO:0005584; C:collagen type I trimer; IDA:CAFA.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; IDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
GO; GO:0030141; C:secretory granule; IEA:Ensembl.
GO; GO:0005201; F:extracellular matrix structural constituent; IEA:Ensembl.
GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0048407; F:platelet-derived growth factor binding; IDA:MGI.
GO; GO:0002020; F:protease binding; IPI:CAFA.
GO; GO:0007596; P:blood coagulation; TAS:Reactome.
GO; GO:0001568; P:blood vessel development; IMP:UniProtKB.
GO; GO:0060346; P:bone trabecula formation; IEA:Ensembl.
GO; GO:0060351; P:cartilage development involved in endochondral bone morphogenesis; IEA:Ensembl.
GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEA:Ensembl.
GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEA:Ensembl.
GO; GO:1902618; P:cellular response to fluoride; IEA:Ensembl.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl.
GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
GO; GO:0071306; P:cellular response to vitamin E; IEA:Ensembl.
GO; GO:0032964; P:collagen biosynthetic process; IMP:UniProtKB.
GO; GO:0030574; P:collagen catabolic process; TAS:Reactome.
GO; GO:0030199; P:collagen fibril organization; IMP:UniProtKB.
GO; GO:0038063; P:collagen-activated tyrosine kinase receptor signaling pathway; IEA:Ensembl.
GO; GO:0048706; P:embryonic skeletal system development; IMP:UniProtKB.
GO; GO:0001958; P:endochondral ossification; IEA:Ensembl.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0060325; P:face morphogenesis; IEA:Ensembl.
GO; GO:0001957; P:intramembranous ossification; IEA:Ensembl.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0010812; P:negative regulation of cell-substrate adhesion; IEA:Ensembl.
GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
GO; GO:0030168; P:platelet activation; TAS:Reactome.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IDA:UniProtKB.
GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0070208; P:protein heterotrimerization; IEA:Ensembl.
GO; GO:0034504; P:protein localization to nucleus; IDA:UniProtKB.
GO; GO:0015031; P:protein transport; IEA:Ensembl.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
GO; GO:0031960; P:response to corticosteroid; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0042542; P:response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0055093; P:response to hyperoxia; IEA:Ensembl.
GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
GO; GO:0007605; P:sensory perception of sound; IMP:UniProtKB.
GO; GO:0001501; P:skeletal system development; IMP:UniProtKB.
GO; GO:0043589; P:skin morphogenesis; IMP:UniProtKB.
GO; GO:0044691; P:tooth eruption; IEA:Ensembl.
GO; GO:0034505; P:tooth mineralization; IMP:UniProtKB.
GO; GO:0007601; P:visual perception; IMP:UniProtKB.
Gene3D; 2.160.20.50; -; 10.
Gene3D; 3.90.215.10; -; 1.
InterPro; IPR008160; Collagen.
InterPro; IPR000885; Fib_collagen_C.
InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
InterPro; IPR016133; Insect_cyst_antifreeze_prot.
InterPro; IPR001007; VWF_dom.
Pfam; PF01410; COLFI; 1.
Pfam; PF01391; Collagen; 11.
Pfam; PF00093; VWC; 1.
ProDom; PD002078; Fib_collagen_C; 1.
SMART; SM00038; COLFI; 1.
SMART; SM00214; VWC; 1.
PROSITE; PS51461; NC1_FIB; 1.
PROSITE; PS01208; VWFC_1; 1.
PROSITE; PS50184; VWFC_2; 1.
1: Evidence at protein level;
3D-structure; Calcium; Chromosomal rearrangement; Collagen;
Complete proteome; Direct protein sequencing; Disease mutation;
Disulfide bond; Dwarfism; Ehlers-Danlos syndrome;
Extracellular matrix; Glycoprotein; Hydroxylation; Metal-binding;
Osteogenesis imperfecta; Phosphoprotein; Polymorphism;
Pyrrolidone carboxylic acid; Reference proteome; Repeat; Secreted;
Signal.
SIGNAL 1 22
PROPEP 23 161 N-terminal propeptide.
{ECO:0000269|PubMed:5529814}.
/FTId=PRO_0000005719.
CHAIN 162 1218 Collagen alpha-1(I) chain.
/FTId=PRO_0000005720.
PROPEP 1219 1464 C-terminal propeptide.
/FTId=PRO_0000005721.
DOMAIN 38 96 VWFC. {ECO:0000255|PROSITE-
ProRule:PRU00220}.
DOMAIN 1229 1464 Fibrillar collagen NC1.
{ECO:0000255|PROSITE-ProRule:PRU00793}.
REGION 162 178 Nonhelical region (N-terminal).
REGION 179 1192 Triple-helical region.
REGION 1193 1218 Nonhelical region (C-terminal).
MOTIF 745 747 Cell attachment site. {ECO:0000255}.
MOTIF 1093 1095 Cell attachment site. {ECO:0000255}.
METAL 1277 1277 Calcium. {ECO:0000250}.
METAL 1279 1279 Calcium. {ECO:0000250}.
METAL 1280 1280 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 1282 1282 Calcium; via carbonyl oxygen.
{ECO:0000250}.
METAL 1285 1285 Calcium. {ECO:0000250}.
SITE 161 162 Cleavage; by procollagen N-endopeptidase.
SITE 953 954 Cleavage; by collagenase. {ECO:0000250}.
SITE 1218 1219 Cleavage; by procollagen C-endopeptidase.
MOD_RES 162 162 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:5529814}.
MOD_RES 170 170 Allysine.
MOD_RES 171 171 Phosphoserine.
{ECO:0000250|UniProtKB:P02454}.
MOD_RES 190 190 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 193 193 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 196 196 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 205 205 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 208 208 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 211 211 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 226 226 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 241 241 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 247 247 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 256 256 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 262 262 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 265 265 5-hydroxylysine; alternate.
{ECO:0000269|PubMed:4319110}.
MOD_RES 271 271 Phosphoserine.
{ECO:0000250|UniProtKB:P02454}.
MOD_RES 289 289 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 292 292 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 298 298 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 307 307 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 313 313 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 334 334 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 343 343 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 346 346 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 373 373 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 376 376 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 388 388 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 394 394 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 403 403 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 409 409 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 412 412 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 427 427 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 430 430 5-hydroxylysine.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 436 436 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 439 439 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 451 451 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 460 460 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 475 475 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 481 481 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 490 490 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 496 496 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 505 505 5-hydroxylysine.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 514 514 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 523 523 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 529 529 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 535 535 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 544 544 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 547 547 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 556 556 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 565 565 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 571 571 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 583 583 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 592 592 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 601 601 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 604 604 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 622 622 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 640 640 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 646 646 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 652 652 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 658 658 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 664 664 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 670 670 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 682 682 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 691 691 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 703 703 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 715 715 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 718 718 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 724 724 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 730 730 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 739 739 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 751 751 5-hydroxylysine.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 757 757 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 772 772 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 778 778 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 787 787 Phosphoserine.
{ECO:0000250|UniProtKB:P02454}.
MOD_RES 799 799 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 805 805 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 808 808 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 817 817 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 823 823 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 841 841 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 850 850 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 859 859 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 862 862 5-hydroxylysine.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 871 871 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 877 877 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 885 885 3-hydroxyproline.
{ECO:0000250|UniProtKB:P11087}.
MOD_RES 886 886 4-hydroxyproline.
{ECO:0000250|UniProtKB:P11087}.
MOD_RES 895 895 4-hydroxyproline.
{ECO:0000250|UniProtKB:P11087}.
MOD_RES 898 898 4-hydroxyproline.
{ECO:0000250|UniProtKB:P11087}.
MOD_RES 919 919 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 928 928 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 937 937 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 946 946 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 964 964 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 973 973 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 976 976 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 982 982 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 997 997 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 1003 1003 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 1009 1009 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 1018 1018 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 1024 1024 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 1033 1033 5-hydroxylysine.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 1045 1045 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 1048 1048 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 1051 1051 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 1096 1096 5-hydroxylysine.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 1108 1108 5-hydroxylysine; alternate.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 1120 1120 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 1123 1123 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 1126 1126 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 1144 1144 4-hydroxyproline.
{ECO:0000250|UniProtKB:P02457}.
MOD_RES 1159 1159 4-hydroxyproline.
{ECO:0000250|UniProtKB:P11087}.
MOD_RES 1164 1164 3-hydroxyproline.
{ECO:0000250|UniProtKB:P11087}.
MOD_RES 1165 1165 4-hydroxyproline.
{ECO:0000250|UniProtKB:P11087}.
MOD_RES 1179 1179 3-hydroxyproline.
{ECO:0000250|UniProtKB:P11087}.
MOD_RES 1180 1180 4-hydroxyproline.
{ECO:0000250|UniProtKB:P11087}.
MOD_RES 1182 1182 3-hydroxyproline.
{ECO:0000250|UniProtKB:P11087}.
MOD_RES 1183 1183 4-hydroxyproline.
{ECO:0000250|UniProtKB:P11087}.
MOD_RES 1185 1185 3-hydroxyproline.
{ECO:0000250|UniProtKB:P11087}.
MOD_RES 1186 1186 4-hydroxyproline.
{ECO:0000250|UniProtKB:P11087}.
MOD_RES 1189 1189 4-hydroxyproline.
{ECO:0000250|UniProtKB:P11087}.
MOD_RES 1192 1192 4-hydroxyproline.
{ECO:0000250|UniProtKB:P11087}.
MOD_RES 1208 1208 Allysine. {ECO:0000250}.
CARBOHYD 265 265 O-linked (Gal...) hydroxylysine;
alternate. {ECO:0000269|PubMed:4319110}.
CARBOHYD 1108 1108 O-linked (Gal...) hydroxylysine;
alternate.
{ECO:0000250|UniProtKB:P02457}.
CARBOHYD 1365 1365 N-linked (GlcNAc...) asparagine.
DISULFID 1259 1291 {ECO:0000255|PROSITE-ProRule:PRU00793}.
DISULFID 1265 1265 Interchain. {ECO:0000255|PROSITE-
ProRule:PRU00793}.
DISULFID 1282 1282 Interchain. {ECO:0000255|PROSITE-
ProRule:PRU00793}.
DISULFID 1299 1462 {ECO:0000255|PROSITE-ProRule:PRU00793}.
DISULFID 1370 1415 {ECO:0000255|PROSITE-ProRule:PRU00793}.
VARIANT 22 22 G -> R (in OI2).
{ECO:0000269|PubMed:16786509}.
/FTId=VAR_063290.
VARIANT 146 146 P -> T (in OI2; rare variant; unknown
pathological significance).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_063291.
VARIANT 194 194 G -> R (in OI1).
{ECO:0000269|PubMed:16705691}.
/FTId=VAR_063292.
VARIANT 197 197 G -> C (in dbSNP:rs8179178).
/FTId=VAR_001642.
VARIANT 197 197 G -> R (in OI4).
{ECO:0000269|PubMed:16786509}.
/FTId=VAR_063293.
VARIANT 200 200 G -> V (in OI1; patient diagnosed with
OI1/OI4). {ECO:0000269|PubMed:18670065}.
/FTId=VAR_063294.
VARIANT 203 203 G -> V (in OI3).
{ECO:0000269|PubMed:16879195}.
/FTId=VAR_063295.
VARIANT 205 205 P -> A (in dbSNP:rs72667032).
{ECO:0000269|PubMed:16786509}.
/FTId=VAR_001643.
VARIANT 221 221 G -> C (in OI1; mild form).
{ECO:0000269|PubMed:1737847}.
/FTId=VAR_001644.
VARIANT 224 224 G -> C (in OI1; mild phenotype).
/FTId=VAR_001645.
VARIANT 242 242 G -> D (in OI).
{ECO:0000269|PubMed:16705691}.
/FTId=VAR_063296.
VARIANT 257 257 G -> R (in OI4).
{ECO:0000269|PubMed:16705691,
ECO:0000269|PubMed:16879195}.
/FTId=VAR_063297.
VARIANT 263 263 G -> R (in OI1; mild form).
{ECO:0000269|PubMed:1718984}.
/FTId=VAR_001646.
VARIANT 263 263 G -> V (in OI1; mild form).
{ECO:0000269|PubMed:8223589}.
/FTId=VAR_001647.
VARIANT 266 266 G -> E (in OI1).
{ECO:0000269|PubMed:17875077}.
/FTId=VAR_063298.
VARIANT 272 272 G -> C (in OI1).
{ECO:0000269|PubMed:2794057}.
/FTId=VAR_001648.
VARIANT 275 275 G -> D (in OI2).
/FTId=VAR_001649.
VARIANT 287 287 G -> S (in OI1).
{ECO:0000269|PubMed:17875077}.
/FTId=VAR_063299.
VARIANT 288 288 E -> K (in OI1; the patient also has
mutation Glu-1219; unknown pathological
significance).
{ECO:0000269|PubMed:16786509}.
/FTId=VAR_063300.
VARIANT 288 288 E -> V (in OI2; rare variant; unknown
pathological significance).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_063301.
VARIANT 312 312 R -> C (in EDS).
{ECO:0000269|PubMed:10739762,
ECO:0000269|PubMed:17211858}.
/FTId=VAR_013579.
VARIANT 320 320 G -> V (in OI1).
{ECO:0000269|PubMed:16786509}.
/FTId=VAR_063302.
VARIANT 332 332 G -> R (in OI3; mild to moderate form).
{ECO:0000269|PubMed:2037280,
ECO:0000269|PubMed:8669434}.
/FTId=VAR_001650.
VARIANT 338 338 G -> C (in OI4).
{ECO:0000269|PubMed:16786509}.
/FTId=VAR_063303.
VARIANT 349 349 V -> F (in OI1).
{ECO:0000269|PubMed:18670065}.
/FTId=VAR_063304.
VARIANT 350 350 G -> R (in OI3).
{ECO:0000269|PubMed:8019571}.
/FTId=VAR_001651.
VARIANT 353 353 G -> C (in OI4).
{ECO:0000269|PubMed:8339541}.
/FTId=VAR_001652.
VARIANT 353 353 G -> D (in OI2).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_063305.
VARIANT 353 353 G -> S (in OI4).
{ECO:0000269|PubMed:17875077}.
/FTId=VAR_063306.
VARIANT 356 356 G -> C (in OI4; mild form).
{ECO:0000269|PubMed:1988452}.
/FTId=VAR_001653.
VARIANT 368 368 G -> V (in OI2).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_063307.
VARIANT 383 383 G -> C (in OI4).
/FTId=VAR_001654.
VARIANT 389 389 G -> C (in OI; moderate form).
/FTId=VAR_001655.
VARIANT 389 389 G -> R (in OI2).
{ECO:0000269|PubMed:7520724}.
/FTId=VAR_001656.
VARIANT 390 390 A -> T (in OI2; rare variant; unknown
pathological significance;
dbSNP:rs116794104).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_063308.
VARIANT 398 398 G -> A (in OI4).
{ECO:0000269|PubMed:9600458}.
/FTId=VAR_001657.
VARIANT 398 398 G -> D (in OI2).
/FTId=VAR_001658.
VARIANT 401 401 G -> C (in OI4).
/FTId=VAR_001659.
VARIANT 404 404 G -> C (in OI; moderate form).
/FTId=VAR_001660.
VARIANT 422 422 G -> C (in OI2). {ECO:0000269|Ref.47}.
/FTId=VAR_001661.
VARIANT 425 425 G -> S (in OI2; lethal form).
{ECO:0000269|PubMed:18996919,
ECO:0000269|PubMed:7691343}.
/FTId=VAR_001662.
VARIANT 434 434 G -> V (in OI2).
{ECO:0000269|PubMed:1613761,
ECO:0000269|PubMed:2470760}.
/FTId=VAR_001663.
VARIANT 455 455 G -> D (in OI2).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_063309.
VARIANT 470 470 G -> V (in OI2).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_063310.
VARIANT 476 476 G -> R (in OI2; dbSNP:rs57377812).
/FTId=VAR_001664.
VARIANT 509 509 G -> V (in OI2).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_063311.
VARIANT 527 527 G -> C (in OI4).
{ECO:0000269|PubMed:9600458}.
/FTId=VAR_001665.
VARIANT 530 530 G -> S (in OI2, OI3 and OI4; mild to
lethal form).
{ECO:0000269|PubMed:7691343,
ECO:0000269|PubMed:8094076,
ECO:0000269|PubMed:8456809}.
/FTId=VAR_001666.
VARIANT 533 533 G -> D (in OI2).
/FTId=VAR_001667.
VARIANT 548 548 G -> A (in OI2).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_063312.
VARIANT 555 555 P -> R (in OI1).
{ECO:0000269|PubMed:16786509}.
/FTId=VAR_063313.
VARIANT 560 560 G -> C (in OI4).
/FTId=VAR_001669.
VARIANT 560 560 G -> R (in OI2).
/FTId=VAR_001670.
VARIANT 560 560 G -> S (in OI4).
{ECO:0000269|PubMed:7691343}.
/FTId=VAR_001668.
VARIANT 564 564 R -> H (in dbSNP:rs1800211).
/FTId=VAR_001671.
VARIANT 569 569 G -> R (in OI2).
{ECO:0000269|PubMed:3108247}.
/FTId=VAR_001672.
VARIANT 574 574 R -> C (found in a patient with isolated
osteopenia and vascular rupture; unknown
pathological significance).
{ECO:0000269|PubMed:17211858}.
/FTId=VAR_063314.
VARIANT 581 581 G -> R (in OI2).
{ECO:0000269|PubMed:16786509}.
/FTId=VAR_063315.
VARIANT 593 593 G -> C (in OI3 and OI4).
{ECO:0000269|PubMed:1770532}.
/FTId=VAR_001673.
VARIANT 593 593 G -> S (in OI2 and OI3; moderate to
lethal form).
{ECO:0000269|PubMed:8364588}.
/FTId=VAR_001674.
VARIANT 602 602 G -> R (in OI2).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_063316.
VARIANT 605 605 G -> D (in OI2).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_063317.
VARIANT 614 614 G -> R (in OI2).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_063318.
VARIANT 647 647 G -> S (in OI1).
{ECO:0000269|PubMed:16786509}.
/FTId=VAR_063319.
VARIANT 656 656 G -> S (in OI2).
{ECO:0000269|PubMed:10627137}.
/FTId=VAR_001676.
VARIANT 683 683 G -> S (in OI4).
{ECO:0000269|PubMed:16879195}.
/FTId=VAR_063320.
VARIANT 701 701 G -> C (in OI4).
{ECO:0000269|PubMed:9600458}.
/FTId=VAR_001677.
VARIANT 704 704 G -> C (in OI3).
{ECO:0000269|PubMed:2794057}.
/FTId=VAR_001678.
VARIANT 719 719 G -> D (in OI2).
{ECO:0000269|PubMed:2035536}.
/FTId=VAR_001679.
VARIANT 719 719 G -> S (in OI3).
{ECO:0000269|PubMed:7691343}.
/FTId=VAR_001680.
VARIANT 722 722 G -> S (in OI1).
{ECO:0000269|PubMed:16705691}.
/FTId=VAR_063321.
VARIANT 728 728 G -> R (in OI2).
{ECO:0000269|PubMed:2339700}.
/FTId=VAR_001681.
VARIANT 734 734 G -> V (in OI2).
{ECO:0000269|PubMed:16786509}.
/FTId=VAR_063322.
VARIANT 737 737 G -> D (in OI2).
/FTId=VAR_001682.
VARIANT 740 740 G -> R (in OI2).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_063323.
VARIANT 743 743 G -> S (in OI2).
/FTId=VAR_001683.
VARIANT 743 743 G -> V (in OI2).
{ECO:0000269|PubMed:8100209}.
/FTId=VAR_001684.
VARIANT 764 764 G -> V (in OI2).
{ECO:0000269|PubMed:9143923}.
/FTId=VAR_001685.
VARIANT 767 767 G -> S (in OI3; severe).
{ECO:0000269|PubMed:16705691,
ECO:0000269|PubMed:7881420}.
/FTId=VAR_001686.
VARIANT 773 773 G -> C (in OI2; de novo mutation).
{ECO:0000269|PubMed:25958000}.
/FTId=VAR_074158.
VARIANT 776 776 G -> S (in OI2).
{ECO:0000269|PubMed:2116413}.
/FTId=VAR_001687.
VARIANT 809 809 G -> S (in OI2).
{ECO:0000269|PubMed:18996919,
ECO:0000269|PubMed:2116413}.
/FTId=VAR_001688.
VARIANT 815 815 G -> V (in OI2).
{ECO:0000269|PubMed:1874719}.
/FTId=VAR_001689.
VARIANT 821 821 G -> S (in OI3).
{ECO:0000269|PubMed:16705691,
ECO:0000269|PubMed:16879195,
ECO:0000269|PubMed:9101304}.
/FTId=VAR_001690.
VARIANT 823 823 P -> A (in dbSNP:rs1800214).
{ECO:0000269|PubMed:7691343}.
/FTId=VAR_001691.
VARIANT 824 824 G -> R (in OI2).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_063324.
VARIANT 833 833 G -> D (in OI2).
{ECO:0000269|PubMed:16566045}.
/FTId=VAR_063325.
VARIANT 839 839 G -> S (in OI2; mild to moderate form).
{ECO:0000269|PubMed:8786074}.
/FTId=VAR_001692.
VARIANT 842 842 G -> R (in OI2).
{ECO:0000269|PubMed:3403550}.
/FTId=VAR_001693.
VARIANT 845 845 G -> R (in OI2).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_001694.
VARIANT 848 848 G -> R (in OI2).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_063342.
VARIANT 851 851 G -> D (in OI2).
/FTId=VAR_001695.
VARIANT 855 855 N -> H (in OI2; rare variant; unknown
pathological significance).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_063326.
VARIANT 866 866 G -> S (in OI3 and OI2).
{ECO:0000269|PubMed:10408781,
ECO:0000269|PubMed:18670065,
ECO:0000269|PubMed:18996919}.
/FTId=VAR_008118.
VARIANT 869 869 G -> C (in OI2).
{ECO:0000269|PubMed:1953667}.
/FTId=VAR_001696.
VARIANT 875 875 G -> S (in OI2).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_063327.
VARIANT 884 884 G -> S (in OI2 and OI3; extremely severe
form). {ECO:0000269|PubMed:18996919}.
/FTId=VAR_001697.
VARIANT 896 896 G -> C (in OI2).
{ECO:0000269|PubMed:2794057}.
/FTId=VAR_001698.
VARIANT 896 896 G -> D (in OI2).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_063328.
VARIANT 906 906 G -> S (found in a patient with mild
osteogenesis imperfecta; uncertain
pathological significance).
{ECO:0000269|PubMed:16786509}.
/FTId=VAR_063329.
VARIANT 926 926 G -> C (in OI2).
{ECO:0000269|PubMed:2036375,
ECO:0000269|PubMed:3667599}.
/FTId=VAR_001699.
VARIANT 947 947 G -> C (in OI2).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_063330.
VARIANT 977 977 G -> D (in OI2).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_063331.
VARIANT 980 980 G -> V (in OI2).
{ECO:0000269|PubMed:1511982}.
/FTId=VAR_001700.
VARIANT 1001 1001 G -> C (in OI2).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_063332.
VARIANT 1010 1010 G -> S (in OI4).
{ECO:0000269|PubMed:2745420}.
/FTId=VAR_001701.
VARIANT 1014 1014 R -> C (in CAFFD).
{ECO:0000269|PubMed:15864348}.
/FTId=VAR_033097.
VARIANT 1019 1019 G -> A (in dbSNP:rs1135348).
{ECO:0000269|PubMed:6689127,
ECO:0000269|Ref.1}.
/FTId=VAR_030013.
VARIANT 1022 1022 G -> S (in OI3; severe form).
{ECO:0000269|PubMed:2511192}.
/FTId=VAR_001702.
VARIANT 1022 1022 G -> V (in OI2).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_001703.
VARIANT 1025 1025 G -> R (in OI2).
{ECO:0000269|PubMed:2211725}.
/FTId=VAR_001704.
VARIANT 1040 1040 G -> S (in OI2 and OI3; moderate to
lethal form).
{ECO:0000269|PubMed:18670065,
ECO:0000269|PubMed:9101304}.
/FTId=VAR_001705.
VARIANT 1043 1043 G -> S (in OI2).
/FTId=VAR_001706.
VARIANT 1046 1048 Missing (in OI2).
{ECO:0000269|PubMed:1460047,
ECO:0000269|PubMed:1939261}.
/FTId=VAR_001707.
VARIANT 1049 1049 G -> S (in OI3).
{ECO:0000269|PubMed:9101304}.
/FTId=VAR_001708.
VARIANT 1052 1052 G -> GAPG (in OI2).
/FTId=VAR_063333.
VARIANT 1055 1055 G -> D (in OI2).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_063334.
VARIANT 1058 1058 G -> S (in OI3 and OI4; mild form).
{ECO:0000269|PubMed:16705691,
ECO:0000269|PubMed:9101304}.
/FTId=VAR_001709.
VARIANT 1061 1061 G -> D (in OI2).
/FTId=VAR_001710.
VARIANT 1061 1061 G -> S (in OI4).
{ECO:0000269|PubMed:7982948}.
/FTId=VAR_001711.
VARIANT 1066 1066 R -> C (probable disease-associated
mutation found in a patient with
overlapping features of osteogenesis
imperfecta and Ehlers-Danlos syndrome;
affects dimer formation, helix stability
and organization of collagen fibrils).
{ECO:0000269|PubMed:17206620}.
/FTId=VAR_063335.
VARIANT 1075 1075 T -> A (in dbSNP:rs1800215).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:18272325,
ECO:0000269|PubMed:1870989,
ECO:0000269|PubMed:18996919,
ECO:0000269|PubMed:1995349,
ECO:0000269|PubMed:6689127,
ECO:0000269|PubMed:9443882,
ECO:0000269|Ref.1, ECO:0000269|Ref.24,
ECO:0000269|Ref.4}.
/FTId=VAR_001712.
VARIANT 1076 1076 G -> S (in OI3; severe form).
{ECO:0000269|PubMed:9101304}.
/FTId=VAR_001713.
VARIANT 1079 1079 G -> S (in OI1 and OI2; mild to moderate
form). {ECO:0000269|PubMed:1634225}.
/FTId=VAR_001714.
VARIANT 1082 1082 G -> C (in OI2).
{ECO:0000269|PubMed:2913053}.
/FTId=VAR_001715.
VARIANT 1088 1088 G -> A (in OI2).
{ECO:0000269|PubMed:7679635}.
/FTId=VAR_001716.
VARIANT 1088 1088 G -> E (in OI1; de novo mutation; unknown
pathological significance).
{ECO:0000269|PubMed:24682174}.
/FTId=VAR_074159.
VARIANT 1091 1091 G -> S (in OI2). {ECO:0000269|Ref.50}.
/FTId=VAR_001717.
VARIANT 1093 1093 R -> C (found in a patient with isolated
osteopenia and vascular rupture; unknown
pathological significance).
{ECO:0000269|PubMed:17211858}.
/FTId=VAR_063336.
VARIANT 1094 1094 G -> S (in OI2).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_063337.
VARIANT 1100 1100 G -> D (in OI2).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_001718.
VARIANT 1106 1106 G -> A (in OI2).
{ECO:0000269|PubMed:2777764}.
/FTId=VAR_001719.
VARIANT 1124 1124 G -> C (in OI2).
{ECO:0000269|PubMed:7961597}.
/FTId=VAR_001720.
VARIANT 1141 1141 R -> Q (in dbSNP:rs41316713).
{ECO:0000269|PubMed:18272325}.
/FTId=VAR_033778.
VARIANT 1142 1142 G -> S (in OI2).
/FTId=VAR_001721.
VARIANT 1151 1151 G -> S (in OI3).
/FTId=VAR_001722.
VARIANT 1151 1151 G -> V (in OI2).
{ECO:0000269|PubMed:1613761,
ECO:0000269|PubMed:2777764}.
/FTId=VAR_001723.
VARIANT 1154 1154 G -> R (in OI2).
{ECO:0000269|PubMed:2777764}.
/FTId=VAR_001724.
VARIANT 1157 1157 G -> D (in OI1).
{ECO:0000269|PubMed:16638323}.
/FTId=VAR_063338.
VARIANT 1166 1166 G -> C (in OI2).
{ECO:0000269|PubMed:3016737}.
/FTId=VAR_001725.
VARIANT 1172 1172 G -> D (in OI2).
{ECO:0000269|PubMed:10627137}.
/FTId=VAR_001726.
VARIANT 1177 1177 V -> I (in dbSNP:rs41316719).
{ECO:0000269|PubMed:18272325}.
/FTId=VAR_033779.
VARIANT 1181 1181 G -> S (in OI2).
{ECO:0000269|PubMed:2037280,
ECO:0000269|Ref.50}.
/FTId=VAR_001727.
VARIANT 1184 1184 G -> V (in OI2).
{ECO:0000269|PubMed:1613761,
ECO:0000269|PubMed:2777764}.
/FTId=VAR_001728.
VARIANT 1187 1187 G -> S (in OI2 and OI3; extremely severe
form). {ECO:0000269|Ref.50}.
/FTId=VAR_001729.
VARIANT 1187 1187 G -> V (in OI2). {ECO:0000269|Ref.50}.
/FTId=VAR_001730.
VARIANT 1195 1195 G -> C (in OI1; mild form).
{ECO:0000269|PubMed:3170557,
ECO:0000269|PubMed:3244312}.
/FTId=VAR_001731.
VARIANT 1219 1219 D -> E (in OI1).
{ECO:0000269|PubMed:16786509}.
/FTId=VAR_063339.
VARIANT 1219 1219 D -> N (found in a patient with mild
osteogenesis imperfecta associated with
increased bone mineral density; results
in defective type I procollagen
processing; incorporation of the immature
procollagen into the matrix leads to
increased bone matrix mineralization and
altered collagen fibril structure).
{ECO:0000269|PubMed:21344539}.
/FTId=VAR_066385.
VARIANT 1251 1251 S -> T (in dbSNP:rs3205325).
{ECO:0000269|PubMed:8349697}.
/FTId=VAR_030014.
VARIANT 1277 1277 D -> H (in OI2; impaired pro-alpha chain
association).
{ECO:0000269|PubMed:8349697}.
/FTId=VAR_001732.
VARIANT 1312 1312 W -> C (in OI2).
{ECO:0000269|PubMed:8456808}.
/FTId=VAR_001733.
VARIANT 1337 1338 Missing (in OI2; impaired pro-alpha chain
association).
{ECO:0000269|PubMed:8349697}.
/FTId=VAR_001734.
VARIANT 1356 1356 R -> H. {ECO:0000269|PubMed:16786509}.
/FTId=VAR_063340.
VARIANT 1388 1388 L -> R (in OI2; impaired pro-alpha chain
association).
{ECO:0000269|PubMed:8349697}.
/FTId=VAR_001735.
VARIANT 1391 1391 Q -> K (in dbSNP:rs2586486).
{ECO:0000269|PubMed:3340531,
ECO:0000269|PubMed:9443882,
ECO:0000269|Ref.1}.
/FTId=VAR_030015.
VARIANT 1413 1413 D -> N (in OI2).
{ECO:0000269|PubMed:16786509,
ECO:0000269|PubMed:18996919}.
/FTId=VAR_063341.
VARIANT 1430 1430 K -> N (in dbSNP:rs1059454).
/FTId=VAR_033780.
VARIANT 1431 1431 T -> P (in dbSNP:rs1059454).
/FTId=VAR_033781.
VARIANT 1434 1434 T -> S (in dbSNP:rs1800220).
{ECO:0000269|PubMed:8349697,
ECO:0000269|Ref.1}.
/FTId=VAR_001736.
VARIANT 1438 1438 P -> R (in dbSNP:rs17857117).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_030016.
VARIANT 1460 1460 P -> H (in dbSNP:rs17853657).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_030017.
VARIANT 1464 1464 L -> P (in OI3).
{ECO:0000269|PubMed:8723681}.
/FTId=VAR_001737.
CONFLICT 59 59 R -> Q (in Ref. 8; CAA25394).
{ECO:0000305}.
CONFLICT 112 114 Missing (in Ref. 2; AAB94054).
{ECO:0000305}.
CONFLICT 288 288 E -> P (in Ref. 15; AA sequence).
{ECO:0000305}.
CONFLICT 370 370 R -> L (in Ref. 6; AAB59373).
{ECO:0000305}.
CONFLICT 484 484 P -> L (in Ref. 19; AAA52289).
{ECO:0000305}.
CONFLICT 595 595 A -> R (in Ref. 20; AAA51847).
{ECO:0000305}.
CONFLICT 721 721 Q -> E (in Ref. 22; no nucleotide entry).
{ECO:0000305}.
CONFLICT 738 738 L -> E (in Ref. 22; no nucleotide entry).
{ECO:0000305}.
CONFLICT 975 976 LP -> PL (in Ref. 19; AAA52291).
{ECO:0000305}.
CONFLICT 1081 1081 V -> A (in Ref. 18; AAA51995).
{ECO:0000305}.
CONFLICT 1329 1329 S -> T (in Ref. 25; AAB27856).
{ECO:0000305}.
STRAND 264 266 {ECO:0000244|PDB:3GXE}.
STRAND 966 968 {ECO:0000244|PDB:3EJH}.
HELIX 1227 1246 {ECO:0000244|PDB:5K31}.
STRAND 1251 1254 {ECO:0000244|PDB:5K31}.
HELIX 1259 1265 {ECO:0000244|PDB:5K31}.
STRAND 1271 1276 {ECO:0000244|PDB:5K31}.
HELIX 1283 1285 {ECO:0000244|PDB:5K31}.
STRAND 1287 1292 {ECO:0000244|PDB:5K31}.
TURN 1293 1296 {ECO:0000244|PDB:5K31}.
STRAND 1297 1300 {ECO:0000244|PDB:5K31}.
STRAND 1306 1310 {ECO:0000244|PDB:5K31}.
HELIX 1326 1329 {ECO:0000244|PDB:5K31}.
HELIX 1345 1357 {ECO:0000244|PDB:5K31}.
STRAND 1362 1372 {ECO:0000244|PDB:5K31}.
TURN 1379 1382 {ECO:0000244|PDB:5K31}.
STRAND 1389 1391 {ECO:0000244|PDB:5K31}.
STRAND 1397 1403 {ECO:0000244|PDB:5K31}.
STRAND 1409 1413 {ECO:0000244|PDB:5K31}.
STRAND 1420 1432 {ECO:0000244|PDB:5K31}.
HELIX 1434 1436 {ECO:0000244|PDB:5K31}.
STRAND 1441 1443 {ECO:0000244|PDB:5K31}.
STRAND 1453 1463 {ECO:0000244|PDB:5K31}.
SEQUENCE 1464 AA; 138941 MW; F0EC4DE778FFFC11 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 PAGPTGPVGP
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


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