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P08123 (CO1A2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 171. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Collagen alpha-2(I) chain
Alternative name(s):
Alpha-2 type I collagen
Gene names
Name:COL1A2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1366 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Secretedextracellular spaceextracellular 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]: 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.
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]: 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.
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]: 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.
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]: 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.
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 componentExtracellular matrix
Secreted
   Coding sequence diversityChromosomal rearrangement
Polymorphism
   DiseaseDisease mutation
Dwarfism
Ehlers-Danlos syndrome
Osteogenesis imperfecta
   DomainCollagen
Repeat
Signal
   LigandCalcium
Metal-binding
   PTMDisulfide bond
Glycoprotein
Hydroxylation
Pyrrolidone carboxylic acid
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processRho protein signal transduction

Inferred from direct assay PubMed 17217948. Source: UniProtKB

blood coagulation

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: Ensembl

collagen catabolic process

Traceable author statement. Source: Reactome

collagen fibril organization

Inferred from mutant phenotype PubMed 17211858PubMed 18375391. Source: UniProtKB

extracellular matrix disassembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

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: Ensembl

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_componentcollagen type I trimer

Inferred from direct assay PubMed 18375391. Source: UniProtKB

endoplasmic reticulum lumen

Traceable author statement. Source: Reactome

extracellular region

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_functionextracellular 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

Inferred from physical interaction PubMed 18375391. Source: UniProtKB

protein binding, bridging

Inferred from mutant phenotype PubMed 18375391. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Propeptide25 – 7955N-terminal propeptide
PRO_0000005804
Chain80 – 11021023Collagen alpha-2(I) chain
PRO_0000005805
Propeptide1103 – 1366264C-terminal propeptide
PRO_0000005806

Regions

Domain1133 – 1366234Fibrillar collagen NC1

Sites

Metal binding11811Calcium By similarity
Metal binding11831Calcium By similarity
Metal binding11841Calcium; via carbonyl oxygen By similarity
Metal binding11861Calcium; via carbonyl oxygen By similarity
Metal binding11891Calcium By similarity

Amino acid modifications

Modified residue801Pyrrolidone carboxylic acid By similarity
Modified residue841Allysine
Modified residue4201Hydroxyproline
Modified residue4411Hydroxyproline
Modified residue4441Hydroxyproline
Glycosylation12671N-linked (GlcNAc...) Potential
Disulfide bond1163 ↔ 1195 By similarity
Disulfide bond1203 ↔ 1364 By similarity
Disulfide bond1272 ↔ 1317 By similarity

Natural variations

Natural variant591T → P. Ref.6
Corresponds to variant rs1800221 [ dbSNP | Ensembl ].
VAR_030116
Natural variant76 – 9318Missing in EDS7B.
VAR_001851
Natural variant181 – 19818Missing in OI4.
VAR_030117
Natural variant1931G → S in OI4. Ref.61
VAR_063343
Natural variant2021G → R in OI4. Ref.63
VAR_063344
Natural variant2111G → D in OI1. Ref.54
VAR_001852
Natural variant2341R → C in OI2. Ref.65
VAR_063345
Natural variant2471G → R in OI1. Ref.63
VAR_063346
Natural variant2491I → N. Ref.1
Corresponds to variant rs1800228 [ dbSNP | Ensembl ].
VAR_001853
Natural variant2531G → D in OI2. Ref.63
VAR_063347
Natural variant2561G → V in OI4. Ref.63
VAR_063348
Natural variant2701V → I. Ref.3
Corresponds to variant rs368468 [ dbSNP | Ensembl ].
VAR_030118
Natural variant2761A → T. Ref.1
Corresponds to variant rs1800231 [ dbSNP | Ensembl ].
VAR_001854
Natural variant2831G → R in OI2. Ref.65
VAR_063349
Natural variant3191G → R in OI1. Ref.63
VAR_063350
Natural variant3251G → E in OI4. Ref.62
VAR_063351
Natural variant3281G → S in OI1, OI3 AND OI4. Ref.51 Ref.62
VAR_001855
Natural variant3311G → D in OI3. Ref.57
VAR_008119
Natural variant3341G → C in OI2.
VAR_001856
Natural variant3371G → C in OI3. Ref.57
VAR_001857
Natural variant3371G → S in OI3. Ref.54
VAR_001858
Natural variant3441L → V.
Corresponds to variant rs16868573 [ dbSNP | Ensembl ].
VAR_055677
Natural variant3451Missing in OI3. Ref.40
VAR_001859
Natural variant3491G → C in OI3. Ref.33 Ref.38
VAR_001860
Natural variant3581G → S in OI3. Ref.62
VAR_063352
Natural variant3971G → E in OI2. Ref.65
VAR_063353
Natural variant4091G → V in OI2. Ref.56
VAR_001861
Natural variant4331G → E in OI2. Ref.42
VAR_001862
Natural variant4541G → C in OI2. Ref.65
VAR_063354
Natural variant4571G → L in OI2; requires 2 nucleotide substitutions. Ref.65
VAR_063355
Natural variant4601G → S in OI3. Ref.54
VAR_001863
Natural variant461 – 4666Missing in OI2.
VAR_063356
Natural variant4831A → V. Ref.1 Ref.3
Corresponds to variant rs414408 [ dbSNP | Ensembl ].
VAR_030119
Natural variant5111G → D in OI2.
VAR_001864
Natural variant5171G → R in OI3. Ref.45
VAR_001865
Natural variant5261G → E in OI2. Ref.65
VAR_063357
Natural variant5281N → S. Ref.64
Corresponds to variant rs41317144 [ dbSNP | Ensembl ].
VAR_033040
Natural variant5471G → R in OI2. Ref.36
VAR_001866
Natural variant5491P → A. Ref.1 Ref.2 Ref.4 Ref.15 Ref.39 Ref.64 Ref.65
Corresponds to variant rs42524 [ dbSNP | Ensembl ].
VAR_001867
Natural variant5621G → C in OI2.
VAR_001868
Natural variant5621G → V in OI2. Ref.65
VAR_063358
Natural variant5641A → T. Ref.64
Corresponds to variant rs41317153 [ dbSNP | Ensembl ].
VAR_033041
Natural variant5861G → R in OI2.
VAR_001869
Natural variant5921G → S in OI2. Ref.46
VAR_001870
Natural variant6011G → S in OI. Ref.62
VAR_063359
Natural variant6251G → D in OI2. Ref.61
VAR_063360
Natural variant6341G → V in OI4. Ref.41
VAR_001871
Natural variant6371G → D in OI2.
VAR_001872
Natural variant6401G → S in OI2.
VAR_001873
Natural variant6701G → D in OI2. Ref.37
VAR_001874
Natural variant676 – 855180Missing in OI2.
VAR_030120
Natural variant6761G → D in OI3. Ref.62
VAR_063361
Natural variant6761G → V in OI3 and OI4. Ref.19 Ref.32
VAR_001875
Natural variant6781P → H. Ref.1 Ref.2 Ref.3 Ref.5 Ref.17
Corresponds to variant rs409108 [ dbSNP | Ensembl ].
VAR_030121
Natural variant705 – 7073Missing in OI2.
VAR_063362
Natural variant7081R → Q in Marfan syndrome.
VAR_001876
Natural variant7151G → D in OI2.
VAR_001877
Natural variant7301G → C in OI2. Ref.49
VAR_001878
Natural variant7331G → C in OI1. Ref.63
VAR_063363
Natural variant7361G → C in OI1; mild. Ref.33 Ref.38
VAR_001879
Natural variant7391G → R in OI2. Ref.65
VAR_063364
Natural variant7431A → G. Ref.1 Ref.3 Ref.5
Corresponds to variant rs408535 [ dbSNP | Ensembl ].
VAR_001880
Natural variant7481G → V in OI2. Ref.65
VAR_063365
Natural variant7511G → S in OI4. Ref.35
VAR_001881
Natural variant7541G → C in OI4. Ref.61
VAR_063366
Natural variant7541G → R in OI2.
VAR_001882
Natural variant7661G → V in OI4. Ref.44
VAR_001883
Natural variant7781G → S in OI3. Ref.50
VAR_001884
Natural variant7841G → R in OI2. Ref.34
VAR_001885
Natural variant7871G → C in OI2. Ref.56
VAR_001886
Natural variant7901G → D in OI2. Ref.48 Ref.65
VAR_001887
Natural variant7961G → S in OI2. Ref.44
VAR_001888
Natural variant7981P → PP in OI2. Ref.65
VAR_063367
Natural variant806 – 8116Missing in OI2.
VAR_063368
Natural variant8111G → GPPG in OI4.
VAR_063369
Natural variant8201G → S in OI3. Ref.62
VAR_063370
Natural variant8221R → H. Ref.54
Corresponds to variant rs1800240 [ dbSNP | Ensembl ].
VAR_001889
Natural variant8351G → C in OI3. Ref.61
VAR_063371
Natural variant8351G → S in OI1. Ref.54
VAR_001890
Natural variant8561G → R in OI3. Ref.62
VAR_063372
Natural variant8561G → V in OI2. Ref.65
VAR_063373
Natural variant8771G → C in OI2. Ref.31
VAR_001891
Natural variant8921G → D in OI3 and OI4. Ref.53
VAR_001892
Natural variant8951G → D in OI2.
VAR_001893
Natural variant9491G → S in OI3; moderate. Ref.47 Ref.65
VAR_001894
Natural variant9551G → D in OI2. Ref.65
VAR_063374
Natural variant9551G → S in OI2. Ref.30
VAR_001895
Natural variant9731G → V in OI3. Ref.57
VAR_008120
Natural variant9821G → D in OI2. Ref.63
VAR_063375
Natural variant9891P → PVGP in OI4.
VAR_063376
Natural variant9911G → V in OI3. Ref.61
VAR_063377
Natural variant9971G → D in OI2. Ref.29
VAR_001896
Natural variant10031G → D in OI2. Ref.63
VAR_063378
Natural variant10121G → S in OI3 and OI4; moderate. Ref.43 Ref.62
VAR_001897
Natural variant10221L → F. Ref.1 Ref.3 Ref.17
Corresponds to variant rs392609 [ dbSNP | Ensembl ].
VAR_001898
Natural variant10271G → E in OI2. Ref.65
VAR_063379
Natural variant1058 – 10625Missing in OI2.
VAR_063380
Natural variant10661G → D in OI2.
VAR_001899
Natural variant10671R → H. Ref.67
VAR_069633
Natural variant10781G → C in OI2.
VAR_001900
Natural variant10871G → D in OI3. Ref.63
VAR_063381
Natural variant1094 – 10963Missing in OI4.
VAR_063382
Natural variant10961G → A in OI3. Ref.52
VAR_001901
Natural variant11011P → L.
VAR_001903
Natural variant11021G → R in OI4. Ref.22
VAR_001902
Natural variant11191A → 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 variant11481T → P in OI3. Ref.55
Corresponds to variant rs1800250 [ dbSNP | Ensembl ].
VAR_001904
Natural variant11891D → E. Ref.1 Ref.3 Ref.17
Corresponds to variant rs422361 [ dbSNP | Ensembl ].
VAR_001905
Natural variant11951C → Y in OI1. Ref.63
VAR_063383
Natural variant11981S → P. Ref.1 Ref.3 Ref.17
Corresponds to variant rs384487 [ dbSNP | Ensembl ].
VAR_001906
Natural variant13541Q → 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 conflict551E → G in CAA26320. Ref.6
Sequence conflict3331V → P in AAB59374. Ref.1
Sequence conflict3381A → T in AAB59374. Ref.1
Sequence conflict5491P → D in CAA68709. Ref.5
Sequence conflict8281V → A in CAA23761. Ref.17
Sequence conflict8311T → P in CAA23761. Ref.17
Sequence conflict8371V → P in CAA23761. Ref.17
Sequence conflict9801E → V in AAA51996. Ref.21
Sequence conflict10981P → L in CAA23761. Ref.17
Sequence conflict1122 – 11254Missing in CAA23761. Ref.17
Sequence conflict13381R → A in AAA51887. Ref.23

Sequences

Sequence LengthMass (Da)Tools
P08123 [UniParc].

Last modified May 18, 2010. Version 7.
Checksum: 1E68A5970FB4210A

FASTA1,366129,314
        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 

« Hide

References

« Hide '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.
[67]"WNT1 mutations in early-onset osteoporosis and osteogenesis imperfecta."
Laine C.M., Joeng K.S., Campeau P.M., Kiviranta R., Tarkkonen K., Grover M., Lu J.T., Pekkinen M., Wessman M., Heino T.J., Nieminen-Pihala V., Aronen M., Laine T., Kroeger H., Cole W.G., Lehesjoki A.E., Nevarez L., Krakow D. expand/collapse author list , Curry C.J., Cohn D.H., Gibbs R.A., Lee B.H., Maekitie O.
N. Engl. J. Med. 368:1809-1816(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HIS-1067.
+Additional computationally mapped references.

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.
CCDSCCDS34682.1.
PIRCGHU2S. A28500.
RefSeqNP_000080.2. NM_000089.3.
UniGeneHs.489142.

3D structure databases

ProteinModelPortalP08123.
SMRP08123. Positions 1151-1365.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107675. 8 interactions.
DIPDIP-36079N.
IntActP08123. 7 interactions.
MINTMINT-4791958.

Chemistry

ChEMBLCHEMBL2685.
DrugBankDB00048. Collagenase.

PTM databases

PhosphoSiteP08123.

Polymorphism databases

DMDM296439507.

Proteomic databases

MaxQBP08123.
PaxDbP08123.
PRIDEP08123.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000297268; ENSP00000297268; ENSG00000164692.
GeneID1278.
KEGGhsa:1278.
UCSCuc003ung.1. human.

Organism-specific databases

CTD1278.
GeneCardsGC07P094023.
GeneReviewsCOL1A2.
H-InvDBHIX0006854.
HGNCHGNC:2198. COL1A2.
HPACAB032650.
MIM120160. gene.
130060. phenotype.
166200. phenotype.
166210. phenotype.
166220. phenotype.
225320. phenotype.
259420. phenotype.
neXtProtNX_P08123.
Orphanet99876. 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.
PharmGKBPA35042.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOVERGENHBG004933.
KOK06236.
OMAKNGDKGH.
OrthoDBEOG7TJ3HH.
PhylomeDBP08123.
TreeFamTF344135.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.
REACT_160300. Binding and Uptake of Ligands by Scavenger Receptors.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP08123.
BgeeP08123.
GenevestigatorP08123.

Family and domain databases

InterProIPR008160. Collagen.
IPR000885. Fib_collagen_C.
[Graphical view]
PfamPF01410. COLFI. 1 hit.
PF01391. Collagen. 6 hits.
[Graphical view]
ProDomPD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00038. COLFI. 1 hit.
[Graphical view]
PROSITEPS51461. NC1_FIB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCOL1A2. human.
GeneWikiCOL1A2.
GenomeRNAi1278.
NextBio5165.
PROP08123.
SOURCESearch...

Entry information

Entry nameCO1A2_HUMAN
AccessionPrimary (citable) accession number: P08123
Secondary accession number(s): P02464 expand/collapse secondary AC list , 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: July 9, 2014
This is version 171 of the entry and version 7 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM