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Collagen alpha-2(I) chain (Alpha-2 type I collagen)

 CO1A2_HUMAN             Reviewed;        1366 AA.
P08123; P02464; Q13897; Q13997; Q13998; Q14038; Q14057; Q15177;
Q15947; Q16480; Q16511; Q7Z5S6; Q9UEB6; Q9UEF9; Q9UM83; Q9UMI1;
Q9UML5; Q9UMM6; Q9UPH0;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 7.
27-SEP-2017, entry version 205.
RecName: Full=Collagen alpha-2(I) chain;
AltName: Full=Alpha-2 type I collagen;
Flags: Precursor;
Name=COL1A2;
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 ASN-249; THR-276; VAL-483;
ALA-549; HIS-678; GLY-743; PHE-1022; GLU-1189; PRO-1198 AND HIS-1354.
PubMed=2824475;
de Wet W.J., Bernard M.P., Benson-Chanda V., Chu M.-L., Dickson L.A.,
Weil D., Ramirez F.;
"Organization of the human pro-alpha 2(I) collagen gene.";
J. Biol. Chem. 262:16032-16036(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA], REVIEW ON OI VARIANTS, AND VARIANTS
ALA-549; HIS-678 AND HIS-1354.
PubMed=9016532; DOI=10.1093/nar/25.1.181;
Dalgleish R.;
"The human type I collagen mutation database.";
Nucleic Acids Res. 25:181-187(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-270; VAL-483;
HIS-678; GLY-743; PHE-1022; GLU-1189; PRO-1198 AND HIS-1354.
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-549.
TISSUE=Skin, and Uterus;
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-765, AND VARIANTS HIS-678 AND GLY-743.
TISSUE=Placenta;
PubMed=3421913; DOI=10.1042/bj2520633;
Kuivaniemi H., Tromp G., Chu M.-L., Prockop D.J.;
"Structure of a full-length cDNA clone for the prepro alpha 2(I) chain
of human type I procollagen. Comparison with the chicken gene confirms
unusual patterns of gene conservation.";
Biochem. J. 252:633-640(1988).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-93, AND VARIANT PRO-59.
PubMed=4011429; DOI=10.1093/nar/13.10.3427;
Dickson L.A., de Wet W., Di Liberto M., Weil D., Ramirez F.;
"Analysis of the promoter region and the N-propeptide domain of the
human pro alpha 2(I) collagen gene.";
Nucleic Acids Res. 13:3427-3438(1985).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32.
Akai J., Kimura A., Arai K., Uehara K., Hata R.;
"Fine structural analysis of the unique 5' region of the human COL1A2
gene containing two regions of dinucleotide repeats adjacent to the
transcriptional start site.";
Connect. Tissue Res. 30:1-6(1998).
[8]
PROTEIN SEQUENCE OF 32-111, HYDROXYLATION AT PRO-47; PRO-50; PRO-62;
PRO-65; PRO-68; PRO-71; PRO-102 AND PRO-108, AND VARIANT EDS7B
76-ASN--MET-93 DEL.
PubMed=3680255;
Wirtz M.K., Glanville R.W., Steinmann B., Rao V.H., Hollister D.W.;
"Ehlers-Danlos syndrome type VIIB. Deletion of 18 amino acids
comprising the N-telopeptide region of a pro-alpha 2(I) chain.";
J. Biol. Chem. 262:16376-16385(1987).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-93, PROTEIN SEQUENCE OF 23-96,
HYDROXYLATION AT PRO-47; PRO-50; PRO-62; PRO-65; PRO-68 AND PRO-71,
PYROGLUTAMATE FORMATION AT GLN-23, AND VARIANT EDS7B 76-ASN--MET-93
DEL.
PubMed=2394758;
Weil D., D'Alessio M., Ramirez F., Eyre D.R.;
"Structural and functional characterization of a splicing mutation in
the pro-alpha 2(I) collagen gene of an Ehlers-Danlos type VII
patient.";
J. Biol. Chem. 265:16007-16011(1990).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-93, AND VARIANT EDS7B
76-ASN--MET-93 DEL.
PubMed=1577745;
Watson R.B., Wallis G.A., Holmes D.F., Viljoen D., Byers P.H.,
Kadler K.E.;
"Ehlers Danlos syndrome type VIIB. Incomplete cleavage of abnormal
type I procollagen by N-proteinase in vitro results in the formation
of copolymers of collagen and partially cleaved pNcollagen that are
near circular in cross-section.";
J. Biol. Chem. 267:9093-9100(1992).
[11]
PROTEIN SEQUENCE OF 80-96, ALLYSINE AT LYS-84, AND PYROGLUTAMATE
FORMATION AT GLN-80.
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).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 145-198.
PubMed=3403536;
Kuivaniemi H., Sabol C., Tromp G., Sippola-Thiele M., Prockop D.J.;
"A 19-base pair deletion in the pro-alpha 2(I) gene of type I
procollagen that causes in-frame RNA splicing from exon 10 to exon 12
in a proband with atypical osteogenesis imperfecta and in his
asymptomatic mother.";
J. Biol. Chem. 263:11407-11413(1988).
[13]
NUCLEOTIDE SEQUENCE [MRNA] OF 163-213, AND VARIANT OI4
181-GLY--LYS-198 DEL.
PubMed=1642148; DOI=10.1002/jbmr.5650070709;
Chipman S.D., Shapiro J.R., McKinstry M.B., Stover M.L., Branson P.,
Rowe D.W.;
"Expression of mutant alpha (I)-procollagen in osteoblast and
fibroblast cultures from a proband with osteogenesis imperfecta type
IV.";
J. Bone Miner. Res. 7:793-805(1992).
[14]
PROTEIN SEQUENCE OF 175-180, HYDROXYLATION AT LYS-177, AND
GLYCOSYLATION AT LYS-177.
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).
[15]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 181-1366.
Kalicki J., Wamsley P., Gibson A.;
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
[16]
PROTEIN SEQUENCE OF 417-447, AND HYDROXYLATION AT PRO-420; PRO-441 AND
PRO-444.
TISSUE=Skin;
PubMed=4412529; DOI=10.1111/j.1432-1033.1974.tb03689.x;
Fietzek P.P., Furthmayr H., Kuehn K.;
"Comparative sequence studies on alpha2-CB2 from calf, human, rabbit
and pig-skin collagen.";
Eur. J. Biochem. 47:257-261(1974).
[17]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 520-573, AND VARIANT ALA-549.
PubMed=2839839; DOI=10.1073/pnas.85.14.5254;
Tromp G., Prockop D.J.;
"Single base mutation in the pro alpha 2(I) collagen gene that causes
efficient splicing of RNA from exon 27 to exon 29 and synthesis of a
shortened but in-frame pro alpha 2(I) chain.";
Proc. Natl. Acad. Sci. U.S.A. 85:5254-5258(1988).
[18]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 622-657.
PubMed=6321602; DOI=10.1111/1523-1747.ep12260213;
Tajima S., Ting J.P., Pinnell S.R., Kaufman R.E.;
"Isolation and characterization of a human pro alpha 2(I) collagen
gene segment.";
J. Invest. Dermatol. 82:265-269(1984).
[19]
NUCLEOTIDE SEQUENCE [MRNA] OF 623-1366, AND VARIANTS HIS-678;
PHE-1022; GLU-1189; PRO-1198 AND HIS-1354.
PubMed=6687691; DOI=10.1021/bi00274a023;
Bernard M.P., Myers J.C., Chu M.-L., Ramirez F., Eikenberry E.F.,
Prockop D.J.;
"Structure of a cDNA for the pro alpha 2 chain of human type I
procollagen. Comparison with chick cDNA for pro alpha 2(I) identifies
structurally conserved features of the protein and the gene.";
Biochemistry 22:1139-1145(1983).
[20]
NUCLEOTIDE SEQUENCE [MRNA] OF 631-864, AND VARIANT OI2
676-GLY--ALA-855 DEL.
PubMed=1339453;
Chessler S.D., Byers P.H.;
"Defective folding and stable association with protein disulfide
isomerase/prolyl hydroxylase of type I procollagen with a deletion in
the pro alpha 2(I) chain that preserves the Gly-X-Y repeat pattern.";
J. Biol. Chem. 267:7751-7757(1992).
[21]
NUCLEOTIDE SEQUENCE [MRNA] OF 663-746, AND VARIANT OI3 VAL-676.
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).
[22]
NUCLEOTIDE SEQUENCE [MRNA] OF 960-1356, AND VARIANT HIS-1354.
TISSUE=Skin;
PubMed=2364107;
Maekelae J.K., Vuorio T., Vuorio E.;
"Growth-dependent modulation of type I collagen production and mRNA
levels in cultured human skin fibroblasts.";
Biochim. Biophys. Acta 1049:171-176(1990).
[23]
NUCLEOTIDE SEQUENCE [MRNA] OF 964-1019.
PubMed=6267597; DOI=10.1073/pnas.78.6.3516;
Myers J.C., Chu M.-L., Faro S.H., Clark W.J., Prockop D.J.,
Ramirez F.;
"Cloning a cDNA for the pro-alpha 2 chain of human type I collagen.";
Proc. Natl. Acad. Sci. U.S.A. 78:3516-3520(1981).
[24]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1090-1107, AND VARIANT OI4
ARG-1102.
PubMed=2897363;
Wenstrup R.J., Cohn D.H., Cohen T., Byers P.H.;
"Arginine for glycine substitution in the triple-helical domain of the
products of one alpha 2(I) collagen allele (COL1A2) produces the
osteogenesis imperfecta type IV phenotype.";
J. Biol. Chem. 263:7734-7740(1988).
[25]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1319-1366, AND VARIANT HIS-1354.
PubMed=6309769;
Myers J.C., Dickson L.A., de Wet W.J., Bernard M.P., Chu M.-L.,
Di Liberto M., Pepe G., Sangiorgi F.O., Ramirez F.;
"Analysis of the 3' end of the human pro-alpha 2(I) collagen gene.
Utilization of multiple polyadenylation sites in cultured
fibroblasts.";
J. Biol. Chem. 258:10128-10135(1983).
[26]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1319-1366, AND VARIANT HIS-1354.
TISSUE=Skin;
PubMed=6092353;
Pihlajaniemi T., Dickson L.A., Pope F.M., Korhonen V.R., Nicholls A.,
Prockop D.J., Myers J.C.;
"Osteogenesis imperfecta: cloning of a pro-alpha 2(I) collagen gene
with a frameshift mutation.";
J. Biol. Chem. 259:12941-12944(1984).
[27]
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).
[28]
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).
[29]
REVIEW ON OI 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).
[30]
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).
[31]
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).
[32]
VARIANT OI2 ASP-997.
PubMed=2914942;
Baldwin C.T., Constantinou C., Dumars K.W., Prockop D.J.;
"A single base mutation that converts glycine 907 of the alpha 2(I)
chain of type I procollagen to aspartate in a lethal variant of
osteogenesis imperfecta. The single amino acid substitution near the
carboxyl terminus destabilizes the whole triple helix.";
J. Biol. Chem. 264:3002-3006(1989).
[33]
VARIANT OI2 SER-955.
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).
[34]
VARIANT OI2 CYS-877.
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).
[35]
VARIANT OI4 VAL-676.
PubMed=2064612; DOI=10.1042/bj2760765;
Bateman J.F., Hannagan M., Chan D., Cole W.G.;
"Characterization of a type I collagen alpha 2(I) glycine-586 to
valine substitution in osteogenesis imperfecta type IV. Detection of
the mutation and prenatal diagnosis by a chemical cleavage method.";
Biochem. J. 276:765-770(1991).
[36]
VARIANT OI3 CYS-349, AND VARIANT OI1 CYS-736.
PubMed=1990009;
Wenstrup R.J., Shrago-Howe A.W., Lever L.W., Phillips C.L.,
Byers P.H., Cohn D.H.;
"The effects of different cysteine for glycine substitutions within
alpha 2(I) chains. Evidence of distinct structural domains within the
type I collagen triple helix.";
J. Biol. Chem. 266:2590-2594(1991).
[37]
VARIANT OI2 ARG-784.
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).
[38]
VARIANT OI4 SER-751.
PubMed=2052622; DOI=10.1073/pnas.88.12.5423;
Spotila L.D., Constantinou C.D., Sereda L., Ganguly A., Riggs B.L.,
Prockop D.J.;
"Mutation in a gene for type I procollagen (COL1A2) in a woman with
postmenopausal osteoporosis: evidence for phenotypic and genotypic
overlap with mild osteogenesis imperfecta.";
Proc. Natl. Acad. Sci. U.S.A. 88:5423-5427(1991).
[39]
VARIANT OI2 ARG-547.
PubMed=1284475; DOI=10.1002/humu.1380010109;
Bateman J.F., Moeller I., Hannagan M., Chan D., Cole W.G.;
"Lethal perinatal osteogenesis imperfecta due to a type I collagen
alpha 2(I) Gly to Arg substitution detected by chemical cleavage of an
mRNA:cDNA sequence mismatch.";
Hum. Mutat. 1:55-62(1992).
[40]
VARIANT OI2 ASP-670.
PubMed=1385413;
Niyibizi C., Bonadio J., Byers P.H., Eyre D.R.;
"Incorporation of type I collagen molecules that contain a mutant
alpha 2(I) chain (Gly580-->Asp) into bone matrix in a lethal case of
osteogenesis imperfecta.";
J. Biol. Chem. 267:23108-23112(1992).
[41]
VARIANT OI3 CYS-349, AND VARIANT OI1 CYS-736.
PubMed=8456807; DOI=10.1002/ajmg.1320450215;
Wenstrup R.J., Lever L.W., Phillips C.L., Quarles L.D.;
"Mutations in the COL1A2 gene of type I collagen that result in
nonlethal forms of osteogenesis imperfecta.";
Am. J. Med. Genet. 45:228-232(1993).
[42]
VARIANT ALA-549.
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).
[43]
VARIANT OI3 VAL-345 DEL.
PubMed=8444468; DOI=10.1007/BF00202479;
Molyneux K., Starman B.J., Byers P.H., Dalgleish R.;
"A single amino acid deletion in the alpha 2(I) chain of type I
collagen produces osteogenesis imperfecta type III.";
Hum. Genet. 90:621-628(1993).
[44]
VARIANT OI4 VAL-634.
PubMed=8401517; DOI=10.1093/hmg/2.8.1319;
Sztrolovics R., Glorieux F.H., van der Rest M., Roughley P.J.;
"Identification of type I collagen gene (COL1A2) mutations in
nonlethal osteogenesis imperfecta.";
Hum. Mol. Genet. 2:1319-1321(1993).
[45]
VARIANT OI2 GLU-433.
PubMed=7906591; DOI=10.1093/hmg/2.12.2175;
Rose N.J., Mackay K., Byers P.H., Dalgleish R.;
"A novel glycine to glutamic acid substitution at position 343 in the
alpha 2 chain of type I collagen in an individual with lethal
osteogenesis imperfecta.";
Hum. Mol. Genet. 2:2175-2177(1993).
[46]
VARIANT OI4 SER-1012.
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).
[47]
VARIANT OI4 VAL-766, AND VARIANT OI2 SER-796.
PubMed=7693712;
Wang Q., Orrison B.M., Marini J.C.;
"Two additional cases of osteogenesis imperfecta with substitutions
for glycine in the alpha 2(I) collagen chain. A regional model
relating mutation location with phenotype.";
J. Biol. Chem. 268:25162-25167(1993).
[48]
VARIANT OI3 ARG-517.
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).
[49]
VARIANT OI2 SER-592.
PubMed=7959683; DOI=10.1007/BF00211014;
Rose N.J., Mackay K., de Paepe A., Steinmann B., Punnett H.H.,
Dalgleish R.;
"Three unrelated individuals with perinatally lethal osteogenesis
imperfecta resulting from identical Gly502Ser substitutions in the
alpha 2-chain of type I collagen.";
Hum. Genet. 94:497-503(1994).
[50]
VARIANT OI3 SER-949.
PubMed=8081394; DOI=10.1002/humu.1380030411;
Rose N.J., Mackay K., Byers P.H., Dalgleish R.;
"A Gly859Ser substitution in the triple helical domain of the alpha 2
chain of type I collagen resulting in osteogenesis imperfecta type III
in two unrelated individuals.";
Hum. Mutat. 3:391-394(1994).
[51]
VARIANT OI2 ASP-790.
PubMed=8182080;
Cohen-Solal L., Zylberberg L., Sangalli A., Gomez Lira M., Mottes M.;
"Substitution of an aspartic acid for glycine 700 in the alpha 2(I)
chain of type I collagen in a recurrent lethal type II osteogenesis
imperfecta dramatically affects the mineralization of bone.";
J. Biol. Chem. 269:14751-14758(1994).
[52]
VARIANT OI2 CYS-730.
PubMed=7891382; DOI=10.1136/jmg.31.12.965;
Gomez Lira M., Sangalli A., Pignatti P.F., Digilio M.C., Giannotti A.,
Carnevale E., Mottes M.;
"Determination of a new collagen type I alpha 2 gene point mutation
which causes a Gly640 Cys substitution in osteogenesis imperfecta and
prenatal diagnosis by DNA hybridisation.";
J. Med. Genet. 31:965-968(1994).
[53]
VARIANT OI3 SER-778.
PubMed=7720740; DOI=10.1007/BF01991915;
Raghunath M., Mackay K., Dalgleish R., Steinmann B.;
"Genetic counselling on brittle grounds: recurring osteogenesis
imperfecta due to parental mosaicism for a dominant mutation.";
Eur. J. Pediatr. 154:123-129(1995).
[54]
VARIANT OI3 SER-328.
PubMed=7860070; DOI=10.1007/BF00209405;
Rose N.J., Mackay K., Byers P.H., Dalgleish R.;
"A Gly238Ser substitution in the alpha 2 chain of type I collagen
results in osteogenesis imperfecta type III.";
Hum. Genet. 95:215-218(1995).
[55]
VARIANT OI3 ALA-1096.
PubMed=7749416; DOI=10.1002/humu.1380050212;
Lu J., Costa T., Cole W.G.;
"A novel G1006A substitution in the alpha 2(I) chain of type I
collagen produces osteogenesis imperfecta type III.";
Hum. Mutat. 5:175-178(1995).
[56]
VARIANT OI3 ASP-892, AND VARIANT OI4 ASP-892.
PubMed=8800927;
Lund A.M., Schwartz M., Raghunath M., Steinmann B., Skovby F.;
"Gly802Asp substitution in the pro alpha 2(I) collagen chain in a
family with recurrent osteogenesis imperfecta due to paternal
mosaicism.";
Eur. J. Hum. Genet. 4:39-45(1996).
[57]
VARIANTS OI1 ASP-211 AND SER-835, VARIANTS OI3 SER-337 AND SER-460,
AND VARIANT HIS-822.
PubMed=8829649;
DOI=10.1002/(SICI)1098-1004(1996)7:2<89::AID-HUMU1>3.0.CO;2-K;
Zhuang J., Tromp G., Kuivaniemi H., Castells S., Bugge M.,
Prockop D.J.;
"Direct sequencing of PCR products derived from cDNAs for the pro
alpha 1 and pro alpha 2 chains of type I procollagen as a screening
method to detect mutations in patients with osteogenesis imperfecta.";
Hum. Mutat. 7:89-99(1996).
[58]
VARIANT OI3 PRO-1148.
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).
[59]
VARIANTS OI2 VAL-409 AND CYS-787.
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).
[60]
VARIANTS OI3 ASP-331; CYS-337 AND VAL-973.
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).
[61]
CHROMOSOMAL REARRANGEMENT WITH PLAG1.
PubMed=10987300;
Hibbard M.K., Kozakewich H.P., Dal Cin P., Sciot R., Tan X., Xiao S.,
Fletcher J.A.;
"PLAG1 fusion oncogenes in lipoblastoma.";
Cancer Res. 60:4869-4872(2000).
[62]
INVOLVEMENT IN CARDIAC VALVULAR EDS.
PubMed=15077201; DOI=10.1086/420794;
Schwarze U., Hata R., McKusick V.A., Shinkai H., Hoyme H.E.,
Pyeritz R.E., Byers P.H.;
"Rare autosomal recessive cardiac valvular form of Ehlers-Danlos
syndrome results from mutations in the COL1A2 gene that activate the
nonsense-mediated RNA decay pathway.";
Am. J. Hum. Genet. 74:917-930(2004).
[63]
INVOLVEMENT IN EDSCV.
PubMed=16816023; DOI=10.1136/jmg.2005.038224;
Malfait F., Symoens S., Coucke P., Nunes L., De Almeida S.,
De Paepe A.;
"Total absence of the alpha2(I) chain of collagen type I causes a rare
form of Ehlers-Danlos syndrome with hypermobility and propensity to
cardiac valvular problems.";
J. Med. Genet. 43:E36-E36(2006).
[64]
VARIANTS OI4 SER-193 AND CYS-754, VARIANT OI2 ASP-625, AND VARIANTS
OI3 CYS-835 AND VAL-991.
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).
[65]
VARIANTS OI1/OI3/OI4 GLU-325; SER-328; SER-358; SER-601; ASP-676;
SER-820; ARG-856; SER-1012; PRO-PRO-GLY-811 INS; VAL-GLY-PRO-989 INS
AND 1094-PRO--GLY-1096 DEL.
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).
[66]
VARIANTS OI4 ARG-202 AND VAL-256, VARIANTS OI1 ARG-247; ARG-319;
CYS-733 AND TYR-1195, VARIANTS OI2 ASP-253; ASP-982 AND ASP-1003, AND
VARIANT OI3 ASP-1087.
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).
[67]
VARIANTS SER-528; ALA-549 AND THR-564.
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).
[68]
VARIANTS OI2 CYS-234; ARG-283; GLU-397; CYS-454; LEU-457;
461-PRO--GLY-466 DEL; GLU-526; VAL-562; 705-ALA--PRO-707 DEL; ARG-739;
VAL-748; ASP-790; PRO-798 INS; 806-PRO--GLY-811 DEL; VAL-856; SER-949;
ASP-955; GLU-1027 AND 1058-PRO--ALA-1062 DEL, AND VARIANT ALA-549.
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).
[69]
VARIANT THR-1119, AND CHARACTERIZATION OF VARIANT THR-1119.
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).
[70]
VARIANT HIS-1067.
PubMed=23656646; DOI=10.1056/NEJMoa1215458;
Laine C.M., Joeng K.S., Campeau P.M., Kiviranta R., Tarkkonen K.,
Grover M., Lu J.T., Pekkinen M., Wessman M., Heino T.J.,
Nieminen-Pihala V., Aronen M., Laine T., Kroeger H., Cole W.G.,
Lehesjoki A.E., Nevarez L., Krakow D., Curry C.J., Cohn D.H.,
Gibbs R.A., Lee B.H., Maekitie O.;
"WNT1 mutations in early-onset osteoporosis and osteogenesis
imperfecta.";
N. Engl. J. Med. 368:1809-1816(2013).
-!- 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.
-!- INTERACTION:
O43765:SGTA; NbExp=5; IntAct=EBI-983038, EBI-347996;
Q9UMX0:UBQLN1; NbExp=5; IntAct=EBI-983038, EBI-741480;
Q9UMX0-2:UBQLN1; NbExp=3; IntAct=EBI-983038, EBI-10173939;
-!- 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. {ECO:0000250}.
-!- PTM: Prolines at the third position of the tripeptide repeating
unit (G-X-Y) are hydroxylated in some or all of the chains.
{ECO:0000269|PubMed:4412529}.
-!- DISEASE: Ehlers-Danlos syndrome 7B (EDS7B) [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.
{ECO:0000269|PubMed:1577745, ECO:0000269|PubMed:2394758,
ECO:0000269|PubMed:3680255}. 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:16705691,
ECO:0000269|PubMed:16786509, ECO:0000269|PubMed:1990009,
ECO:0000269|PubMed:8456807, ECO:0000269|PubMed:8829649}. 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:1284475, ECO:0000269|PubMed:1339453,
ECO:0000269|PubMed:1385413, ECO:0000269|PubMed:16786509,
ECO:0000269|PubMed:16879195, ECO:0000269|PubMed:1874719,
ECO:0000269|PubMed:18996919, ECO:0000269|PubMed:2777764,
ECO:0000269|PubMed:2914942, ECO:0000269|PubMed:7693712,
ECO:0000269|PubMed:7891382, ECO:0000269|PubMed:7906591,
ECO:0000269|PubMed:7959683, ECO:0000269|PubMed:8182080,
ECO:0000269|Ref.34}. Note=The disease is caused by mutations
affecting the gene represented in this entry.
-!- DISEASE: Ehlers-Danlos syndrome, autosomal recessive, cardiac
valvular form (EDSCV) [MIM:225320]: A connective tissue disorder
characterized by hyperextensible skin, atrophic cutaneous scars
due to tissue fragility and joint hyperlaxity. In addition to
joint laxity, skin hyperextensibility and friability, and abnormal
scar formation, patients have mitral valve prolapse and
insufficiency, mitral regurgitation, and aortic insufficiency.
{ECO:0000269|PubMed:16816023}. 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:16786509, ECO:0000269|PubMed:16879195,
ECO:0000269|PubMed:1990009, ECO:0000269|PubMed:7520724,
ECO:0000269|PubMed:7720740, ECO:0000269|PubMed:7749416,
ECO:0000269|PubMed:7860070, ECO:0000269|PubMed:7881420,
ECO:0000269|PubMed:8081394, ECO:0000269|PubMed:8444468,
ECO:0000269|PubMed:8456807, ECO:0000269|PubMed:8723681,
ECO:0000269|PubMed:8800927, ECO:0000269|PubMed:8829649}. 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:1642148, ECO:0000269|PubMed:16786509,
ECO:0000269|PubMed:16879195, ECO:0000269|PubMed:2052622,
ECO:0000269|PubMed:2064612, ECO:0000269|PubMed:2897363,
ECO:0000269|PubMed:7693712, ECO:0000269|PubMed:8094076,
ECO:0000269|PubMed:8401517, ECO:0000269|PubMed:8800927}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Note=A chromosomal aberration involving COL1A2 may be a
cause of lipoblastomas, which are benign tumors resulting from
transformation of adipocytes, usually diagnosed in children.
Translocation t(7;8)(p22;q13) with PLAG1.
-!- SIMILARITY: Belongs to the fibrillar collagen family.
{ECO:0000255|PROSITE-ProRule:PRU00793}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/COL1A2ID411ch7q22.html";
-!- WEB RESOURCE: Name=Osteogenesis imperfecta variant database;
Note=Collagen type I alpha 2 (COL1A2);
URL="http://oi.gene.le.ac.uk/home.php?select_db=COL1A2";
-----------------------------------------------------------------------
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EMBL; J03464; AAB59374.1; -; mRNA.
EMBL; Z74616; CAA98969.1; -; mRNA.
EMBL; AF004877; AAB93981.1; -; Genomic_DNA.
EMBL; BC042586; AAH42586.1; -; mRNA.
EMBL; BC054498; AAH54498.1; -; mRNA.
EMBL; Y00724; CAA68709.1; -; mRNA.
EMBL; X02488; CAA26320.1; -; mRNA.
EMBL; AB004317; BAA25383.1; -; Genomic_DNA.
EMBL; M35391; AAA60041.1; -; Genomic_DNA.
EMBL; S98904; AAB22126.1; -; Genomic_DNA.
EMBL; M21671; AAA59994.1; -; Genomic_DNA.
EMBL; S41099; AAB22761.1; -; mRNA.
EMBL; AC002528; AAB69977.1; -; Genomic_DNA.
EMBL; M21353; AAA52053.1; -; Genomic_DNA.
EMBL; M28985; AAA60356.1; -; Genomic_DNA.
EMBL; V00503; CAA23761.1; -; mRNA.
EMBL; S96821; AAB22020.2; -; mRNA.
EMBL; L47668; AAB59577.1; -; mRNA.
EMBL; X55525; CAA39142.1; -; mRNA.
EMBL; J00114; AAA51996.1; -; mRNA.
EMBL; M22816; AAA51844.1; -; mRNA.
EMBL; M22817; AAA51846.1; -; Genomic_DNA.
EMBL; K01078; AAA51887.1; -; Genomic_DNA.
EMBL; K02568; AAA51850.1; -; Genomic_DNA.
CCDS; CCDS34682.1; -.
PIR; A28500; CGHU2S.
RefSeq; NP_000080.2; NM_000089.3.
UniGene; Hs.489142; -.
PDB; 5CTD; X-ray; 1.60 A; B=484-495.
PDB; 5CTI; X-ray; 1.90 A; B=484-495.
PDB; 5CVA; X-ray; 2.10 A; A/D=484-495.
PDBsum; 5CTD; -.
PDBsum; 5CTI; -.
PDBsum; 5CVA; -.
ProteinModelPortal; P08123; -.
SMR; P08123; -.
BioGrid; 107675; 21.
DIP; DIP-36079N; -.
IntAct; P08123; 17.
MINT; MINT-4791958; -.
STRING; 9606.ENSP00000297268; -.
ChEMBL; CHEMBL2685; -.
DrugBank; DB00048; Collagenase clostridium histolyticum.
iPTMnet; P08123; -.
PhosphoSitePlus; P08123; -.
BioMuta; COL1A2; -.
DMDM; 296439507; -.
EPD; P08123; -.
MaxQB; P08123; -.
PaxDb; P08123; -.
PeptideAtlas; P08123; -.
PRIDE; P08123; -.
Ensembl; ENST00000297268; ENSP00000297268; ENSG00000164692.
GeneID; 1278; -.
KEGG; hsa:1278; -.
UCSC; uc003ung.1; human.
CTD; 1278; -.
DisGeNET; 1278; -.
EuPathDB; HostDB:ENSG00000164692.17; -.
GeneCards; COL1A2; -.
GeneReviews; COL1A2; -.
H-InvDB; HIX0006854; -.
HGNC; HGNC:2198; COL1A2.
HPA; CAB032650; -.
HPA; HPA059738; -.
MalaCards; COL1A2; -.
MIM; 120160; gene.
MIM; 130060; phenotype.
MIM; 166200; phenotype.
MIM; 166210; phenotype.
MIM; 166220; phenotype.
MIM; 225320; phenotype.
MIM; 259420; phenotype.
neXtProt; NX_P08123; -.
OpenTargets; ENSG00000164692; -.
Orphanet; 99876; Ehlers-Danlos syndrome type 7B.
Orphanet; 230851; Ehlers-Danlos syndrome, cardiac valvular 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; PA35042; -.
eggNOG; KOG3544; Eukaryota.
eggNOG; ENOG410XNMM; LUCA.
GeneTree; ENSGT00840000129673; -.
HOVERGEN; HBG004933; -.
InParanoid; P08123; -.
KO; K06236; -.
OMA; PEWSSGY; -.
OrthoDB; EOG091G03LV; -.
PhylomeDB; P08123; -.
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-6785807; Interleukin-4 and 13 signaling.
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-8948216; Collagen chain trimerization.
SIGNOR; P08123; -.
ChiTaRS; COL1A2; human.
GeneWiki; COL1A2; -.
GenomeRNAi; 1278; -.
PRO; PR:P08123; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000164692; -.
ExpressionAtlas; P08123; baseline and differential.
Genevisible; P08123; HS.
GO; GO:0005584; C:collagen type I trimer; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005201; F:extracellular matrix structural constituent; NAS:UniProtKB.
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:0030674; F:protein binding, bridging; IMP:UniProtKB.
GO; GO:0046332; F:SMAD binding; IEA:Ensembl.
GO; GO:0007596; P:blood coagulation; TAS:Reactome.
GO; GO:0001568; P:blood vessel development; IMP:UniProtKB.
GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
GO; GO:0030574; P:collagen catabolic process; TAS:Reactome.
GO; GO:0030199; P:collagen fibril organization; IMP:UniProtKB.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0042476; P:odontogenesis; NAS:UniProtKB.
GO; GO:0030168; P:platelet activation; TAS:Reactome.
GO; GO:0070208; P:protein heterotrimerization; IEA:Ensembl.
GO; GO:0008217; P:regulation of blood pressure; IMP:UniProtKB.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
GO; GO:0007266; P:Rho protein signal transduction; IDA:UniProtKB.
GO; GO:0001501; P:skeletal system development; IMP:UniProtKB.
GO; GO:0043589; P:skin morphogenesis; IMP:UniProtKB.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:UniProtKB.
Gene3D; 3.90.215.10; -; 1.
InterPro; IPR008160; Collagen.
InterPro; IPR000885; Fib_collagen_C.
InterPro; IPR014716; Fibrinogen_a/b/g_C_1.
Pfam; PF01410; COLFI; 1.
Pfam; PF01391; Collagen; 6.
ProDom; PD002078; Fib_collagen_C; 1.
SMART; SM00038; COLFI; 1.
PROSITE; PS51461; NC1_FIB; 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; Polymorphism; Pyrrolidone carboxylic acid;
Reference proteome; Repeat; Secreted; Signal.
SIGNAL 1 22 {ECO:0000250|UniProtKB:P02466}.
PROPEP 23 79 N-terminal propeptide.
{ECO:0000269|PubMed:5529814}.
/FTId=PRO_0000005804.
CHAIN 80 1119 Collagen alpha-2(I) chain.
/FTId=PRO_0000005805.
PROPEP 1120 1366 C-terminal propeptide.
/FTId=PRO_0000005806.
DOMAIN 1133 1366 Fibrillar collagen NC1.
{ECO:0000255|PROSITE-ProRule:PRU00793}.
METAL 1181 1181 Calcium. {ECO:0000250|UniProtKB:Q03692}.
METAL 1183 1183 Calcium. {ECO:0000250|UniProtKB:Q03692}.
METAL 1184 1184 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q03692}.
METAL 1186 1186 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q03692}.
METAL 1189 1189 Calcium. {ECO:0000250|UniProtKB:Q03692}.
MOD_RES 23 23 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:2394758}.
MOD_RES 47 47 4-hydroxyproline.
{ECO:0000269|PubMed:2394758,
ECO:0000269|PubMed:3680255}.
MOD_RES 50 50 4-hydroxyproline.
{ECO:0000269|PubMed:2394758,
ECO:0000269|PubMed:3680255}.
MOD_RES 62 62 4-hydroxyproline.
{ECO:0000269|PubMed:2394758,
ECO:0000269|PubMed:3680255}.
MOD_RES 65 65 4-hydroxyproline.
{ECO:0000269|PubMed:2394758,
ECO:0000269|PubMed:3680255}.
MOD_RES 68 68 4-hydroxyproline.
{ECO:0000269|PubMed:2394758,
ECO:0000269|PubMed:3680255}.
MOD_RES 71 71 4-hydroxyproline.
{ECO:0000269|PubMed:2394758,
ECO:0000269|PubMed:3680255}.
MOD_RES 80 80 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:5529814}.
MOD_RES 84 84 Allysine. {ECO:0000269|PubMed:5529814}.
MOD_RES 102 102 4-hydroxyproline.
{ECO:0000269|PubMed:3680255}.
MOD_RES 108 108 4-hydroxyproline.
{ECO:0000269|PubMed:3680255}.
MOD_RES 177 177 5-hydroxylysine; alternate.
{ECO:0000269|PubMed:4319110}.
MOD_RES 420 420 4-hydroxyproline.
{ECO:0000269|PubMed:4412529}.
MOD_RES 441 441 4-hydroxyproline.
{ECO:0000269|PubMed:4412529}.
MOD_RES 444 444 4-hydroxyproline.
{ECO:0000269|PubMed:4412529}.
CARBOHYD 177 177 O-linked (Gal...) hydroxylysine;
alternate. {ECO:0000269|PubMed:4319110}.
CARBOHYD 1267 1267 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 1163 1195 {ECO:0000255|PROSITE-ProRule:PRU00793}.
DISULFID 1203 1364 {ECO:0000255|PROSITE-ProRule:PRU00793}.
DISULFID 1272 1317 {ECO:0000255|PROSITE-ProRule:PRU00793}.
VARIANT 59 59 T -> P (in dbSNP:rs1800221).
{ECO:0000269|PubMed:4011429}.
/FTId=VAR_030116.
VARIANT 76 93 Missing (in EDS7B).
{ECO:0000269|PubMed:1577745,
ECO:0000269|PubMed:2394758,
ECO:0000269|PubMed:3680255}.
/FTId=VAR_001851.
VARIANT 181 198 Missing (in OI4).
{ECO:0000269|PubMed:1642148}.
/FTId=VAR_030117.
VARIANT 193 193 G -> S (in OI4; dbSNP:rs72656370).
{ECO:0000269|PubMed:16879195}.
/FTId=VAR_063343.
VARIANT 202 202 G -> R (in OI4; dbSNP:rs72656376).
{ECO:0000269|PubMed:16786509}.
/FTId=VAR_063344.
VARIANT 211 211 G -> D (in OI1; dbSNP:rs72656378).
{ECO:0000269|PubMed:8829649}.
/FTId=VAR_001852.
VARIANT 234 234 R -> C (in OI2).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_063345.
VARIANT 247 247 G -> R (in OI1).
{ECO:0000269|PubMed:16786509}.
/FTId=VAR_063346.
VARIANT 249 249 I -> N (in dbSNP:rs1800228).
{ECO:0000269|PubMed:2824475}.
/FTId=VAR_001853.
VARIANT 253 253 G -> D (in OI2; dbSNP:rs72656385).
{ECO:0000269|PubMed:16786509}.
/FTId=VAR_063347.
VARIANT 256 256 G -> V (in OI4; dbSNP:rs67525025).
{ECO:0000269|PubMed:16786509}.
/FTId=VAR_063348.
VARIANT 270 270 V -> I (in dbSNP:rs368468).
{ECO:0000269|PubMed:9443882}.
/FTId=VAR_030118.
VARIANT 276 276 A -> T (in dbSNP:rs1800231).
{ECO:0000269|PubMed:2824475}.
/FTId=VAR_001854.
VARIANT 283 283 G -> R (in OI2).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_063349.
VARIANT 319 319 G -> R (in OI1; dbSNP:rs72656393).
{ECO:0000269|PubMed:16786509}.
/FTId=VAR_063350.
VARIANT 325 325 G -> E (in OI4; dbSNP:rs72656395).
{ECO:0000269|PubMed:16705691}.
/FTId=VAR_063351.
VARIANT 328 328 G -> S (in OI1, OI3 AND OI4;
dbSNP:rs66612022).
{ECO:0000269|PubMed:16705691,
ECO:0000269|PubMed:7860070}.
/FTId=VAR_001855.
VARIANT 331 331 G -> D (in OI3; dbSNP:rs67729041).
{ECO:0000269|PubMed:10408781}.
/FTId=VAR_008119.
VARIANT 334 334 G -> C (in OI2).
/FTId=VAR_001856.
VARIANT 337 337 G -> C (in OI3; dbSNP:rs67865220).
{ECO:0000269|PubMed:10408781}.
/FTId=VAR_001857.
VARIANT 337 337 G -> S (in OI3; dbSNP:rs67865220).
{ECO:0000269|PubMed:8829649}.
/FTId=VAR_001858.
VARIANT 344 344 L -> V (in dbSNP:rs16868573).
/FTId=VAR_055677.
VARIANT 345 345 Missing (in OI3).
{ECO:0000269|PubMed:8444468}.
/FTId=VAR_001859.
VARIANT 349 349 G -> C (in OI3; dbSNP:rs66773001).
{ECO:0000269|PubMed:1990009,
ECO:0000269|PubMed:8456807}.
/FTId=VAR_001860.
VARIANT 358 358 G -> S (in OI3; dbSNP:rs66619856).
{ECO:0000269|PubMed:16705691}.
/FTId=VAR_063352.
VARIANT 397 397 G -> E (in OI2).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_063353.
VARIANT 409 409 G -> V (in OI2; dbSNP:rs72658109).
{ECO:0000269|PubMed:10627137}.
/FTId=VAR_001861.
VARIANT 433 433 G -> E (in OI2; dbSNP:rs72658114).
{ECO:0000269|PubMed:7906591}.
/FTId=VAR_001862.
VARIANT 454 454 G -> C (in OI2; dbSNP:rs72658117).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_063354.
VARIANT 457 457 G -> L (in OI2; requires 2 nucleotide
substitutions).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_063355.
VARIANT 460 460 G -> S (in OI3; dbSNP:rs72658118).
{ECO:0000269|PubMed:8829649}.
/FTId=VAR_001863.
VARIANT 461 466 Missing (in OI2).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_063356.
VARIANT 483 483 A -> V (in dbSNP:rs414408).
{ECO:0000269|PubMed:2824475,
ECO:0000269|PubMed:9443882}.
/FTId=VAR_030119.
VARIANT 511 511 G -> D (in OI2; dbSNP:rs66999265).
/FTId=VAR_001864.
VARIANT 517 517 G -> R (in OI3; dbSNP:rs72658126).
{ECO:0000269|PubMed:7520724}.
/FTId=VAR_001865.
VARIANT 526 526 G -> E (in OI2; dbSNP:rs72658130).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_063357.
VARIANT 528 528 N -> S (in dbSNP:rs41317144).
{ECO:0000269|PubMed:18272325}.
/FTId=VAR_033040.
VARIANT 547 547 G -> R (in OI2; dbSNP:rs72658136).
{ECO:0000269|PubMed:1284475}.
/FTId=VAR_001866.
VARIANT 549 549 P -> A (in dbSNP:rs42524).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:18272325,
ECO:0000269|PubMed:18996919,
ECO:0000269|PubMed:2824475,
ECO:0000269|PubMed:2839839,
ECO:0000269|PubMed:8456808,
ECO:0000269|PubMed:9016532}.
/FTId=VAR_001867.
VARIANT 562 562 G -> C (in OI2; dbSNP:rs72658138).
/FTId=VAR_001868.
VARIANT 562 562 G -> V (in OI2).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_063358.
VARIANT 564 564 A -> T (in dbSNP:rs41317153).
{ECO:0000269|PubMed:18272325}.
/FTId=VAR_033041.
VARIANT 586 586 G -> R (in OI2; dbSNP:rs72658139).
/FTId=VAR_001869.
VARIANT 592 592 G -> S (in OI2; dbSNP:rs72658141).
{ECO:0000269|PubMed:7959683}.
/FTId=VAR_001870.
VARIANT 601 601 G -> S (in OI; dbSNP:rs72658143).
{ECO:0000269|PubMed:16705691}.
/FTId=VAR_063359.
VARIANT 625 625 G -> D (in OI2; dbSNP:rs72658145).
{ECO:0000269|PubMed:16879195}.
/FTId=VAR_063360.
VARIANT 634 634 G -> V (in OI4; dbSNP:rs72658147).
{ECO:0000269|PubMed:8401517}.
/FTId=VAR_001871.
VARIANT 637 637 G -> D (in OI2; dbSNP:rs72658148).
/FTId=VAR_001872.
VARIANT 640 640 G -> S (in OI2).
/FTId=VAR_001873.
VARIANT 670 670 G -> D (in OI2; dbSNP:rs72658155).
{ECO:0000269|PubMed:1385413}.
/FTId=VAR_001874.
VARIANT 676 855 Missing (in OI2).
{ECO:0000269|PubMed:1339453}.
/FTId=VAR_030120.
VARIANT 676 676 G -> D (in OI3; dbSNP:rs66883877).
{ECO:0000269|PubMed:16705691}.
/FTId=VAR_063361.
VARIANT 676 676 G -> V (in OI3 and OI4;
dbSNP:rs66883877).
{ECO:0000269|PubMed:2064612,
ECO:0000269|PubMed:7881420}.
/FTId=VAR_001875.
VARIANT 678 678 P -> H (in dbSNP:rs409108).
{ECO:0000269|PubMed:2824475,
ECO:0000269|PubMed:3421913,
ECO:0000269|PubMed:6687691,
ECO:0000269|PubMed:9016532,
ECO:0000269|PubMed:9443882}.
/FTId=VAR_030121.
VARIANT 705 707 Missing (in OI2).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_063362.
VARIANT 708 708 R -> Q (in Marfan syndrome;
dbSNP:rs72658163).
/FTId=VAR_001876.
VARIANT 715 715 G -> D (in OI2; dbSNP:rs72658167).
/FTId=VAR_001877.
VARIANT 730 730 G -> C (in OI2; dbSNP:rs72658171).
{ECO:0000269|PubMed:7891382}.
/FTId=VAR_001878.
VARIANT 733 733 G -> C (in OI1; dbSNP:rs72658172).
{ECO:0000269|PubMed:16786509}.
/FTId=VAR_063363.
VARIANT 736 736 G -> C (in OI1; mild; dbSNP:rs72658173).
{ECO:0000269|PubMed:1990009,
ECO:0000269|PubMed:8456807}.
/FTId=VAR_001879.
VARIANT 739 739 G -> R (in OI2; dbSNP:rs72658174).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_063364.
VARIANT 743 743 A -> G (in dbSNP:rs408535).
{ECO:0000269|PubMed:2824475,
ECO:0000269|PubMed:3421913,
ECO:0000269|PubMed:9443882}.
/FTId=VAR_001880.
VARIANT 748 748 G -> V (in OI2).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_063365.
VARIANT 751 751 G -> S (in OI4; dbSNP:rs72658176).
{ECO:0000269|PubMed:2052622}.
/FTId=VAR_001881.
VARIANT 754 754 G -> C (in OI4; dbSNP:rs72658177).
{ECO:0000269|PubMed:16879195}.
/FTId=VAR_063366.
VARIANT 754 754 G -> R (in OI2).
/FTId=VAR_001882.
VARIANT 766 766 G -> V (in OI4; dbSNP:rs72658183).
{ECO:0000269|PubMed:7693712}.
/FTId=VAR_001883.
VARIANT 778 778 G -> S (in OI3; dbSNP:rs72658186).
{ECO:0000269|PubMed:7720740}.
/FTId=VAR_001884.
VARIANT 784 784 G -> R (in OI2; dbSNP:rs66592844).
{ECO:0000269|PubMed:1874719}.
/FTId=VAR_001885.
VARIANT 787 787 G -> C (in OI2; dbSNP:rs72658187).
{ECO:0000269|PubMed:10627137}.
/FTId=VAR_001886.
VARIANT 790 790 G -> D (in OI2; dbSNP:rs72658188).
{ECO:0000269|PubMed:18996919,
ECO:0000269|PubMed:8182080}.
/FTId=VAR_001887.
VARIANT 796 796 G -> S (in OI2; dbSNP:rs66716547).
{ECO:0000269|PubMed:7693712}.
/FTId=VAR_001888.
VARIANT 798 798 P -> PP (in OI2).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_063367.
VARIANT 806 811 Missing (in OI2).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_063368.
VARIANT 811 811 G -> GPPG (in OI4).
/FTId=VAR_063369.
VARIANT 820 820 G -> S (in OI3; dbSNP:rs72658191).
{ECO:0000269|PubMed:16705691}.
/FTId=VAR_063370.
VARIANT 822 822 R -> H (in dbSNP:rs1800240).
{ECO:0000269|PubMed:8829649}.
/FTId=VAR_001889.
VARIANT 835 835 G -> C (in OI3).
{ECO:0000269|PubMed:16879195}.
/FTId=VAR_063371.
VARIANT 835 835 G -> S (in OI1; dbSNP:rs72658193).
{ECO:0000269|PubMed:8829649}.
/FTId=VAR_001890.
VARIANT 856 856 G -> R (in OI3).
{ECO:0000269|PubMed:16705691}.
/FTId=VAR_063372.
VARIANT 856 856 G -> V (in OI2).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_063373.
VARIANT 877 877 G -> C (in OI2; dbSNP:rs72658201).
{ECO:0000269|Ref.34}.
/FTId=VAR_001891.
VARIANT 892 892 G -> D (in OI3 and OI4;
dbSNP:rs72659304).
{ECO:0000269|PubMed:8800927}.
/FTId=VAR_001892.
VARIANT 895 895 G -> D (in OI2; dbSNP:rs72659305).
/FTId=VAR_001893.
VARIANT 949 949 G -> S (in OI3; moderate;
dbSNP:rs72659312).
{ECO:0000269|PubMed:18996919,
ECO:0000269|PubMed:8081394}.
/FTId=VAR_001894.
VARIANT 955 955 G -> D (in OI2).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_063374.
VARIANT 955 955 G -> S (in OI2; dbSNP:rs66507857).
{ECO:0000269|PubMed:2777764}.
/FTId=VAR_001895.
VARIANT 973 973 G -> V (in OI3; dbSNP:rs67609234).
{ECO:0000269|PubMed:10408781}.
/FTId=VAR_008120.
VARIANT 982 982 G -> D (in OI2; dbSNP:rs67422093).
{ECO:0000269|PubMed:16786509}.
/FTId=VAR_063375.
VARIANT 989 989 P -> PVGP (in OI4).
/FTId=VAR_063376.
VARIANT 991 991 G -> V (in OI3; dbSNP:rs72659316).
{ECO:0000269|PubMed:16879195}.
/FTId=VAR_063377.
VARIANT 997 997 G -> D (in OI2; dbSNP:rs72659317).
{ECO:0000269|PubMed:2914942}.
/FTId=VAR_001896.
VARIANT 1003 1003 G -> D (in OI2).
{ECO:0000269|PubMed:16786509}.
/FTId=VAR_063378.
VARIANT 1012 1012 G -> S (in OI3 and OI4; moderate;
dbSNP:rs72659319).
{ECO:0000269|PubMed:16705691,
ECO:0000269|PubMed:8094076}.
/FTId=VAR_001897.
VARIANT 1022 1022 L -> F (in dbSNP:rs392609).
{ECO:0000269|PubMed:2824475,
ECO:0000269|PubMed:6687691,
ECO:0000269|PubMed:9443882}.
/FTId=VAR_001898.
VARIANT 1027 1027 G -> E (in OI2; dbSNP:rs72659323).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_063379.
VARIANT 1058 1062 Missing (in OI2).
{ECO:0000269|PubMed:18996919}.
/FTId=VAR_063380.
VARIANT 1066 1066 G -> D (in OI2; dbSNP:rs72659331).
/FTId=VAR_001899.
VARIANT 1067 1067 R -> H (in dbSNP:rs530026906).
{ECO:0000269|PubMed:23656646}.
/FTId=VAR_069633.
VARIANT 1078 1078 G -> C (in OI2).
/FTId=VAR_001900.
VARIANT 1087 1087 G -> D (in OI3; dbSNP:rs72659335).
{ECO:0000269|PubMed:16786509}.
/FTId=VAR_063381.
VARIANT 1094 1096 Missing (in OI4).
{ECO:0000269|PubMed:16705691}.
/FTId=VAR_063382.
VARIANT 1096 1096 G -> A (in OI3; dbSNP:rs72659337).
{ECO:0000269|PubMed:7749416}.
/FTId=VAR_001901.
VARIANT 1101 1101 P -> L.
/FTId=VAR_001903.
VARIANT 1102 1102 G -> R (in OI4; dbSNP:rs67768540).
{ECO:0000269|PubMed:2897363}.
/FTId=VAR_001902.
VARIANT 1119 1119 A -> T (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_066386.
VARIANT 1148 1148 T -> P (in OI3; dbSNP:rs1800250).
{ECO:0000269|PubMed:8723681}.
/FTId=VAR_001904.
VARIANT 1189 1189 D -> E (in dbSNP:rs422361).
{ECO:0000269|PubMed:2824475,
ECO:0000269|PubMed:6687691,
ECO:0000269|PubMed:9443882}.
/FTId=VAR_001905.
VARIANT 1195 1195 C -> Y (in OI1; dbSNP:rs72659342).
{ECO:0000269|PubMed:16786509}.
/FTId=VAR_063383.
VARIANT 1198 1198 S -> P (in dbSNP:rs384487).
{ECO:0000269|PubMed:2824475,
ECO:0000269|PubMed:6687691,
ECO:0000269|PubMed:9443882}.
/FTId=VAR_001906.
VARIANT 1354 1354 Q -> H (in dbSNP:rs418570).
{ECO:0000269|PubMed:2364107,
ECO:0000269|PubMed:2824475,
ECO:0000269|PubMed:6092353,
ECO:0000269|PubMed:6309769,
ECO:0000269|PubMed:6687691,
ECO:0000269|PubMed:9016532,
ECO:0000269|PubMed:9443882}.
/FTId=VAR_030122.
CONFLICT 55 55 E -> G (in Ref. 6; CAA26320).
{ECO:0000305}.
CONFLICT 333 333 V -> P (in Ref. 1; AAB59374).
{ECO:0000305}.
CONFLICT 338 338 A -> T (in Ref. 1; AAB59374).
{ECO:0000305}.
CONFLICT 549 549 P -> D (in Ref. 5; CAA68709).
{ECO:0000305}.
CONFLICT 828 828 V -> A (in Ref. 19; CAA23761).
{ECO:0000305}.
CONFLICT 831 831 T -> P (in Ref. 19; CAA23761).
{ECO:0000305}.
CONFLICT 837 837 V -> P (in Ref. 19; CAA23761).
{ECO:0000305}.
CONFLICT 980 980 E -> V (in Ref. 23; AAA51996).
{ECO:0000305}.
CONFLICT 1098 1098 P -> L (in Ref. 19; CAA23761).
{ECO:0000305}.
CONFLICT 1122 1125 Missing (in Ref. 19; CAA23761).
{ECO:0000305}.
CONFLICT 1338 1338 R -> A (in Ref. 25; AAA51887).
{ECO:0000305}.
SEQUENCE 1366 AA; 129314 MW; 1E68A5970FB4210A CRC64;
MLSFVDTRTL LLLAVTLCLA TCQSLQEETV RKGPAGDRGP RGERGPPGPP GRDGEDGPTG
PPGPPGPPGP PGLGGNFAAQ YDGKGVGLGP GPMGLMGPRG PPGAAGAPGP QGFQGPAGEP
GEPGQTGPAG ARGPAGPPGK AGEDGHPGKP GRPGERGVVG PQGARGFPGT PGLPGFKGIR
GHNGLDGLKG QPGAPGVKGE PGAPGENGTP GQTGARGLPG ERGRVGAPGP AGARGSDGSV
GPVGPAGPIG SAGPPGFPGA PGPKGEIGAV GNAGPAGPAG PRGEVGLPGL SGPVGPPGNP
GANGLTGAKG AAGLPGVAGA PGLPGPRGIP GPVGAAGATG ARGLVGEPGP AGSKGESGNK
GEPGSAGPQG PPGPSGEEGK RGPNGEAGSA GPPGPPGLRG SPGSRGLPGA DGRAGVMGPP
GSRGASGPAG VRGPNGDAGR PGEPGLMGPR GLPGSPGNIG PAGKEGPVGL PGIDGRPGPI
GPAGARGEPG NIGFPGPKGP TGDPGKNGDK GHAGLAGARG APGPDGNNGA QGPPGPQGVQ
GGKGEQGPPG PPGFQGLPGP SGPAGEVGKP GERGLHGEFG LPGPAGPRGE RGPPGESGAA
GPTGPIGSRG PSGPPGPDGN KGEPGVVGAV GTAGPSGPSG LPGERGAAGI PGGKGEKGEP
GLRGEIGNPG RDGARGAPGA VGAPGPAGAT GDRGEAGAAG PAGPAGPRGS PGERGEVGPA
GPNGFAGPAG AAGQPGAKGE RGAKGPKGEN GVVGPTGPVG AAGPAGPNGP PGPAGSRGDG
GPPGMTGFPG AAGRTGPPGP SGISGPPGPP GPAGKEGLRG PRGDQGPVGR TGEVGAVGPP
GFAGEKGPSG EAGTAGPPGT PGPQGLLGAP GILGLPGSRG ERGLPGVAGA VGEPGPLGIA
GPPGARGPPG AVGSPGVNGA PGEAGRDGNP GNDGPPGRDG QPGHKGERGY PGNIGPVGAA
GAPGPHGPVG PAGKHGNRGE TGPSGPVGPA GAVGPRGPSG PQGIRGDKGE PGEKGPRGLP
GLKGHNGLQG LPGIAGHHGD QGAPGSVGPA GPRGPAGPSG PAGKDGRTGH PGTVGPAGIR
GPQGHQGPAG PPGPPGPPGP PGVSGGGYDF GYDGDFYRAD QPRSAPSLRP KDYEVDATLK
SLNNQIETLL TPEGSRKNPA RTCRDLRLSH PEWSSGYYWI DPNQGCTMDA IKVYCDFSTG
ETCIRAQPEN IPAKNWYRSS KDKKHVWLGE TINAGSQFEY NVEGVTSKEM ATQLAFMRLL
ANYASQNITY HCKNSIAYMD EETGNLKKAV ILQGSNDVEL VAEGNSRFTY TVLVDGCSKK
TNEWGKTIIE YKTNKPSRLP FLDIAPLDIG GADQEFFVDI GPVCFK


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E0572r ELISA Alpha-1 type II collagen,Col2a1,Collagen alpha-1(II) chain,Rat,Rattus norvegicus 96T
E0572m ELISA Alpha-1 type II collagen,Col2a1,Collagen alpha-1(II) chain,Mouse,Mus musculus 96T
E0572b ELISA Alpha-1 type II collagen,Bos taurus,Bovine,COL2A1,Collagen alpha-1(II) chain 96T
U0572b CLIA Alpha-1 type II collagen,Bos taurus,Bovine,COL2A1,Collagen alpha-1(II) chain 96T
EIAAB08374 Alpha-2 type I collagen,COL1A2,Collagen alpha-2(I) chain,Homo sapiens,Human
E0571r ELISA kit Alpha-1 type I collagen,Col1a1,Collagen alpha-1(I) chain,Rat,Rattus norvegicus 96T
E0571b ELISA Alpha-1 type I collagen,Bos taurus,Bovine,COL1A1,Collagen alpha-1(I) chain 96T


 

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