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P08123

- CO1A2_HUMAN

UniProt

P08123 - CO1A2_HUMAN

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Protein

Collagen alpha-2(I) chain

Gene

COL1A2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Type I collagen is a member of group I collagen (fibrillar forming collagen).

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi1181 – 11811CalciumBy similarity
Metal bindingi1183 – 11831CalciumBy similarity
Metal bindingi1184 – 11841Calcium; via carbonyl oxygenBy similarity
Metal bindingi1186 – 11861Calcium; via carbonyl oxygenBy similarity
Metal bindingi1189 – 11891CalciumBy similarity

GO - Molecular functioni

  1. extracellular matrix structural constituent Source: UniProtKB
  2. identical protein binding Source: UniProtKB
  3. metal ion binding Source: UniProtKB-KW
  4. platelet-derived growth factor binding Source: MGI
  5. protein binding, bridging Source: UniProtKB

GO - Biological processi

  1. blood coagulation Source: Reactome
  2. blood vessel development Source: UniProtKB
  3. cellular response to amino acid stimulus Source: Ensembl
  4. collagen catabolic process Source: Reactome
  5. collagen fibril organization Source: UniProtKB
  6. extracellular matrix disassembly Source: Reactome
  7. extracellular matrix organization Source: Reactome
  8. leukocyte migration Source: Reactome
  9. odontogenesis Source: UniProtKB
  10. platelet activation Source: Reactome
  11. protein heterotrimerization Source: Ensembl
  12. regulation of blood pressure Source: UniProtKB
  13. Rho protein signal transduction Source: UniProtKB
  14. skeletal system development Source: UniProtKB
  15. skin morphogenesis Source: UniProtKB
  16. transforming growth factor beta receptor signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_118779. Extracellular matrix organization.
REACT_12051. Cell surface interactions at the vascular wall.
REACT_121139. Collagen biosynthesis and modifying enzymes.
REACT_1230. Platelet Adhesion to exposed collagen.
REACT_13552. Integrin cell surface interactions.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_150206. Crosslinking of collagen fibrils.
REACT_150268. Anchoring fibril formation.
REACT_150401. Collagen degradation.
REACT_163699. Scavenging by Class A Receptors.
REACT_163874. Non-integrin membrane-ECM interactions.
REACT_163906. ECM proteoglycans.
REACT_163942. Syndecan interactions.
REACT_1695. GPVI-mediated activation cascade.

Names & Taxonomyi

Protein namesi
Recommended name:
Collagen alpha-2(I) chain
Alternative name(s):
Alpha-2 type I collagen
Gene namesi
Name:COL1A2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:2198. COL1A2.

Subcellular locationi

Secretedextracellular spaceextracellular matrix PROSITE-ProRule annotation

GO - Cellular componenti

  1. collagen type I trimer Source: UniProtKB
  2. endoplasmic reticulum lumen Source: Reactome
  3. extracellular matrix Source: UniProtKB
  4. extracellular region Source: Reactome
  5. extracellular space Source: UniProtKB
  6. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

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.3 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti76 – 9318Missing in EDS7B. 3 Publications
VAR_001851Add
BLAST
Osteogenesis imperfecta 1 (OI1) [MIM:166200]: An autosomal dominant form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI1 is a non-deforming form with normal height or mild short stature, and no dentinogenesis imperfecta.5 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti211 – 2111G → D in OI1. 1 Publication
VAR_001852
Natural varianti247 – 2471G → R in OI1. 1 Publication
VAR_063346
Natural varianti319 – 3191G → R in OI1. 1 Publication
VAR_063350
Natural varianti328 – 3281G → S in OI1, OI3 AND OI4. 2 Publications
VAR_001855
Natural varianti733 – 7331G → C in OI1. 1 Publication
VAR_063363
Natural varianti736 – 7361G → C in OI1; mild. 2 Publications
VAR_001879
Natural varianti835 – 8351G → S in OI1. 1 Publication
VAR_001890
Natural varianti1195 – 11951C → Y in OI1. 1 Publication
VAR_063383
Osteogenesis imperfecta 2 (OI2) [MIM:166210]: An autosomal dominant form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI2 is characterized by bone fragility, with many perinatal fractures, severe bowing of long bones, undermineralization, and death in the perinatal period due to respiratory insufficiency.16 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti234 – 2341R → C in OI2. 1 Publication
VAR_063345
Natural varianti253 – 2531G → D in OI2. 1 Publication
VAR_063347
Natural varianti283 – 2831G → R in OI2. 1 Publication
VAR_063349
Natural varianti334 – 3341G → C in OI2.
VAR_001856
Natural varianti397 – 3971G → E in OI2. 1 Publication
VAR_063353
Natural varianti409 – 4091G → V in OI2. 1 Publication
VAR_001861
Natural varianti433 – 4331G → E in OI2. 1 Publication
VAR_001862
Natural varianti454 – 4541G → C in OI2. 1 Publication
VAR_063354
Natural varianti457 – 4571G → L in OI2; requires 2 nucleotide substitutions. 1 Publication
VAR_063355
Natural varianti461 – 4666Missing in OI2. 1 Publication
VAR_063356
Natural varianti511 – 5111G → D in OI2.
VAR_001864
Natural varianti526 – 5261G → E in OI2. 1 Publication
VAR_063357
Natural varianti547 – 5471G → R in OI2. 1 Publication
VAR_001866
Natural varianti562 – 5621G → C in OI2.
VAR_001868
Natural varianti562 – 5621G → V in OI2. 1 Publication
VAR_063358
Natural varianti586 – 5861G → R in OI2.
VAR_001869
Natural varianti592 – 5921G → S in OI2. 1 Publication
VAR_001870
Natural varianti625 – 6251G → D in OI2. 1 Publication
VAR_063360
Natural varianti637 – 6371G → D in OI2.
VAR_001872
Natural varianti640 – 6401G → S in OI2.
VAR_001873
Natural varianti670 – 6701G → D in OI2. 1 Publication
VAR_001874
Natural varianti676 – 855180Missing in OI2. 1 Publication
VAR_030120Add
BLAST
Natural varianti705 – 7073Missing in OI2. 1 Publication
VAR_063362
Natural varianti715 – 7151G → D in OI2.
VAR_001877
Natural varianti730 – 7301G → C in OI2. 1 Publication
VAR_001878
Natural varianti739 – 7391G → R in OI2. 1 Publication
VAR_063364
Natural varianti748 – 7481G → V in OI2. 1 Publication
VAR_063365
Natural varianti754 – 7541G → R in OI2.
VAR_001882
Natural varianti784 – 7841G → R in OI2. 1 Publication
VAR_001885
Natural varianti787 – 7871G → C in OI2. 1 Publication
VAR_001886
Natural varianti790 – 7901G → D in OI2. 2 Publications
VAR_001887
Natural varianti796 – 7961G → S in OI2. 1 Publication
VAR_001888
Natural varianti798 – 7981P → PP in OI2. 1 Publication
VAR_063367
Natural varianti806 – 8116Missing in OI2. 1 Publication
VAR_063368
Natural varianti856 – 8561G → V in OI2. 1 Publication
VAR_063373
Natural varianti877 – 8771G → C in OI2. 1 Publication
VAR_001891
Natural varianti895 – 8951G → D in OI2.
VAR_001893
Natural varianti955 – 9551G → D in OI2. 1 Publication
VAR_063374
Natural varianti955 – 9551G → S in OI2. 1 Publication
VAR_001895
Natural varianti982 – 9821G → D in OI2. 1 Publication
VAR_063375
Natural varianti997 – 9971G → D in OI2. 1 Publication
VAR_001896
Natural varianti1003 – 10031G → D in OI2. 1 Publication
VAR_063378
Natural varianti1027 – 10271G → E in OI2. 1 Publication
VAR_063379
Natural varianti1058 – 10625Missing in OI2. 1 Publication
VAR_063380
Natural varianti1066 – 10661G → D in OI2.
VAR_001899
Natural varianti1078 – 10781G → C in OI2.
VAR_001900
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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Osteogenesis imperfecta 3 (OI3) [MIM:259420]: An autosomal dominant form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI3 is characterized by progressively deforming bones, very short stature, a triangular face, severe scoliosis, grayish sclera and dentinogenesis imperfecta.15 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti328 – 3281G → S in OI1, OI3 AND OI4. 2 Publications
VAR_001855
Natural varianti331 – 3311G → D in OI3. 1 Publication
VAR_008119
Natural varianti337 – 3371G → C in OI3. 1 Publication
VAR_001857
Natural varianti337 – 3371G → S in OI3. 1 Publication
VAR_001858
Natural varianti345 – 3451Missing in OI3. 1 Publication
VAR_001859
Natural varianti349 – 3491G → C in OI3. 2 Publications
VAR_001860
Natural varianti358 – 3581G → S in OI3. 1 Publication
VAR_063352
Natural varianti460 – 4601G → S in OI3. 1 Publication
VAR_001863
Natural varianti517 – 5171G → R in OI3. 1 Publication
VAR_001865
Natural varianti676 – 6761G → D in OI3. 1 Publication
VAR_063361
Natural varianti676 – 6761G → V in OI3 and OI4. 2 Publications
VAR_001875
Natural varianti778 – 7781G → S in OI3. 1 Publication
VAR_001884
Natural varianti820 – 8201G → S in OI3. 1 Publication
VAR_063370
Natural varianti835 – 8351G → C in OI3. 1 Publication
VAR_063371
Natural varianti856 – 8561G → R in OI3. 1 Publication
VAR_063372
Natural varianti892 – 8921G → D in OI3 and OI4. 1 Publication
VAR_001892
Natural varianti949 – 9491G → S in OI3; moderate. 2 Publications
VAR_001894
Natural varianti973 – 9731G → V in OI3. 1 Publication
VAR_008120
Natural varianti991 – 9911G → V in OI3. 1 Publication
VAR_063377
Natural varianti1012 – 10121G → S in OI3 and OI4; moderate. 2 Publications
VAR_001897
Natural varianti1087 – 10871G → D in OI3. 1 Publication
VAR_063381
Natural varianti1096 – 10961G → A in OI3. 1 Publication
VAR_001901
Natural varianti1148 – 11481T → P in OI3. 1 Publication
Corresponds to variant rs1800250 [ dbSNP | Ensembl ].
VAR_001904
Osteogenesis imperfecta 4 (OI4) [MIM:166220]: An autosomal dominant form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI4 is characterized by moderately short stature, mild to moderate scoliosis, grayish or white sclera and dentinogenesis imperfecta.10 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti181 – 19818Missing in OI4. 1 Publication
VAR_030117Add
BLAST
Natural varianti193 – 1931G → S in OI4. 1 Publication
VAR_063343
Natural varianti202 – 2021G → R in OI4. 1 Publication
VAR_063344
Natural varianti256 – 2561G → V in OI4. 1 Publication
VAR_063348
Natural varianti325 – 3251G → E in OI4. 1 Publication
VAR_063351
Natural varianti328 – 3281G → S in OI1, OI3 AND OI4. 2 Publications
VAR_001855
Natural varianti634 – 6341G → V in OI4. 1 Publication
VAR_001871
Natural varianti676 – 6761G → V in OI3 and OI4. 2 Publications
VAR_001875
Natural varianti751 – 7511G → S in OI4. 1 Publication
VAR_001881
Natural varianti754 – 7541G → C in OI4. 1 Publication
VAR_063366
Natural varianti766 – 7661G → V in OI4. 1 Publication
VAR_001883
Natural varianti811 – 8111G → GPPG in OI4.
VAR_063369
Natural varianti892 – 8921G → D in OI3 and OI4. 1 Publication
VAR_001892
Natural varianti989 – 9891P → PVGP in OI4.
VAR_063376
Natural varianti1012 – 10121G → S in OI3 and OI4; moderate. 2 Publications
VAR_001897
Natural varianti1094 – 10963Missing in OI4. 1 Publication
VAR_063382
Natural varianti1102 – 11021G → R in OI4. 1 Publication
VAR_001902
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.

Keywords - Diseasei

Disease mutation, Dwarfism, Ehlers-Danlos syndrome, Osteogenesis imperfecta

Organism-specific databases

MIMi130060. phenotype.
166200. phenotype.
166210. phenotype.
166220. phenotype.
225320. phenotype.
259420. phenotype.
Orphaneti99876. Ehlers-Danlos syndrome type 7B.
230851. Ehlers-Danlos syndrome, cardiac valvular type.
230857. Ehlers-Danlos/osteogenesis imperfecta syndrome.
314029. High bone mass osteogenesis imperfecta.
216796. Osteogenesis imperfecta type 1.
216804. Osteogenesis imperfecta type 2.
216812. Osteogenesis imperfecta type 3.
216820. Osteogenesis imperfecta type 4.
PharmGKBiPA35042.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Propeptidei25 – 7955N-terminal propeptide1 PublicationPRO_0000005804Add
BLAST
Chaini80 – 11021023Collagen alpha-2(I) chainPRO_0000005805Add
BLAST
Propeptidei1103 – 1366264C-terminal propeptidePRO_0000005806Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei80 – 801Pyrrolidone carboxylic acidBy similarity
Modified residuei84 – 841Allysine
Modified residuei420 – 4201Hydroxyproline1 Publication
Modified residuei441 – 4411Hydroxyproline1 Publication
Modified residuei444 – 4441Hydroxyproline1 Publication
Disulfide bondi1163 ↔ 1195PROSITE-ProRule annotation
Disulfide bondi1203 ↔ 1364PROSITE-ProRule annotation
Glycosylationi1267 – 12671N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1272 ↔ 1317PROSITE-ProRule annotation

Post-translational modificationi

Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Hydroxylation, Pyrrolidone carboxylic acid

Proteomic databases

MaxQBiP08123.
PaxDbiP08123.
PRIDEiP08123.

PTM databases

PhosphoSiteiP08123.

Expressioni

Tissue specificityi

Forms the fibrils of tendon, ligaments and bones. In bones the fibrils are mineralized with calcium hydroxyapatite.

Gene expression databases

BgeeiP08123.
ExpressionAtlasiP08123. baseline and differential.
GenevestigatoriP08123.

Organism-specific databases

HPAiCAB032650.

Interactioni

Subunit structurei

Trimers of one alpha 2(I) and two alpha 1(I) chains.

Protein-protein interaction databases

BioGridi107675. 10 interactions.
DIPiDIP-36079N.
IntActiP08123. 9 interactions.
MINTiMINT-4791958.

Structurei

3D structure databases

ProteinModelPortaliP08123.
SMRiP08123. Positions 1151-1365.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1133 – 1366234Fibrillar collagen NC1PROSITE-ProRule annotationAdd
BLAST

Domaini

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).By similarity

Sequence similaritiesi

Belongs to the fibrillar collagen family.PROSITE-ProRule annotation
Contains 1 fibrillar collagen NC1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Collagen, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00770000120467.
HOVERGENiHBG004933.
InParanoidiP08123.
KOiK06236.
OMAiKNGDKGH.
OrthoDBiEOG7TJ3HH.
PhylomeDBiP08123.
TreeFamiTF344135.

Family and domain databases

InterProiIPR008160. Collagen.
IPR000885. Fib_collagen_C.
[Graphical view]
PfamiPF01410. COLFI. 1 hit.
PF01391. Collagen. 6 hits.
[Graphical view]
ProDomiPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00038. COLFI. 1 hit.
[Graphical view]
PROSITEiPS51461. NC1_FIB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P08123-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MLSFVDTRTL LLLAVTLCLA TCQSLQEETV RKGPAGDRGP RGERGPPGPP
60 70 80 90 100
GRDGEDGPTG PPGPPGPPGP PGLGGNFAAQ YDGKGVGLGP GPMGLMGPRG
110 120 130 140 150
PPGAAGAPGP QGFQGPAGEP GEPGQTGPAG ARGPAGPPGK AGEDGHPGKP
160 170 180 190 200
GRPGERGVVG PQGARGFPGT PGLPGFKGIR GHNGLDGLKG QPGAPGVKGE
210 220 230 240 250
PGAPGENGTP GQTGARGLPG ERGRVGAPGP AGARGSDGSV GPVGPAGPIG
260 270 280 290 300
SAGPPGFPGA PGPKGEIGAV GNAGPAGPAG PRGEVGLPGL SGPVGPPGNP
310 320 330 340 350
GANGLTGAKG AAGLPGVAGA PGLPGPRGIP GPVGAAGATG ARGLVGEPGP
360 370 380 390 400
AGSKGESGNK GEPGSAGPQG PPGPSGEEGK RGPNGEAGSA GPPGPPGLRG
410 420 430 440 450
SPGSRGLPGA DGRAGVMGPP GSRGASGPAG VRGPNGDAGR PGEPGLMGPR
460 470 480 490 500
GLPGSPGNIG PAGKEGPVGL PGIDGRPGPI GPAGARGEPG NIGFPGPKGP
510 520 530 540 550
TGDPGKNGDK GHAGLAGARG APGPDGNNGA QGPPGPQGVQ GGKGEQGPPG
560 570 580 590 600
PPGFQGLPGP SGPAGEVGKP GERGLHGEFG LPGPAGPRGE RGPPGESGAA
610 620 630 640 650
GPTGPIGSRG PSGPPGPDGN KGEPGVVGAV GTAGPSGPSG LPGERGAAGI
660 670 680 690 700
PGGKGEKGEP GLRGEIGNPG RDGARGAPGA VGAPGPAGAT GDRGEAGAAG
710 720 730 740 750
PAGPAGPRGS PGERGEVGPA GPNGFAGPAG AAGQPGAKGE RGAKGPKGEN
760 770 780 790 800
GVVGPTGPVG AAGPAGPNGP PGPAGSRGDG GPPGMTGFPG AAGRTGPPGP
810 820 830 840 850
SGISGPPGPP GPAGKEGLRG PRGDQGPVGR TGEVGAVGPP GFAGEKGPSG
860 870 880 890 900
EAGTAGPPGT PGPQGLLGAP GILGLPGSRG ERGLPGVAGA VGEPGPLGIA
910 920 930 940 950
GPPGARGPPG AVGSPGVNGA PGEAGRDGNP GNDGPPGRDG QPGHKGERGY
960 970 980 990 1000
PGNIGPVGAA GAPGPHGPVG PAGKHGNRGE TGPSGPVGPA GAVGPRGPSG
1010 1020 1030 1040 1050
PQGIRGDKGE PGEKGPRGLP GLKGHNGLQG LPGIAGHHGD QGAPGSVGPA
1060 1070 1080 1090 1100
GPRGPAGPSG PAGKDGRTGH PGTVGPAGIR GPQGHQGPAG PPGPPGPPGP
1110 1120 1130 1140 1150
PGVSGGGYDF GYDGDFYRAD QPRSAPSLRP KDYEVDATLK SLNNQIETLL
1160 1170 1180 1190 1200
TPEGSRKNPA RTCRDLRLSH PEWSSGYYWI DPNQGCTMDA IKVYCDFSTG
1210 1220 1230 1240 1250
ETCIRAQPEN IPAKNWYRSS KDKKHVWLGE TINAGSQFEY NVEGVTSKEM
1260 1270 1280 1290 1300
ATQLAFMRLL ANYASQNITY HCKNSIAYMD EETGNLKKAV ILQGSNDVEL
1310 1320 1330 1340 1350
VAEGNSRFTY TVLVDGCSKK TNEWGKTIIE YKTNKPSRLP FLDIAPLDIG
1360
GADQEFFVDI GPVCFK
Length:1,366
Mass (Da):129,314
Last modified:May 18, 2010 - v7
Checksum:i1E68A5970FB4210A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551E → G in CAA26320. (PubMed:4011429)Curated
Sequence conflicti333 – 3331V → P in AAB59374. (PubMed:2824475)Curated
Sequence conflicti338 – 3381A → T in AAB59374. (PubMed:2824475)Curated
Sequence conflicti549 – 5491P → D in CAA68709. (PubMed:3421913)Curated
Sequence conflicti828 – 8281V → A in CAA23761. (PubMed:6687691)Curated
Sequence conflicti831 – 8311T → P in CAA23761. (PubMed:6687691)Curated
Sequence conflicti837 – 8371V → P in CAA23761. (PubMed:6687691)Curated
Sequence conflicti980 – 9801E → V in AAA51996. (PubMed:6267597)Curated
Sequence conflicti1098 – 10981P → L in CAA23761. (PubMed:6687691)Curated
Sequence conflicti1122 – 11254Missing in CAA23761. (PubMed:6687691)Curated
Sequence conflicti1338 – 13381R → A in AAA51887. (PubMed:6309769)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti59 – 591T → P.1 Publication
Corresponds to variant rs1800221 [ dbSNP | Ensembl ].
VAR_030116
Natural varianti76 – 9318Missing in EDS7B. 3 Publications
VAR_001851Add
BLAST
Natural varianti181 – 19818Missing in OI4. 1 Publication
VAR_030117Add
BLAST
Natural varianti193 – 1931G → S in OI4. 1 Publication
VAR_063343
Natural varianti202 – 2021G → R in OI4. 1 Publication
VAR_063344
Natural varianti211 – 2111G → D in OI1. 1 Publication
VAR_001852
Natural varianti234 – 2341R → C in OI2. 1 Publication
VAR_063345
Natural varianti247 – 2471G → R in OI1. 1 Publication
VAR_063346
Natural varianti249 – 2491I → N.1 Publication
Corresponds to variant rs1800228 [ dbSNP | Ensembl ].
VAR_001853
Natural varianti253 – 2531G → D in OI2. 1 Publication
VAR_063347
Natural varianti256 – 2561G → V in OI4. 1 Publication
VAR_063348
Natural varianti270 – 2701V → I.1 Publication
Corresponds to variant rs368468 [ dbSNP | Ensembl ].
VAR_030118
Natural varianti276 – 2761A → T.1 Publication
Corresponds to variant rs1800231 [ dbSNP | Ensembl ].
VAR_001854
Natural varianti283 – 2831G → R in OI2. 1 Publication
VAR_063349
Natural varianti319 – 3191G → R in OI1. 1 Publication
VAR_063350
Natural varianti325 – 3251G → E in OI4. 1 Publication
VAR_063351
Natural varianti328 – 3281G → S in OI1, OI3 AND OI4. 2 Publications
VAR_001855
Natural varianti331 – 3311G → D in OI3. 1 Publication
VAR_008119
Natural varianti334 – 3341G → C in OI2.
VAR_001856
Natural varianti337 – 3371G → C in OI3. 1 Publication
VAR_001857
Natural varianti337 – 3371G → S in OI3. 1 Publication
VAR_001858
Natural varianti344 – 3441L → V.
Corresponds to variant rs16868573 [ dbSNP | Ensembl ].
VAR_055677
Natural varianti345 – 3451Missing in OI3. 1 Publication
VAR_001859
Natural varianti349 – 3491G → C in OI3. 2 Publications
VAR_001860
Natural varianti358 – 3581G → S in OI3. 1 Publication
VAR_063352
Natural varianti397 – 3971G → E in OI2. 1 Publication
VAR_063353
Natural varianti409 – 4091G → V in OI2. 1 Publication
VAR_001861
Natural varianti433 – 4331G → E in OI2. 1 Publication
VAR_001862
Natural varianti454 – 4541G → C in OI2. 1 Publication
VAR_063354
Natural varianti457 – 4571G → L in OI2; requires 2 nucleotide substitutions. 1 Publication
VAR_063355
Natural varianti460 – 4601G → S in OI3. 1 Publication
VAR_001863
Natural varianti461 – 4666Missing in OI2. 1 Publication
VAR_063356
Natural varianti483 – 4831A → V.2 Publications
Corresponds to variant rs414408 [ dbSNP | Ensembl ].
VAR_030119
Natural varianti511 – 5111G → D in OI2.
VAR_001864
Natural varianti517 – 5171G → R in OI3. 1 Publication
VAR_001865
Natural varianti526 – 5261G → E in OI2. 1 Publication
VAR_063357
Natural varianti528 – 5281N → S.1 Publication
Corresponds to variant rs41317144 [ dbSNP | Ensembl ].
VAR_033040
Natural varianti547 – 5471G → R in OI2. 1 Publication
VAR_001866
Natural varianti549 – 5491P → A.7 Publications
Corresponds to variant rs42524 [ dbSNP | Ensembl ].
VAR_001867
Natural varianti562 – 5621G → C in OI2.
VAR_001868
Natural varianti562 – 5621G → V in OI2. 1 Publication
VAR_063358
Natural varianti564 – 5641A → T.1 Publication
Corresponds to variant rs41317153 [ dbSNP | Ensembl ].
VAR_033041
Natural varianti586 – 5861G → R in OI2.
VAR_001869
Natural varianti592 – 5921G → S in OI2. 1 Publication
VAR_001870
Natural varianti601 – 6011G → S in OI. 1 Publication
VAR_063359
Natural varianti625 – 6251G → D in OI2. 1 Publication
VAR_063360
Natural varianti634 – 6341G → V in OI4. 1 Publication
VAR_001871
Natural varianti637 – 6371G → D in OI2.
VAR_001872
Natural varianti640 – 6401G → S in OI2.
VAR_001873
Natural varianti670 – 6701G → D in OI2. 1 Publication
VAR_001874
Natural varianti676 – 855180Missing in OI2. 1 Publication
VAR_030120Add
BLAST
Natural varianti676 – 6761G → D in OI3. 1 Publication
VAR_063361
Natural varianti676 – 6761G → V in OI3 and OI4. 2 Publications
VAR_001875
Natural varianti678 – 6781P → H.5 Publications
Corresponds to variant rs409108 [ dbSNP | Ensembl ].
VAR_030121
Natural varianti705 – 7073Missing in OI2. 1 Publication
VAR_063362
Natural varianti708 – 7081R → Q in Marfan syndrome.
VAR_001876
Natural varianti715 – 7151G → D in OI2.
VAR_001877
Natural varianti730 – 7301G → C in OI2. 1 Publication
VAR_001878
Natural varianti733 – 7331G → C in OI1. 1 Publication
VAR_063363
Natural varianti736 – 7361G → C in OI1; mild. 2 Publications
VAR_001879
Natural varianti739 – 7391G → R in OI2. 1 Publication
VAR_063364
Natural varianti743 – 7431A → G.3 Publications
Corresponds to variant rs408535 [ dbSNP | Ensembl ].
VAR_001880
Natural varianti748 – 7481G → V in OI2. 1 Publication
VAR_063365
Natural varianti751 – 7511G → S in OI4. 1 Publication
VAR_001881
Natural varianti754 – 7541G → C in OI4. 1 Publication
VAR_063366
Natural varianti754 – 7541G → R in OI2.
VAR_001882
Natural varianti766 – 7661G → V in OI4. 1 Publication
VAR_001883
Natural varianti778 – 7781G → S in OI3. 1 Publication
VAR_001884
Natural varianti784 – 7841G → R in OI2. 1 Publication
VAR_001885
Natural varianti787 – 7871G → C in OI2. 1 Publication
VAR_001886
Natural varianti790 – 7901G → D in OI2. 2 Publications
VAR_001887
Natural varianti796 – 7961G → S in OI2. 1 Publication
VAR_001888
Natural varianti798 – 7981P → PP in OI2. 1 Publication
VAR_063367
Natural varianti806 – 8116Missing in OI2. 1 Publication
VAR_063368
Natural varianti811 – 8111G → GPPG in OI4.
VAR_063369
Natural varianti820 – 8201G → S in OI3. 1 Publication
VAR_063370
Natural varianti822 – 8221R → H.1 Publication
Corresponds to variant rs1800240 [ dbSNP | Ensembl ].
VAR_001889
Natural varianti835 – 8351G → C in OI3. 1 Publication
VAR_063371
Natural varianti835 – 8351G → S in OI1. 1 Publication
VAR_001890
Natural varianti856 – 8561G → R in OI3. 1 Publication
VAR_063372
Natural varianti856 – 8561G → V in OI2. 1 Publication
VAR_063373
Natural varianti877 – 8771G → C in OI2. 1 Publication
VAR_001891
Natural varianti892 – 8921G → D in OI3 and OI4. 1 Publication
VAR_001892
Natural varianti895 – 8951G → D in OI2.
VAR_001893
Natural varianti949 – 9491G → S in OI3; moderate. 2 Publications
VAR_001894
Natural varianti955 – 9551G → D in OI2. 1 Publication
VAR_063374
Natural varianti955 – 9551G → S in OI2. 1 Publication
VAR_001895
Natural varianti973 – 9731G → V in OI3. 1 Publication
VAR_008120
Natural varianti982 – 9821G → D in OI2. 1 Publication
VAR_063375
Natural varianti989 – 9891P → PVGP in OI4.
VAR_063376
Natural varianti991 – 9911G → V in OI3. 1 Publication
VAR_063377
Natural varianti997 – 9971G → D in OI2. 1 Publication
VAR_001896
Natural varianti1003 – 10031G → D in OI2. 1 Publication
VAR_063378
Natural varianti1012 – 10121G → S in OI3 and OI4; moderate. 2 Publications
VAR_001897
Natural varianti1022 – 10221L → F.3 Publications
Corresponds to variant rs392609 [ dbSNP | Ensembl ].
VAR_001898
Natural varianti1027 – 10271G → E in OI2. 1 Publication
VAR_063379
Natural varianti1058 – 10625Missing in OI2. 1 Publication
VAR_063380
Natural varianti1066 – 10661G → D in OI2.
VAR_001899
Natural varianti1067 – 10671R → H.1 Publication
VAR_069633
Natural varianti1078 – 10781G → C in OI2.
VAR_001900
Natural varianti1087 – 10871G → D in OI3. 1 Publication
VAR_063381
Natural varianti1094 – 10963Missing in OI4. 1 Publication
VAR_063382
Natural varianti1096 – 10961G → A in OI3. 1 Publication
VAR_001901
Natural varianti1101 – 11011P → L.
VAR_001903
Natural varianti1102 – 11021G → R in OI4. 1 Publication
VAR_001902
Natural varianti1119 – 11191A → 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. 1 Publication
VAR_066386
Natural varianti1148 – 11481T → P in OI3. 1 Publication
Corresponds to variant rs1800250 [ dbSNP | Ensembl ].
VAR_001904
Natural varianti1189 – 11891D → E.3 Publications
Corresponds to variant rs422361 [ dbSNP | Ensembl ].
VAR_001905
Natural varianti1195 – 11951C → Y in OI1. 1 Publication
VAR_063383
Natural varianti1198 – 11981S → P.3 Publications
Corresponds to variant rs384487 [ dbSNP | Ensembl ].
VAR_001906
Natural varianti1354 – 13541Q → H.7 Publications
Corresponds to variant rs418570 [ dbSNP | Ensembl ].
VAR_030122

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS34682.1.
PIRiA28500. CGHU2S.
RefSeqiNP_000080.2. NM_000089.3.
UniGeneiHs.489142.

Genome annotation databases

EnsembliENST00000297268; ENSP00000297268; ENSG00000164692.
GeneIDi1278.
KEGGihsa:1278.
UCSCiuc003ung.1. human.

Polymorphism databases

DMDMi296439507.

Keywords - Coding sequence diversityi

Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
Osteogenesis imperfecta variant database

Collagen type I alpha 2 (COL1A2)

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS34682.1.
PIRi A28500. CGHU2S.
RefSeqi NP_000080.2. NM_000089.3.
UniGenei Hs.489142.

3D structure databases

ProteinModelPortali P08123.
SMRi P08123. Positions 1151-1365.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107675. 10 interactions.
DIPi DIP-36079N.
IntActi P08123. 9 interactions.
MINTi MINT-4791958.

Chemistry

ChEMBLi CHEMBL2364188.
DrugBanki DB00048. Collagenase.

PTM databases

PhosphoSitei P08123.

Polymorphism databases

DMDMi 296439507.

Proteomic databases

MaxQBi P08123.
PaxDbi P08123.
PRIDEi P08123.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000297268 ; ENSP00000297268 ; ENSG00000164692 .
GeneIDi 1278.
KEGGi hsa:1278.
UCSCi uc003ung.1. human.

Organism-specific databases

CTDi 1278.
GeneCardsi GC07P094023.
GeneReviewsi COL1A2.
H-InvDB HIX0006854.
HGNCi HGNC:2198. COL1A2.
HPAi CAB032650.
MIMi 120160. gene.
130060. phenotype.
166200. phenotype.
166210. phenotype.
166220. phenotype.
225320. phenotype.
259420. phenotype.
neXtProti NX_P08123.
Orphaneti 99876. Ehlers-Danlos syndrome type 7B.
230851. Ehlers-Danlos syndrome, cardiac valvular type.
230857. Ehlers-Danlos/osteogenesis imperfecta syndrome.
314029. High bone mass osteogenesis imperfecta.
216796. Osteogenesis imperfecta type 1.
216804. Osteogenesis imperfecta type 2.
216812. Osteogenesis imperfecta type 3.
216820. Osteogenesis imperfecta type 4.
PharmGKBi PA35042.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00770000120467.
HOVERGENi HBG004933.
InParanoidi P08123.
KOi K06236.
OMAi KNGDKGH.
OrthoDBi EOG7TJ3HH.
PhylomeDBi P08123.
TreeFami TF344135.

Enzyme and pathway databases

Reactomei REACT_118779. Extracellular matrix organization.
REACT_12051. Cell surface interactions at the vascular wall.
REACT_121139. Collagen biosynthesis and modifying enzymes.
REACT_1230. Platelet Adhesion to exposed collagen.
REACT_13552. Integrin cell surface interactions.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_150206. Crosslinking of collagen fibrils.
REACT_150268. Anchoring fibril formation.
REACT_150401. Collagen degradation.
REACT_163699. Scavenging by Class A Receptors.
REACT_163874. Non-integrin membrane-ECM interactions.
REACT_163906. ECM proteoglycans.
REACT_163942. Syndecan interactions.
REACT_1695. GPVI-mediated activation cascade.

Miscellaneous databases

ChiTaRSi COL1A2. human.
GeneWikii COL1A2.
GenomeRNAii 1278.
NextBioi 5165.
PROi P08123.
SOURCEi Search...

Gene expression databases

Bgeei P08123.
ExpressionAtlasi P08123. baseline and differential.
Genevestigatori P08123.

Family and domain databases

InterProi IPR008160. Collagen.
IPR000885. Fib_collagen_C.
[Graphical view ]
Pfami PF01410. COLFI. 1 hit.
PF01391. Collagen. 6 hits.
[Graphical view ]
ProDomi PD002078. Fib_collagen_C. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00038. COLFI. 1 hit.
[Graphical view ]
PROSITEi PS51461. NC1_FIB. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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, HYDROXYLATION AT PRO-420; PRO-441 AND PRO-444.
    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. 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. Cited for: VARIANT THR-1119, CHARACTERIZATION OF VARIANT THR-1119.
  67. Cited for: VARIANT HIS-1067.

Entry info