[1]	NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ALA-1019; LYS-1391 AND SER-1434. Dalgleish R.; Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LYS-1391. DOI=10.1086/301689; PubMed=9443882 [NCBI, ExPASy, EBI, Israel, Japan] 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]. 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 ARG-1438 AND HIS-1460. TISSUE=Brain; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1016/0378-1119(88)90013-3; PubMed=2843432 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1038/310337a0; PubMed=6462220 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1073/pnas.84.24.8869; PubMed=3480516 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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; DOI=10.1021/bi00826a012; PubMed=5529814 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1111/j.1432-1033.1990.tb19208.x; PubMed=2169412 [NCBI, ExPASy, EBI, Israel, Japan] 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. TISSUE=Skin; PubMed=4319110 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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 VARIANT ALA-1019. DOI=10.1021/bi00291a023; PubMed=6689127 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1093/nar/10.19.5925; PubMed=6183642 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1073/pnas.82.9.2870; PubMed=3857621 [NCBI, ExPASy, EBI, Israel, Japan] 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 OI-II ARG-728. PubMed=2339700 [NCBI, ExPASy, EBI, Israel, Japan] 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 OI-III SER-767. DOI=10.1093/hmg/3.12.2201; PubMed=7881420 [NCBI, ExPASy, EBI, Israel, Japan] 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, AND MASS SPECTROMETRY. TISSUE=Fetal brain cortex; Lubec G., Chen W.-Q., Sun Y.; Submitted (DEC-2008) to UniProtKB.
[25]	NUCLEOTIDE SEQUENCE [MRNA] OF 1179-1464, VARIANTS OI-II HIS-1277; ARG-1388 AND 1337-GLU-TYR-1338 DEL, AND VARIANTS THR-1251 AND SER-1434. PubMed=8349697 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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; DOI=10.1093/nar/16.1.349; PubMed=3340531 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1016/0014-5793(91)80237-W; PubMed=1995349 [NCBI, ExPASy, EBI, Israel, Japan] 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 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1002/(SICI)1098-1004(1997)9:4<300::AID-HUMU2>3.3.CO;2-8; PubMed=9101290 [NCBI, ExPASy, EBI, Israel, Japan] 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 OI VARIANTS. PubMed=1895312 [NCBI, ExPASy, EBI, Israel, Japan] Byers P.H., Wallis G.A., Willing M.C.; "Osteogenesis imperfecta: translation of mutation to phenotype."; J. Med. Genet. 28:433-442(1991).
[33]	VARIANT OI-II CYS-1166. DOI=10.1073/pnas.83.16.6045; PubMed=3016737 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[34]	VARIANT OI-II ARG-569. PubMed=3108247 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[35]	VARIANT OI-II CYS-926. PubMed=3667599 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[36]	VARIANT OI-II ARG-842. PubMed=3403550 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[37]	VARIANT OI CYS-1195. PubMed=3244312 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[38]	VARIANT OI-II VAL-434. PubMed=2470760 [NCBI, ExPASy, EBI, Israel, Japan] Patterson E., Smiley E., Bonadio J.; "RNA sequence analysis of a perinatal lethal osteogenesis imperfecta mutation."; J. Biol. Chem. 264:10083-10087(1989).
[39]	VARIANT OI-IV SER-1010. PubMed=2745420 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[40]	VARIANTS OI-II ALA-1106; VAL-1151; ARG-1154 AND VAL-1184. PubMed=2777764 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[41]	VARIANT OI SER-1022. PubMed=2511192 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[42]	VARIANT OI-II CYS-1082. PubMed=2913053 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[43]	VARIANTS OI CYS-272; CYS-704 AND CYS-896. PubMed=2794057 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[44]	VARIANT OI-II 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 effets on protein function or phenotype."; Am. J. Hum. Genet. 47:A216-A216(1990).
[45]	VARIANTS OI-II SER-776 AND SER-809. PubMed=2116413 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[46]	VARIANT OI-II ARG-1025. PubMed=2211725 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[47]	VARIANTS OI-II 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).
[48]	VARIANT OI-II ASP-719. PubMed=2035536 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[49]	VARIANT OI-II CYS-869. PubMed=1953667 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[50]	VARIANT OI-II CYS-926. DOI=10.1021/bi00234a035; PubMed=2036375 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[51]	VARIANT OI-III ARG-332, AND VARIANT OI-II SER-1181. DOI=10.1007/BF01213088; PubMed=2037280 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[52]	VARIANT OI CYS-356. PubMed=1988452 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[53]	VARIANT OI-II VAL-815. PubMed=1874719 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[54]	VARIANT OI-I ARG-263. PubMed=1718984 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[55]	VARIANT OI-II 1046-GLY--PRO-1048 DEL. PubMed=1939261 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[56]	VARIANT OI-III/IV CYS-593. PubMed=1770532 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[57]	VARIANT THR-1075. DOI=10.1093/nar/19.15.4302; PubMed=1870989 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[58]	VARIANT OI-I SER-1079. DOI=10.1007/BF00219169; PubMed=1634225 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[59]	VARIANT OI-II VAL-980. DOI=10.1007/BF00221955; PubMed=1511982 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[60]	VARIANT OI-II 1046-GLY--PRO-1048 DEL. PubMed=1460047 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[61]	VARIANT OI CYS-221. PubMed=1737847 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[62]	VARIANTS OI-II VAL-434; VAL-1151 AND VAL-1184. PubMed=1613761 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[63]	VARIANT OI-II CYS-1312. DOI=10.1002/ajmg.1320450216; PubMed=8456808 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[64]	VARIANT OI-III SER-530. DOI=10.1002/ajmg.1320450217; PubMed=8456809 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[65]	VARIANT OI-IV CYS-353. PubMed=8339541 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[66]	VARIANT OI-II ALA-1088. DOI=10.1111/j.1432-1033.1993.tb17565.x; PubMed=7679635 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[67]	VARIANT OI VAL-263. DOI=10.1111/j.1432-1033.1993.tb18220.x; PubMed=8223589 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[68]	VARIANT OI-II VAL-743. DOI=10.1007/BF00217768; PubMed=8100209 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[69]	VARIANTS OI SER-425; SER-530; SER-560 AND SER-719, AND VARIANT ALA-823. DOI=10.1093/hmg/2.8.1155; PubMed=7691343 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[70]	VARIANT OI-II/III SER-593. DOI=10.1002/humu.1380020308; PubMed=8364588 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[71]	VARIANT OI-IV SER-530. PubMed=8094076 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[72]	VARIANTS OI-II. PubMed=8349698 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[73]	VARIANT OI-II ARG-389. DOI=10.1016/8756-3282(94)90295-X; PubMed=7520724 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[74]	VARIANT OI-III ARG-350. DOI=10.1002/humu.1380030327; PubMed=8019571 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[75]	VARIANT OI-II CYS-1124. PubMed=7961597 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[76]	VARIANT OI-IV SER-1061. PubMed=7982948 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[77]	VARIANT OI-III ARG-332. DOI=10.1002/(SICI)1096-8628(19960111)61:2<111::AID-AJMG1>3.0.CO;2-#; PubMed=8669434 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[78]	VARIANT OI-II SER-839. DOI=10.1007/s004390050043; PubMed=8786074 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[79]	VARIANT OI-III PRO-1464. DOI=10.1002/(SICI)1098-1004(1996)7:4<318::AID-HUMU5>3.3.CO;2-S; PubMed=8723681 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[80]	INVOLVEMENT IN INVOLUTIONAL OSTEOPOROSIS. DOI=10.1038/ng1096-203; PubMed=8841196 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[81]	VARIANTS OI SER-821; SER-1040; SER-1049; SER-1058 AND SER-1076. DOI=10.1002/(SICI)1098-1004(1997)9:4<378::AID-HUMU16>3.3.CO;2-5; PubMed=9101304 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[82]	VARIANT OI-II VAL-764. DOI=10.1002/(SICI)1098-1004(1997)9:5<431::AID-HUMU9>3.3.CO;2-C; PubMed=9143923 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[83]	VARIANTS OI-IV ALA-398; CYS-527 AND CYS-701. DOI=10.1002/(SICI)1098-1004(1998)11:5<395::AID-HUMU7>3.3.CO;2-W; PubMed=9600458 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[84]	VARIANTS OI-II SER-656 AND ASP-1172. DOI=10.1002/(SICI)1098-1004(1998)12:1<71::AID-HUMU16>3.3.CO;2-W; PubMed=10627137 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[85]	INVOLVEMENT IN INVOLUTIONAL OSTEOPOROSIS. DOI=10.1056/NEJM199804093381502; PubMed=9535665 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[86]	VARIANT OI-III SER-866. DOI=10.1002/(SICI)1098-1004(1999)13:6<503::AID-HUMU11>3.0.CO;2-L; PubMed=10408781 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[87]	VARIANT EDS1 CYS-312. DOI=10.1086/302859; PubMed=10739762 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[88]	DISEASE, AND CHROMOSOMAL TRANSLOCATION WITH PDGFB. DOI=10.1038/ng0197-95; PubMed=8988177 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[89]	DISEASE, AND CHROMOSOMAL TRANSLOCATION WITH PDGFB. DOI=10.1016/S0165-4608(02)00844-0; PubMed=12660034 [NCBI, ExPASy, EBI, Israel, Japan] Sandberg A.A., Anderson W.D., Fredenberg C., Hashimoto H.; "Dermatofibrosarcoma protuberans of breast."; Cancer Genet. Cytogenet. 142:56-59(2003).
[90]	VARIANT CAFFEY DISEASE CYS-1014. DOI=10.1172/JCI200522760; PubMed=15864348 [NCBI, ExPASy, EBI, Israel, Japan] 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).

Comments

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).
INTERACTION:
Q5YB85:- (xeno); NbExp=1; IntAct=EBI-982999, EBI-982988;
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix (By similarity).
TISSUE SPECIFICITY: Forms the fibrils of tendon, ligaments and bones. In bones the fibrils are mineralized with calcium hydroxyapatite.
PTM: Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
PTM: O-linked glycan consists of a Glc-Gal disaccharide bound to the oxygen atom of a post-translationally added hydroxyl group.
DISEASE: Defects in COL1A1 are the cause of Caffey disease [MIM:114000]; also known as infantile cortical hyperostosis. Caffey disease is 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.
DISEASE: Defects in COL1A1 are a cause of Ehlers-Danlos syndrome type 1 (EDS1) [MIM:130000]; also known as Ehlers-Danlos syndrome gravis. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS1 is the severe form of classic Ehlers-Danlos syndrome.
DISEASE: Defects in COL1A1 are the cause of Ehlers-Danlos syndrome type 7A (EDS7A) [MIM:130060]; also known as autosomal dominant Ehlers-Danlos syndrome type VII. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS7A is marked by bilateral congenital hip dislocation, hyperlaxity of the joints, and recurrent partial dislocations.
DISEASE: Defects in COL1A1 are a cause of osteogenesis imperfecta type I (OI-I) [MIM:166200]. OI-I is a dominantly inherited serious newborn disease characterized by bone fragility, normal stature, little or no deformity, blue sclerae and hearing loss in 50% of families. Dentinogenesis imperfecta is rare and may distinguish a subset of OI type I (formation of dentine).
DISEASE: Defects in COL1A1 are a cause of osteogenesis imperfecta type II (OI-II) [MIM:166210]; also known as osteogenesis imperfecta congenita. OI-II is lethal in the perinatal period and is charaterized by calvarial mineralization, beaded ribs, compressed femurs, marked long bone deformity and platyspondyly (congenital flattening of the vertebral bodies).
DISEASE: Defects in COL1A1 are a cause of osteogenesis imperfecta type III (OI-III) [MIM:259420]; also called progressively deforming osteogenesis imperfecta with normal sclerae. OI-III is characterized by progressively deforming bones, usually with moderate deformity at birth, sclerae is variable in color, dentinogenesis imperfecta and hearing loss are common. The stature is very short.
DISEASE: Defects in COL1A1 are a cause of osteogenesis imperfecta type IV (OI-IV) [MIM:166220]. OI-IV is charaterized by normal sclerae, moderate to mild deformity and variable short stature. Dentinogenesis imperfecta is common and hearing loss occurs in some patients.
DISEASE: Genetic variations in COL1A1 are associated with susceptibility to involutional osteoporosis [MIM:166710]; also known as senile osteoporosis or postmenopausal osteoporosis. Osteoporosis is characterized by reduced bone mineral density, disrutption of bone microarchitecture, and the alteration of the amount and variety of non-collagenous proteins in bone. Osteoporotic bones are more at risk of fracture.
DISEASE: A chromosomal aberration involving COL1A1 is a cause of dermatofibrosarcoma protuberans (DFSP) [MIM:607907]. Translocation t(17;22)(q22;q13) with PDGF. DFSP is an uncommon, locally aggressive, but rarely metastasizing tumor of the deep dermis and subcutaneous tissue. It typically occurs during early or middle adult life and is most frequently located on the trunk and proximal extremities.
SIMILARITY: Belongs to the fibrillar collagen family.
SIMILARITY: Contains 1 VWFC domain.
WEB RESOURCE: Name=COL1A1; Note=Collagen type I alpha-1 chain mutations; URL="http://www.le.ac.uk/genetics/collagen/col1a1.html";.
WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/COL1A1ID186.html";.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=COL1A1";.
WEB RESOURCE: Name=Wikipedia; Note=Type-I collagen entry; URL="http://en.wikipedia.org/wiki/Type-I_collagen";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

Z74615; CAA98968.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF017178; AAB94054.3; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB209597; BAD92834.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC036531; AAH36531.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M20789; AAB59373.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M36546; AAA60150.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X07884; CAA30731.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X00820; CAA25394.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J02829; AAA51993.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M10627; AAA51992.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J03559; AAA52052.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
K01228; AAA51995.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J00110; AAA52289.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J00111; AAA52290.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J00112; AAA52291.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
J00113; AAN86574.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
K03179; AAA51847.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M11162; AAA75386.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L47667; AAB59576.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S64596; AAB27856.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M23213; AAB59363.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X06269; CAA29605.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M32798; AAA52049.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M55998; AAA52036.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00297646; -.

I60114; CGHU1S.

NP_000079.2; -.

3D structure databases

PDB

1Q7D; X-ray; 1.80 A; A/B/C=914-930.	[ExPASy / RCSB / EBI]
3EJH; X-ray; 2.10 A; E/F=956-977.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1Q7D; -.
3EJH; -.

ModBase

P02452.

Protein-protein interaction databases

IntAct

P02452; 1.

PTM databases

PhosphoSite

P02452; -.

Enzyme and pathway databases

Pathway_Interaction_DB

il4_2pathway; IL4-mediated signaling events.
lymphangiogenesis_pathway; VEGFR3 signaling in lymphatic endothelium.

Reactome

REACT_13552; Integrin cell surface interactions.
REACT_604; Hemostasis.
REACT_6900; Signaling in Immune system.

2D gel databases

DOSAC-COBS-2DPAGE

P02452; -.

Siena-2DPAGE

P02452; -.

Organism-specific databases

GC17M045617; -.

HIX0016617; -.

HGNC:2197; COL1A1.

HPA008405; -.
HPA011795; -.

MIM

114000; phenotype. [NCBI / EBI]
120150; gene. [NCBI / EBI]
130000; phenotype. [NCBI / EBI]
130060; phenotype. [NCBI / EBI]
166200; phenotype. [NCBI / EBI]
166210; phenotype. [NCBI / EBI]
166220; phenotype. [NCBI / EBI]
166710; phenotype. [NCBI / EBI]
259420; phenotype. [NCBI / EBI]
607907; phenotype. [NCBI / EBI]

Orphanet

1310; Caffey disease.
287; Classic Ehlers-Danlos syndrome.
31112; Dermatofibrosarcoma protuberans.
1899; Ehlers-Danlos syndrome, type 7.
666; Osteogenesis imperfecta.

PharmGKB

PA35041; -.

Gene expression databases

ArrayExpress

P02452; -.

Bgee

P02452; -.

GermOnline

ENSG00000108821; Homo sapiens.

Ontologies

GO:0005584;	Cellular component: collagen type I (inferred from mutant phenotype from UniProtKB).
GO:0005615;	Cellular component: extracellular space (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005886;	Cellular component: plasma membrane (inferred from experiment from Reactome).
GO:0005201;	Molecular function: extracellular matrix structural constituent (inferred from electronic annotation from InterPro).
GO:0042802;	Molecular function: identical protein binding (inferred from direct assay from UniProtKB).
GO:0048407;	Molecular function: platelet-derived growth factor binding (inferred from direct assay from MGI).
GO:0001568;	Biological process: blood vessel development (inferred from mutant phenotype from UniProtKB).
GO:0032964;	Biological process: collagen biosynthetic process (inferred from mutant phenotype from UniProtKB).
GO:0030199;	Biological process: collagen fibril organization (inferred from mutant phenotype from UniProtKB).
GO:0048706;	Biological process: embryonic skeletal system development (inferred from mutant phenotype from UniProtKB).
GO:0007605;	Biological process: sensory perception of sound (inferred from mutant phenotype from UniProtKB).
GO:0043589;	Biological process: skin morphogenesis (inferred from mutant phenotype from UniProtKB).
GO:0034505;	Biological process: tooth mineralization (inferred from mutant phenotype from UniProtKB).
GO:0007601;	Biological process: visual perception (inferred from mutant phenotype from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR008160; Collagen.
IPR000885; Fib_collagen_C.
IPR001007; VWF_C.
Graphical view of domain structure.

Pfam

PF01410; COLFI; 1.
PF01391; Collagen; 18.
PF00093; VWC; 1.
Pfam graphical view of domain structure.

ProDom

PD000007; Clg_helix; 2.
PD002078; Fib_collagen_C; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00038; COLFI; 1.
SM00214; VWC; 1.
SMART graphical view of domain structure.

PROSITE

PS01208; VWFC_1; 1.
PS50184; VWFC_2; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

P02452; -.

Genome annotation databases

Ensembl

ENSG00000108821; Homo sapiens. [Contig view]

GeneID

1277; -.

KEGG

hsa:1277; -.

Phylogenomic databases

HOVERGEN

P02452; -.

Other

DrugBank

DB00048; Collagenase.
DB00039; Palifermin.

NextBio

5161; -.

PMAP-CutDB

P02452; -.

SOURCE

COL1A1; Homo sapiens.

ProtoNet

P02452.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Chromosomal rearrangement; Collagen; Direct protein sequencing; Disease mutation; Disulfide bond; Dwarfism; Ehlers-Danlos syndrome; Extracellular matrix; Glycoprotein; Hydroxylation; Polymorphism; Pyrrolidone carboxylic acid; Repeat; Secreted; Signal.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 22`	`22`
`PROPEP`	`23 161`	`139`	`N-terminal propeptide.`	`PRO_0000005719`
`CHAIN`	`162 1218`	`1057`	`Collagen alpha-1(I) chain.`	`PRO_0000005720`
`PROPEP`	`1219 1464`	`246`	`C-terminal propeptide.`	`PRO_0000005721`
`DOMAIN`	`38 96`	`59`	`VWFC.`
`REGION`	`162 178`	`17`	`Nonhelical region (N-terminal).`
`REGION`	`179 1192`	`1014`	`Triple-helical region.`
`REGION`	`1193 1218`	`26`	`Nonhelical region (C-terminal).`
`MOTIF`	`745 747`	`3`	`Cell attachment site (Potential).`
`MOTIF`	`1093 1095`	`3`	`Cell attachment site (Potential).`
`SITE`	`161 162`	`2`	`Cleavage; by procollagen N-endopeptidase.`
`SITE`	`953 954`	`2`	`Cleavage; by collagenase (By similarity).`
`SITE`	`1218 1219`	`2`	`Cleavage; by procollagen C-endopeptidase.`
`MOD_RES`	`162 162`		`Pyrrolidone carboxylic acid.`
`MOD_RES`	`170 170`		`Allysine.`
`MOD_RES`	`265 265`		`5-hydroxylysine.`
`MOD_RES`	`1108 1108`		`5-hydroxylysine (By similarity).`
`MOD_RES`	`1164 1164`		`3-hydroxyproline (By similarity).`
`MOD_RES`	`1208 1208`		`Allysine (By similarity).`
`CARBOHYD`	`265 265`		`O-linked (Gal...).`
`CARBOHYD`	`1108 1108`		`O-linked (Gal...) (By similarity).`
`CARBOHYD`	`1365 1365`		`N-linked (GlcNAc...).`
`DISULFID`	`1259 1259`		`Interchain (By similarity).`
`DISULFID`	`1265 1265`		`Interchain (By similarity).`
`DISULFID`	`1282 1282`		`Interchain (By similarity).`
`DISULFID`	`1291 1291`		`Interchain (By similarity).`
`DISULFID`	`1299 1462`		`By similarity.`
`DISULFID`	`1370 1415`		`By similarity.`
`VARIANT`	`197 197`	`1`	`G -> C (mild phenotype; dbSNP:rs8179178 [NCBI]).`	`VAR_001642`
`VARIANT`	`205 205`	`1`	`P -> A.`	`VAR_001643`
`VARIANT`	`221 221`	`1`	`G -> C (in OI; mild form).`	`VAR_001644`
`VARIANT`	`224 224`	`1`	`G -> C (in OI-I; mild phenotype).`	`VAR_001645`
`VARIANT`	`263 263`	`1`	`G -> R (in OI-I; mild form).`	`VAR_001646`
`VARIANT`	`263 263`	`1`	`G -> V (in OI; mild form).`	`VAR_001647`
`VARIANT`	`272 272`	`1`	`G -> C (in OI-I).`	`VAR_001648`
`VARIANT`	`275 275`	`1`	`G -> D (in OI-II).`	`VAR_001649`
`VARIANT`	`312 312`	`1`	`R -> C (in EDS1).`	`VAR_013579`
`VARIANT`	`332 332`	`1`	`G -> R (in OI-III; mild to moderate form).`	`VAR_001650`
`VARIANT`	`350 350`	`1`	`G -> R (in OI-III).`	`VAR_001651`
`VARIANT`	`353 353`	`1`	`G -> C (in OI-IV).`	`VAR_001652`
`VARIANT`	`356 356`	`1`	`G -> C (in OI-IV; mild form).`	`VAR_001653`
`VARIANT`	`383 383`	`1`	`G -> C (in OI-IV).`	`VAR_001654`
`VARIANT`	`389 389`	`1`	`G -> C (in OI; moderate form).`	`VAR_001655`
`VARIANT`	`389 389`	`1`	`G -> R (in OI-II).`	`VAR_001656`
`VARIANT`	`398 398`	`1`	`G -> A (in OI-IV).`	`VAR_001657`
`VARIANT`	`398 398`	`1`	`G -> D (in OI-II).`	`VAR_001658`
`VARIANT`	`401 401`	`1`	`G -> C (in OI-IV).`	`VAR_001659`
`VARIANT`	`404 404`	`1`	`G -> C (in OI; moderate form).`	`VAR_001660`
`VARIANT`	`422 422`	`1`	`G -> C (in OI-II).`	`VAR_001661`
`VARIANT`	`425 425`	`1`	`G -> S (in OI-II; lethal form).`	`VAR_001662`
`VARIANT`	`434 434`	`1`	`G -> V (in OI-II).`	`VAR_001663`
`VARIANT`	`476 476`	`1`	`G -> R (in OI-II).`	`VAR_001664`
`VARIANT`	`527 527`	`1`	`G -> C (in OI-IV).`	`VAR_001665`
`VARIANT`	`530 530`	`1`	`G -> S (in OI-II/III/IV; mild to lethal form).`	`VAR_001666`
`VARIANT`	`533 533`	`1`	`G -> D (in OI-II).`	`VAR_001667`
`VARIANT`	`560 560`	`1`	`G -> C (in OI-IV).`	`VAR_001669`
`VARIANT`	`560 560`	`1`	`G -> R (in OI-II).`	`VAR_001670`
`VARIANT`	`560 560`	`1`	`G -> S (in OI-IV).`	`VAR_001668`
`VARIANT`	`564 564`	`1`	`R -> H (in dbSNP:rs1800211 [NCBI]).`	`VAR_001671`
`VARIANT`	`569 569`	`1`	`G -> R (in OI-II).`	`VAR_001672`
`VARIANT`	`593 593`	`1`	`G -> C (in OI-III/IV).`	`VAR_001673`
`VARIANT`	`593 593`	`1`	`G -> S (in OI-II/III; moderate to lethal form).`	`VAR_001674`
`VARIANT`	`638 638`	`1`	`G -> S (in OI-III/IV).`	`VAR_001675`
`VARIANT`	`656 656`	`1`	`G -> S (in OI-II).`	`VAR_001676`
`VARIANT`	`701 701`	`1`	`G -> C (in OI-IV).`	`VAR_001677`
`VARIANT`	`704 704`	`1`	`G -> C (in OI-III).`	`VAR_001678`
`VARIANT`	`719 719`	`1`	`G -> D (in OI-II).`	`VAR_001679`
`VARIANT`	`719 719`	`1`	`G -> S (in OI-III).`	`VAR_001680`
`VARIANT`	`728 728`	`1`	`G -> R (in OI-II).`	`VAR_001681`
`VARIANT`	`737 737`	`1`	`G -> D (in OI-II).`	`VAR_001682`
`VARIANT`	`743 743`	`1`	`G -> S (in OI-II).`	`VAR_001683`
`VARIANT`	`743 743`	`1`	`G -> V (in OI-II).`	`VAR_001684`
`VARIANT`	`764 764`	`1`	`G -> V (in OI-II).`	`VAR_001685`
`VARIANT`	`767 767`	`1`	`G -> S (in OI-III; severe).`	`VAR_001686`
`VARIANT`	`776 776`	`1`	`G -> S (in OI-II).`	`VAR_001687`
`VARIANT`	`809 809`	`1`	`G -> S (in OI-II).`	`VAR_001688`
`VARIANT`	`815 815`	`1`	`G -> V (in OI-II).`	`VAR_001689`
`VARIANT`	`821 821`	`1`	`G -> S (in OI-III).`	`VAR_001690`
`VARIANT`	`823 823`	`1`	`P -> A (in dbSNP:rs1800214 [NCBI]).`	`VAR_001691`
`VARIANT`	`839 839`	`1`	`G -> S (in OI-II; mild to moderate form).`	`VAR_001692`
`VARIANT`	`842 842`	`1`	`G -> R (in OI-II).`	`VAR_001693`
`VARIANT`	`845 845`	`1`	`G -> R (in OI-II).`	`VAR_001694`
`VARIANT`	`851 851`	`1`	`G -> D (in OI-II).`	`VAR_001695`
`VARIANT`	`866 866`	`1`	`G -> S (in OI-III).`	`VAR_008118`
`VARIANT`	`869 869`	`1`	`G -> C (in OI-II).`	`VAR_001696`
`VARIANT`	`884 884`	`1`	`G -> S (in OI-II/III; extremely severe form).`	`VAR_001697`
`VARIANT`	`896 896`	`1`	`G -> C (in OI-II).`	`VAR_001698`
`VARIANT`	`926 926`	`1`	`G -> C (in OI-II).`	`VAR_001699`
`VARIANT`	`980 980`	`1`	`G -> V (in OI-II).`	`VAR_001700`
`VARIANT`	`1010 1010`	`1`	`G -> S (in OI-IV).`	`VAR_001701`
`VARIANT`	`1014 1014`	`1`	`R -> C (in Caffey disease).`	`VAR_033097`
`VARIANT`	`1019 1019`	`1`	`G -> A (in dbSNP:rs1135348 [NCBI]).`	`VAR_030013`
`VARIANT`	`1022 1022`	`1`	`G -> S (in OI-III; severe form).`	`VAR_001702`
`VARIANT`	`1022 1022`	`1`	`G -> V (in OI-II).`	`VAR_001703`
`VARIANT`	`1025 1025`	`1`	`G -> R (in OI-II).`	`VAR_001704`
`VARIANT`	`1040 1040`	`1`	`G -> S (in OI-II/III; moderate to lethal form).`	`VAR_001705`
`VARIANT`	`1043 1043`	`1`	`G -> S (in OI-II).`	`VAR_001706`
`VARIANT`	`1046 1048`	`3`	`Missing (in OI-II).`	`VAR_001707`
`VARIANT`	`1049 1049`	`1`	`G -> S (in OI-III).`	`VAR_001708`
`VARIANT`	`1058 1058`	`1`	`G -> S (in OI-IV; mild form).`	`VAR_001709`
`VARIANT`	`1061 1061`	`1`	`G -> D (in OI-II).`	`VAR_001710`
`VARIANT`	`1061 1061`	`1`	`G -> S (in OI-IV).`	`VAR_001711`
`VARIANT`	`1075 1075`	`1`	`A -> T (in dbSNP:rs1800215 [NCBI]).`	`VAR_001712`
`VARIANT`	`1076 1076`	`1`	`G -> S (in OI-III; severe form).`	`VAR_001713`
`VARIANT`	`1079 1079`	`1`	`G -> S (in OI-I/II; mild to moderate form).`	`VAR_001714`
`VARIANT`	`1082 1082`	`1`	`G -> C (in OI-II).`	`VAR_001715`
`VARIANT`	`1088 1088`	`1`	`G -> A (in OI-II).`	`VAR_001716`
`VARIANT`	`1091 1091`	`1`	`G -> S (in OI-II).`	`VAR_001717`
`VARIANT`	`1100 1100`	`1`	`G -> S (in OI-II; mild to moderate form).`	`VAR_001718`
`VARIANT`	`1106 1106`	`1`	`G -> A (in OI-II).`	`VAR_001719`
`VARIANT`	`1124 1124`	`1`	`G -> C (in OI-II).`	`VAR_001720`
`VARIANT`	`1141 1141`	`1`	`R -> Q (in dbSNP:rs41316713 [NCBI]).`	`VAR_033778`
`VARIANT`	`1142 1142`	`1`	`G -> S (in OI-II).`	`VAR_001721`
`VARIANT`	`1151 1151`	`1`	`G -> S (in OI-III).`	`VAR_001722`
`VARIANT`	`1151 1151`	`1`	`G -> V (in OI-II).`	`VAR_001723`
`VARIANT`	`1154 1154`	`1`	`G -> R (in OI-II).`	`VAR_001724`
`VARIANT`	`1166 1166`	`1`	`G -> C (in OI-II).`	`VAR_001725`
`VARIANT`	`1172 1172`	`1`	`G -> D (in OI-II).`	`VAR_001726`
`VARIANT`	`1177 1177`	`1`	`V -> I (in dbSNP:rs41316719 [NCBI]).`	`VAR_033779`
`VARIANT`	`1181 1181`	`1`	`G -> S (in OI-II).`	`VAR_001727`
`VARIANT`	`1184 1184`	`1`	`G -> V (in OI-II).`	`VAR_001728`
`VARIANT`	`1187 1187`	`1`	`G -> S (in OI-II/III; extremely severe form).`	`VAR_001729`
`VARIANT`	`1187 1187`	`1`	`G -> V (in OI-II).`	`VAR_001730`
`VARIANT`	`1195 1195`	`1`	`G -> C (in OI-II; mild form).`	`VAR_001731`
`VARIANT`	`1251 1251`	`1`	`S -> T (in dbSNP:rs3205325 [NCBI]).`	`VAR_030014`
`VARIANT`	`1277 1277`	`1`	`D -> H (in OI-II; impaired pro-alpha chain association).`	`VAR_001732`
`VARIANT`	`1312 1312`	`1`	`W -> C (in OI-II).`	`VAR_001733`
`VARIANT`	`1337 1338`	`2`	`Missing (in OI-II; impaired pro-alpha chain association).`	`VAR_001734`
`VARIANT`	`1388 1388`	`1`	`L -> R (in OI-II; impaired pro-alpha chain association).`	`VAR_001735`
`VARIANT`	`1391 1391`	`1`	`Q -> K (in dbSNP:rs2586486 [NCBI]).`	`VAR_030015`
`VARIANT`	`1430 1430`	`1`	`K -> N (in dbSNP:rs1059454 [NCBI]).`	`VAR_033780`
`VARIANT`	`1431 1431`	`1`	`T -> P (in dbSNP:rs1059454 [NCBI]).`	`VAR_033781`
`VARIANT`	`1434 1434`	`1`	`T -> S (in dbSNP:rs1800220 [NCBI]).`	`VAR_001736`
`VARIANT`	`1438 1438`	`1`	`P -> R (in dbSNP:rs17857117 [NCBI]).`	`VAR_030016`
`VARIANT`	`1460 1460`	`1`	`P -> H (in dbSNP:rs17853657 [NCBI]).`	`VAR_030017`
`VARIANT`	`1464 1464`	`1`	`L -> P (in OI-III).`	`VAR_001737`
`CONFLICT`	`59 59`		`R -> Q (in Ref. 8; CAA25394).`
`CONFLICT`	`112 114`		`Missing (in Ref. 2; AAB94054).`
`CONFLICT`	`288 288`		`E -> P (in Ref. 15; AA sequence).`
`CONFLICT`	`370 370`		`R -> L (in Ref. 6; AAB59373).`
`CONFLICT`	`484 484`		`P -> L (in Ref. 19; AAA52289).`
`CONFLICT`	`595 595`		`A -> R (in Ref. 20; AAA51847).`
`CONFLICT`	`721 721`		`Q -> E (in Ref. 22).`
`CONFLICT`	`738 738`		`L -> E (in Ref. 22).`
`CONFLICT`	`975 976`		`LP -> PL (in Ref. 19; AAA52291).`
`CONFLICT`	`1081 1081`		`V -> A (in Ref. 18; AAA51995).`
`CONFLICT`	`1329 1329`		`S -> T (in Ref. 25; AAB27856).`

Sequence information

Length: 1464 AA [This is the length of the unprocessed precursor]

Molecular weight: 138911 Da [This is the MW of the unprocessed precursor]

CRC64: B0581DAD2809DDE8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MFSFVDLRLL LLLAATALLT HGQEEGQVEG QDEDIPPITC VQNGLRYHDR DVWKPEPCRI 

        70         80         90        100        110        120 
CVCDNGKVLC DDVICDETKN CPGAEVPEGE CCPVCPDGSE SPTDQETTGV EGPKGDTGPR 

       130        140        150        160        170        180 
GPRGPAGPPG RDGIPGQPGL PGPPGPPGPP GPPGLGGNFA PQLSYGYDEK STGGISVPGP 

       190        200        210        220        230        240 
MGPSGPRGLP GPPGAPGPQG FQGPPGEPGE PGASGPMGPR GPPGPPGKNG DDGEAGKPGR 

       250        260        270        280        290        300 
PGERGPPGPQ GARGLPGTAG LPGMKGHRGF SGLDGAKGDA GPAGPKGEPG SPGENGAPGQ 

       310        320        330        340        350        360 
MGPRGLPGER GRPGAPGPAG ARGNDGATGA AGPPGPTGPA GPPGFPGAVG AKGEAGPQGP 

       370        380        390        400        410        420 
RGSEGPQGVR GEPGPPGPAG AAGPAGNPGA DGQPGAKGAN GAPGIAGAPG FPGARGPSGP 

       430        440        450        460        470        480 
QGPGGPPGPK GNSGEPGAPG SKGDTGAKGE PGPVGVQGPP GPAGEEGKRG ARGEPGPTGL 

       490        500        510        520        530        540 
PGPPGERGGP GSRGFPGADG VAGPKGPAGE RGSPGPAGPK GSPGEAGRPG EAGLPGAKGL 

       550        560        570        580        590        600 
TGSPGSPGPD GKTGPPGPAG QDGRPGPPGP PGARGQAGVM GFPGPKGAAG EPGKAGERGV 

       610        620        630        640        650        660 
PGPPGAVGPA GKDGEAGAQG PPGPAGPAGE RGEQGPAGSP GFQGLPGPAG PPGEAGKPGE 

       670        680        690        700        710        720 
QGVPGDLGAP GPSGARGERG FPGERGVQGP PGPAGPRGAN GAPGNDGAKG DAGAPGAPGS 

       730        740        750        760        770        780 
QGAPGLQGMP GERGAAGLPG PKGDRGDAGP KGADGSPGKD GVRGLTGPIG PPGPAGAPGD 

       790        800        810        820        830        840 
KGESGPSGPA GPTGARGAPG DRGEPGPPGP AGFAGPPGAD GQPGAKGEPG DAGAKGDAGP 

       850        860        870        880        890        900 
PGPAGPAGPP GPIGNVGAPG AKGARGSAGP PGATGFPGAA GRVGPPGPSG NAGPPGPPGP 

       910        920        930        940        950        960 
AGKEGGKGPR GETGPAGRPG EVGPPGPPGP AGEKGSPGAD GPAGAPGTPG PQGIAGQRGV 

       970        980        990       1000       1010       1020 
VGLPGQRGER GFPGLPGPSG EPGKQGPSGA SGERGPPGPM GPPGLAGPPG ESGREGAPGA 

      1030       1040       1050       1060       1070       1080 
EGSPGRDGSP GAKGDRGETG PAGPPGAPGA PGAPGPVGPA GKSGDRGETG PAGPAGPVGP 

      1090       1100       1110       1120       1130       1140 
VGARGPAGPQ GPRGDKGETG EQGDRGIKGH RGFSGLQGPP GPPGSPGEQG PSGASGPAGP 

      1150       1160       1170       1180       1190       1200 
RGPPGSAGAP GKDGLNGLPG PIGPPGPRGR TGDAGPVGPP GPPGPPGPPG PPSAGFDFSF 

      1210       1220       1230       1240       1250       1260 
LPQPPQEKAH DGGRYYRADD ANVVRDRDLE VDTTLKSLSQ QIENIRSPEG SRKNPARTCR 

      1270       1280       1290       1300       1310       1320 
DLKMCHSDWK SGEYWIDPNQ GCNLDAIKVF CNMETGETCV YPTQPSVAQK NWYISKNPKD 

      1330       1340       1350       1360       1370       1380 
KRHVWFGESM TDGFQFEYGG QGSDPADVAI QLTFLRLMST EASQNITYHC KNSVAYMDQQ 

      1390       1400       1410       1420       1430       1440 
TGNLKKALLL QGSNEIEIRA EGNSRFTYSV TVDGCTSHTG AWGKTVIEYK TTKTSRLPII 

      1450       1460 
DVAPLDVGAP DQEFGFDVGP VCFL

P02452 in FASTA format

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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools