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Reviewed, UniProtKB/Swiss-Prot P02452 (CO1A1_HUMAN)

Last modified June 16, 2009. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Collagen alpha-1(I) chain
Alternative name(s):
    Alpha-1 type I collagen
Gene names
Name: COL1A1
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1464 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. Interacts with MRC2 By similarity.

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.

Post-translational modification

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

O-linked glycan consists of a Glc-Gal disaccharide bound to the oxygen atom of a post-translationally added hydroxyl group.

Involvement in disease

Defects in COL1A1 are the cause of Caffey disease [MIM:114000]; also known as infantile cortical hyperostosis. Caffey disease is characterized by an infantile episode of massive subperiosteal new bone formation that typically involves the diaphyses of the long bones, mandible, and clavicles. The involved bones may also appear inflamed, with painful swelling and systemic fever often accompanying the illness. The bone changes usually begin before 5 months of age and resolve before 2 years of age. Ref.88 Ref.89 Ref.90

Defects in COL1A1 are a cause of Ehlers-Danlos syndrome type 1 (EDS1) [MIM:130000]; also known as Ehlers-Danlos syndrome gravis. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS1 is the severe form of classic Ehlers-Danlos syndrome. Ref.88 Ref.89 Ref.90 Ref.87

Defects in COL1A1 are the cause of Ehlers-Danlos syndrome type 7A (EDS7A) [MIM:130060]; also known as autosomal dominant Ehlers-Danlos syndrome type VII. EDS is a connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. EDS7A is marked by bilateral congenital hip dislocation, hyperlaxity of the joints, and recurrent partial dislocations. Ref.88 Ref.89 Ref.90

Defects in COL1A1 are a cause of osteogenesis imperfecta type I (OI-I) [MIM:166200]. OI-I is a dominantly inherited serious newborn disease characterized by bone fragility, normal stature, little or no deformity, blue sclerae and hearing loss in 50% of families. Dentinogenesis imperfecta is rare and may distinguish a subset of OI type I (formation of dentine). Ref.88 Ref.89 Ref.90 Ref.22 Ref.23 Ref.25 Ref.33 Ref.34 Ref.35 Ref.36 Ref.38 Ref.39 Ref.40 Ref.42 Ref.44 Ref.45 Ref.46 Ref.47 Ref.48 Ref.49 Ref.50 Ref.51 Ref.53 Ref.54 Ref.55 Ref.56 Ref.58 Ref.59 Ref.60 Ref.62 Ref.63 Ref.64 Ref.65 Ref.66 Ref.68 Ref.70 Ref.71 Ref.72 Ref.73 Ref.74 Ref.75 Ref.76 Ref.77 Ref.78 Ref.79 Ref.82 Ref.83 Ref.84 Ref.86

Defects in COL1A1 are a cause of osteogenesis imperfecta type II (OI-II) [MIM:166210]; also known as osteogenesis imperfecta congenita. OI-II is lethal in the perinatal period and is charaterized by calvarial mineralization, beaded ribs, compressed femurs, marked long bone deformity and platyspondyly (congenital flattening of the vertebral bodies).

Defects in COL1A1 are a cause of osteogenesis imperfecta type III (OI-III) [MIM:259420]; also called progressively deforming osteogenesis imperfecta with normal sclerae. OI-III is characterized by progressively deforming bones, usually with moderate deformity at birth, sclerae is variable in color, dentinogenesis imperfecta and hearing loss are common. The stature is very short.

Defects in COL1A1 are a cause of osteogenesis imperfecta type IV (OI-IV) [MIM:166220]. OI-IV is charaterized by normal sclerae, moderate to mild deformity and variable short stature. Dentinogenesis imperfecta is common and hearing loss occurs in some patients.

Genetic variations in COL1A1 are associated with susceptibility to involutional osteoporosis [MIM:166710]; also known as senile osteoporosis or postmenopausal osteoporosis. Osteoporosis is characterized by reduced bone mineral density, disrutption of bone microarchitecture, and the alteration of the amount and variety of non-collagenous proteins in bone. Osteoporotic bones are more at risk of fracture. Ref.88 Ref.89 Ref.90

A chromosomal aberration involving COL1A1 is a cause of dermatofibrosarcoma protuberans (DFSP) [MIM:607907]. Translocation t(17;22)(q22;q13) with PDGF. DFSP is an uncommon, locally aggressive, but rarely metastasizing tumor of the deep dermis and subcutaneous tissue. It typically occurs during early or middle adult life and is most frequently located on the trunk and proximal extremities. Ref.88 Ref.89 Ref.90

Sequence similarities

Belongs to the fibrillar collagen family.

Contains 1 VWFC domain.

Ontologies

Keywords
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityChromosomal rearrangement
Polymorphism
   DiseaseDisease mutation
Dwarfism
Ehlers-Danlos syndrome
   DomainCollagen
Repeat
Signal
   PTMDisulfide bond
Glycoprotein
Hydroxylation
Pyrrolidone carboxylic acid
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processblood vessel development

Inferred from mutant phenotype. Source: UniProtKB

collagen biosynthetic process

Inferred from mutant phenotype. Source: UniProtKB

collagen fibril organization

Inferred from mutant phenotype. Source: UniProtKB

embryonic skeletal system development

Inferred from mutant phenotype. Source: UniProtKB

sensory perception of sound

Inferred from mutant phenotype. Source: UniProtKB

skin morphogenesis

Inferred from mutant phenotype. Source: UniProtKB

tooth mineralization

Inferred from mutant phenotype. Source: UniProtKB

visual perception

Inferred from mutant phenotype. Source: UniProtKB

   Cellular componentcollagen type I

Inferred from mutant phenotype. Source: UniProtKB

extracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from Experiment. Source: Reactome

   Molecular functionextracellular matrix structural constituent

Inferred from electronic annotation. Source: InterPro

identical protein binding

Inferred from direct assay. Source: UniProtKB

platelet-derived growth factor binding

Inferred from direct assay. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Q5YB851EBI-982999,EBI-982988From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222
Propeptide23 – 161139N-terminal propeptide Ref.14
PRO_0000005719
Chain162 – 12181057Collagen alpha-1(I) chain
PRO_0000005720
Propeptide1219 – 1464246C-terminal propeptide
PRO_0000005721

Regions

Domain38 – 9659VWFC
Region162 – 17817Nonhelical region (N-terminal)
Region179 – 11921014Triple-helical region
Region1193 – 121826Nonhelical region (C-terminal)
Motif745 – 7473Cell attachment site Potential
Motif1093 – 10953Cell attachment site Potential

Sites

Site161 – 1622Cleavage; by procollagen N-endopeptidase
Site953 – 9542Cleavage; by collagenase By similarity
Site1218 – 12192Cleavage; by procollagen C-endopeptidase

Amino acid modifications

Modified residue1621Pyrrolidone carboxylic acid
Modified residue1701Allysine
Modified residue26515-hydroxylysine
Modified residue110815-hydroxylysine By similarity
Modified residue116413-hydroxyproline By similarity
Modified residue12081Allysine By similarity
Glycosylation2651O-linked (Gal...)
Glycosylation11081O-linked (Gal...) By similarity
Glycosylation13651N-linked (GlcNAc...)
Disulfide bond1259Interchain By similarity
Disulfide bond1265Interchain By similarity
Disulfide bond1282Interchain By similarity
Disulfide bond1291Interchain By similarity
Disulfide bond1299 ↔ 1462 By similarity
Disulfide bond1370 ↔ 1415 By similarity

Natural variations

Natural variant1971G → C Mild phenotype. dbSNP rs8179178.
VAR_001642
Natural variant2051P → A
VAR_001643
Natural variant2211G → C in OI; mild form. Ref.61
VAR_001644
Natural variant2241G → C in OI-I; mild phenotype.
VAR_001645
Natural variant2631G → R in OI-I; mild form. Ref.54
VAR_001646
Natural variant2631G → V in OI; mild form. Ref.54 Ref.67
VAR_001647
Natural variant2721G → C in OI-I.
VAR_001648
Natural variant2751G → D in OI-II.
VAR_001649
Natural variant3121R → C in EDS1. Ref.87
VAR_013579
Natural variant3321G → R in OI-III; mild to moderate form. Ref.51 Ref.77
VAR_001650
Natural variant3501G → R in OI-III. Ref.74
VAR_001651
Natural variant3531G → C in OI-IV. Ref.65
VAR_001652
Natural variant3561G → C in OI-IV; mild form.
VAR_001653
Natural variant3831G → C in OI-IV.
VAR_001654
Natural variant3891G → C in OI; moderate form. Ref.73
VAR_001655
Natural variant3891G → R in OI-II. Ref.73
VAR_001656
Natural variant3981G → A in OI-IV. Ref.83
VAR_001657
Natural variant3981G → D in OI-II.
VAR_001658
Natural variant4011G → C in OI-IV.
VAR_001659
Natural variant4041G → C in OI; moderate form.
VAR_001660
Natural variant4221G → C in OI-II. Ref.44
VAR_001661
Natural variant4251G → S in OI-II; lethal form.
VAR_001662
Natural variant4341G → V in OI-II. Ref.38 Ref.62
VAR_001663
Natural variant4761G → R in OI-II.
VAR_001664
Natural variant5271G → C in OI-IV. Ref.83
VAR_001665
Natural variant5301G → S in OI-II/III/IV; mild to lethal form.
VAR_001666
Natural variant5331G → D in OI-II.
VAR_001667
Natural variant5601G → C in OI-IV.
VAR_001669
Natural variant5601G → R in OI-II.
VAR_001670
Natural variant5601G → S in OI-IV.
VAR_001668
Natural variant5641R → H: dbSNP rs1800211.
VAR_001671
Natural variant5691G → R in OI-II. Ref.34
VAR_001672
Natural variant5931G → C in OI-III/IV. Ref.56
VAR_001673
Natural variant5931G → S in OI-II/III; moderate to lethal form. Ref.70
VAR_001674
Natural variant6381G → S in OI-III/IV.
VAR_001675
Natural variant6561G → S in OI-II. Ref.84
VAR_001676
Natural variant7011G → C in OI-IV. Ref.83
VAR_001677
Natural variant7041G → C in OI-III.
VAR_001678
Natural variant7191G → D in OI-II. Ref.48
VAR_001679
Natural variant7191G → S in OI-III.
VAR_001680
Natural variant7281G → R in OI-II. Ref.22
VAR_001681
Natural variant7371G → D in OI-II.
VAR_001682
Natural variant7431G → S in OI-II. Ref.68
VAR_001683
Natural variant7431G → V in OI-II. Ref.68
VAR_001684
Natural variant7641G → V in OI-II. Ref.82
VAR_001685
Natural variant7671G → S in OI-III; severe. Ref.23
VAR_001686
Natural variant7761G → S in OI-II. Ref.45
VAR_001687
Natural variant8091G → S in OI-II. Ref.45
VAR_001688
Natural variant8151G → V in OI-II. Ref.53
VAR_001689
Natural variant8211G → S in OI-III.
VAR_001690
Natural variant8231P → A: dbSNP rs1800214. Ref.69
VAR_001691
Natural variant8391G → S in OI-II; mild to moderate form. Ref.78
VAR_001692
Natural variant8421G → R in OI-II. Ref.36
VAR_001693
Natural variant8451G → R in OI-II.
VAR_001694
Natural variant8511G → D in OI-II.
VAR_001695
Natural variant8661G → S in OI-III. Ref.86
VAR_008118
Natural variant8691G → C in OI-II. Ref.49
VAR_001696
Natural variant8841G → S in OI-II/III; extremely severe form.
VAR_001697
Natural variant8961G → C in OI-II.
VAR_001698
Natural variant9261G → C in OI-II. Ref.35 Ref.50
VAR_001699
Natural variant9801G → V in OI-II. Ref.59
VAR_001700
Natural variant10101G → S in OI-IV. Ref.39
VAR_001701
Natural variant10141R → C in Caffey disease.
VAR_033097
Natural variant10191G → A: dbSNP rs1135348. Ref.1 Ref.18
VAR_030013
Natural variant10221G → S in OI-III; severe form.
VAR_001702
Natural variant10221G → V in OI-II.
VAR_001703
Natural variant10251G → R in OI-II. Ref.46
VAR_001704
Natural variant10401G → S in OI-II/III; moderate to lethal form.
VAR_001705
Natural variant10431G → S in OI-II.
VAR_001706
Natural variant1046 – 10483Missing in OI-II. Ref.55 Ref.60
VAR_001707
Natural variant10491G → S in OI-III.
VAR_001708
Natural variant10581G → S in OI-IV; mild form.
VAR_001709
Natural variant10611G → D in OI-II.
VAR_001710
Natural variant10611G → S in OI-IV. Ref.76
VAR_001711
Natural variant10751A → T: dbSNP rs1800215. Ref.57
VAR_001712
Natural variant10761G → S in OI-III; severe form.
VAR_001713
Natural variant10791G → S in OI-I/II; mild to moderate form.
VAR_001714
Natural variant10821G → C in OI-II. Ref.42
VAR_001715
Natural variant10881G → A in OI-II. Ref.66
VAR_001716
Natural variant10911G → S in OI-II. Ref.47
VAR_001717
Natural variant11001G → S in OI-II; mild to moderate form.
VAR_001718
Natural variant11061G → A in OI-II. Ref.40
VAR_001719
Natural variant11241G → C in OI-II. Ref.75
VAR_001720
Natural variant11411R → Q: dbSNP rs41316713.
VAR_033778
Natural variant11421G → S in OI-II.
VAR_001721
Natural variant11511G → S in OI-III.
VAR_001722
Natural variant11511G → V in OI-II. Ref.40 Ref.62
VAR_001723
Natural variant11541G → R in OI-II. Ref.40
VAR_001724
Natural variant11661G → C in OI-II. Ref.33
VAR_001725
Natural variant11721G → D in OI-II. Ref.84
VAR_001726
Natural variant11771V → I: dbSNP rs41316719.
VAR_033779
Natural variant11811G → S in OI-II. Ref.47 Ref.51
VAR_001727
Natural variant11841G → V in OI-II. Ref.40 Ref.62
VAR_001728
Natural variant11871G → S in OI-II/III; extremely severe form.
VAR_001729
Natural variant11871G → V in OI-II. Ref.47
VAR_001730
Natural variant11951G → C in OI-II; mild form.
VAR_001731
Natural variant12511S → T: dbSNP rs3205325. Ref.25
VAR_030014
Natural variant12771D → H in OI-II; impaired pro-alpha chain association. Ref.25
VAR_001732
Natural variant13121W → C in OI-II. Ref.63
VAR_001733
Natural variant1337 – 13382Missing in OI-II; impaired pro-alpha chain association.
VAR_001734
Natural variant13881L → R in OI-II; impaired pro-alpha chain association. Ref.25
VAR_001735
Natural variant13911Q → K: dbSNP rs2586486. Ref.1 Ref.2 Ref.27
VAR_030015
Natural variant14301K → N: dbSNP rs1059454.
VAR_033780
Natural variant14311T → P: dbSNP rs1059454.
VAR_033781
Natural variant14341T → S: dbSNP rs1800220. Ref.25 Ref.1
VAR_001736
Natural variant14381P → R: dbSNP rs17857117. Ref.5
VAR_030016
Natural variant14601P → H: dbSNP rs17853657. Ref.5
VAR_030017
Natural variant14641L → P in OI-III. Ref.79
VAR_001737

Experimental info

Sequence conflict591R → Q in CAA25394. Ref.8
Sequence conflict112 – 1143Missing in AAB94054. Ref.2
Sequence conflict2881E → P AA sequence Ref.15
Sequence conflict3701R → L in AAB59373. Ref.6
Sequence conflict4841P → L in AAA52289. Ref.19
Sequence conflict5951A → R in AAA51847. Ref.20
Sequence conflict7211Q → E Ref.22
Sequence conflict7381L → E Ref.22
Sequence conflict975 – 9762LP → PL in AAA52291. Ref.19
Sequence conflict10811V → A in AAA51995. Ref.18
Sequence conflict13291S → T in AAB27856. Ref.25

Sequences

Sequence LengthMass (Da)Tools
P02452-1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: B0581DAD2809DDE8

FASTA1,464138,911
        10         20         30         40         50         60 
MFSFVDLRLL LLLAATALLT HGQEEGQVEG QDEDIPPITC VQNGLRYHDR DVWKPEPCRI 

        70         80         90        100        110        120 
CVCDNGKVLC DDVICDETKN CPGAEVPEGE CCPVCPDGSE SPTDQETTGV EGPKGDTGPR 

       130        140        150        160        170        180 
GPRGPAGPPG RDGIPGQPGL PGPPGPPGPP GPPGLGGNFA PQLSYGYDEK STGGISVPGP 

       190        200        210        220        230        240 
MGPSGPRGLP GPPGAPGPQG FQGPPGEPGE PGASGPMGPR GPPGPPGKNG DDGEAGKPGR 

       250        260        270        280        290        300 
PGERGPPGPQ GARGLPGTAG LPGMKGHRGF SGLDGAKGDA GPAGPKGEPG SPGENGAPGQ 

       310        320        330        340        350        360 
MGPRGLPGER GRPGAPGPAG ARGNDGATGA AGPPGPTGPA GPPGFPGAVG AKGEAGPQGP 

       370        380        390        400        410        420 
RGSEGPQGVR GEPGPPGPAG AAGPAGNPGA DGQPGAKGAN GAPGIAGAPG FPGARGPSGP 

       430        440        450        460        470        480 
QGPGGPPGPK GNSGEPGAPG SKGDTGAKGE PGPVGVQGPP GPAGEEGKRG ARGEPGPTGL 

       490        500        510        520        530        540 
PGPPGERGGP GSRGFPGADG VAGPKGPAGE RGSPGPAGPK GSPGEAGRPG EAGLPGAKGL 

       550        560        570        580        590        600 
TGSPGSPGPD GKTGPPGPAG QDGRPGPPGP PGARGQAGVM GFPGPKGAAG EPGKAGERGV 

       610        620        630        640        650        660 
PGPPGAVGPA GKDGEAGAQG PPGPAGPAGE RGEQGPAGSP GFQGLPGPAG PPGEAGKPGE 

       670        680        690        700        710        720 
QGVPGDLGAP GPSGARGERG FPGERGVQGP PGPAGPRGAN GAPGNDGAKG DAGAPGAPGS 

       730        740        750        760        770        780 
QGAPGLQGMP GERGAAGLPG PKGDRGDAGP KGADGSPGKD GVRGLTGPIG PPGPAGAPGD 

       790        800        810        820        830        840 
KGESGPSGPA GPTGARGAPG DRGEPGPPGP AGFAGPPGAD GQPGAKGEPG DAGAKGDAGP 

       850        860        870        880        890        900 
PGPAGPAGPP GPIGNVGAPG AKGARGSAGP PGATGFPGAA GRVGPPGPSG NAGPPGPPGP 

       910        920        930        940        950        960 
AGKEGGKGPR GETGPAGRPG EVGPPGPPGP AGEKGSPGAD GPAGAPGTPG PQGIAGQRGV 

       970        980        990       1000       1010       1020 
VGLPGQRGER GFPGLPGPSG EPGKQGPSGA SGERGPPGPM GPPGLAGPPG ESGREGAPGA 

      1030       1040       1050       1060       1070       1080 
EGSPGRDGSP GAKGDRGETG PAGPPGAPGA PGAPGPVGPA GKSGDRGETG PAGPAGPVGP 

      1090       1100       1110       1120       1130       1140 
VGARGPAGPQ GPRGDKGETG EQGDRGIKGH RGFSGLQGPP GPPGSPGEQG PSGASGPAGP 

      1150       1160       1170       1180       1190       1200 
RGPPGSAGAP GKDGLNGLPG PIGPPGPRGR TGDAGPVGPP GPPGPPGPPG PPSAGFDFSF 

      1210       1220       1230       1240       1250       1260 
LPQPPQEKAH DGGRYYRADD ANVVRDRDLE VDTTLKSLSQ QIENIRSPEG SRKNPARTCR 

      1270       1280       1290       1300       1310       1320 
DLKMCHSDWK SGEYWIDPNQ GCNLDAIKVF CNMETGETCV YPTQPSVAQK NWYISKNPKD 

      1330       1340       1350       1360       1370       1380 
KRHVWFGESM TDGFQFEYGG QGSDPADVAI QLTFLRLMST EASQNITYHC KNSVAYMDQQ 

      1390       1400       1410       1420       1430       1440 
TGNLKKALLL QGSNEIEIRA EGNSRFTYSV TVDGCTSHTG AWGKTVIEYK TTKTSRLPII 

      1450       1460 
DVAPLDVGAP DQEFGFDVGP VCFL 

« Hide

References

« Hide 'large scale' references
[1]Dalgleish R.
Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ALA-1019; LYS-1391 AND SER-1434.
[2]"Analysis of the COL1A1 and COL1A2 genes by PCR amplification and scanning by conformation-sensitive gel electrophoresis identifies only COL1A1 mutations in 15 patients with osteogenesis imperfecta type I: identification of common sequences of null-allele mutations."
Korkko J.M., Ala-Kokko L., De Paepe A., Nuytinck L., Earley J.J., Prockop D.J.
Am. J. Hum. Genet. 62:98-110(1998) [PubMed: 9443882] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LYS-1391.
[3]Korkko J.M., Earley J.J., Nuytinck L., DePaepe A., Prockop D.J., Ala-Kokko L.
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 1049.
[4]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Spleen.
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ARG-1438 AND HIS-1460.
Tissue: Brain.
[6]"Complete nucleotide sequence of the region encompassing the first twenty-five exons of the human pro alpha 1(I) collagen gene (COL1A1)."
D'Alessio M., Bernard M.P., Pretorius P.J., de Wet W., Ramirez F., Pretorious P.J.
Gene 67:105-115(1988) [PubMed: 2843432] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-589.
[7]"Structure of a full-length cDNA clone for the prepro alpha 1(I) chain of human type I procollagen."
Tromp G., Kuivaniemi H., Stacey A., Shikata H., Baldwin C.T., Jaenisch R., Prockup D.J.
Biochem. J. 253:919-922(1988) [PubMed: 3178743] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-472.
[8]"Human pro alpha 1(I) collagen gene structure reveals evolutionary conservation of a pattern of introns and exons."
Chu M.-L., de Wet W.J., Bernard M.P., Ding J.-F., Morabito M., Myers J., Williams C., Ramirez F.
Nature 310:337-340(1984) [PubMed: 6462220] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-181.
[9]"DNA sequences in the first intron of the human pro-alpha 1(I) collagen gene enhance transcription."
Rossouw C.M.S., Vergeer W.P., du Plooy S.J., Bernard M.P., Ramirez F., de Wet W.
J. Biol. Chem. 262:15151-15157(1987) [PubMed: 2822714] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44.
[10]"Fine structural analysis of the human pro-alpha 1 (I) collagen gene. Promoter structure, AluI repeats, and polymorphic transcripts."
Chu M.-L., de Wet W., Bernard M.P., Ramirez F.
J. Biol. Chem. 260:2315-2320(1985) [PubMed: 2857713] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
[11]"Regulatory elements in the first intron contribute to transcriptional control of the human alpha 1(I) collagen gene."
Bornstein P., McKay J., Morishima J.K., Devarayalu S., Gelinas R.E.
Proc. Natl. Acad. Sci. U.S.A. 84:8869-8873(1987) [PubMed: 3480516] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
[12]"In vivo and in vitro noncovalent association of excised alpha 1 (I) amino-terminal propeptides with mutant pN alpha 2(I) collagen chains in native mutant collagen in a case of Ehlers-Danlos syndrome, type VII."
Wirtz M.K., Keene D.R., Hori H., Glanville R.W., Steinmann B., Rao V.H., Hollister D.W.
J. Biol. Chem. 265:6312-6317(1990) [PubMed: 2318855] [Abstract]
Cited for: PROTEIN SEQUENCE OF 33-52.
[13]"A base substitution in the exon of a collagen gene causes alternative splicing and generates a structurally abnormal polypeptide in a patient with Ehlers-Danlos syndrome type VII."
Weil D., D'Alessio M., Ramirez F., de Wet W., Cole W.G., Chan D., Bateman J.F.
EMBO J. 8:1705-1710(1989) [PubMed: 2767050] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 156-183.
[14]"Isolation and characterization of the cyanogen bromide peptides from the alpha 1 and alpha 2 chains of human skin collagen."
Click E.M., Bornstein P.
Biochemistry 9:4699-4706(1970) [PubMed: 5529814] [Abstract]
Cited for: PROTEIN SEQUENCE OF 162-301, ALLYSINE AT LYS-170, PYROGLUTAMATE FORMATION AT GLN-162.
Tissue: Skin.
[15]"A critical crosslink region in human-bone-derived collagen type I. Specific cleavage site at residue Leu95."
Baetge B., Notbohm H., Diebold J., Lehmann H., Bodo M., Deutzmann R., Muller P.K.
Eur. J. Biochem. 192:153-159(1990) [PubMed: 2169412] [Abstract]
Cited for: PROTEIN SEQUENCE OF 175-187 AND 274-289.
[16]"A comparative study of glycopeptides derived from selected vertebrate collagens. A possible role of the carbohydrate in fibril formation."
Morgan P.H., Jacobs H.G., Segrest J.P., Cunningham L.W.
J. Biol. Chem. 245:5042-5048(1970) [PubMed: 4319110] [Abstract]
Cited for: PROTEIN SEQUENCE OF 263-268.
Tissue: Skin.
[17]"Segmental amplification of the entire helical and telopeptide regions of the cDNA for human alpha 1 (I) collagen."
Labhard M.E., Hollister D.W.
Matrix 10:124-130(1990) [PubMed: 2374517] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 281-302; 402-420; 823-842; 924-944; 1026-1045 AND 1143-1162.
[18]"Nucleotide sequences of complementary deoxyribonucleic acids for the pro alpha 1 chain of human type I procollagen. Statistical evaluation of structures that are conserved during evolution."
Bernard M.P., Chu M.-L., Myers J.C., Ramirez F., Eikenberry E.F., Prockop D.J.
Biochemistry 22:5213-5223(1983) [PubMed: 6689127] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 425-1464, VARIANT ALA-1019.
[19]"Cloning and characterization of five overlapping cDNAs specific for the human pro alpha 1(I) collagen chain."
Chu M.-L., Myers J.C., Bernard M.P., Ding J.-F., Ramirez F.
Nucleic Acids Res. 10:5925-5934(1982) [PubMed: 6183642] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 425-490; 965-1024; 999-1039 AND 1453-1464.
[20]"Multiexon deletion in an osteogenesis imperfecta variant with increased type III collagen mRNA."
Chu M.-L., Gargiulo V., Williams C.J., Ramirez F.
J. Biol. Chem. 260:691-694(1985) [PubMed: 2981843] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 472-607.
[21]"Intron-mediated recombination may cause a deletion in an alpha 1 type I collagen chain in a lethal form of osteogenesis imperfecta."
Barsh G.S., Roush C.L., Bonadio J., Byers P.H., Gelinas R.E.
Proc. Natl. Acad. Sci. U.S.A. 82:2870-2874(1985) [PubMed: 3857621] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 488-625.
[22]"Variable expression of osteogenesis imperfecta in a nuclear family is explained by somatic mosaicism for a lethal point mutation in the alpha 1(I) gene (COL1A1) of type I collagen in a parent."
Wallis G.A., Starman B.J., Zinn A.B., Byers P.H.
Am. J. Hum. Genet. 46:1034-1040(1990) [PubMed: 2339700] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 710-745, VARIANT OI-II ARG-728.
[23]"Severe (type III) osteogenesis imperfecta due to glycine substitutions in the central domain of the collagen triple helix."
Forlino A., Zolezzi F., Valli M., Pignatti P.F., Cetta G., Brunelli P.C., Mottes M.
Hum. Mol. Genet. 3:2201-2206(1994) [PubMed: 7881420] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 746-781, VARIANT OI-III SER-767.
[24]Lubec G., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1063-1084, MASS SPECTROMETRY.
Tissue: Fetal brain cortex.
[25]"Mutations in the carboxyl-terminal propeptide of the pro alpha 1(I) chain of type I collagen result in defective chain association and produce lethal osteogenesis imperfecta."
Chessler S.D., Wallis G.A., Byers P.H.
J. Biol. Chem. 268:18218-18225(1993) [PubMed: 8349697] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1179-1464, VARIANTS OI-II HIS-1277; ARG-1388 AND 1337-GLU-TYR-1338 DEL, VARIANTS THR-1251 AND SER-1434.
[26]"Substitution of cysteine for glycine within the carboxyl-terminal telopeptide of the alpha 1 chain of type I collagen produces mild osteogenesis imperfecta."
Cohn D.H., Apone S., Eyre D.R., Starman B.J., Andreassen P., Charbonneau H., Nicholls A.C., Pope F.M., Byers P.H.
J. Biol. Chem. 263:14605-14607(1988) [PubMed: 3170557] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1187-1220, VARIANT CYS-1195.
[27]"Human pro alpha 1(I) collagen: cDNA sequence for the C-propeptide domain."
Maekelae J.K., Raassina M., Virta A., Vuorio E.
Nucleic Acids Res. 16:349-349(1988) [PubMed: 3340531] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1229-1454, VARIANT LYS-1391.
Tissue: Bone.
[28]"Frameshift mutation near the 3' end of the COL1A1 gene of type I collagen predicts an elongated Pro alpha 1(I) chain and results in osteogenesis imperfecta type I."
Willing M.C., Cohn D.H., Byers P.H.
J. Clin. Invest. 85:282-290(1990) [PubMed: 2295701] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1440-1464.
[29]"Highly conserved sequences in the 3'-untranslated region of the COL1A1 gene bind cell-specific nuclear proteins."
Maatta A., Bornstein P., Penttinen R.P.
FEBS Lett. 279:9-13(1991) [PubMed: 1995349] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1454-1464.
[30]"Mutations in collagen genes: causes of rare and some common diseases in humans."
Kuivaniemi H., Tromp G., Prockop D.J.
FASEB J. 5:2052-2060(1991) [PubMed: 2010058] [Abstract]
Cited for: REVIEW ON VARIANTS.
[31]"Mutations in fibrillar collagens (types I, II, III, and XI), fibril-associated collagen (type IX), and network-forming collagen (type X) cause a spectrum of diseases of bone, cartilage, and blood vessels."
Kuivaniemi H., Tromp G., Prockop D.J.
Hum. Mutat. 9:300-315(1997) [PubMed: 9101290] [Abstract]
Cited for: REVIEW ON VARIANTS.
[32]"Osteogenesis imperfecta: translation of mutation to phenotype."
Byers P.H., Wallis G.A., Willing M.C.
J. Med. Genet. 28:433-442(1991) [PubMed: 1895312] [Abstract]
Cited for: REVIEW ON OI VARIANTS.
[33]"Lethal osteogenesis imperfecta resulting from a single nucleotide change in one human pro alpha 1(I) collagen allele."
Cohn D.H., Byers P.H., Steinmann B., Gelinas R.E.
Proc. Natl. Acad. Sci. U.S.A. 83:6045-6047(1986) [PubMed: 3016737] [Abstract]
Cited for: VARIANT OI-II CYS-1166.
[34]"Lethal perinatal osteogenesis imperfecta due to the substitution of arginine for glycine at residue 391 of the alpha 1(I) chain of type I collagen."
Bateman J.F., Chan D., Walkers I.D., Rogers J.G., Cole W.G.
J. Biol. Chem. 262:7021-7027(1987) [PubMed: 3108247] [Abstract]
Cited for: VARIANT OI-II ARG-569.
[35]"A point mutation in a type I procollagen gene converts glycine 748 of the alpha 1 chain to cysteine and destabilizes the triple helix in a lethal variant of osteogenesis imperfecta."
Vogel B.E., Minor R.R., Freund M., Prockop D.J.
J. Biol. Chem. 262:14737-14744(1987) [PubMed: 3667599] [Abstract]
Cited for: VARIANT OI-II CYS-926.
[36]"Substitution of arginine for glycine 664 in the collagen alpha 1(I) chain in lethal perinatal osteogenesis imperfecta. Demonstration of the peptide defect by in vitro expression of the mutant cDNA."
Bateman J.F., Lamande S.R., Dahl H.-H.M., Chan D., Cole W.G.
J. Biol. Chem. 263:11627-11630(1988) [PubMed: 3403550] [Abstract]
Cited for: VARIANT OI-II ARG-842.
[37]"A cysteine for glycine substitution at position 1017 in an alpha 1(I) chain of type I collagen in a patient with mild dominantly inherited osteogenesis imperfecta."
Labhard M.E., Wirtz M.K., Pope F.M., Nicholls A.C., Hollister D.W.
Mol. Biol. Med. 5:197-207(1988) [PubMed: 3244312] [Abstract]
Cited for: VARIANT OI CYS-1195.
[38]"RNA sequence analysis of a perinatal lethal osteogenesis imperfecta mutation."
Patterson E., Smiley E., Bonadio J.
J. Biol. Chem. 264:10083-10087(1989) [PubMed: 2470760] [Abstract]
Cited for: VARIANT OI-II VAL-434.
[39]"Osteogenesis imperfecta type IV. Detection of a point mutation in one alpha 1(I) collagen allele (COL1A1) by RNA/RNA hybrid analysis."
Marini J.C., Grange D.K., Gottesman G.S., Lewis M.B., Koeplin D.A.
J. Biol. Chem. 264:11893-11900(1989) [PubMed: 2745420] [Abstract]
Cited for: VARIANT OI-IV SER-1010.
[40]"Characterization of point mutations in the collagen COL1A1 and COL1A2 genes causing lethal perinatal osteogenesis imperfecta."
Lamande S.R., Dahl H.-H.M., Cole W.G., Bateman J.F.
J. Biol. Chem. 264:15809-15812(1989) [PubMed: 2777764] [Abstract]
Cited for: VARIANTS OI-II ALA-1106; VAL-1151; ARG-1154 AND VAL-1184.
[41]"Substitution of serine for alpha 1(I)-glycine 844 in a severe variant of osteogenesis imperfecta minimally destabilizes the triple helix of type I procollagen. The effects of glycine substitutions on thermal stability are either position of amino acid specific."
Pack M., Constantinou C.D., Kalia K., Nielsen K.B., Prockop D.J.
J. Biol. Chem. 264:19694-19699(1989) [PubMed: 2511192] [Abstract]
Cited for: VARIANT OI SER-1022.
[42]"A lethal variant of osteogenesis imperfecta has a single base mutation that substitutes cysteine for glycine 904 of the alpha 1(I) chain of type I procollagen. The asymptomatic mother has an unidentified mutation producing an overmodified and unstable type I procollagen."
Constantinou C.D., Nielsen K.B., Prockop D.J.
J. Clin. Invest. 83:574-584(1989) [PubMed: 2913053] [Abstract]
Cited for: VARIANT OI-II CYS-1082.
[43]"Osteogenesis imperfecta. The position of substitution for glycine by cysteine in the triple helical domain of the pro alpha 1(I) chains of type I collagen determines the clinical phenotype."
Starman B.J., Eyre D.R., Charbonneau H., Harrylock M., Weis M.A., Weiss L., Graham J.M. Jr., Byers P.H.
J. Clin. Invest. 84:1206-1214(1989) [PubMed: 2794057] [Abstract]
Cited for: VARIANTS OI CYS-272; CYS-704 AND CYS-896.
[44]"Two cysteine substitutions in the type I procollagen genes (COL1A1 and COL1A2) that cause lethal osteogenesis imperfecta. The location of glycine substitutions does not in any simple way predict their effets on protein function or phenotype."
Fertala A., Westerhausen A., Morris G.M., Rooney J.E., Prockop D.J.
Am. J. Hum. Genet. 47:A216-A216(1990)
Cited for: VARIANT OI-II CYS-422.
[45]"Mutations that substitute serine for glycine alpha 1-598 and glycine alpha 1-631 in type I procollagen. The effects on thermal unfolding of the triple helix are position-specific and demonstrate that the protein unfolds through a series of cooperative blocks."
Westerhausen A., Kishi J., Prockop D.J.
J. Biol. Chem. 265:13995-14000(1990) [PubMed: 2116413] [Abstract]
Cited for: VARIANTS OI-II SER-776 AND SER-809.
[46]"Substitution of arginine for glycine at position 847 in the triple-helical domain of the alpha 1 (I) chain of type I collagen produces lethal osteogenesis imperfecta. Molecules that contain one or two abnormal chains differ in stability and secretion."
Wallis G.A., Starman B.J., Schwartz M.F., Byers P.H.
J. Biol. Chem. 265:18628-18633(1990) [PubMed: 2211725] [Abstract]
Cited for: VARIANT OI-II ARG-1025.
[47]"Serine for glycine substitutions in the alpha1(I) chain of type I collagen: biological plasticity in the Gly-Pro-Hyp clamp at the carboxyl-terminal end of triple helicalH domain."
Cohn D.H., Wallis G.A., Zhang X., Byers P.H.
Matrix 10:236-236(1990)
Cited for: VARIANTS OI-II SER-1091; SER-1181; SER-1187 AND VAL-1187.
[48]"A single base mutation in type I procollagen (COL1A1) that converts glycine alpha 1-541 to aspartate in a lethal variant of osteogenesis imperfecta: detection of the mutation with a carbodiimide reaction of DNA heteroduplexes and direct sequencing of products of the PCR."
Zhuang J., Constantinou C.D., Ganguly A., Prockop D.J.
Am. J. Hum. Genet. 48:1186-1191(1991) [PubMed: 2035536] [Abstract]
Cited for: VARIANT OI-II ASP-719.
[49]"Substitution of cysteine for glycine-alpha 1-691 in the pro alpha 1(I) chain of type I procollagen in a proband with lethal osteogenesis imperfecta destabilizes the triple helix at a site C-terminal to the substitution."
Steinmann B., Westerhausen A., Constantinou C.D., Superti-Furga A., Prockop D.J.
Biochem. J. 279:747-752(1991) [PubMed: 1953667] [Abstract]
Cited for: VARIANT OI-II CYS-869.
[50]"A type I collagen with substitution of a cysteine for glycine-748 in the alpha 1(I) chain copolymerizes with normal type I collagen and can generate fractallike structures."
Kadler K.E., Torre-Blanco A., Adachi E., Vogel B.E., Hojima Y., Prockop D.J.
Biochemistry 30:5081-5088(1991) [PubMed: 2036375] [Abstract]
Cited for: VARIANT OI-II CYS-926.
[51]"Osteogenesis imperfecta due to recurrent point mutations at CpG dinucleotides in the COL1A1 gene of type I collagen."
Pruchno C.J., Cohn D.H., Wallis G.A., Willing M.C., Starman B.J., Zhang X., Byers P.H.
Hum. Genet. 87:33-40(1991) [PubMed: 2037280] [Abstract]
Cited for: VARIANT OI-III ARG-332, VARIANT OI-II SER-1181.
[52]"A de novo G to T transversion in a pro-alpha 1 (I) collagen gene for a moderate case of osteogenesis imperfecta. Substitution of cysteine for glycine 178 in the triple helical domain."
Valli M., Mottes M., Tenni R., Sangalli A., Gomez Lira M., Rossi A., Antoniazzi F., Cetta G., Pignatti P.F.
J. Biol. Chem. 266:1872-1878(1991) [PubMed: 1988452] [Abstract]
Cited for: VARIANT OI CYS-356.
[53]"Substitutions for glycine alpha 1-637 and glycine alpha 2-694 of type I procollagen in lethal osteogenesis imperfecta. The conformational strain on the triple helix introduced by a glycine substitution can be transmitted along the helix."
Tsuneyoshi T., Westerhausen A., Constantinou C.D., Prockop D.J.
J. Biol. Chem. 266:15608-15613(1991) [PubMed: 1874719] [Abstract]
Cited for: VARIANT OI-II VAL-815.
[54]"The substitution of arginine for glycine 85 of the alpha 1(I) procollagen chain results in mild osteogenesis imperfecta. The mutation provides direct evidence for three discrete domains of cooperative melting of intact type I collagen."
Deak S.B., Scholz P.M., Amenta P.S., Constantinou C.D., Levi-Minzi S.A., Gonzalez-Lavin L., MacKenzie J.W.
J. Biol. Chem. 266:21827-21832(1991) [PubMed: 1718984] [Abstract]
Cited for: VARIANT OI-I ARG-263.
[55]"A 9-base pair deletion in COL1A1 in a lethal variant of osteogenesis imperfecta."
Hawkins J.R., Superti-Furga A., Steinmann B., Dalgleish R.
J. Biol. Chem. 266:22370-22374(1991) [PubMed: 1939261] [Abstract]
Cited for: VARIANT OI-II 1046-GLY--PRO-1048 DEL.
[56]"Substitution of cysteine for glycine at residue 415 of one allele of the alpha 1(I) chain of type I procollagen in type III/IV osteogenesis imperfecta."
Nicholls A.C., Oliver J.E., Renouf D.V., Keston M., Pope F.M.
J. Med. Genet. 28:757-764(1991) [PubMed: 1770532] [Abstract]
Cited for: VARIANT OI-III/IV CYS-593.
[57]"G to A polymorphism in exon 45 of the COL1A1 gene."
Sokolov B.P., Constantinou C.D., Tsuneyoshi T., Zhuang J., Prockop D.J.
Nucleic Acids Res. 19:4302-4302(1991) [PubMed: 1870989] [Abstract]
Cited for: VARIANT THR-1075.
[58]"Mild dominant osteogenesis imperfecta with intrafamilial variability: the cause is a serine for glycine alpha 1(I) 901 substitution in a type-I collagen gene."
Mottes M., Sangalli A., Valli M., Gomez Lira M., Tenni R., Buttitta P., Pignatti P.F., Cetta G.
Hum. Genet. 89:480-484(1992) [PubMed: 1634225] [Abstract]
Cited for: VARIANT OI-I SER-1079.
[59]"A dominant mutation in the COL1A1 gene that substitutes glycine for valine causes recurrent lethal osteogenesis imperfecta."
Bonaventure J., Cohen-Solal L., Lasselin C., Maroteaux P.
Hum. Genet. 89:640-646(1992) [PubMed: 1511982] [Abstract]
Cited for: VARIANT OI-II VAL-980.
[60]"A tripeptide deletion in the triple-helical domain of the pro alpha 1(I) chain of type I procollagen in a patient with lethal osteogenesis imperfecta does not alter cleavage of the molecule by N-proteinase."
Wallis G.A., Kadler K.E., Starman B.J., Byers P.H.
J. Biol. Chem. 267:25529-25534(1992) [PubMed: 1460047] [Abstract]
Cited for: VARIANT OI-II 1046-GLY--PRO-1048 DEL.
[61]"An osteopenic nonfracture syndrome with features of mild osteogenesis imperfecta associated with the substitution of a cysteine for glycine at triple helix position 43 in the pro alpha 1(I) chain of type I collagen."
Shapiro J.R., Stover M.L., Burn V.E., McKinstry M.B., Burshell A.L., Chipman S.D., Rowe D.W.
J. Clin. Invest. 89:567-573(1992) [PubMed: 1737847] [Abstract]
Cited for: VARIANT OI CYS-221.
[62]"The clinicopathological features of three babies with osteogenesis imperfecta resulting from the substitution of glycine by valine in the pro alpha 1 (I) chain of type I procollagen."
Cole W.G., Patterson E., Bonadio J., Campbell P.E., Fortune D.W.
J. Med. Genet. 29:112-118(1992) [PubMed: 1613761] [Abstract]
Cited for: VARIANTS OI-II VAL-434; VAL-1151 AND VAL-1184.
[63]"Chemical cleavage method for the detection of RNA base changes: experience in the application to collagen mutations in osteogenesis imperfecta."
Bateman J.F., Lamande S.R., Hannagan M., Moeller I., Dahl H.-H.M., Cole W.G.
Am. J. Med. Genet. 45:233-240(1993) [PubMed: 8456808] [Abstract]
Cited for: VARIANT OI-II CYS-1312.
[64]"Moderately severe osteogenesis imperfecta associated with substitutions of serine for glycine in the alpha 1(I) chain of type I collagen."
Marini J.C., Lewis M.B., Chen K.J.
Am. J. Med. Genet. 45:241-245(1993) [PubMed: 8456809] [Abstract]
Cited for: VARIANT OI-III SER-530.
[65]"A cysteine for glycine substitution at position 175 in an alpha 1 (I) chain of type I collagen produces a clinically heterogeneous form of osteogenesis imperfecta."
Wirtz M.K., Rao V.H., Glanville R.W., Labhard M.E., Pretorius P.J., de Vries W.N., de Wet W., Hollister D.W.
Connect. Tissue Res. 29:1-11(1993) [PubMed: 8339541] [Abstract]
Cited for: VARIANT OI-IV CYS-353.
[66]"Osteogenesis imperfecta and type-I collagen mutations. A lethal variant caused by a Gly910-->Ala substitution in the alpha 1 (I) chain."
Valli M., Sangalli A., Rossi A., Mottes M., Forlino A., Tenni R., Pignatti P.F., Cetta G.
Eur. J. Biochem. 211:415-419(1993) [PubMed: 7679635] [Abstract]
Cited for: VARIANT OI-II ALA-1088.
[67]"Gly85 to Val substitution in pro alpha 1(I) chain causes mild osteogenesis imperfecta and introduces a susceptibility to protease digestion."
Valli M., Zolezzi F., Mottes M., Antoniazzi F., Stanzial F., Tenni R., Pignatti P.F., Cetta G.
Eur. J. Biochem. 217:77-82(1993) [PubMed: 8223589] [Abstract]
Cited for: VARIANT OI VAL-263.
[68]"SSCP detection of a Gly565Val substitution in the pro alpha 1(I) collagen chain resulting in osteogenesis imperfecta type II."
Mackay K., Lund A.M., Raghunath M., Steinmann B., Dalgleish R.
Hum. Genet. 91:439-444(1993) [PubMed: 8100209] [Abstract]
Cited for: VARIANT OI-II VAL-743.
[69]"An RT-PCR-SSCP screening strategy for detection of mutations in the gene encoding the alpha 1 chain of type I collagen: application to four patients with osteogenesis imperfecta."
Mackay K., Byers P.H., Dalgleish R.
Hum. Mol. Genet. 2:1155-1160(1993) [PubMed: 7691343] [Abstract]
Cited for: VARIANTS OI SER-425; SER-530; SER-560 AND SER-719, VARIANT ALA-823.
[70]"Paternal mosaicism for a COL1A1 dominant mutation (alpha 1 Ser-415) causes recurrent osteogenesis imperfecta."
Mottes M., Gomez Lira M., Valli M., Scarano G., Lonardo F., Forlino A., Cetta G., Pignatti P.F.
Hum. Mutat. 2:196-204(1993) [PubMed: 8364588] [Abstract]
Cited for: VARIANT OI-II/III SER-593.
[71]"Serine for glycine substitutions in type I collagen in two cases of type IV osteogenesis imperfecta (OI). Additional evidence for a regional model of OI pathophysiology."
Marini J.C., Lewis M.B., Wang Q., Chen K.J., Orrison B.M.
J. Biol. Chem. 268:2667-2673(1993) [PubMed: 8094076] [Abstract]
Cited for: VARIANT OI-IV SER-530.
[72]"BiP binds type I procollagen pro alpha chains with mutations in the carboxyl-terminal propeptide synthesized by cells from patients with osteogenesis imperfecta."
Chessler S.D., Byers P.H.
J. Biol. Chem. 268:18226-18233(1993) [PubMed: 8349698] [Abstract]
Cited for: VARIANTS OI-II.
[73]"Osteogenesis imperfecta: comparison of molecular defects with bone histological changes."
Sztrolovics R., Glorieux F.H., Travers R., van der Rest M., Roughley P.J.
Bone 15:321-328(1994) [PubMed: 7520724] [Abstract]
Cited for: VARIANT OI-II ARG-389.
[74]"Substitution of glycine-172 by arginine in the alpha 1 chain of type I collagen in a patient with osteogenesis imperfecta, type III."
Mackay K., de Paepe A., Nuytinck L., Dalgleish R.
Hum. Mutat. 3:324-326(1994) [PubMed: 8019571] [Abstract]
Cited for: VARIANT OI-III ARG-350.
[75]"Substitution of cysteine for glycine-946 in the alpha 1(I) chain of type I procollagen causes lethal osteogenesis imperfecta."
Kurosaka D., Hattori S., Hori H., Yamaguchi N., Hasegawa T., Akimoto H., Nagai Y.
J. Biochem. 115:853-857(1994) [PubMed: 7961597] [Abstract]
Cited for: VARIANT OI-II CYS-1124.
[76]"Substitution of serine for glycine 883 in the triple helix of the pro alpha 1 (I) chain of type I procollagen produces osteogenesis imperfecta type IV and introduces a structural change in the triple helix that does not alter cleavage of the molecule by procollagen N-proteinase."
Lightfoot S.J., Atkinson M.S., Murphy G., Byers P.H., Kadler K.E.
J. Biol. Chem. 269:30352-30357(1994) [PubMed: 7982948] [Abstract]
Cited for: VARIANT OI-IV SER-1061.
[77]"Substitution of arginine for glycine at position 154 of the alpha 1 chain of type I collagen in a variant of osteogenesis imperfecta: comparison to previous cases with the same mutation."
Zhuang J., Tromp G., Kuivaniemi H., Castells S., Prockop D.J.
Am. J. Med. Genet. 61:111-116(1996) [PubMed: 8669434] [Abstract]
Cited for: VARIANT OI-III ARG-332.
[78]"Substitution of glycine-661 by serine in the alpha1(I) and alpha2(I) chains of type I collagen results in different clinical and biochemical phenotypes."
Nuytinck L., Dalgleish R., Spotila L., Renard J.-P., van Regemorter N., de Paepe A.
Hum. Genet. 97:324-329(1996) [PubMed: 8786074] [Abstract]
Cited for: VARIANT OI-II SER-839.
[79]"Mutation in the carboxy-terminal propeptide of the Pro alpha 1(I) chain of type I collagen in a child with severe osteogenesis imperfecta (OI type III): possible implications for protein folding."
Oliver J.E., Thompson E.M., Pope F.M., Nicholls A.C.
Hum. Mutat. 7:318-326(1996) [PubMed: 8723681] [Abstract]
Cited for: VARIANT OI-III PRO-1464.
[80]"Reduced bone density and osteoporosis associated with a polymorphic Sp1 binding site in the collagen type I alpha 1 gene."
Grant S.F.A., Reid D.M., Blake G., Herd R., Fogelman I., Ralston S.H.
Nat. Genet. 14:203-205(1996) [PubMed: 8841196] [Abstract]
Cited for: INVOLVEMENT IN INVOLUTIONAL OSTEOPOROSIS.
[81]"Serine for glycine substitutions in the C-terminal third of the alpha 1(I) chain of collagen I in five patients with nonlethal osteogenesis imperfecta."
Lund A.M., Skovby F., Schwartz M.
Hum. Mutat. 9:378-382(1997) [PubMed: 9101304] [Abstract]
Cited for: VARIANTS OI SER-821; SER-1040; SER-1049; SER-1058 AND SER-1076.
[82]"(G586V) substitutions in the alpha 1 and alpha 2 chains of collagen I: effect of alpha-chain stoichiometry on the phenotype of osteogenesis imperfecta?"
Lund A.M., Skovby F., Schwartz M.
Hum. Mutat. 9:431-436(1997) [PubMed: 9143923] [Abstract]
Cited for: VARIANT OI-II VAL-764.
[83]"Three novel type I collagen mutations in osteogenesis imperfecta type IV probands are associated with discrepancies between electrophoretic migration of osteoblast and fibroblast collagen."
Sarafova A.P., Choi H., Forlino A., Gajko A., Cabral W.A., Tosi L., Reing C.M., Marini J.C.
Hum. Mutat. 11:395-403(1998) [PubMed: 9600458] [Abstract]
Cited for: VARIANTS OI-IV ALA-398; CYS-527 AND CYS-701.
[84]"Four new cases of lethal osteogenesis imperfecta due to glycine substitutions in COL1A1 and genes."
Mottes M., Gomez Lira M., Zolezzi F., Valli M., Lisi V., Freising P.
Hum. Mutat. 12:71-72(1998) [PubMed: 10627137] [Abstract]
Cited for: VARIANTS OI-II SER-656 AND ASP-1172.
[85]"Relation of alleles of the collagen type Ialpha1 gene to bone density and the risk of osteoporotic fractures in postmenopausal women."
Uitterlinden A.G., Burger H., Huang Q., Yue F., McGuigan F.E.A., Grant S.F.A., Hofman A., van Leeuwen J.P.T.M., Pols H.A.P., Ralston S.H.
N. Engl. J. Med. 338:1016-1021(1998) [PubMed: 9535665] [Abstract]
Cited for: INVOLVEMENT IN INVOLUTIONAL OSTEOPOROSIS.
[86]"Osteogenesis imperfecta: mosaicism and refinement of the genotype-phenotype map in OI type III."
Lund A.M., Astroem E., Soederhaell S., Schwartz M., Skovby F.
Hum. Mutat. 13:503-503(1999) [PubMed: 10408781] [Abstract]
Cited for: VARIANT OI-III SER-866.
[87]"Classical Ehlers-Danlos syndrome caused by a mutation in type I collagen."
Nuytinck L., Freund M., Lagae L., Pierard G.E., Hermanns-Le T., De Paepe A.
Am. J. Hum. Genet. 66:1398-1402(2000) [PubMed: 10739762] [Abstract]
Cited for: VARIANT EDS1 CYS-312.
[88]"Deregulation of the platelet-derived growth factor B-chain gene via fusion with collagen gene COL1A1 in dermatofibrosarcoma protuberans and giant-cell fibroblastoma."
Simon M.-P., Pedeutour F., Sirvent N., Grosgeorge J., Minoletti F., Coindre J.-M., Terrier-Lacombe M.-J., Mandahl N., Craver R.D., Blin N., Sozzi G., Turc-Carel C., O'Brien K.P., Kedra D., Fransson I., Guilbaud C., Dumanski J.P.
Nat. Genet. 15:95-98(1997) [PubMed: 8988177] [Abstract]
Cited for: DISEASE, CHROMOSOMAL TRANSLOCATION WITH PDGFB.
[89]"Dermatofibrosarcoma protuberans of breast."
Sandberg A.A., Anderson W.D., Fredenberg C., Hashimoto H.
Cancer Genet. Cytogenet. 142:56-59(2003) [PubMed: 12660034] [Abstract]
Cited for: DISEASE, CHROMOSOMAL TRANSLOCATION WITH PDGFB.
[90]"A novel COL1A1 mutation in infantile cortical hyperostosis (Caffey disease) expands the spectrum of collagen-related disorders."
Gensure R.C., Maekitie O., Barclay C., Chan C., Depalma S.R., Bastepe M., Abuzahra H., Couper R., Mundlos S., Sillence D., Ala-Kokko L., Seidman J.G., Cole W.G., Jueppner H.
J. Clin. Invest. 115:1250-1257(2005) [PubMed: 15864348] [Abstract]
Cited for: VARIANT CAFFEY DISEASE CYS-1014.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

Z74615 mRNA. Translation: CAA98968.1.
AF017178 Genomic DNA. Translation: AAB94054.3.
AB209597 mRNA. Translation: BAD92834.1. Different initiation.
BC036531 mRNA. Translation: AAH36531.1.
M20789 Genomic DNA. Translation: AAB59373.1.
M36546 mRNA. Translation: AAA60150.1.
X07884 mRNA. Translation: CAA30731.1.
X00820 Genomic DNA. Translation: CAA25394.1.
J02829 Genomic DNA. Translation: AAA51993.1.
M10627 Genomic DNA. Translation: AAA51992.1.
J03559 Genomic DNA. Translation: AAA52052.1.
K01228 mRNA. Translation: AAA51995.1.
J00110 mRNA. Translation: AAA52289.1.
J00111 mRNA. Translation: AAA52290.1.
J00112 mRNA. Translation: AAA52291.1.
J00113 mRNA. Translation: AAN86574.1.
K03179 Genomic DNA. Translation: AAA51847.1.
M11162 Genomic DNA. Translation: AAA75386.1.
L47667 Genomic DNA. Translation: AAB59576.1.
S64596 mRNA. Translation: AAB27856.1.
M23213 Genomic DNA. Translation: AAB59363.1.
X06269 mRNA. Translation: CAA29605.1.
M32798 mRNA. Translation: AAA52049.1.
M55998 Genomic DNA. Translation: AAA52036.1.
IPIIPI00297646.
PIRCGHU1S. I60114.
RefSeqNP_000079.2.
UniGeneHs.172928
Hs.681002

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1Q7DX-ray1.80A/B/C914-930[»]
3EJHX-ray2.10E/F956-977[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP02452. 1 interaction.

PTM databases

PhosphoSiteP02452.

2-D gel databases

DOSAC-COBS-2DPAGEP02452.
Siena-2DPAGEP02452.

Proteomic databases

PRIDEP02452.

Genome annotation databases

EnsemblENSG00000108821. Homo sapiens. [Contig view]
GeneID1277.
KEGGhsa:1277.

Organism-specific databases

GeneCardsGC17M045617.
H-InvDBHIX0016617.
HGNCHGNC:2197. COL1A1.
HPAHPA008405.
HPA011795.
MIM114000. phenotype.
120150. gene.
130000. phenotype.
130060. phenotype.
166200. phenotype.
166210. phenotype.
166220. phenotype.
166710. phenotype.
259420. phenotype.
607907. phenotype.
Orphanet1310. Caffey disease.
287. Classic Ehlers-Danlos syndrome.
31112. Dermatofibrosarcoma protuberans.
1899. Ehlers-Danlos syndrome, type 7.
666. Osteogenesis imperfecta.
PharmGKBPA35041.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP02452.

Enzyme and pathway databases

Pathway_Interaction_DBil4_2pathway. IL4-mediated signaling events.
lymphangiogenesis_pathway. VEGFR3 signaling in lymphatic endothelium.
ReactomeREACT_13552. Integrin cell surface interactions.
REACT_604. Hemostasis.
REACT_6900. Signaling in Immune system.

Gene expression databases

ArrayExpressP02452.
BgeeP02452.
GermOnlineENSG00000108821. Homo sapiens.

Family and domain databases

InterProIPR008160. Collagen.
IPR000885. Fib_collagen_C.
IPR001007. VWF_C.
[Graphical view]
PfamPF01410. COLFI. 1 hit.
PF01391. Collagen. 18 hits.
PF00093. VWC. 1 hit.
[Graphical view]
ProDomPD000007. Clg_helix. 2 hits.
PD002078. Fib_collagen_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00038. COLFI. 1 hit.
SM00214. VWC. 1 hit.
[Graphical view]
PROSITEPS01208. VWFC_1. 1 hit.
PS50184. VWFC_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00048. Collagenase.
DB00039. Palifermin.
NextBio5161.
PMAP-CutDBP02452.
SOURCESearch...

Entry information

Entry nameCO1A1_HUMAN
AccessionPrimary (citable) accession number: P02452
Secondary accession number(s): O76045 expand/collapse secondary AC list , P78441, Q13896, Q13902, Q13903, Q14037, Q14992, Q15176, Q15201, Q16050, Q59F64, Q7KZ30, Q7KZ34, Q8IVI5, Q8N473, Q9UML6, Q9UMM7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 132 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents