P08123 (CO1A2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Collagen alpha-2(I) chain

Alternative name(s):
Alpha-2 type I collagen

Gene names

Name:

COL1A2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1366 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.
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.
Domain	The C-terminal propeptide, also known as COLFI domain, have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. It binds a calcium ion which is essential for its function By similarity.
Post-translational modification	Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.
Involvement in 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8 Ref.9 Ref.28 Osteogenesis imperfecta 1 (OI1) [MIM:166200]: A dominantly inherited connective tissue disorder characterized by bone fragility and blue sclerae. Osteogenesis imperfecta type 1 is non-deforming with normal height or mild short stature, and no dentinogenesis imperfecta. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.33 Ref.38 Ref.54 Ref.62 Ref.63 Osteogenesis imperfecta 2 (OI2) [MIM:166210]: A connective tissue disorder characterized by bone fragility, with many perinatal fractures, severe bowing of long bones, undermineralization, and death in the perinatal period due to respiratory insufficiency. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18 Ref.29 Ref.30 Ref.31 Ref.34 Ref.36 Ref.37 Ref.42 Ref.44 Ref.46 Ref.48 Ref.49 Ref.56 Ref.61 Ref.63 Ref.65 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.60 Osteogenesis imperfecta 3 (OI3) [MIM:259420]: A connective tissue disorder characterized by progressively deforming bones, very short stature, a triangular face, severe scoliosis, grayish sclera and dentinogenesis imperfecta. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.19 Ref.33 Ref.38 Ref.40 Ref.45 Ref.47 Ref.50 Ref.51 Ref.52 Ref.53 Ref.54 Ref.55 Ref.57 Ref.61 Ref.63 Osteogenesis imperfecta 4 (OI4) [MIM:166220]: A connective tissue disorder characterized by moderately short stature, mild to moderate scoliosis, grayish or white sclera and dentinogenesis imperfecta. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12 Ref.22 Ref.32 Ref.35 Ref.41 Ref.43 Ref.44 Ref.53 Ref.61 Ref.63 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.
Sequence similarities	Belongs to the fibrillar collagen family. Contains 1 fibrillar collagen NC1 domain.

Ontologies

Keywords
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Chromosomal rearrangement Polymorphism
Disease	Disease mutation Dwarfism Ehlers-Danlos syndrome Osteogenesis imperfecta
Domain	Collagen Repeat Signal
Ligand	Calcium Metal-binding
PTM	Disulfide bond Glycoprotein Hydroxylation Pyrrolidone carboxylic acid
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	Rho protein signal transduction Inferred from direct assay PubMed 17217948. Source: UniProtKB axon guidance Traceable author statement. Source: Reactome blood vessel development Inferred from mutant phenotype PubMed 17211858. Source: UniProtKB cellular response to amino acid stimulus Inferred from electronic annotation. Source: Compara collagen fibril organization Inferred from mutant phenotype PubMed 17211858PubMed 18375391. Source: UniProtKB leukocyte migration Traceable author statement. Source: Reactome odontogenesis Non-traceable author statement PubMed 1740554. Source: UniProtKB platelet activation Traceable author statement. Source: Reactome protein heterotrimerization Inferred from electronic annotation. Source: Compara regulation of blood pressure Inferred from mutant phenotype PubMed 17334644. Source: UniProtKB skeletal system development Inferred from mutant phenotype PubMed 17955022PubMed 18375391PubMed 8841196. Source: UniProtKB skin morphogenesis Inferred from mutant phenotype PubMed 17211858. Source: UniProtKB transforming growth factor beta receptor signaling pathway Inferred from direct assay PubMed 17217948. Source: UniProtKB
Cellular_component	collagen type I Inferred from direct assay PubMed 18375391. Source: UniProtKB endoplasmic reticulum lumen Traceable author statement. Source: Reactome extracellular space Inferred from direct assay PubMed 18375391. Source: UniProtKB extracellular vesicular exosome Inferred from direct assay PubMed 21362503. Source: UniProtKB
Molecular_function	extracellular matrix structural constituent Non-traceable author statement PubMed 8982144. Source: UniProtKB identical protein binding Inferred from direct assay PubMed 17211858. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW platelet-derived growth factor binding Inferred from direct assay PubMed 8900172. Source: MGI protein binding, bridging Inferred from mutant phenotype PubMed 18375391. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 24	24	Potential
	Propeptide	25 – 79	55	N-terminal propeptide		PRO_0000005804
	Chain	80 – 1102	1023	Collagen alpha-2(I) chain		PRO_0000005805
	Propeptide	1103 – 1366	264	C-terminal propeptide		PRO_0000005806
Regions
	Domain	1133 – 1366	234	Fibrillar collagen NC1
Sites
	Metal binding	1181	1	Calcium By similarity
	Metal binding	1183	1	Calcium By similarity
	Metal binding	1184	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	1186	1	Calcium; via carbonyl oxygen By similarity
	Metal binding	1189	1	Calcium By similarity
Amino acid modifications
	Modified residue	80	1	Pyrrolidone carboxylic acid By similarity
	Modified residue	84	1	Allysine
	Modified residue	420	1	Hydroxyproline
	Modified residue	441	1	Hydroxyproline
	Modified residue	444	1	Hydroxyproline
	Glycosylation	1267	1	N-linked (GlcNAc...) Potential
	Disulfide bond	1163 ↔ 1195		By similarity
	Disulfide bond	1203 ↔ 1364		By similarity
	Disulfide bond	1272 ↔ 1317		By similarity
Natural variations
	Natural variant	59	1	T → P. Ref.6 Corresponds to variant rs1800221 [ dbSNP | Ensembl ].		VAR_030116
	Natural variant	76 – 93	18	Missing in EDS7B.		VAR_001851
	Natural variant	181 – 198	18	Missing in OI4.		VAR_030117
	Natural variant	193	1	G → S in OI4. Ref.61		VAR_063343
	Natural variant	202	1	G → R in OI4. Ref.63		VAR_063344
	Natural variant	211	1	G → D in OI1. Ref.54		VAR_001852
	Natural variant	234	1	R → C in OI2. Ref.65		VAR_063345
	Natural variant	247	1	G → R in OI1. Ref.63		VAR_063346
	Natural variant	249	1	I → N. Ref.1 Corresponds to variant rs1800228 [ dbSNP | Ensembl ].		VAR_001853
	Natural variant	253	1	G → D in OI2. Ref.63		VAR_063347
	Natural variant	256	1	G → V in OI4. Ref.63		VAR_063348
	Natural variant	270	1	V → I. Ref.3 Corresponds to variant rs368468 [ dbSNP | Ensembl ].		VAR_030118
	Natural variant	276	1	A → T. Ref.1 Corresponds to variant rs1800231 [ dbSNP | Ensembl ].		VAR_001854
	Natural variant	283	1	G → R in OI2. Ref.65		VAR_063349
	Natural variant	319	1	G → R in OI1. Ref.63		VAR_063350
	Natural variant	325	1	G → E in OI4. Ref.62		VAR_063351
	Natural variant	328	1	G → S in OI1, OI3 AND OI4. Ref.51 Ref.62		VAR_001855
	Natural variant	331	1	G → D in OI3. Ref.57		VAR_008119
	Natural variant	334	1	G → C in OI2.		VAR_001856
	Natural variant	337	1	G → C in OI3. Ref.57		VAR_001857
	Natural variant	337	1	G → S in OI3. Ref.54		VAR_001858
	Natural variant	344	1	L → V. Corresponds to variant rs16868573 [ dbSNP | Ensembl ].		VAR_055677
	Natural variant	345	1	Missing in OI3. Ref.40		VAR_001859
	Natural variant	349	1	G → C in OI3. Ref.33 Ref.38		VAR_001860
	Natural variant	358	1	G → S in OI3. Ref.62		VAR_063352
	Natural variant	397	1	G → E in OI2. Ref.65		VAR_063353
	Natural variant	409	1	G → V in OI2. Ref.56		VAR_001861
	Natural variant	433	1	G → E in OI2. Ref.42		VAR_001862
	Natural variant	454	1	G → C in OI2. Ref.65		VAR_063354
	Natural variant	457	1	G → L in OI2; requires 2 nucleotide substitutions. Ref.65		VAR_063355
	Natural variant	460	1	G → S in OI3. Ref.54		VAR_001863
	Natural variant	461 – 466	6	Missing in OI2.		VAR_063356
	Natural variant	483	1	A → V. Ref.1 Ref.3 Corresponds to variant rs414408 [ dbSNP | Ensembl ].		VAR_030119
	Natural variant	511	1	G → D in OI2.		VAR_001864
	Natural variant	517	1	G → R in OI3. Ref.45		VAR_001865
	Natural variant	526	1	G → E in OI2. Ref.65		VAR_063357
	Natural variant	528	1	N → S. Ref.64 Corresponds to variant rs41317144 [ dbSNP | Ensembl ].		VAR_033040
	Natural variant	547	1	G → R in OI2. Ref.36		VAR_001866
	Natural variant	549	1	P → A. Ref.1 Ref.2 Ref.4 Ref.15 Ref.39 Ref.64 Ref.65 Corresponds to variant rs42524 [ dbSNP | Ensembl ].		VAR_001867
	Natural variant	562	1	G → C in OI2.		VAR_001868
	Natural variant	562	1	G → V in OI2. Ref.65		VAR_063358
	Natural variant	564	1	A → T. Ref.64 Corresponds to variant rs41317153 [ dbSNP | Ensembl ].		VAR_033041
	Natural variant	586	1	G → R in OI2.		VAR_001869
	Natural variant	592	1	G → S in OI2. Ref.46		VAR_001870
	Natural variant	601	1	G → S in OI. Ref.62		VAR_063359
	Natural variant	625	1	G → D in OI2. Ref.61		VAR_063360
	Natural variant	634	1	G → V in OI4. Ref.41		VAR_001871
	Natural variant	637	1	G → D in OI2.		VAR_001872
	Natural variant	640	1	G → S in OI2.		VAR_001873
	Natural variant	670	1	G → D in OI2. Ref.37		VAR_001874
	Natural variant	676 – 855	180	Missing in OI2.		VAR_030120
	Natural variant	676	1	G → D in OI3. Ref.62		VAR_063361
	Natural variant	676	1	G → V in OI3 and OI4. Ref.19 Ref.32		VAR_001875
	Natural variant	678	1	P → H. Ref.1 Ref.2 Ref.3 Ref.5 Ref.17 Corresponds to variant rs409108 [ dbSNP | Ensembl ].		VAR_030121
	Natural variant	705 – 707	3	Missing in OI2.		VAR_063362
	Natural variant	708	1	R → Q in Marfan syndrome.		VAR_001876
	Natural variant	715	1	G → D in OI2.		VAR_001877
	Natural variant	730	1	G → C in OI2. Ref.49		VAR_001878
	Natural variant	733	1	G → C in OI1. Ref.63		VAR_063363
	Natural variant	736	1	G → C in OI1; mild. Ref.33 Ref.38		VAR_001879
	Natural variant	739	1	G → R in OI2. Ref.65		VAR_063364
	Natural variant	743	1	A → G. Ref.1 Ref.3 Ref.5 Corresponds to variant rs408535 [ dbSNP | Ensembl ].		VAR_001880
	Natural variant	748	1	G → V in OI2. Ref.65		VAR_063365
	Natural variant	751	1	G → S in OI4. Ref.35		VAR_001881
	Natural variant	754	1	G → C in OI4. Ref.61		VAR_063366
	Natural variant	754	1	G → R in OI2.		VAR_001882
	Natural variant	766	1	G → V in OI4. Ref.44		VAR_001883
	Natural variant	778	1	G → S in OI3. Ref.50		VAR_001884
	Natural variant	784	1	G → R in OI2. Ref.34		VAR_001885
	Natural variant	787	1	G → C in OI2. Ref.56		VAR_001886
	Natural variant	790	1	G → D in OI2. Ref.48 Ref.65		VAR_001887
	Natural variant	796	1	G → S in OI2. Ref.44		VAR_001888
	Natural variant	798	1	P → PP in OI2. Ref.65		VAR_063367
	Natural variant	806 – 811	6	Missing in OI2.		VAR_063368
	Natural variant	811	1	G → GPPG in OI4.		VAR_063369
	Natural variant	820	1	G → S in OI3. Ref.62		VAR_063370
	Natural variant	822	1	R → H. Ref.54 Corresponds to variant rs1800240 [ dbSNP | Ensembl ].		VAR_001889
	Natural variant	835	1	G → C in OI3. Ref.61		VAR_063371
	Natural variant	835	1	G → S in OI1. Ref.54		VAR_001890
	Natural variant	856	1	G → R in OI3. Ref.62		VAR_063372
	Natural variant	856	1	G → V in OI2. Ref.65		VAR_063373
	Natural variant	877	1	G → C in OI2. Ref.31		VAR_001891
	Natural variant	892	1	G → D in OI3 and OI4. Ref.53		VAR_001892
	Natural variant	895	1	G → D in OI2.		VAR_001893
	Natural variant	949	1	G → S in OI3; moderate. Ref.47 Ref.65		VAR_001894
	Natural variant	955	1	G → D in OI2. Ref.65		VAR_063374
	Natural variant	955	1	G → S in OI2. Ref.30		VAR_001895
	Natural variant	973	1	G → V in OI3. Ref.57		VAR_008120
	Natural variant	982	1	G → D in OI2. Ref.63		VAR_063375
	Natural variant	989	1	P → PVGP in OI4.		VAR_063376
	Natural variant	991	1	G → V in OI3. Ref.61		VAR_063377
	Natural variant	997	1	G → D in OI2. Ref.29		VAR_001896
	Natural variant	1003	1	G → D in OI2. Ref.63		VAR_063378
	Natural variant	1012	1	G → S in OI3 and OI4; moderate. Ref.43 Ref.62		VAR_001897
	Natural variant	1022	1	L → F. Ref.1 Ref.3 Ref.17 Corresponds to variant rs392609 [ dbSNP | Ensembl ].		VAR_001898
	Natural variant	1027	1	G → E in OI2. Ref.65		VAR_063379
	Natural variant	1058 – 1062	5	Missing in OI2.		VAR_063380
	Natural variant	1066	1	G → D in OI2.		VAR_001899
	Natural variant	1078	1	G → C in OI2.		VAR_001900
	Natural variant	1087	1	G → D in OI3. Ref.63		VAR_063381
	Natural variant	1094 – 1096	3	Missing in OI4.		VAR_063382
	Natural variant	1096	1	G → A in OI3. Ref.52		VAR_001901
	Natural variant	1101	1	P → L.		VAR_001903
	Natural variant	1102	1	G → R in OI4. Ref.22		VAR_001902
	Natural variant	1119	1	A → T 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. Ref.66		VAR_066386
	Natural variant	1148	1	T → P in OI3. Ref.55 Corresponds to variant rs1800250 [ dbSNP | Ensembl ].		VAR_001904
	Natural variant	1189	1	D → E. Ref.1 Ref.3 Ref.17 Corresponds to variant rs422361 [ dbSNP | Ensembl ].		VAR_001905
	Natural variant	1195	1	C → Y in OI1. Ref.63		VAR_063383
	Natural variant	1198	1	S → P. Ref.1 Ref.3 Ref.17 Corresponds to variant rs384487 [ dbSNP | Ensembl ].		VAR_001906
	Natural variant	1354	1	Q → H. Ref.1 Ref.2 Ref.3 Ref.17 Ref.20 Ref.23 Ref.24 Corresponds to variant rs418570 [ dbSNP | Ensembl ].		VAR_030122
Experimental info
	Sequence conflict	55	1	E → G in CAA26320. Ref.6
	Sequence conflict	333	1	V → P in AAB59374. Ref.1
	Sequence conflict	338	1	A → T in AAB59374. Ref.1
	Sequence conflict	549	1	P → D in CAA68709. Ref.5
	Sequence conflict	828	1	V → A in CAA23761. Ref.17
	Sequence conflict	831	1	T → P in CAA23761. Ref.17
	Sequence conflict	837	1	V → P in CAA23761. Ref.17
	Sequence conflict	980	1	E → V in AAA51996. Ref.21
	Sequence conflict	1098	1	P → L in CAA23761. Ref.17
	Sequence conflict	1122 – 1125	4	Missing in CAA23761. Ref.17
	Sequence conflict	1338	1	R → A in AAA51887. Ref.23

Sequences

	Sequence		Length	Mass (Da)
	P08123 [UniParc]. Last modified May 18, 2010. Version 7. Checksum: 1E68A5970FB4210A	FASTA	1,366	129,314
	10 20 30 40 50 60 MLSFVDTRTL LLLAVTLCLA TCQSLQEETV RKGPAGDRGP RGERGPPGPP GRDGEDGPTG 70 80 90 100 110 120 PPGPPGPPGP PGLGGNFAAQ YDGKGVGLGP GPMGLMGPRG PPGAAGAPGP QGFQGPAGEP 130 140 150 160 170 180 GEPGQTGPAG ARGPAGPPGK AGEDGHPGKP GRPGERGVVG PQGARGFPGT PGLPGFKGIR 190 200 210 220 230 240 GHNGLDGLKG QPGAPGVKGE PGAPGENGTP GQTGARGLPG ERGRVGAPGP AGARGSDGSV 250 260 270 280 290 300 GPVGPAGPIG SAGPPGFPGA PGPKGEIGAV GNAGPAGPAG PRGEVGLPGL SGPVGPPGNP 310 320 330 340 350 360 GANGLTGAKG AAGLPGVAGA PGLPGPRGIP GPVGAAGATG ARGLVGEPGP AGSKGESGNK 370 380 390 400 410 420 GEPGSAGPQG PPGPSGEEGK RGPNGEAGSA GPPGPPGLRG SPGSRGLPGA DGRAGVMGPP 430 440 450 460 470 480 GSRGASGPAG VRGPNGDAGR PGEPGLMGPR GLPGSPGNIG PAGKEGPVGL PGIDGRPGPI 490 500 510 520 530 540 GPAGARGEPG NIGFPGPKGP TGDPGKNGDK GHAGLAGARG APGPDGNNGA QGPPGPQGVQ 550 560 570 580 590 600 GGKGEQGPPG PPGFQGLPGP SGPAGEVGKP GERGLHGEFG LPGPAGPRGE RGPPGESGAA 610 620 630 640 650 660 GPTGPIGSRG PSGPPGPDGN KGEPGVVGAV GTAGPSGPSG LPGERGAAGI PGGKGEKGEP 670 680 690 700 710 720 GLRGEIGNPG RDGARGAPGA VGAPGPAGAT GDRGEAGAAG PAGPAGPRGS PGERGEVGPA 730 740 750 760 770 780 GPNGFAGPAG AAGQPGAKGE RGAKGPKGEN GVVGPTGPVG AAGPAGPNGP PGPAGSRGDG 790 800 810 820 830 840 GPPGMTGFPG AAGRTGPPGP SGISGPPGPP GPAGKEGLRG PRGDQGPVGR TGEVGAVGPP 850 860 870 880 890 900 GFAGEKGPSG EAGTAGPPGT PGPQGLLGAP GILGLPGSRG ERGLPGVAGA VGEPGPLGIA 910 920 930 940 950 960 GPPGARGPPG AVGSPGVNGA PGEAGRDGNP GNDGPPGRDG QPGHKGERGY PGNIGPVGAA 970 980 990 1000 1010 1020 GAPGPHGPVG PAGKHGNRGE TGPSGPVGPA GAVGPRGPSG PQGIRGDKGE PGEKGPRGLP 1030 1040 1050 1060 1070 1080 GLKGHNGLQG LPGIAGHHGD QGAPGSVGPA GPRGPAGPSG PAGKDGRTGH PGTVGPAGIR 1090 1100 1110 1120 1130 1140 GPQGHQGPAG PPGPPGPPGP PGVSGGGYDF GYDGDFYRAD QPRSAPSLRP KDYEVDATLK 1150 1160 1170 1180 1190 1200 SLNNQIETLL TPEGSRKNPA RTCRDLRLSH PEWSSGYYWI DPNQGCTMDA IKVYCDFSTG 1210 1220 1230 1240 1250 1260 ETCIRAQPEN IPAKNWYRSS KDKKHVWLGE TINAGSQFEY NVEGVTSKEM ATQLAFMRLL 1270 1280 1290 1300 1310 1320 ANYASQNITY HCKNSIAYMD EETGNLKKAV ILQGSNDVEL VAEGNSRFTY TVLVDGCSKK 1330 1340 1350 1360 TNEWGKTIIE YKTNKPSRLP FLDIAPLDIG GADQEFFVDI GPVCFK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Organization of the human pro-alpha 2(I) collagen gene." de Wet W.J., Bernard M.P., Benson-Chanda V., Chu M.-L., Dickson L.A., Weil D., Ramirez F. J. Biol. Chem. 262:16032-16036(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ASN-249; THR-276; VAL-483; ALA-549; HIS-678; GLY-743; PHE-1022; GLU-1189; PRO-1198 AND HIS-1354.
[2]	"The human type I collagen mutation database." Dalgleish R. Nucleic Acids Res. 25:181-187(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], REVIEW ON OI VARIANTS, VARIANTS ALA-549; HIS-678 AND HIS-1354.
[3]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ILE-270; VAL-483; HIS-678; GLY-743; PHE-1022; GLU-1189; PRO-1198 AND HIS-1354.
[4]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-549. Tissue: Skin and Uterus.
[5]	"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." Kuivaniemi H., Tromp G., Chu M.-L., Prockop D.J. Biochem. J. 252:633-640(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-765, VARIANTS HIS-678 AND GLY-743. Tissue: Placenta.
[6]	"Analysis of the promoter region and the N-propeptide domain of the human pro alpha 2(I) collagen gene." Dickson L.A., de Wet W., Di Liberto M., Weil D., Ramirez F. Nucleic Acids Res. 13:3427-3438(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-93, VARIANT PRO-59.
[7]	"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." Akai J., Kimura A., Arai K., Uehara K., Hata R. Connect. Tissue Res. 30:1-6(1998) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32.
[8]	"Structural and functional characterization of a splicing mutation in the pro-alpha 2(I) collagen gene of an Ehlers-Danlos type VII patient." Weil D., D'Alessio M., Ramirez F., Eyre D.R. J. Biol. Chem. 265:16007-16011(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-93, VARIANT EDS7B 76-ASN--MET-93 DEL.
[9]	"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." Watson R.B., Wallis G.A., Holmes D.F., Viljoen D., Byers P.H., Kadler K.E. J. Biol. Chem. 267:9093-9100(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-93, VARIANT EDS7B 76-ASN--MET-93 DEL.
[10]	"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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 80-96. Tissue: Skin.
[11]	"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." Kuivaniemi H., Sabol C., Tromp G., Sippola-Thiele M., Prockop D.J. J. Biol. Chem. 263:11407-11413(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 145-198.
[12]	"Expression of mutant alpha (I)-procollagen in osteoblast and fibroblast cultures from a proband with osteogenesis imperfecta type IV." Chipman S.D., Shapiro J.R., McKinstry M.B., Stover M.L., Branson P., Rowe D.W. J. Bone Miner. Res. 7:793-805(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 163-213, VARIANT OI4 181-GLY--LYS-198 DEL.
[13]	Kalicki J., Wamsley P., Gibson A. Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 181-1366.
[14]	"Comparative sequence studies on alpha2-CB2 from calf, human, rabbit and pig-skin collagen." Fietzek P.P., Furthmayr H., Kuehn K. Eur. J. Biochem. 47:257-261(1974) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 417-447. Tissue: Skin.
[15]	"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." Tromp G., Prockop D.J. Proc. Natl. Acad. Sci. U.S.A. 85:5254-5258(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 520-573, VARIANT ALA-549.
[16]	"Isolation and characterization of a human pro alpha 2(I) collagen gene segment." Tajima S., Ting J.P., Pinnell S.R., Kaufman R.E. J. Invest. Dermatol. 82:265-269(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 622-657.
[17]	"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." Bernard M.P., Myers J.C., Chu M.-L., Ramirez F., Eikenberry E.F., Prockop D.J. Biochemistry 22:1139-1145(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 623-1366, VARIANTS HIS-678; PHE-1022; GLU-1189; PRO-1198 AND HIS-1354.
[18]	"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." Chessler S.D., Byers P.H. J. Biol. Chem. 267:7751-7757(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 631-864, VARIANT OI2 676-GLY--ALA-855 DEL.
[19]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 663-746, VARIANT OI3 VAL-676.
[20]	"Growth-dependent modulation of type I collagen production and mRNA levels in cultured human skin fibroblasts." Maekelae J.K., Vuorio T., Vuorio E. Biochim. Biophys. Acta 1049:171-176(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 960-1356, VARIANT HIS-1354. Tissue: Skin.
[21]	"Cloning a cDNA for the pro-alpha 2 chain of human type I collagen." Myers J.C., Chu M.-L., Faro S.H., Clark W.J., Prockop D.J., Ramirez F. Proc. Natl. Acad. Sci. U.S.A. 78:3516-3520(1981) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 964-1019.
[22]	"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." Wenstrup R.J., Cohn D.H., Cohen T., Byers P.H. J. Biol. Chem. 263:7734-7740(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1090-1107, VARIANT OI4 ARG-1102.
[23]	"Analysis of the 3' end of the human pro-alpha 2(I) collagen gene. Utilization of multiple polyadenylation sites in cultured fibroblasts." 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. J. Biol. Chem. 258:10128-10135(1983) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1319-1366, VARIANT HIS-1354.
[24]	"Osteogenesis imperfecta: cloning of a pro-alpha 2(I) collagen gene with a frameshift mutation." Pihlajaniemi T., Dickson L.A., Pope F.M., Korhonen V.R., Nicholls A., Prockop D.J., Myers J.C. J. Biol. Chem. 259:12941-12944(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1319-1366, VARIANT HIS-1354. Tissue: Skin.
[25]	"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] [Europe PMC] [Abstract] Cited for: REVIEW ON VARIANTS.
[26]	"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] [Europe PMC] [Abstract] Cited for: REVIEW ON VARIANTS.
[27]	"Osteogenesis imperfecta: translation of mutation to phenotype." Byers P.H., Wallis G.A., Willing M.C. J. Med. Genet. 28:433-442(1991) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON OI VARIANTS.
[28]	"Ehlers-Danlos syndrome type VIIB. Deletion of 18 amino acids comprising the N-telopeptide region of a pro-alpha 2(I) chain." Wirtz M.K., Glanville R.W., Steinmann B., Rao V.H., Hollister D.W. J. Biol. Chem. 262:16376-16385(1987) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT EDS7B 76-ASN--MET-93 DEL.
[29]	"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." Baldwin C.T., Constantinou C., Dumars K.W., Prockop D.J. J. Biol. Chem. 264:3002-3006(1989) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT OI2 ASP-997.
[30]	"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] [Europe PMC] [Abstract] Cited for: VARIANT OI2 SER-955.
[31]	"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." Fertala A., Westerhausen A., Morris G.M., Rooney J.E., Prockop D.J. Am. J. Hum. Genet. 47:A216-A216(1990) Cited for: VARIANT OI2 CYS-877.
[32]	"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." Bateman J.F., Hannagan M., Chan D., Cole W.G. Biochem. J. 276:765-770(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT OI4 VAL-676.
[33]	"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." Wenstrup R.J., Shrago-Howe A.W., Lever L.W., Phillips C.L., Byers P.H., Cohn D.H. J. Biol. Chem. 266:2590-2594(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT OI3 CYS-349, VARIANT OI1 CYS-736.
[34]	"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] [Europe PMC] [Abstract] Cited for: VARIANT OI2 ARG-784.
[35]	"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." Spotila L.D., Constantinou C.D., Sereda L., Ganguly A., Riggs B.L., Prockop D.J. Proc. Natl. Acad. Sci. U.S.A. 88:5423-5427(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT OI4 SER-751.
[36]	"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." Bateman J.F., Moeller I., Hannagan M., Chan D., Cole W.G. Hum. Mutat. 1:55-62(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT OI2 ARG-547.
[37]	"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." Niyibizi C., Bonadio J., Byers P.H., Eyre D.R. J. Biol. Chem. 267:23108-23112(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT OI2 ASP-670.
[38]	"Mutations in the COL1A2 gene of type I collagen that result in nonlethal forms of osteogenesis imperfecta." Wenstrup R.J., Lever L.W., Phillips C.L., Quarles L.D. Am. J. Med. Genet. 45:228-232(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT OI3 CYS-349, VARIANT OI1 CYS-736.
[39]	"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] [Europe PMC] [Abstract] Cited for: VARIANT ALA-549.
[40]	"A single amino acid deletion in the alpha 2(I) chain of type I collagen produces osteogenesis imperfecta type III." Molyneux K., Starman B.J., Byers P.H., Dalgleish R. Hum. Genet. 90:621-628(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT OI3 VAL-345 DEL.
[41]	"Identification of type I collagen gene (COL1A2) mutations in nonlethal osteogenesis imperfecta." Sztrolovics R., Glorieux F.H., van der Rest M., Roughley P.J. Hum. Mol. Genet. 2:1319-1321(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT OI4 VAL-634.
[42]	"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." Rose N.J., Mackay K., Byers P.H., Dalgleish R. Hum. Mol. Genet. 2:2175-2177(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT OI2 GLU-433.
[43]	"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] [Europe PMC] [Abstract] Cited for: VARIANT OI4 SER-1012.
[44]	"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." Wang Q., Orrison B.M., Marini J.C. J. Biol. Chem. 268:25162-25167(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT OI4 VAL-766, VARIANT OI2 SER-796.
[45]	"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] [Europe PMC] [Abstract] Cited for: VARIANT OI3 ARG-517.
[46]	"Three unrelated individuals with perinatally lethal osteogenesis imperfecta resulting from identical Gly502Ser substitutions in the alpha 2-chain of type I collagen." Rose N.J., Mackay K., de Paepe A., Steinmann B., Punnett H.H., Dalgleish R. Hum. Genet. 94:497-503(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT OI2 SER-592.
[47]	"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." Rose N.J., Mackay K., Byers P.H., Dalgleish R. Hum. Mutat. 3:391-394(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT OI3 SER-949.
[48]	"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." Cohen-Solal L., Zylberberg L., Sangalli A., Gomez Lira M., Mottes M. J. Biol. Chem. 269:14751-14758(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT OI2 ASP-790.
[49]	"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." Gomez Lira M., Sangalli A., Pignatti P.F., Digilio M.C., Giannotti A., Carnevale E., Mottes M. J. Med. Genet. 31:965-968(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT OI2 CYS-730.
[50]	"Genetic counselling on brittle grounds: recurring osteogenesis imperfecta due to parental mosaicism for a dominant mutation." Raghunath M., Mackay K., Dalgleish R., Steinmann B. Eur. J. Pediatr. 154:123-129(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT OI3 SER-778.
[51]	"A Gly238Ser substitution in the alpha 2 chain of type I collagen results in osteogenesis imperfecta type III." Rose N.J., Mackay K., Byers P.H., Dalgleish R. Hum. Genet. 95:215-218(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT OI3 SER-328.
[52]	"A novel G1006A substitution in the alpha 2(I) chain of type I collagen produces osteogenesis imperfecta type III." Lu J., Costa T., Cole W.G. Hum. Mutat. 5:175-178(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT OI3 ALA-1096.
[53]	"Gly802Asp substitution in the pro alpha 2(I) collagen chain in a family with recurrent osteogenesis imperfecta due to paternal mosaicism." Lund A.M., Schwartz M., Raghunath M., Steinmann B., Skovby F. Eur. J. Hum. Genet. 4:39-45(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT OI3 ASP-892, VARIANT OI4 ASP-892.
[54]	"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." Zhuang J., Tromp G., Kuivaniemi H., Castells S., Bugge M., Prockop D.J. Hum. Mutat. 7:89-99(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS OI1 ASP-211 AND SER-835, VARIANTS OI3 SER-337 AND SER-460, VARIANT HIS-822.
[55]	"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] [Europe PMC] [Abstract] Cited for: VARIANT OI3 PRO-1148.
[56]	"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] [Europe PMC] [Abstract] Cited for: VARIANTS OI2 VAL-409 AND CYS-787.
[57]	"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] [Europe PMC] [Abstract] Cited for: VARIANTS OI3 ASP-331; CYS-337 AND VAL-973.
[58]	"PLAG1 fusion oncogenes in lipoblastoma." Hibbard M.K., Kozakewich H.P., Dal Cin P., Sciot R., Tan X., Xiao S., Fletcher J.A. Cancer Res. 60:4869-4872(2000) [PubMed] [Europe PMC] [Abstract] Cited for: CHROMOSOMAL REARRANGEMENT WITH PLAG1.
[59]	"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." Schwarze U., Hata R., McKusick V.A., Shinkai H., Hoyme H.E., Pyeritz R.E., Byers P.H. Am. J. Hum. Genet. 74:917-930(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN CARDIAC VALVULAR EDS.
[60]	"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." Malfait F., Symoens S., Coucke P., Nunes L., De Almeida S., De Paepe A. J. Med. Genet. 43:E36-E36(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN EDSCV.
[61]	"Osteogenesis imperfecta: clinical, biochemical and molecular findings." Venturi G., Tedeschi E., Mottes M., Valli M., Camilot M., Viglio S., Antoniazzi F., Tato L. Clin. Genet. 70:131-139(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS OI4 SER-193 AND CYS-754, VARIANT OI2 ASP-625, VARIANTS OI3 CYS-835 AND VAL-991.
[62]	"Mutational spectrum of type I collagen genes in Korean patients with osteogenesis imperfecta." 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. Hum. Mutat. 27:599-599(2006) [PubMed] [Europe PMC] [Abstract] Cited for: 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.
[63]	"Mutation analysis of COL1A1 and COL1A2 in patients diagnosed with osteogenesis imperfecta type I-IV." Pollitt R., McMahon R., Nunn J., Bamford R., Afifi A., Bishop N., Dalton A. Hum. Mutat. 27:716-716(2006) [PubMed] [Europe PMC] [Abstract] Cited for: 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, VARIANT OI3 ASP-1087.
[64]	"Natural variation in four human collagen genes across an ethnically diverse population." Chan T.F., Poon A., Basu A., Addleman N.R., Chen J., Phong A., Byers P.H., Klein T.E., Kwok P.Y. Genomics 91:307-314(2008) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS SER-528; ALA-549 AND THR-564.
[65]	"Mutation and polymorphism spectrum in osteogenesis imperfecta type II: implications for genotype-phenotype relationships." Bodian D.L., Chan T.F., Poon A., Schwarze U., Yang K., Byers P.H., Kwok P.Y., Klein T.E. Hum. Mol. Genet. 18:463-471(2009) [PubMed] [Europe PMC] [Abstract] Cited for: 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, VARIANT ALA-549.
[66]	"COL1 C-propeptide cleavage site mutations cause high bone mass osteogenesis imperfecta." 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. Hum. Mutat. 32:598-609(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT THR-1119, CHARACTERIZATION OF VARIANT THR-1119.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Osteogenesis imperfecta variant database

Collagen type I alpha 2 (COL1A2)

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	J03464 mRNA. Translation: AAB59374.1. Z74616 mRNA. Translation: CAA98969.1. AF004877 Genomic DNA. Translation: AAB93981.1. BC042586 mRNA. Translation: AAH42586.1. BC054498 mRNA. Translation: AAH54498.1. Y00724 mRNA. Translation: CAA68709.1. X02488 mRNA. Translation: CAA26320.1. AB004317 Genomic DNA. Translation: BAA25383.1. M35391 Genomic DNA. Translation: AAA60041.1. S98904 Genomic DNA. Translation: AAB22126.1. M21671 Genomic DNA. Translation: AAA59994.1. S41099 mRNA. Translation: AAB22761.1. AC002528 Genomic DNA. Translation: AAB69977.1. M21353 Genomic DNA. Translation: AAA52053.1. M28985 Genomic DNA. Translation: AAA60356.1. V00503 mRNA. Translation: CAA23761.1. S96821 mRNA. Translation: AAB22020.2. L47668 mRNA. Translation: AAB59577.1. X55525 mRNA. Translation: CAA39142.1. J00114 mRNA. Translation: AAA51996.1. M22816 mRNA. Translation: AAA51844.1. M22817 Genomic DNA. Translation: AAA51846.1. K01078 Genomic DNA. Translation: AAA51887.1. K02568 Genomic DNA. Translation: AAA51850.1.
IPI	IPI00304962.
PIR	CGHU2S. A28500.
RefSeq	NP_000080.2. NM_000089.3.
UniGene	Hs.489142.
3D structure databases
ProteinModelPortal	P08123.
SMR	P08123. Positions 1151-1365.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-36079N.
IntAct	P08123. 4 interactions.
MINT	MINT-4791958.
PTM databases
PhosphoSite	P08123.
Polymorphism databases
DMDM	296439507.
Proteomic databases
PaxDb	P08123.
PRIDE	P08123.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000297268; ENSP00000297268; ENSG00000164692.
GeneID	1278.
KEGG	hsa:1278.
UCSC	uc003ung.1. human.
Organism-specific databases
CTD	1278.
GeneCards	GC07P094023.
H-InvDB	HIX0006854.
HGNC	HGNC:2198. COL1A2.
HPA	CAB032650.
MIM	120160. gene. 130060. phenotype. 166200. phenotype. 166210. phenotype. 166220. phenotype. 225320. phenotype. 259420. phenotype.
neXtProt	NX_P08123.
Orphanet	99876. Ehlers-Danlos syndrome type 7B. 230851. Ehlers-Danlos syndrome, cardiac valvular type. 230857. Ehlers-Danlos/osteogenesis imperfecta syndrome. 216796. Osteogenesis imperfecta type 1. 216804. Osteogenesis imperfecta type 2. 216812. Osteogenesis imperfecta type 3. 216820. Osteogenesis imperfecta type 4.
PharmGKB	PA35042.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG12793.
HOVERGEN	HBG004933.
KO	K06236.
OrthoDB	EOG412M65.
Enzyme and pathway databases
Pathway_Interaction_DB	endothelinpathway. Endothelins. il4_2pathway. IL4-mediated signaling events. smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling. lymphangiogenesis_pathway. VEGFR3 signaling in lymphatic endothelium.
Reactome	REACT_111045. Developmental Biology. REACT_111102. Signal Transduction. REACT_118779. Extracellular matrix organization. REACT_604. Hemostasis.
Gene expression databases
ArrayExpress	P08123.
Bgee	P08123.
Genevestigator	P08123.
GermOnline	ENSG00000164692. Homo sapiens.
Family and domain databases
InterPro	IPR008160. Collagen. IPR000885. Fib_collagen_C. [Graphical view]
Pfam	PF01410. COLFI. 1 hit. PF01391. Collagen. 6 hits. [Graphical view]
ProDom	PD002078. Fib_collagen_C. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00038. COLFI. 1 hit. [Graphical view]
PROSITE	PS51461. NC1_FIB. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL2685.
ChiTaRS	COL1A2. human.
DrugBank	DB00048. Collagenase.
GenomeRNAi	1278.
NextBio	5165.
SOURCE	Search...

Entry information

Entry name

CO1A2_HUMAN

Accession

Primary (citable) accession number: P08123
Secondary accession number(s): P02464 , Q13897, Q13997, Q13998, Q14038, Q14057, Q15177, Q15947, Q16480, Q16511, Q7Z5S6, Q9UEB6, Q9UEF9, Q9UM83, Q9UMI1, Q9UML5, Q9UMM6, Q9UPH0

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	May 18, 2010
Last modified:	May 1, 2013
This is version 158 of the entry and version 7 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.