Reviewed, UniProtKB/Swiss-Prot P02452 (CO1A1_HUMAN)

Names and origin

Protein names

Recommended name:
    Collagen alpha-1(I) chain
Alternative name(s):
    Alpha-1 type I collagen

Gene names

Name:

COL1A1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1464 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Type I collagen is a member of group I collagen (fibrillar forming collagen).
Subunit structure	Trimers of one alpha 2(I) and two alpha 1(I) chains. Interacts with MRC2 By similarity.
Subcellular location	Secreted › extracellular space › extracellular matrix By similarity.
Tissue specificity	Forms the fibrils of tendon, ligaments and bones. In bones the fibrils are mineralized with calcium hydroxyapatite.
Post-translational modification	Proline residues at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. O-linked glycan consists of a Glc-Gal disaccharide bound to the oxygen atom of a post-translationally added hydroxyl group.
Involvement in 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. Ref.88 Ref.89 Ref.90 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. Ref.88 Ref.89 Ref.90 Ref.87 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. Ref.88 Ref.89 Ref.90 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). Ref.88 Ref.89 Ref.90 Ref.22 Ref.23 Ref.25 Ref.33 Ref.34 Ref.35 Ref.36 Ref.38 Ref.39 Ref.40 Ref.42 Ref.44 Ref.45 Ref.46 Ref.47 Ref.48 Ref.49 Ref.50 Ref.51 Ref.53 Ref.54 Ref.55 Ref.56 Ref.58 Ref.59 Ref.60 Ref.62 Ref.63 Ref.64 Ref.65 Ref.66 Ref.68 Ref.70 Ref.71 Ref.72 Ref.73 Ref.74 Ref.75 Ref.76 Ref.77 Ref.78 Ref.79 Ref.82 Ref.83 Ref.84 Ref.86 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). 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. 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. 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. Ref.88 Ref.89 Ref.90 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. Ref.88 Ref.89 Ref.90
Sequence similarities	Belongs to the fibrillar collagen family. Contains 1 VWFC domain.

Ontologies

Keywords
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Chromosomal rearrangement Polymorphism
Disease	Disease mutation Dwarfism Ehlers-Danlos syndrome
Domain	Collagen Repeat Signal
PTM	Disulfide bond Glycoprotein Hydroxylation Pyrrolidone carboxylic acid
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	blood vessel development Inferred from mutant phenotype. Source: UniProtKB collagen biosynthetic process Inferred from mutant phenotype. Source: UniProtKB collagen fibril organization Inferred from mutant phenotype. Source: UniProtKB embryonic skeletal system development Inferred from mutant phenotype. Source: UniProtKB sensory perception of sound Inferred from mutant phenotype. Source: UniProtKB skin morphogenesis Inferred from mutant phenotype. Source: UniProtKB tooth mineralization Inferred from mutant phenotype. Source: UniProtKB visual perception Inferred from mutant phenotype. Source: UniProtKB
Cellular component	collagen type I Inferred from mutant phenotype. Source: UniProtKB extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from Experiment. Source: Reactome
Molecular function	extracellular matrix structural constituent Inferred from electronic annotation. Source: InterPro identical protein binding Inferred from direct assay. Source: UniProtKB platelet-derived growth factor binding Inferred from direct assay. Source: MGI
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	Q5YB85	1	EBI-982999,EBI-982988	From a different organism.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22
	Propeptide	23 – 161	139	N-terminal propeptide Ref.14		PRO_0000005719
	Chain	162 – 1218	1057	Collagen alpha-1(I) chain		PRO_0000005720
	Propeptide	1219 – 1464	246	C-terminal propeptide		PRO_0000005721
Regions
	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
Sites
	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
Amino acid modifications
	Modified residue	162	1	Pyrrolidone carboxylic acid
	Modified residue	170	1	Allysine
	Modified residue	265	1	5-hydroxylysine
	Modified residue	1108	1	5-hydroxylysine By similarity
	Modified residue	1164	1	3-hydroxyproline By similarity
	Modified residue	1208	1	Allysine By similarity
	Glycosylation	265	1	O-linked (Gal...)
	Glycosylation	1108	1	O-linked (Gal...) By similarity
	Glycosylation	1365	1	N-linked (GlcNAc...)
	Disulfide bond	1259		Interchain By similarity
	Disulfide bond	1265		Interchain By similarity
	Disulfide bond	1282		Interchain By similarity
	Disulfide bond	1291		Interchain By similarity
	Disulfide bond	1299 ↔ 1462		By similarity
	Disulfide bond	1370 ↔ 1415		By similarity
Natural variations
	Natural variant	197	1	G → C Mild phenotype. dbSNP rs8179178.		VAR_001642
	Natural variant	205	1	P → A		VAR_001643
	Natural variant	221	1	G → C in OI; mild form. Ref.61		VAR_001644
	Natural variant	224	1	G → C in OI-I; mild phenotype.		VAR_001645
	Natural variant	263	1	G → R in OI-I; mild form. Ref.54		VAR_001646
	Natural variant	263	1	G → V in OI; mild form. Ref.54 Ref.67		VAR_001647
	Natural variant	272	1	G → C in OI-I.		VAR_001648
	Natural variant	275	1	G → D in OI-II.		VAR_001649
	Natural variant	312	1	R → C in EDS1. Ref.87		VAR_013579
	Natural variant	332	1	G → R in OI-III; mild to moderate form. Ref.51 Ref.77		VAR_001650
	Natural variant	350	1	G → R in OI-III. Ref.74		VAR_001651
	Natural variant	353	1	G → C in OI-IV. Ref.65		VAR_001652
	Natural variant	356	1	G → C in OI-IV; mild form.		VAR_001653
	Natural variant	383	1	G → C in OI-IV.		VAR_001654
	Natural variant	389	1	G → C in OI; moderate form. Ref.73		VAR_001655
	Natural variant	389	1	G → R in OI-II. Ref.73		VAR_001656
	Natural variant	398	1	G → A in OI-IV. Ref.83		VAR_001657
	Natural variant	398	1	G → D in OI-II.		VAR_001658
	Natural variant	401	1	G → C in OI-IV.		VAR_001659
	Natural variant	404	1	G → C in OI; moderate form.		VAR_001660
	Natural variant	422	1	G → C in OI-II. Ref.44		VAR_001661
	Natural variant	425	1	G → S in OI-II; lethal form.		VAR_001662
	Natural variant	434	1	G → V in OI-II. Ref.38 Ref.62		VAR_001663
	Natural variant	476	1	G → R in OI-II.		VAR_001664
	Natural variant	527	1	G → C in OI-IV. Ref.83		VAR_001665
	Natural variant	530	1	G → S in OI-II/III/IV; mild to lethal form.		VAR_001666
	Natural variant	533	1	G → D in OI-II.		VAR_001667
	Natural variant	560	1	G → C in OI-IV.		VAR_001669
	Natural variant	560	1	G → R in OI-II.		VAR_001670
	Natural variant	560	1	G → S in OI-IV.		VAR_001668
	Natural variant	564	1	R → H: dbSNP rs1800211.		VAR_001671
	Natural variant	569	1	G → R in OI-II. Ref.34		VAR_001672
	Natural variant	593	1	G → C in OI-III/IV. Ref.56		VAR_001673
	Natural variant	593	1	G → S in OI-II/III; moderate to lethal form. Ref.70		VAR_001674
	Natural variant	638	1	G → S in OI-III/IV.		VAR_001675
	Natural variant	656	1	G → S in OI-II. Ref.84		VAR_001676
	Natural variant	701	1	G → C in OI-IV. Ref.83		VAR_001677
	Natural variant	704	1	G → C in OI-III.		VAR_001678
	Natural variant	719	1	G → D in OI-II. Ref.48		VAR_001679
	Natural variant	719	1	G → S in OI-III.		VAR_001680
	Natural variant	728	1	G → R in OI-II. Ref.22		VAR_001681
	Natural variant	737	1	G → D in OI-II.		VAR_001682
	Natural variant	743	1	G → S in OI-II. Ref.68		VAR_001683
	Natural variant	743	1	G → V in OI-II. Ref.68		VAR_001684
	Natural variant	764	1	G → V in OI-II. Ref.82		VAR_001685
	Natural variant	767	1	G → S in OI-III; severe. Ref.23		VAR_001686
	Natural variant	776	1	G → S in OI-II. Ref.45		VAR_001687
	Natural variant	809	1	G → S in OI-II. Ref.45		VAR_001688
	Natural variant	815	1	G → V in OI-II. Ref.53		VAR_001689
	Natural variant	821	1	G → S in OI-III.		VAR_001690
	Natural variant	823	1	P → A: dbSNP rs1800214. Ref.69		VAR_001691
	Natural variant	839	1	G → S in OI-II; mild to moderate form. Ref.78		VAR_001692
	Natural variant	842	1	G → R in OI-II. Ref.36		VAR_001693
	Natural variant	845	1	G → R in OI-II.		VAR_001694
	Natural variant	851	1	G → D in OI-II.		VAR_001695
	Natural variant	866	1	G → S in OI-III. Ref.86		VAR_008118
	Natural variant	869	1	G → C in OI-II. Ref.49		VAR_001696
	Natural variant	884	1	G → S in OI-II/III; extremely severe form.		VAR_001697
	Natural variant	896	1	G → C in OI-II.		VAR_001698
	Natural variant	926	1	G → C in OI-II. Ref.35 Ref.50		VAR_001699
	Natural variant	980	1	G → V in OI-II. Ref.59		VAR_001700
	Natural variant	1010	1	G → S in OI-IV. Ref.39		VAR_001701
	Natural variant	1014	1	R → C in Caffey disease.		VAR_033097
	Natural variant	1019	1	G → A: dbSNP rs1135348. Ref.1 Ref.18		VAR_030013
	Natural variant	1022	1	G → S in OI-III; severe form.		VAR_001702
	Natural variant	1022	1	G → V in OI-II.		VAR_001703
	Natural variant	1025	1	G → R in OI-II. Ref.46		VAR_001704
	Natural variant	1040	1	G → S in OI-II/III; moderate to lethal form.		VAR_001705
	Natural variant	1043	1	G → S in OI-II.		VAR_001706
	Natural variant	1046 – 1048	3	Missing in OI-II. Ref.55 Ref.60		VAR_001707
	Natural variant	1049	1	G → S in OI-III.		VAR_001708
	Natural variant	1058	1	G → S in OI-IV; mild form.		VAR_001709
	Natural variant	1061	1	G → D in OI-II.		VAR_001710
	Natural variant	1061	1	G → S in OI-IV. Ref.76		VAR_001711
	Natural variant	1075	1	A → T: dbSNP rs1800215. Ref.57		VAR_001712
	Natural variant	1076	1	G → S in OI-III; severe form.		VAR_001713
	Natural variant	1079	1	G → S in OI-I/II; mild to moderate form.		VAR_001714
	Natural variant	1082	1	G → C in OI-II. Ref.42		VAR_001715
	Natural variant	1088	1	G → A in OI-II. Ref.66		VAR_001716
	Natural variant	1091	1	G → S in OI-II. Ref.47		VAR_001717
	Natural variant	1100	1	G → S in OI-II; mild to moderate form.		VAR_001718
	Natural variant	1106	1	G → A in OI-II. Ref.40		VAR_001719
	Natural variant	1124	1	G → C in OI-II. Ref.75		VAR_001720
	Natural variant	1141	1	R → Q: dbSNP rs41316713.		VAR_033778
	Natural variant	1142	1	G → S in OI-II.		VAR_001721
	Natural variant	1151	1	G → S in OI-III.		VAR_001722
	Natural variant	1151	1	G → V in OI-II. Ref.40 Ref.62		VAR_001723
	Natural variant	1154	1	G → R in OI-II. Ref.40		VAR_001724
	Natural variant	1166	1	G → C in OI-II. Ref.33		VAR_001725
	Natural variant	1172	1	G → D in OI-II. Ref.84		VAR_001726
	Natural variant	1177	1	V → I: dbSNP rs41316719.		VAR_033779
	Natural variant	1181	1	G → S in OI-II. Ref.47 Ref.51		VAR_001727
	Natural variant	1184	1	G → V in OI-II. Ref.40 Ref.62		VAR_001728
	Natural variant	1187	1	G → S in OI-II/III; extremely severe form.		VAR_001729
	Natural variant	1187	1	G → V in OI-II. Ref.47		VAR_001730
	Natural variant	1195	1	G → C in OI-II; mild form.		VAR_001731
	Natural variant	1251	1	S → T: dbSNP rs3205325. Ref.25		VAR_030014
	Natural variant	1277	1	D → H in OI-II; impaired pro-alpha chain association. Ref.25		VAR_001732
	Natural variant	1312	1	W → C in OI-II. Ref.63		VAR_001733
	Natural variant	1337 – 1338	2	Missing in OI-II; impaired pro-alpha chain association.		VAR_001734
	Natural variant	1388	1	L → R in OI-II; impaired pro-alpha chain association. Ref.25		VAR_001735
	Natural variant	1391	1	Q → K: dbSNP rs2586486. Ref.1 Ref.2 Ref.27		VAR_030015
	Natural variant	1430	1	K → N: dbSNP rs1059454.		VAR_033780
	Natural variant	1431	1	T → P: dbSNP rs1059454.		VAR_033781
	Natural variant	1434	1	T → S: dbSNP rs1800220. Ref.25 Ref.1		VAR_001736
	Natural variant	1438	1	P → R: dbSNP rs17857117. Ref.5		VAR_030016
	Natural variant	1460	1	P → H: dbSNP rs17853657. Ref.5		VAR_030017
	Natural variant	1464	1	L → P in OI-III. Ref.79		VAR_001737
Experimental info
	Sequence conflict	59	1	R → Q in CAA25394. Ref.8
	Sequence conflict	112 – 114	3	Missing in AAB94054. Ref.2
	Sequence conflict	288	1	E → P AA sequence Ref.15
	Sequence conflict	370	1	R → L in AAB59373. Ref.6
	Sequence conflict	484	1	P → L in AAA52289. Ref.19
	Sequence conflict	595	1	A → R in AAA51847. Ref.20
	Sequence conflict	721	1	Q → E Ref.22
	Sequence conflict	738	1	L → E Ref.22
	Sequence conflict	975 – 976	2	LP → PL in AAA52291. Ref.19
	Sequence conflict	1081	1	V → A in AAA51995. Ref.18
	Sequence conflict	1329	1	S → T in AAB27856. Ref.25

Sequences

	Sequence		Length	Mass (Da)
	P02452-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: B0581DAD2809DDE8	FASTA	1,464	138,911
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Dalgleish R. Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ALA-1019; LYS-1391 AND SER-1434.
[2]	"Analysis of the COL1A1 and COL1A2 genes by PCR amplification and scanning by conformation-sensitive gel electrophoresis identifies only COL1A1 mutations in 15 patients with osteogenesis imperfecta type I: identification of common sequences of null-allele mutations." Korkko J.M., Ala-Kokko L., De Paepe A., Nuytinck L., Earley J.J., Prockop D.J. Am. J. Hum. Genet. 62:98-110(1998) [PubMed: 9443882] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LYS-1391.
[3]	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 Cited for: SEQUENCE REVISION TO 1049.
[4]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Spleen.
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ARG-1438 AND HIS-1460. Tissue: Brain.
[6]	"Complete nucleotide sequence of the region encompassing the first twenty-five exons of the human pro alpha 1(I) collagen gene (COL1A1)." D'Alessio M., Bernard M.P., Pretorius P.J., de Wet W., Ramirez F., Pretorious P.J. Gene 67:105-115(1988) [PubMed: 2843432] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-589.
[7]	"Structure of a full-length cDNA clone for the prepro alpha 1(I) chain of human type I procollagen." Tromp G., Kuivaniemi H., Stacey A., Shikata H., Baldwin C.T., Jaenisch R., Prockup D.J. Biochem. J. 253:919-922(1988) [PubMed: 3178743] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-472.
[8]	"Human pro alpha 1(I) collagen gene structure reveals evolutionary conservation of a pattern of introns and exons." Chu M.-L., de Wet W.J., Bernard M.P., Ding J.-F., Morabito M., Myers J., Williams C., Ramirez F. Nature 310:337-340(1984) [PubMed: 6462220] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-181.
[9]	"DNA sequences in the first intron of the human pro-alpha 1(I) collagen gene enhance transcription." Rossouw C.M.S., Vergeer W.P., du Plooy S.J., Bernard M.P., Ramirez F., de Wet W. J. Biol. Chem. 262:15151-15157(1987) [PubMed: 2822714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44.
[10]	"Fine structural analysis of the human pro-alpha 1 (I) collagen gene. Promoter structure, AluI repeats, and polymorphic transcripts." Chu M.-L., de Wet W., Bernard M.P., Ramirez F. J. Biol. Chem. 260:2315-2320(1985) [PubMed: 2857713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
[11]	"Regulatory elements in the first intron contribute to transcriptional control of the human alpha 1(I) collagen gene." Bornstein P., McKay J., Morishima J.K., Devarayalu S., Gelinas R.E. Proc. Natl. Acad. Sci. U.S.A. 84:8869-8873(1987) [PubMed: 3480516] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
[12]	"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." Wirtz M.K., Keene D.R., Hori H., Glanville R.W., Steinmann B., Rao V.H., Hollister D.W. J. Biol. Chem. 265:6312-6317(1990) [PubMed: 2318855] [Abstract] Cited for: PROTEIN SEQUENCE OF 33-52.
[13]	"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." Weil D., D'Alessio M., Ramirez F., de Wet W., Cole W.G., Chan D., Bateman J.F. EMBO J. 8:1705-1710(1989) [PubMed: 2767050] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 156-183.
[14]	"Isolation and characterization of the cyanogen bromide peptides from the alpha 1 and alpha 2 chains of human skin collagen." Click E.M., Bornstein P. Biochemistry 9:4699-4706(1970) [PubMed: 5529814] [Abstract] Cited for: PROTEIN SEQUENCE OF 162-301, ALLYSINE AT LYS-170, PYROGLUTAMATE FORMATION AT GLN-162. Tissue: Skin.
[15]	"A critical crosslink region in human-bone-derived collagen type I. Specific cleavage site at residue Leu95." Baetge B., Notbohm H., Diebold J., Lehmann H., Bodo M., Deutzmann R., Muller P.K. Eur. J. Biochem. 192:153-159(1990) [PubMed: 2169412] [Abstract] Cited for: PROTEIN SEQUENCE OF 175-187 AND 274-289.
[16]	"A comparative study of glycopeptides derived from selected vertebrate collagens. A possible role of the carbohydrate in fibril formation." Morgan P.H., Jacobs H.G., Segrest J.P., Cunningham L.W. J. Biol. Chem. 245:5042-5048(1970) [PubMed: 4319110] [Abstract] Cited for: PROTEIN SEQUENCE OF 263-268. Tissue: Skin.
[17]	"Segmental amplification of the entire helical and telopeptide regions of the cDNA for human alpha 1 (I) collagen." Labhard M.E., Hollister D.W. Matrix 10:124-130(1990) [PubMed: 2374517] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 281-302; 402-420; 823-842; 924-944; 1026-1045 AND 1143-1162.
[18]	"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." Bernard M.P., Chu M.-L., Myers J.C., Ramirez F., Eikenberry E.F., Prockop D.J. Biochemistry 22:5213-5223(1983) [PubMed: 6689127] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 425-1464, VARIANT ALA-1019.
[19]	"Cloning and characterization of five overlapping cDNAs specific for the human pro alpha 1(I) collagen chain." Chu M.-L., Myers J.C., Bernard M.P., Ding J.-F., Ramirez F. Nucleic Acids Res. 10:5925-5934(1982) [PubMed: 6183642] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 425-490; 965-1024; 999-1039 AND 1453-1464.
[20]	"Multiexon deletion in an osteogenesis imperfecta variant with increased type III collagen mRNA." Chu M.-L., Gargiulo V., Williams C.J., Ramirez F. J. Biol. Chem. 260:691-694(1985) [PubMed: 2981843] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 472-607.
[21]	"Intron-mediated recombination may cause a deletion in an alpha 1 type I collagen chain in a lethal form of osteogenesis imperfecta." Barsh G.S., Roush C.L., Bonadio J., Byers P.H., Gelinas R.E. Proc. Natl. Acad. Sci. U.S.A. 82:2870-2874(1985) [PubMed: 3857621] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 488-625.
[22]	"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." Wallis G.A., Starman B.J., Zinn A.B., Byers P.H. Am. J. Hum. Genet. 46:1034-1040(1990) [PubMed: 2339700] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 710-745, VARIANT OI-II ARG-728.
[23]	"Severe (type III) osteogenesis imperfecta due to glycine substitutions in the central domain of the collagen triple helix." Forlino A., Zolezzi F., Valli M., Pignatti P.F., Cetta G., Brunelli P.C., Mottes M. Hum. Mol. Genet. 3:2201-2206(1994) [PubMed: 7881420] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 746-781, VARIANT OI-III SER-767.
[24]	Lubec G., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 1063-1084, MASS SPECTROMETRY. Tissue: Fetal brain cortex.
[25]	"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." Chessler S.D., Wallis G.A., Byers P.H. J. Biol. Chem. 268:18218-18225(1993) [PubMed: 8349697] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1179-1464, VARIANTS OI-II HIS-1277; ARG-1388 AND 1337-GLU-TYR-1338 DEL, VARIANTS THR-1251 AND SER-1434.
[26]	"Substitution of cysteine for glycine within the carboxyl-terminal telopeptide of the alpha 1 chain of type I collagen produces mild osteogenesis imperfecta." Cohn D.H., Apone S., Eyre D.R., Starman B.J., Andreassen P., Charbonneau H., Nicholls A.C., Pope F.M., Byers P.H. J. Biol. Chem. 263:14605-14607(1988) [PubMed: 3170557] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1187-1220, VARIANT CYS-1195.
[27]	"Human pro alpha 1(I) collagen: cDNA sequence for the C-propeptide domain." Maekelae J.K., Raassina M., Virta A., Vuorio E. Nucleic Acids Res. 16:349-349(1988) [PubMed: 3340531] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1229-1454, VARIANT LYS-1391. Tissue: Bone.
[28]	"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." Willing M.C., Cohn D.H., Byers P.H. J. Clin. Invest. 85:282-290(1990) [PubMed: 2295701] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1440-1464.
[29]	"Highly conserved sequences in the 3'-untranslated region of the COL1A1 gene bind cell-specific nuclear proteins." Maatta A., Bornstein P., Penttinen R.P. FEBS Lett. 279:9-13(1991) [PubMed: 1995349] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1454-1464.
[30]	"Mutations in collagen genes: causes of rare and some common diseases in humans." Kuivaniemi H., Tromp G., Prockop D.J. FASEB J. 5:2052-2060(1991) [PubMed: 2010058] [Abstract] Cited for: REVIEW ON VARIANTS.
[31]	"Mutations in fibrillar collagens (types I, II, III, and XI), fibril-associated collagen (type IX), and network-forming collagen (type X) cause a spectrum of diseases of bone, cartilage, and blood vessels." Kuivaniemi H., Tromp G., Prockop D.J. Hum. Mutat. 9:300-315(1997) [PubMed: 9101290] [Abstract] Cited for: REVIEW ON VARIANTS.
[32]	"Osteogenesis imperfecta: translation of mutation to phenotype." Byers P.H., Wallis G.A., Willing M.C. J. Med. Genet. 28:433-442(1991) [PubMed: 1895312] [Abstract] Cited for: REVIEW ON OI VARIANTS.
[33]	"Lethal osteogenesis imperfecta resulting from a single nucleotide change in one human pro alpha 1(I) collagen allele." Cohn D.H., Byers P.H., Steinmann B., Gelinas R.E. Proc. Natl. Acad. Sci. U.S.A. 83:6045-6047(1986) [PubMed: 3016737] [Abstract] Cited for: VARIANT OI-II CYS-1166.
[34]	"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." Bateman J.F., Chan D., Walkers I.D., Rogers J.G., Cole W.G. J. Biol. Chem. 262:7021-7027(1987) [PubMed: 3108247] [Abstract] Cited for: VARIANT OI-II ARG-569.
[35]	"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." Vogel B.E., Minor R.R., Freund M., Prockop D.J. J. Biol. Chem. 262:14737-14744(1987) [PubMed: 3667599] [Abstract] Cited for: VARIANT OI-II CYS-926.
[36]	"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." Bateman J.F., Lamande S.R., Dahl H.-H.M., Chan D., Cole W.G. J. Biol. Chem. 263:11627-11630(1988) [PubMed: 3403550] [Abstract] Cited for: VARIANT OI-II ARG-842.
[37]	"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." Labhard M.E., Wirtz M.K., Pope F.M., Nicholls A.C., Hollister D.W. Mol. Biol. Med. 5:197-207(1988) [PubMed: 3244312] [Abstract] Cited for: VARIANT OI CYS-1195.
[38]	"RNA sequence analysis of a perinatal lethal osteogenesis imperfecta mutation." Patterson E., Smiley E., Bonadio J. J. Biol. Chem. 264:10083-10087(1989) [PubMed: 2470760] [Abstract] Cited for: VARIANT OI-II VAL-434.
[39]	"Osteogenesis imperfecta type IV. Detection of a point mutation in one alpha 1(I) collagen allele (COL1A1) by RNA/RNA hybrid analysis." Marini J.C., Grange D.K., Gottesman G.S., Lewis M.B., Koeplin D.A. J. Biol. Chem. 264:11893-11900(1989) [PubMed: 2745420] [Abstract] Cited for: VARIANT OI-IV SER-1010.
[40]	"Characterization of point mutations in the collagen COL1A1 and COL1A2 genes causing lethal perinatal osteogenesis imperfecta." Lamande S.R., Dahl H.-H.M., Cole W.G., Bateman J.F. J. Biol. Chem. 264:15809-15812(1989) [PubMed: 2777764] [Abstract] Cited for: VARIANTS OI-II ALA-1106; VAL-1151; ARG-1154 AND VAL-1184.
[41]	"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." Pack M., Constantinou C.D., Kalia K., Nielsen K.B., Prockop D.J. J. Biol. Chem. 264:19694-19699(1989) [PubMed: 2511192] [Abstract] Cited for: VARIANT OI SER-1022.
[42]	"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." Constantinou C.D., Nielsen K.B., Prockop D.J. J. Clin. Invest. 83:574-584(1989) [PubMed: 2913053] [Abstract] Cited for: VARIANT OI-II CYS-1082.
[43]	"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." Starman B.J., Eyre D.R., Charbonneau H., Harrylock M., Weis M.A., Weiss L., Graham J.M. Jr., Byers P.H. J. Clin. Invest. 84:1206-1214(1989) [PubMed: 2794057] [Abstract] Cited for: VARIANTS OI CYS-272; CYS-704 AND CYS-896.
[44]	"Two cysteine substitutions in the type I procollagen genes (COL1A1 and COL1A2) that cause lethal osteogenesis imperfecta. The location of glycine substitutions does not in any simple way predict their effets on protein function or phenotype." Fertala A., Westerhausen A., Morris G.M., Rooney J.E., Prockop D.J. Am. J. Hum. Genet. 47:A216-A216(1990) Cited for: VARIANT OI-II CYS-422.
[45]	"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." Westerhausen A., Kishi J., Prockop D.J. J. Biol. Chem. 265:13995-14000(1990) [PubMed: 2116413] [Abstract] Cited for: VARIANTS OI-II SER-776 AND SER-809.
[46]	"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." Wallis G.A., Starman B.J., Schwartz M.F., Byers P.H. J. Biol. Chem. 265:18628-18633(1990) [PubMed: 2211725] [Abstract] Cited for: VARIANT OI-II ARG-1025.
[47]	"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." Cohn D.H., Wallis G.A., Zhang X., Byers P.H. Matrix 10:236-236(1990) Cited for: VARIANTS OI-II SER-1091; SER-1181; SER-1187 AND VAL-1187.
[48]	"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." Zhuang J., Constantinou C.D., Ganguly A., Prockop D.J. Am. J. Hum. Genet. 48:1186-1191(1991) [PubMed: 2035536] [Abstract] Cited for: VARIANT OI-II ASP-719.
[49]	"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." Steinmann B., Westerhausen A., Constantinou C.D., Superti-Furga A., Prockop D.J. Biochem. J. 279:747-752(1991) [PubMed: 1953667] [Abstract] Cited for: VARIANT OI-II CYS-869.
[50]	"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." Kadler K.E., Torre-Blanco A., Adachi E., Vogel B.E., Hojima Y., Prockop D.J. Biochemistry 30:5081-5088(1991) [PubMed: 2036375] [Abstract] Cited for: VARIANT OI-II CYS-926.
[51]	"Osteogenesis imperfecta due to recurrent point mutations at CpG dinucleotides in the COL1A1 gene of type I collagen." Pruchno C.J., Cohn D.H., Wallis G.A., Willing M.C., Starman B.J., Zhang X., Byers P.H. Hum. Genet. 87:33-40(1991) [PubMed: 2037280] [Abstract] Cited for: VARIANT OI-III ARG-332, VARIANT OI-II SER-1181.
[52]	"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." Valli M., Mottes M., Tenni R., Sangalli A., Gomez Lira M., Rossi A., Antoniazzi F., Cetta G., Pignatti P.F. J. Biol. Chem. 266:1872-1878(1991) [PubMed: 1988452] [Abstract] Cited for: VARIANT OI CYS-356.
[53]	"Substitutions for glycine alpha 1-637 and glycine alpha 2-694 of type I procollagen in lethal osteogenesis imperfecta. The conformational strain on the triple helix introduced by a glycine substitution can be transmitted along the helix." Tsuneyoshi T., Westerhausen A., Constantinou C.D., Prockop D.J. J. Biol. Chem. 266:15608-15613(1991) [PubMed: 1874719] [Abstract] Cited for: VARIANT OI-II VAL-815.
[54]	"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." Deak S.B., Scholz P.M., Amenta P.S., Constantinou C.D., Levi-Minzi S.A., Gonzalez-Lavin L., MacKenzie J.W. J. Biol. Chem. 266:21827-21832(1991) [PubMed: 1718984] [Abstract] Cited for: VARIANT OI-I ARG-263.
[55]	"A 9-base pair deletion in COL1A1 in a lethal variant of osteogenesis imperfecta." Hawkins J.R., Superti-Furga A., Steinmann B., Dalgleish R. J. Biol. Chem. 266:22370-22374(1991) [PubMed: 1939261] [Abstract] Cited for: VARIANT OI-II 1046-GLY--PRO-1048 DEL.
[56]	"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." Nicholls A.C., Oliver J.E., Renouf D.V., Keston M., Pope F.M. J. Med. Genet. 28:757-764(1991) [PubMed: 1770532] [Abstract] Cited for: VARIANT OI-III/IV CYS-593.
[57]	"G to A polymorphism in exon 45 of the COL1A1 gene." Sokolov B.P., Constantinou C.D., Tsuneyoshi T., Zhuang J., Prockop D.J. Nucleic Acids Res. 19:4302-4302(1991) [PubMed: 1870989] [Abstract] Cited for: VARIANT THR-1075.
[58]	"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." Mottes M., Sangalli A., Valli M., Gomez Lira M., Tenni R., Buttitta P., Pignatti P.F., Cetta G. Hum. Genet. 89:480-484(1992) [PubMed: 1634225] [Abstract] Cited for: VARIANT OI-I SER-1079.
[59]	"A dominant mutation in the COL1A1 gene that substitutes glycine for valine causes recurrent lethal osteogenesis imperfecta." Bonaventure J., Cohen-Solal L., Lasselin C., Maroteaux P. Hum. Genet. 89:640-646(1992) [PubMed: 1511982] [Abstract] Cited for: VARIANT OI-II VAL-980.
[60]	"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." Wallis G.A., Kadler K.E., Starman B.J., Byers P.H. J. Biol. Chem. 267:25529-25534(1992) [PubMed: 1460047] [Abstract] Cited for: VARIANT OI-II 1046-GLY--PRO-1048 DEL.
[61]	"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." Shapiro J.R., Stover M.L., Burn V.E., McKinstry M.B., Burshell A.L., Chipman S.D., Rowe D.W. J. Clin. Invest. 89:567-573(1992) [PubMed: 1737847] [Abstract] Cited for: VARIANT OI CYS-221.
[62]	"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." Cole W.G., Patterson E., Bonadio J., Campbell P.E., Fortune D.W. J. Med. Genet. 29:112-118(1992) [PubMed: 1613761] [Abstract] Cited for: VARIANTS OI-II VAL-434; VAL-1151 AND VAL-1184.
[63]	"Chemical cleavage method for the detection of RNA base changes: experience in the application to collagen mutations in osteogenesis imperfecta." Bateman J.F., Lamande S.R., Hannagan M., Moeller I., Dahl H.-H.M., Cole W.G. Am. J. Med. Genet. 45:233-240(1993) [PubMed: 8456808] [Abstract] Cited for: VARIANT OI-II CYS-1312.
[64]	"Moderately severe osteogenesis imperfecta associated with substitutions of serine for glycine in the alpha 1(I) chain of type I collagen." Marini J.C., Lewis M.B., Chen K.J. Am. J. Med. Genet. 45:241-245(1993) [PubMed: 8456809] [Abstract] Cited for: VARIANT OI-III SER-530.
[65]	"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." 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. Connect. Tissue Res. 29:1-11(1993) [PubMed: 8339541] [Abstract] Cited for: VARIANT OI-IV CYS-353.
[66]	"Osteogenesis imperfecta and type-I collagen mutations. A lethal variant caused by a Gly910-->Ala substitution in the alpha 1 (I) chain." Valli M., Sangalli A., Rossi A., Mottes M., Forlino A., Tenni R., Pignatti P.F., Cetta G. Eur. J. Biochem. 211:415-419(1993) [PubMed: 7679635] [Abstract] Cited for: VARIANT OI-II ALA-1088.
[67]	"Gly85 to Val substitution in pro alpha 1(I) chain causes mild osteogenesis imperfecta and introduces a susceptibility to protease digestion." Valli M., Zolezzi F., Mottes M., Antoniazzi F., Stanzial F., Tenni R., Pignatti P.F., Cetta G. Eur. J. Biochem. 217:77-82(1993) [PubMed: 8223589] [Abstract] Cited for: VARIANT OI VAL-263.
[68]	"SSCP detection of a Gly565Val substitution in the pro alpha 1(I) collagen chain resulting in osteogenesis imperfecta type II." Mackay K., Lund A.M., Raghunath M., Steinmann B., Dalgleish R. Hum. Genet. 91:439-444(1993) [PubMed: 8100209] [Abstract] Cited for: VARIANT OI-II VAL-743.
[69]	"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." Mackay K., Byers P.H., Dalgleish R. Hum. Mol. Genet. 2:1155-1160(1993) [PubMed: 7691343] [Abstract] Cited for: VARIANTS OI SER-425; SER-530; SER-560 AND SER-719, VARIANT ALA-823.
[70]	"Paternal mosaicism for a COL1A1 dominant mutation (alpha 1 Ser-415) causes recurrent osteogenesis imperfecta." Mottes M., Gomez Lira M., Valli M., Scarano G., Lonardo F., Forlino A., Cetta G., Pignatti P.F. Hum. Mutat. 2:196-204(1993) [PubMed: 8364588] [Abstract] Cited for: VARIANT OI-II/III SER-593.
[71]	"Serine for glycine substitutions in type I collagen in two cases of type IV osteogenesis imperfecta (OI). Additional evidence for a regional model of OI pathophysiology." Marini J.C., Lewis M.B., Wang Q., Chen K.J., Orrison B.M. J. Biol. Chem. 268:2667-2673(1993) [PubMed: 8094076] [Abstract] Cited for: VARIANT OI-IV SER-530.
[72]	"BiP binds type I procollagen pro alpha chains with mutations in the carboxyl-terminal propeptide synthesized by cells from patients with osteogenesis imperfecta." Chessler S.D., Byers P.H. J. Biol. Chem. 268:18226-18233(1993) [PubMed: 8349698] [Abstract] Cited for: VARIANTS OI-II.
[73]	"Osteogenesis imperfecta: comparison of molecular defects with bone histological changes." Sztrolovics R., Glorieux F.H., Travers R., van der Rest M., Roughley P.J. Bone 15:321-328(1994) [PubMed: 7520724] [Abstract] Cited for: VARIANT OI-II ARG-389.
[74]	"Substitution of glycine-172 by arginine in the alpha 1 chain of type I collagen in a patient with osteogenesis imperfecta, type III." Mackay K., de Paepe A., Nuytinck L., Dalgleish R. Hum. Mutat. 3:324-326(1994) [PubMed: 8019571] [Abstract] Cited for: VARIANT OI-III ARG-350.
[75]	"Substitution of cysteine for glycine-946 in the alpha 1(I) chain of type I procollagen causes lethal osteogenesis imperfecta." Kurosaka D., Hattori S., Hori H., Yamaguchi N., Hasegawa T., Akimoto H., Nagai Y. J. Biochem. 115:853-857(1994) [PubMed: 7961597] [Abstract] Cited for: VARIANT OI-II CYS-1124.
[76]	"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." Lightfoot S.J., Atkinson M.S., Murphy G., Byers P.H., Kadler K.E. J. Biol. Chem. 269:30352-30357(1994) [PubMed: 7982948] [Abstract] Cited for: VARIANT OI-IV SER-1061.
[77]	"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." Zhuang J., Tromp G., Kuivaniemi H., Castells S., Prockop D.J. Am. J. Med. Genet. 61:111-116(1996) [PubMed: 8669434] [Abstract] Cited for: VARIANT OI-III ARG-332.
[78]	"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." Nuytinck L., Dalgleish R., Spotila L., Renard J.-P., van Regemorter N., de Paepe A. Hum. Genet. 97:324-329(1996) [PubMed: 8786074] [Abstract] Cited for: VARIANT OI-II SER-839.
[79]	"Mutation in the carboxy-terminal propeptide of the Pro alpha 1(I) chain of type I collagen in a child with severe osteogenesis imperfecta (OI type III): possible implications for protein folding." Oliver J.E., Thompson E.M., Pope F.M., Nicholls A.C. Hum. Mutat. 7:318-326(1996) [PubMed: 8723681] [Abstract] Cited for: VARIANT OI-III PRO-1464.
[80]	"Reduced bone density and osteoporosis associated with a polymorphic Sp1 binding site in the collagen type I alpha 1 gene." Grant S.F.A., Reid D.M., Blake G., Herd R., Fogelman I., Ralston S.H. Nat. Genet. 14:203-205(1996) [PubMed: 8841196] [Abstract] Cited for: INVOLVEMENT IN INVOLUTIONAL OSTEOPOROSIS.
[81]	"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." Lund A.M., Skovby F., Schwartz M. Hum. Mutat. 9:378-382(1997) [PubMed: 9101304] [Abstract] Cited for: VARIANTS OI SER-821; SER-1040; SER-1049; SER-1058 AND SER-1076.
[82]	"(G586V) substitutions in the alpha 1 and alpha 2 chains of collagen I: effect of alpha-chain stoichiometry on the phenotype of osteogenesis imperfecta?" Lund A.M., Skovby F., Schwartz M. Hum. Mutat. 9:431-436(1997) [PubMed: 9143923] [Abstract] Cited for: VARIANT OI-II VAL-764.
[83]	"Three novel type I collagen mutations in osteogenesis imperfecta type IV probands are associated with discrepancies between electrophoretic migration of osteoblast and fibroblast collagen." Sarafova A.P., Choi H., Forlino A., Gajko A., Cabral W.A., Tosi L., Reing C.M., Marini J.C. Hum. Mutat. 11:395-403(1998) [PubMed: 9600458] [Abstract] Cited for: VARIANTS OI-IV ALA-398; CYS-527 AND CYS-701.
[84]	"Four new cases of lethal osteogenesis imperfecta due to glycine substitutions in COL1A1 and genes." Mottes M., Gomez Lira M., Zolezzi F., Valli M., Lisi V., Freising P. Hum. Mutat. 12:71-72(1998) [PubMed: 10627137] [Abstract] Cited for: VARIANTS OI-II SER-656 AND ASP-1172.
[85]	"Relation of alleles of the collagen type Ialpha1 gene to bone density and the risk of osteoporotic fractures in postmenopausal women." 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. N. Engl. J. Med. 338:1016-1021(1998) [PubMed: 9535665] [Abstract] Cited for: INVOLVEMENT IN INVOLUTIONAL OSTEOPOROSIS.
[86]	"Osteogenesis imperfecta: mosaicism and refinement of the genotype-phenotype map in OI type III." Lund A.M., Astroem E., Soederhaell S., Schwartz M., Skovby F. Hum. Mutat. 13:503-503(1999) [PubMed: 10408781] [Abstract] Cited for: VARIANT OI-III SER-866.
[87]	"Classical Ehlers-Danlos syndrome caused by a mutation in type I collagen." Nuytinck L., Freund M., Lagae L., Pierard G.E., Hermanns-Le T., De Paepe A. Am. J. Hum. Genet. 66:1398-1402(2000) [PubMed: 10739762] [Abstract] Cited for: VARIANT EDS1 CYS-312.
[88]	"Deregulation of the platelet-derived growth factor B-chain gene via fusion with collagen gene COL1A1 in dermatofibrosarcoma protuberans and giant-cell fibroblastoma." 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. Nat. Genet. 15:95-98(1997) [PubMed: 8988177] [Abstract] Cited for: DISEASE, CHROMOSOMAL TRANSLOCATION WITH PDGFB.
[89]	"Dermatofibrosarcoma protuberans of breast." Sandberg A.A., Anderson W.D., Fredenberg C., Hashimoto H. Cancer Genet. Cytogenet. 142:56-59(2003) [PubMed: 12660034] [Abstract] Cited for: DISEASE, CHROMOSOMAL TRANSLOCATION WITH PDGFB.
[90]	"A novel COL1A1 mutation in infantile cortical hyperostosis (Caffey disease) expands the spectrum of collagen-related disorders." 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. J. Clin. Invest. 115:1250-1257(2005) [PubMed: 15864348] [Abstract] Cited for: VARIANT CAFFEY DISEASE CYS-1014.
+	Additional computationally mapped references.

Web resources

COL1A1

Collagen type I alpha-1 chain mutations

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

Wikipedia

Type-I collagen entry

Cross-references

Sequence databases

EMBLGenBankDDBJ

Z74615 mRNA. Translation: CAA98968.1.
AF017178 Genomic DNA. Translation: AAB94054.3.
AB209597 mRNA. Translation: BAD92834.1. Different initiation.
BC036531 mRNA. Translation: AAH36531.1.
M20789 Genomic DNA. Translation: AAB59373.1.
M36546 mRNA. Translation: AAA60150.1.
X07884 mRNA. Translation: CAA30731.1.
X00820 Genomic DNA. Translation: CAA25394.1.
J02829 Genomic DNA. Translation: AAA51993.1.
M10627 Genomic DNA. Translation: AAA51992.1.
J03559 Genomic DNA. Translation: AAA52052.1.
K01228 mRNA. Translation: AAA51995.1.
J00110 mRNA. Translation: AAA52289.1.
J00111 mRNA. Translation: AAA52290.1.
J00112 mRNA. Translation: AAA52291.1.
J00113 mRNA. Translation: AAN86574.1.
K03179 Genomic DNA. Translation: AAA51847.1.
M11162 Genomic DNA. Translation: AAA75386.1.
L47667 Genomic DNA. Translation: AAB59576.1.
S64596 mRNA. Translation: AAB27856.1.
M23213 Genomic DNA. Translation: AAB59363.1.
X06269 mRNA. Translation: CAA29605.1.
M32798 mRNA. Translation: AAA52049.1.
M55998 Genomic DNA. Translation: AAA52036.1.

IPI

IPI00297646.

PIR

CGHU1S. I60114.

RefSeq

NP_000079.2.

UniGene

Hs.172928
Hs.681002

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Q7D	X-ray	1.80	A/B/C	914-930	[»]
3EJH	X-ray	2.10	E/F	956-977	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

P02452. 1 interaction.

PTM databases

PhosphoSite

P02452.

2-D gel databases

DOSAC-COBS-2DPAGE

P02452.

Siena-2DPAGE

P02452.

Proteomic databases

PRIDE

P02452.

Genome annotation databases

Ensembl

ENSG00000108821. Homo sapiens. [Contig view]

GeneID

1277.

KEGG

hsa:1277.

Organism-specific databases

GeneCards

GC17M045617.

H-InvDB

HIX0016617.

HGNC

HGNC:2197. COL1A1.

HPA

HPA008405.
HPA011795.

MIM

114000. phenotype.
120150. gene.
130000. phenotype.
130060. phenotype.
166200. phenotype.
166210. phenotype.
166220. phenotype.
166710. phenotype.
259420. phenotype.
607907. phenotype.

Orphanet

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

PharmGKB

PA35041.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

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.

Gene expression databases

ArrayExpress

P02452.

Bgee

P02452.

GermOnline

ENSG00000108821. Homo sapiens.

Family and domain databases

InterPro

IPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_C.
[Graphical view]

Pfam

PF01410. COLFI. 1 hit.
PF01391. Collagen. 18 hits.
PF00093. VWC. 1 hit.
[Graphical view]

ProDom

PD000007. Clg_helix. 2 hits.
PD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00038. COLFI. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]

PROSITE

PS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00048. Collagenase.
DB00039. Palifermin.

NextBio

5161.

PMAP-CutDB

P02452.

SOURCE

Search...

Entry information

Entry name

CO1A1_HUMAN

Accession

Primary (citable) accession number: P02452
Secondary accession number(s): O76045 , P78441, Q13896, Q13902, Q13903, Q14037, Q14992, Q15176, Q15201, Q16050, Q59F64, Q7KZ30, Q7KZ34, Q8IVI5, Q8N473, Q9UML6, Q9UMM7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 132 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)