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P08123

- CO1A2_HUMAN

UniProt

P08123 - CO1A2_HUMAN

Protein

Collagen alpha-2(I) chain

Gene

COL1A2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 173 (01 Oct 2014)
      Sequence version 7 (18 May 2010)
      Previous versions | rss
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    Functioni

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

    Sites

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

    GO - Molecular functioni

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

    GO - Biological processi

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

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

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

    Names & Taxonomyi

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

    Organism-specific databases

    HGNCiHGNC:2198. COL1A2.

    Subcellular locationi

    Secretedextracellular spaceextracellular matrix PROSITE-ProRule annotation

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Ehlers-Danlos syndrome 7B (EDS7B) [MIM:130060]: A connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. Marked by bilateral congenital hip dislocation, hyperlaxity of the joints, and recurrent partial dislocations.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti76 – 9318Missing in EDS7B. 3 Publications
    VAR_001851Add
    BLAST
    Osteogenesis imperfecta 1 (OI1) [MIM:166200]: An autosomal dominant form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI1 is a non-deforming form with normal height or mild short stature, and no dentinogenesis imperfecta.5 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti211 – 2111G → D in OI1. 1 Publication
    VAR_001852
    Natural varianti247 – 2471G → R in OI1. 1 Publication
    VAR_063346
    Natural varianti319 – 3191G → R in OI1. 1 Publication
    VAR_063350
    Natural varianti328 – 3281G → S in OI1, OI3 AND OI4. 2 Publications
    VAR_001855
    Natural varianti733 – 7331G → C in OI1. 1 Publication
    VAR_063363
    Natural varianti736 – 7361G → C in OI1; mild. 2 Publications
    VAR_001879
    Natural varianti835 – 8351G → S in OI1. 1 Publication
    VAR_001890
    Natural varianti1195 – 11951C → Y in OI1. 1 Publication
    VAR_063383
    Osteogenesis imperfecta 2 (OI2) [MIM:166210]: An autosomal dominant form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI2 is characterized by bone fragility, with many perinatal fractures, severe bowing of long bones, undermineralization, and death in the perinatal period due to respiratory insufficiency.16 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti234 – 2341R → C in OI2. 1 Publication
    VAR_063345
    Natural varianti253 – 2531G → D in OI2. 1 Publication
    VAR_063347
    Natural varianti283 – 2831G → R in OI2. 1 Publication
    VAR_063349
    Natural varianti334 – 3341G → C in OI2.
    VAR_001856
    Natural varianti397 – 3971G → E in OI2. 1 Publication
    VAR_063353
    Natural varianti409 – 4091G → V in OI2. 1 Publication
    VAR_001861
    Natural varianti433 – 4331G → E in OI2. 1 Publication
    VAR_001862
    Natural varianti454 – 4541G → C in OI2. 1 Publication
    VAR_063354
    Natural varianti457 – 4571G → L in OI2; requires 2 nucleotide substitutions. 1 Publication
    VAR_063355
    Natural varianti461 – 4666Missing in OI2.
    VAR_063356
    Natural varianti511 – 5111G → D in OI2.
    VAR_001864
    Natural varianti526 – 5261G → E in OI2. 1 Publication
    VAR_063357
    Natural varianti547 – 5471G → R in OI2. 1 Publication
    VAR_001866
    Natural varianti562 – 5621G → C in OI2.
    VAR_001868
    Natural varianti562 – 5621G → V in OI2. 1 Publication
    VAR_063358
    Natural varianti586 – 5861G → R in OI2.
    VAR_001869
    Natural varianti592 – 5921G → S in OI2. 1 Publication
    VAR_001870
    Natural varianti625 – 6251G → D in OI2. 1 Publication
    VAR_063360
    Natural varianti637 – 6371G → D in OI2.
    VAR_001872
    Natural varianti640 – 6401G → S in OI2.
    VAR_001873
    Natural varianti670 – 6701G → D in OI2. 1 Publication
    VAR_001874
    Natural varianti676 – 855180Missing in OI2. 1 Publication
    VAR_030120Add
    BLAST
    Natural varianti705 – 7073Missing in OI2.
    VAR_063362
    Natural varianti715 – 7151G → D in OI2.
    VAR_001877
    Natural varianti730 – 7301G → C in OI2. 1 Publication
    VAR_001878
    Natural varianti739 – 7391G → R in OI2. 1 Publication
    VAR_063364
    Natural varianti748 – 7481G → V in OI2. 1 Publication
    VAR_063365
    Natural varianti754 – 7541G → R in OI2.
    VAR_001882
    Natural varianti784 – 7841G → R in OI2. 1 Publication
    VAR_001885
    Natural varianti787 – 7871G → C in OI2. 1 Publication
    VAR_001886
    Natural varianti790 – 7901G → D in OI2. 2 Publications
    VAR_001887
    Natural varianti796 – 7961G → S in OI2. 1 Publication
    VAR_001888
    Natural varianti798 – 7981P → PP in OI2. 1 Publication
    VAR_063367
    Natural varianti806 – 8116Missing in OI2.
    VAR_063368
    Natural varianti856 – 8561G → V in OI2. 1 Publication
    VAR_063373
    Natural varianti877 – 8771G → C in OI2. 1 Publication
    VAR_001891
    Natural varianti895 – 8951G → D in OI2.
    VAR_001893
    Natural varianti955 – 9551G → D in OI2. 1 Publication
    VAR_063374
    Natural varianti955 – 9551G → S in OI2. 1 Publication
    VAR_001895
    Natural varianti982 – 9821G → D in OI2. 1 Publication
    VAR_063375
    Natural varianti997 – 9971G → D in OI2. 1 Publication
    VAR_001896
    Natural varianti1003 – 10031G → D in OI2. 1 Publication
    VAR_063378
    Natural varianti1027 – 10271G → E in OI2. 1 Publication
    VAR_063379
    Natural varianti1058 – 10625Missing in OI2.
    VAR_063380
    Natural varianti1066 – 10661G → D in OI2.
    VAR_001899
    Natural varianti1078 – 10781G → C in OI2.
    VAR_001900
    Ehlers-Danlos syndrome, autosomal recessive, cardiac valvular form (EDSCV) [MIM:225320]: A connective tissue disorder characterized by hyperextensible skin, atrophic cutaneous scars due to tissue fragility and joint hyperlaxity. In addition to joint laxity, skin hyperextensibility and friability, and abnormal scar formation, patients have mitral valve prolapse and insufficiency, mitral regurgitation, and aortic insufficiency.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Osteogenesis imperfecta 3 (OI3) [MIM:259420]: An autosomal dominant form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI3 is characterized by progressively deforming bones, very short stature, a triangular face, severe scoliosis, grayish sclera and dentinogenesis imperfecta.15 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti328 – 3281G → S in OI1, OI3 AND OI4. 2 Publications
    VAR_001855
    Natural varianti331 – 3311G → D in OI3. 1 Publication
    VAR_008119
    Natural varianti337 – 3371G → C in OI3. 1 Publication
    VAR_001857
    Natural varianti337 – 3371G → S in OI3. 1 Publication
    VAR_001858
    Natural varianti345 – 3451Missing in OI3. 1 Publication
    VAR_001859
    Natural varianti349 – 3491G → C in OI3. 2 Publications
    VAR_001860
    Natural varianti358 – 3581G → S in OI3. 1 Publication
    VAR_063352
    Natural varianti460 – 4601G → S in OI3. 1 Publication
    VAR_001863
    Natural varianti517 – 5171G → R in OI3. 1 Publication
    VAR_001865
    Natural varianti676 – 6761G → D in OI3. 1 Publication
    VAR_063361
    Natural varianti676 – 6761G → V in OI3 and OI4. 2 Publications
    VAR_001875
    Natural varianti778 – 7781G → S in OI3. 1 Publication
    VAR_001884
    Natural varianti820 – 8201G → S in OI3. 1 Publication
    VAR_063370
    Natural varianti835 – 8351G → C in OI3. 1 Publication
    VAR_063371
    Natural varianti856 – 8561G → R in OI3. 1 Publication
    VAR_063372
    Natural varianti892 – 8921G → D in OI3 and OI4. 1 Publication
    VAR_001892
    Natural varianti949 – 9491G → S in OI3; moderate. 2 Publications
    VAR_001894
    Natural varianti973 – 9731G → V in OI3. 1 Publication
    VAR_008120
    Natural varianti991 – 9911G → V in OI3. 1 Publication
    VAR_063377
    Natural varianti1012 – 10121G → S in OI3 and OI4; moderate. 2 Publications
    VAR_001897
    Natural varianti1087 – 10871G → D in OI3. 1 Publication
    VAR_063381
    Natural varianti1096 – 10961G → A in OI3. 1 Publication
    VAR_001901
    Natural varianti1148 – 11481T → P in OI3. 1 Publication
    Corresponds to variant rs1800250 [ dbSNP | Ensembl ].
    VAR_001904
    Osteogenesis imperfecta 4 (OI4) [MIM:166220]: An autosomal dominant form of osteogenesis imperfecta, a connective tissue disorder characterized by low bone mass, bone fragility and susceptibility to fractures after minimal trauma. Disease severity ranges from very mild forms without fractures to intrauterine fractures and perinatal lethality. Extraskeletal manifestations, which affect a variable number of patients, are dentinogenesis imperfecta, hearing loss, and blue sclerae. OI4 is characterized by moderately short stature, mild to moderate scoliosis, grayish or white sclera and dentinogenesis imperfecta.10 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti181 – 19818Missing in OI4. 1 Publication
    VAR_030117Add
    BLAST
    Natural varianti193 – 1931G → S in OI4. 1 Publication
    VAR_063343
    Natural varianti202 – 2021G → R in OI4. 1 Publication
    VAR_063344
    Natural varianti256 – 2561G → V in OI4. 1 Publication
    VAR_063348
    Natural varianti325 – 3251G → E in OI4. 1 Publication
    VAR_063351
    Natural varianti328 – 3281G → S in OI1, OI3 AND OI4. 2 Publications
    VAR_001855
    Natural varianti634 – 6341G → V in OI4. 1 Publication
    VAR_001871
    Natural varianti676 – 6761G → V in OI3 and OI4. 2 Publications
    VAR_001875
    Natural varianti751 – 7511G → S in OI4. 1 Publication
    VAR_001881
    Natural varianti754 – 7541G → C in OI4. 1 Publication
    VAR_063366
    Natural varianti766 – 7661G → V in OI4. 1 Publication
    VAR_001883
    Natural varianti811 – 8111G → GPPG in OI4.
    VAR_063369
    Natural varianti892 – 8921G → D in OI3 and OI4. 1 Publication
    VAR_001892
    Natural varianti989 – 9891P → PVGP in OI4.
    VAR_063376
    Natural varianti1012 – 10121G → S in OI3 and OI4; moderate. 2 Publications
    VAR_001897
    Natural varianti1094 – 10963Missing in OI4.
    VAR_063382
    Natural varianti1102 – 11021G → R in OI4. 1 Publication
    VAR_001902
    A chromosomal aberration involving COL1A2 may be a cause of lipoblastomas, which are benign tumors resulting from transformation of adipocytes, usually diagnosed in children. Translocation t(7;8)(p22;q13) with PLAG1.

    Keywords - Diseasei

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

    Organism-specific databases

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

    PTM / Processingi

    Molecule processing

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

    Amino acid modifications

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

    Post-translational modificationi

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

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Hydroxylation, Pyrrolidone carboxylic acid

    Proteomic databases

    MaxQBiP08123.
    PaxDbiP08123.
    PRIDEiP08123.

    PTM databases

    PhosphoSiteiP08123.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiP08123.
    BgeeiP08123.
    GenevestigatoriP08123.

    Organism-specific databases

    HPAiCAB032650.

    Interactioni

    Subunit structurei

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

    Protein-protein interaction databases

    BioGridi107675. 8 interactions.
    DIPiDIP-36079N.
    IntActiP08123. 7 interactions.
    MINTiMINT-4791958.

    Structurei

    3D structure databases

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

    Family & Domainsi

    Domains and Repeats

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

    Domaini

    The C-terminal propeptide, also known as COLFI domain, have crucial roles in tissue growth and repair by controlling both the intracellular assembly of procollagen molecules and the extracellular assembly of collagen fibrils. It binds a calcium ion which is essential for its function By similarity.By similarity

    Sequence similaritiesi

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

    Keywords - Domaini

    Collagen, Repeat, Signal

    Phylogenomic databases

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

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

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

    P08123-1 [UniParc]FASTAAdd to Basket

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    MLSFVDTRTL LLLAVTLCLA TCQSLQEETV RKGPAGDRGP RGERGPPGPP     50
    GRDGEDGPTG PPGPPGPPGP PGLGGNFAAQ YDGKGVGLGP GPMGLMGPRG 100
    PPGAAGAPGP QGFQGPAGEP GEPGQTGPAG ARGPAGPPGK AGEDGHPGKP 150
    GRPGERGVVG PQGARGFPGT PGLPGFKGIR GHNGLDGLKG QPGAPGVKGE 200
    PGAPGENGTP GQTGARGLPG ERGRVGAPGP AGARGSDGSV GPVGPAGPIG 250
    SAGPPGFPGA PGPKGEIGAV GNAGPAGPAG PRGEVGLPGL SGPVGPPGNP 300
    GANGLTGAKG AAGLPGVAGA PGLPGPRGIP GPVGAAGATG ARGLVGEPGP 350
    AGSKGESGNK GEPGSAGPQG PPGPSGEEGK RGPNGEAGSA GPPGPPGLRG 400
    SPGSRGLPGA DGRAGVMGPP GSRGASGPAG VRGPNGDAGR PGEPGLMGPR 450
    GLPGSPGNIG PAGKEGPVGL PGIDGRPGPI GPAGARGEPG NIGFPGPKGP 500
    TGDPGKNGDK GHAGLAGARG APGPDGNNGA QGPPGPQGVQ GGKGEQGPPG 550
    PPGFQGLPGP SGPAGEVGKP GERGLHGEFG LPGPAGPRGE RGPPGESGAA 600
    GPTGPIGSRG PSGPPGPDGN KGEPGVVGAV GTAGPSGPSG LPGERGAAGI 650
    PGGKGEKGEP GLRGEIGNPG RDGARGAPGA VGAPGPAGAT GDRGEAGAAG 700
    PAGPAGPRGS PGERGEVGPA GPNGFAGPAG AAGQPGAKGE RGAKGPKGEN 750
    GVVGPTGPVG AAGPAGPNGP PGPAGSRGDG GPPGMTGFPG AAGRTGPPGP 800
    SGISGPPGPP GPAGKEGLRG PRGDQGPVGR TGEVGAVGPP GFAGEKGPSG 850
    EAGTAGPPGT PGPQGLLGAP GILGLPGSRG ERGLPGVAGA VGEPGPLGIA 900
    GPPGARGPPG AVGSPGVNGA PGEAGRDGNP GNDGPPGRDG QPGHKGERGY 950
    PGNIGPVGAA GAPGPHGPVG PAGKHGNRGE TGPSGPVGPA GAVGPRGPSG 1000
    PQGIRGDKGE PGEKGPRGLP GLKGHNGLQG LPGIAGHHGD QGAPGSVGPA 1050
    GPRGPAGPSG PAGKDGRTGH PGTVGPAGIR GPQGHQGPAG PPGPPGPPGP 1100
    PGVSGGGYDF GYDGDFYRAD QPRSAPSLRP KDYEVDATLK SLNNQIETLL 1150
    TPEGSRKNPA RTCRDLRLSH PEWSSGYYWI DPNQGCTMDA IKVYCDFSTG 1200
    ETCIRAQPEN IPAKNWYRSS KDKKHVWLGE TINAGSQFEY NVEGVTSKEM 1250
    ATQLAFMRLL ANYASQNITY HCKNSIAYMD EETGNLKKAV ILQGSNDVEL 1300
    VAEGNSRFTY TVLVDGCSKK TNEWGKTIIE YKTNKPSRLP FLDIAPLDIG 1350
    GADQEFFVDI GPVCFK 1366
    Length:1,366
    Mass (Da):129,314
    Last modified:May 18, 2010 - v7
    Checksum:i1E68A5970FB4210A
    GO

    Experimental Info

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

    Natural variant

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03464 mRNA. Translation: AAB59374.1.
    Z74616 mRNA. Translation: CAA98969.1.
    AF004877 Genomic DNA. Translation: AAB93981.1.
    BC042586 mRNA. Translation: AAH42586.1.
    BC054498 mRNA. Translation: AAH54498.1.
    Y00724 mRNA. Translation: CAA68709.1.
    X02488 mRNA. Translation: CAA26320.1.
    AB004317 Genomic DNA. Translation: BAA25383.1.
    M35391 Genomic DNA. Translation: AAA60041.1.
    S98904 Genomic DNA. Translation: AAB22126.1.
    M21671 Genomic DNA. Translation: AAA59994.1.
    S41099 mRNA. Translation: AAB22761.1.
    AC002528 Genomic DNA. Translation: AAB69977.1.
    M21353 Genomic DNA. Translation: AAA52053.1.
    M28985 Genomic DNA. Translation: AAA60356.1.
    V00503 mRNA. Translation: CAA23761.1.
    S96821 mRNA. Translation: AAB22020.2.
    L47668 mRNA. Translation: AAB59577.1.
    X55525 mRNA. Translation: CAA39142.1.
    J00114 mRNA. Translation: AAA51996.1.
    M22816 mRNA. Translation: AAA51844.1.
    M22817 Genomic DNA. Translation: AAA51846.1.
    K01078 Genomic DNA. Translation: AAA51887.1.
    K02568 Genomic DNA. Translation: AAA51850.1.
    CCDSiCCDS34682.1.
    PIRiA28500. CGHU2S.
    RefSeqiNP_000080.2. NM_000089.3.
    UniGeneiHs.489142.

    Genome annotation databases

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

    Polymorphism databases

    DMDMi296439507.

    Keywords - Coding sequence diversityi

    Chromosomal rearrangement, Polymorphism

    Cross-referencesi

    Web resourcesi

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

    Collagen type I alpha 2 (COL1A2)

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03464 mRNA. Translation: AAB59374.1 .
    Z74616 mRNA. Translation: CAA98969.1 .
    AF004877 Genomic DNA. Translation: AAB93981.1 .
    BC042586 mRNA. Translation: AAH42586.1 .
    BC054498 mRNA. Translation: AAH54498.1 .
    Y00724 mRNA. Translation: CAA68709.1 .
    X02488 mRNA. Translation: CAA26320.1 .
    AB004317 Genomic DNA. Translation: BAA25383.1 .
    M35391 Genomic DNA. Translation: AAA60041.1 .
    S98904 Genomic DNA. Translation: AAB22126.1 .
    M21671 Genomic DNA. Translation: AAA59994.1 .
    S41099 mRNA. Translation: AAB22761.1 .
    AC002528 Genomic DNA. Translation: AAB69977.1 .
    M21353 Genomic DNA. Translation: AAA52053.1 .
    M28985 Genomic DNA. Translation: AAA60356.1 .
    V00503 mRNA. Translation: CAA23761.1 .
    S96821 mRNA. Translation: AAB22020.2 .
    L47668 mRNA. Translation: AAB59577.1 .
    X55525 mRNA. Translation: CAA39142.1 .
    J00114 mRNA. Translation: AAA51996.1 .
    M22816 mRNA. Translation: AAA51844.1 .
    M22817 Genomic DNA. Translation: AAA51846.1 .
    K01078 Genomic DNA. Translation: AAA51887.1 .
    K02568 Genomic DNA. Translation: AAA51850.1 .
    CCDSi CCDS34682.1.
    PIRi A28500. CGHU2S.
    RefSeqi NP_000080.2. NM_000089.3.
    UniGenei Hs.489142.

    3D structure databases

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

    Protein-protein interaction databases

    BioGridi 107675. 8 interactions.
    DIPi DIP-36079N.
    IntActi P08123. 7 interactions.
    MINTi MINT-4791958.

    Chemistry

    ChEMBLi CHEMBL2685.
    DrugBanki DB00048. Collagenase.

    PTM databases

    PhosphoSitei P08123.

    Polymorphism databases

    DMDMi 296439507.

    Proteomic databases

    MaxQBi P08123.
    PaxDbi P08123.
    PRIDEi P08123.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

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

    Organism-specific databases

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

    Phylogenomic databases

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

    Enzyme and pathway databases

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

    Miscellaneous databases

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

    Gene expression databases

    ArrayExpressi P08123.
    Bgeei P08123.
    Genevestigatori P08123.

    Family and domain databases

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

    Publicationsi

    1. "Organization of the human pro-alpha 2(I) collagen gene."
      de Wet W.J., Bernard M.P., Benson-Chanda V., Chu M.-L., Dickson L.A., Weil D., Ramirez F.
      J. Biol. Chem. 262:16032-16036(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ASN-249; THR-276; VAL-483; ALA-549; HIS-678; GLY-743; PHE-1022; GLU-1189; PRO-1198 AND HIS-1354.
    2. "The human type I collagen mutation database."
      Dalgleish R.
      Nucleic Acids Res. 25:181-187(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], REVIEW ON OI VARIANTS, VARIANTS ALA-549; HIS-678 AND HIS-1354.
    3. "Analysis of the COL1A1 and COL1A2 genes by PCR amplification and scanning by conformation-sensitive gel electrophoresis identifies only COL1A1 mutations in 15 patients with osteogenesis imperfecta type I: identification of common sequences of null-allele mutations."
      Korkko J.M., Ala-Kokko L., De Paepe A., Nuytinck L., Earley J.J., Prockop D.J.
      Am. J. Hum. Genet. 62:98-110(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ILE-270; VAL-483; HIS-678; GLY-743; PHE-1022; GLU-1189; PRO-1198 AND HIS-1354.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-549.
      Tissue: Skin and Uterus.
    5. "Structure of a full-length cDNA clone for the prepro alpha 2(I) chain of human type I procollagen. Comparison with the chicken gene confirms unusual patterns of gene conservation."
      Kuivaniemi H., Tromp G., Chu M.-L., Prockop D.J.
      Biochem. J. 252:633-640(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-765, VARIANTS HIS-678 AND GLY-743.
      Tissue: Placenta.
    6. "Analysis of the promoter region and the N-propeptide domain of the human pro alpha 2(I) collagen gene."
      Dickson L.A., de Wet W., Di Liberto M., Weil D., Ramirez F.
      Nucleic Acids Res. 13:3427-3438(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-93, VARIANT PRO-59.
    7. "Fine structural analysis of the unique 5' region of the human COL1A2 gene containing two regions of dinucleotide repeats adjacent to the transcriptional start site."
      Akai J., Kimura A., Arai K., Uehara K., Hata R.
      Connect. Tissue Res. 30:1-6(1998)
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32.
    8. "Structural and functional characterization of a splicing mutation in the pro-alpha 2(I) collagen gene of an Ehlers-Danlos type VII patient."
      Weil D., D'Alessio M., Ramirez F., Eyre D.R.
      J. Biol. Chem. 265:16007-16011(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-93, VARIANT EDS7B 76-ASN--MET-93 DEL.
    9. "Ehlers Danlos syndrome type VIIB. Incomplete cleavage of abnormal type I procollagen by N-proteinase in vitro results in the formation of copolymers of collagen and partially cleaved pNcollagen that are near circular in cross-section."
      Watson R.B., Wallis G.A., Holmes D.F., Viljoen D., Byers P.H., Kadler K.E.
      J. Biol. Chem. 267:9093-9100(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 76-93, VARIANT EDS7B 76-ASN--MET-93 DEL.
    10. "Isolation and characterization of the cyanogen bromide peptides from the alpha 1 and alpha 2 chains of human skin collagen."
      Click E.M., Bornstein P.
      Biochemistry 9:4699-4706(1970) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 80-96.
      Tissue: Skin.
    11. "A 19-base pair deletion in the pro-alpha 2(I) gene of type I procollagen that causes in-frame RNA splicing from exon 10 to exon 12 in a proband with atypical osteogenesis imperfecta and in his asymptomatic mother."
      Kuivaniemi H., Sabol C., Tromp G., Sippola-Thiele M., Prockop D.J.
      J. Biol. Chem. 263:11407-11413(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 145-198.
    12. "Expression of mutant alpha (I)-procollagen in osteoblast and fibroblast cultures from a proband with osteogenesis imperfecta type IV."
      Chipman S.D., Shapiro J.R., McKinstry M.B., Stover M.L., Branson P., Rowe D.W.
      J. Bone Miner. Res. 7:793-805(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 163-213, VARIANT OI4 181-GLY--LYS-198 DEL.
    13. Kalicki J., Wamsley P., Gibson A.
      Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 181-1366.
    14. "Comparative sequence studies on alpha2-CB2 from calf, human, rabbit and pig-skin collagen."
      Fietzek P.P., Furthmayr H., Kuehn K.
      Eur. J. Biochem. 47:257-261(1974) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 417-447, HYDROXYLATION AT PRO-420; PRO-441 AND PRO-444.
      Tissue: Skin.
    15. "Single base mutation in the pro alpha 2(I) collagen gene that causes efficient splicing of RNA from exon 27 to exon 29 and synthesis of a shortened but in-frame pro alpha 2(I) chain."
      Tromp G., Prockop D.J.
      Proc. Natl. Acad. Sci. U.S.A. 85:5254-5258(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 520-573, VARIANT ALA-549.
    16. "Isolation and characterization of a human pro alpha 2(I) collagen gene segment."
      Tajima S., Ting J.P., Pinnell S.R., Kaufman R.E.
      J. Invest. Dermatol. 82:265-269(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 622-657.
    17. "Structure of a cDNA for the pro alpha 2 chain of human type I procollagen. Comparison with chick cDNA for pro alpha 2(I) identifies structurally conserved features of the protein and the gene."
      Bernard M.P., Myers J.C., Chu M.-L., Ramirez F., Eikenberry E.F., Prockop D.J.
      Biochemistry 22:1139-1145(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 623-1366, VARIANTS HIS-678; PHE-1022; GLU-1189; PRO-1198 AND HIS-1354.
    18. "Defective folding and stable association with protein disulfide isomerase/prolyl hydroxylase of type I procollagen with a deletion in the pro alpha 2(I) chain that preserves the Gly-X-Y repeat pattern."
      Chessler S.D., Byers P.H.
      J. Biol. Chem. 267:7751-7757(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 631-864, VARIANT OI2 676-GLY--ALA-855 DEL.
    19. "Severe (type III) osteogenesis imperfecta due to glycine substitutions in the central domain of the collagen triple helix."
      Forlino A., Zolezzi F., Valli M., Pignatti P.F., Cetta G., Brunelli P.C., Mottes M.
      Hum. Mol. Genet. 3:2201-2206(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 663-746, VARIANT OI3 VAL-676.
    20. "Growth-dependent modulation of type I collagen production and mRNA levels in cultured human skin fibroblasts."
      Maekelae J.K., Vuorio T., Vuorio E.
      Biochim. Biophys. Acta 1049:171-176(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 960-1356, VARIANT HIS-1354.
      Tissue: Skin.
    21. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 964-1019.
    22. "Arginine for glycine substitution in the triple-helical domain of the products of one alpha 2(I) collagen allele (COL1A2) produces the osteogenesis imperfecta type IV phenotype."
      Wenstrup R.J., Cohn D.H., Cohen T., Byers P.H.
      J. Biol. Chem. 263:7734-7740(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1090-1107, VARIANT OI4 ARG-1102.
    23. "Analysis of the 3' end of the human pro-alpha 2(I) collagen gene. Utilization of multiple polyadenylation sites in cultured fibroblasts."
      Myers J.C., Dickson L.A., de Wet W.J., Bernard M.P., Chu M.-L., Di Liberto M., Pepe G., Sangiorgi F.O., Ramirez F.
      J. Biol. Chem. 258:10128-10135(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1319-1366, VARIANT HIS-1354.
    24. "Osteogenesis imperfecta: cloning of a pro-alpha 2(I) collagen gene with a frameshift mutation."
      Pihlajaniemi T., Dickson L.A., Pope F.M., Korhonen V.R., Nicholls A., Prockop D.J., Myers J.C.
      J. Biol. Chem. 259:12941-12944(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1319-1366, VARIANT HIS-1354.
      Tissue: Skin.
    25. "Mutations in collagen genes: causes of rare and some common diseases in humans."
      Kuivaniemi H., Tromp G., Prockop D.J.
      FASEB J. 5:2052-2060(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON VARIANTS.
    26. "Mutations in fibrillar collagens (types I, II, III, and XI), fibril-associated collagen (type IX), and network-forming collagen (type X) cause a spectrum of diseases of bone, cartilage, and blood vessels."
      Kuivaniemi H., Tromp G., Prockop D.J.
      Hum. Mutat. 9:300-315(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON VARIANTS.
    27. "Osteogenesis imperfecta: translation of mutation to phenotype."
      Byers P.H., Wallis G.A., Willing M.C.
      J. Med. Genet. 28:433-442(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON OI VARIANTS.
    28. "Ehlers-Danlos syndrome type VIIB. Deletion of 18 amino acids comprising the N-telopeptide region of a pro-alpha 2(I) chain."
      Wirtz M.K., Glanville R.W., Steinmann B., Rao V.H., Hollister D.W.
      J. Biol. Chem. 262:16376-16385(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EDS7B 76-ASN--MET-93 DEL.
    29. "A single base mutation that converts glycine 907 of the alpha 2(I) chain of type I procollagen to aspartate in a lethal variant of osteogenesis imperfecta. The single amino acid substitution near the carboxyl terminus destabilizes the whole triple helix."
      Baldwin C.T., Constantinou C., Dumars K.W., Prockop D.J.
      J. Biol. Chem. 264:3002-3006(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT OI2 ASP-997.
    30. "Characterization of point mutations in the collagen COL1A1 and COL1A2 genes causing lethal perinatal osteogenesis imperfecta."
      Lamande S.R., Dahl H.-H.M., Cole W.G., Bateman J.F.
      J. Biol. Chem. 264:15809-15812(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT OI2 SER-955.
    31. "Two cysteine substitutions in the type I procollagen genes (COL1A1 and COL1A2) that cause lethal osteogenesis imperfecta. The location of glycine substitutions does not in any simple way predict their effects on protein function or phenotype."
      Fertala A., Westerhausen A., Morris G.M., Rooney J.E., Prockop D.J.
      Am. J. Hum. Genet. 47:A216-A216(1990)
      Cited for: VARIANT OI2 CYS-877.
    32. "Characterization of a type I collagen alpha 2(I) glycine-586 to valine substitution in osteogenesis imperfecta type IV. Detection of the mutation and prenatal diagnosis by a chemical cleavage method."
      Bateman J.F., Hannagan M., Chan D., Cole W.G.
      Biochem. J. 276:765-770(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT OI4 VAL-676.
    33. "The effects of different cysteine for glycine substitutions within alpha 2(I) chains. Evidence of distinct structural domains within the type I collagen triple helix."
      Wenstrup R.J., Shrago-Howe A.W., Lever L.W., Phillips C.L., Byers P.H., Cohn D.H.
      J. Biol. Chem. 266:2590-2594(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT OI3 CYS-349, VARIANT OI1 CYS-736.
    34. "Substitutions for glycine alpha 1-637 and glycine alpha 2-694 of type I procollagen in lethal osteogenesis imperfecta. The conformational strain on the triple helix introduced by a glycine substitution can be transmitted along the helix."
      Tsuneyoshi T., Westerhausen A., Constantinou C.D., Prockop D.J.
      J. Biol. Chem. 266:15608-15613(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT OI2 ARG-784.
    35. "Mutation in a gene for type I procollagen (COL1A2) in a woman with postmenopausal osteoporosis: evidence for phenotypic and genotypic overlap with mild osteogenesis imperfecta."
      Spotila L.D., Constantinou C.D., Sereda L., Ganguly A., Riggs B.L., Prockop D.J.
      Proc. Natl. Acad. Sci. U.S.A. 88:5423-5427(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT OI4 SER-751.
    36. "Lethal perinatal osteogenesis imperfecta due to a type I collagen alpha 2(I) Gly to Arg substitution detected by chemical cleavage of an mRNA:cDNA sequence mismatch."
      Bateman J.F., Moeller I., Hannagan M., Chan D., Cole W.G.
      Hum. Mutat. 1:55-62(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT OI2 ARG-547.
    37. "Incorporation of type I collagen molecules that contain a mutant alpha 2(I) chain (Gly580-->Asp) into bone matrix in a lethal case of osteogenesis imperfecta."
      Niyibizi C., Bonadio J., Byers P.H., Eyre D.R.
      J. Biol. Chem. 267:23108-23112(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT OI2 ASP-670.
    38. "Mutations in the COL1A2 gene of type I collagen that result in nonlethal forms of osteogenesis imperfecta."
      Wenstrup R.J., Lever L.W., Phillips C.L., Quarles L.D.
      Am. J. Med. Genet. 45:228-232(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT OI3 CYS-349, VARIANT OI1 CYS-736.
    39. "Chemical cleavage method for the detection of RNA base changes: experience in the application to collagen mutations in osteogenesis imperfecta."
      Bateman J.F., Lamande S.R., Hannagan M., Moeller I., Dahl H.-H.M., Cole W.G.
      Am. J. Med. Genet. 45:233-240(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ALA-549.
    40. "A single amino acid deletion in the alpha 2(I) chain of type I collagen produces osteogenesis imperfecta type III."
      Molyneux K., Starman B.J., Byers P.H., Dalgleish R.
      Hum. Genet. 90:621-628(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT OI3 VAL-345 DEL.
    41. "Identification of type I collagen gene (COL1A2) mutations in nonlethal osteogenesis imperfecta."
      Sztrolovics R., Glorieux F.H., van der Rest M., Roughley P.J.
      Hum. Mol. Genet. 2:1319-1321(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT OI4 VAL-634.
    42. "A novel glycine to glutamic acid substitution at position 343 in the alpha 2 chain of type I collagen in an individual with lethal osteogenesis imperfecta."
      Rose N.J., Mackay K., Byers P.H., Dalgleish R.
      Hum. Mol. Genet. 2:2175-2177(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT OI2 GLU-433.
    43. "Serine for glycine substitutions in type I collagen in two cases of type IV osteogenesis imperfecta (OI). Additional evidence for a regional model of OI pathophysiology."
      Marini J.C., Lewis M.B., Wang Q., Chen K.J., Orrison B.M.
      J. Biol. Chem. 268:2667-2673(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT OI4 SER-1012.
    44. "Two additional cases of osteogenesis imperfecta with substitutions for glycine in the alpha 2(I) collagen chain. A regional model relating mutation location with phenotype."
      Wang Q., Orrison B.M., Marini J.C.
      J. Biol. Chem. 268:25162-25167(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT OI4 VAL-766, VARIANT OI2 SER-796.
    45. "Osteogenesis imperfecta: comparison of molecular defects with bone histological changes."
      Sztrolovics R., Glorieux F.H., Travers R., van der Rest M., Roughley P.J.
      Bone 15:321-328(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT OI3 ARG-517.
    46. "Three unrelated individuals with perinatally lethal osteogenesis imperfecta resulting from identical Gly502Ser substitutions in the alpha 2-chain of type I collagen."
      Rose N.J., Mackay K., de Paepe A., Steinmann B., Punnett H.H., Dalgleish R.
      Hum. Genet. 94:497-503(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT OI2 SER-592.
    47. "A Gly859Ser substitution in the triple helical domain of the alpha 2 chain of type I collagen resulting in osteogenesis imperfecta type III in two unrelated individuals."
      Rose N.J., Mackay K., Byers P.H., Dalgleish R.
      Hum. Mutat. 3:391-394(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT OI3 SER-949.
    48. "Substitution of an aspartic acid for glycine 700 in the alpha 2(I) chain of type I collagen in a recurrent lethal type II osteogenesis imperfecta dramatically affects the mineralization of bone."
      Cohen-Solal L., Zylberberg L., Sangalli A., Gomez Lira M., Mottes M.
      J. Biol. Chem. 269:14751-14758(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT OI2 ASP-790.
    49. "Determination of a new collagen type I alpha 2 gene point mutation which causes a Gly640 Cys substitution in osteogenesis imperfecta and prenatal diagnosis by DNA hybridisation."
      Gomez Lira M., Sangalli A., Pignatti P.F., Digilio M.C., Giannotti A., Carnevale E., Mottes M.
      J. Med. Genet. 31:965-968(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT OI2 CYS-730.
    50. "Genetic counselling on brittle grounds: recurring osteogenesis imperfecta due to parental mosaicism for a dominant mutation."
      Raghunath M., Mackay K., Dalgleish R., Steinmann B.
      Eur. J. Pediatr. 154:123-129(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT OI3 SER-778.
    51. "A Gly238Ser substitution in the alpha 2 chain of type I collagen results in osteogenesis imperfecta type III."
      Rose N.J., Mackay K., Byers P.H., Dalgleish R.
      Hum. Genet. 95:215-218(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT OI3 SER-328.
    52. "A novel G1006A substitution in the alpha 2(I) chain of type I collagen produces osteogenesis imperfecta type III."
      Lu J., Costa T., Cole W.G.
      Hum. Mutat. 5:175-178(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT OI3 ALA-1096.
    53. "Gly802Asp substitution in the pro alpha 2(I) collagen chain in a family with recurrent osteogenesis imperfecta due to paternal mosaicism."
      Lund A.M., Schwartz M., Raghunath M., Steinmann B., Skovby F.
      Eur. J. Hum. Genet. 4:39-45(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT OI3 ASP-892, VARIANT OI4 ASP-892.
    54. "Direct sequencing of PCR products derived from cDNAs for the pro alpha 1 and pro alpha 2 chains of type I procollagen as a screening method to detect mutations in patients with osteogenesis imperfecta."
      Zhuang J., Tromp G., Kuivaniemi H., Castells S., Bugge M., Prockop D.J.
      Hum. Mutat. 7:89-99(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS OI1 ASP-211 AND SER-835, VARIANTS OI3 SER-337 AND SER-460, VARIANT HIS-822.
    55. "Mutation in the carboxy-terminal propeptide of the Pro alpha 1(I) chain of type I collagen in a child with severe osteogenesis imperfecta (OI type III): possible implications for protein folding."
      Oliver J.E., Thompson E.M., Pope F.M., Nicholls A.C.
      Hum. Mutat. 7:318-326(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT OI3 PRO-1148.
    56. "Four new cases of lethal osteogenesis imperfecta due to glycine substitutions in COL1A1 and genes."
      Mottes M., Gomez Lira M., Zolezzi F., Valli M., Lisi V., Freising P.
      Hum. Mutat. 12:71-72(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS OI2 VAL-409 AND CYS-787.
    57. "Osteogenesis imperfecta: mosaicism and refinement of the genotype-phenotype map in OI type III."
      Lund A.M., Astroem E., Soederhaell S., Schwartz M., Skovby F.
      Hum. Mutat. 13:503-503(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS OI3 ASP-331; CYS-337 AND VAL-973.
    58. "PLAG1 fusion oncogenes in lipoblastoma."
      Hibbard M.K., Kozakewich H.P., Dal Cin P., Sciot R., Tan X., Xiao S., Fletcher J.A.
      Cancer Res. 60:4869-4872(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHROMOSOMAL REARRANGEMENT WITH PLAG1.
    59. "Rare autosomal recessive cardiac valvular form of Ehlers-Danlos syndrome results from mutations in the COL1A2 gene that activate the nonsense-mediated RNA decay pathway."
      Schwarze U., Hata R., McKusick V.A., Shinkai H., Hoyme H.E., Pyeritz R.E., Byers P.H.
      Am. J. Hum. Genet. 74:917-930(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN CARDIAC VALVULAR EDS.
    60. "Total absence of the alpha2(I) chain of collagen type I causes a rare form of Ehlers-Danlos syndrome with hypermobility and propensity to cardiac valvular problems."
      Malfait F., Symoens S., Coucke P., Nunes L., De Almeida S., De Paepe A.
      J. Med. Genet. 43:E36-E36(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN EDSCV.
    61. "Osteogenesis imperfecta: clinical, biochemical and molecular findings."
      Venturi G., Tedeschi E., Mottes M., Valli M., Camilot M., Viglio S., Antoniazzi F., Tato L.
      Clin. Genet. 70:131-139(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS OI4 SER-193 AND CYS-754, VARIANT OI2 ASP-625, VARIANTS OI3 CYS-835 AND VAL-991.
    62. "Mutational spectrum of type I collagen genes in Korean patients with osteogenesis imperfecta."
      Lee K.S., Song H.R., Cho T.J., Kim H.J., Lee T.M., Jin H.S., Park H.Y., Kang S., Jung S.C., Koo S.K.
      Hum. Mutat. 27:599-599(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS OI1/OI3/OI4 GLU-325; SER-328; SER-358; SER-601; ASP-676; SER-820; ARG-856; SER-1012; PRO-PRO-GLY-811 INS; VAL-GLY-PRO-989 INS AND 1094-PRO--GLY-1096 DEL.
    63. "Mutation analysis of COL1A1 and COL1A2 in patients diagnosed with osteogenesis imperfecta type I-IV."
      Pollitt R., McMahon R., Nunn J., Bamford R., Afifi A., Bishop N., Dalton A.
      Hum. Mutat. 27:716-716(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS OI4 ARG-202 AND VAL-256, VARIANTS OI1 ARG-247; ARG-319; CYS-733 AND TYR-1195, VARIANTS OI2 ASP-253; ASP-982 AND ASP-1003, VARIANT OI3 ASP-1087.
    64. "Natural variation in four human collagen genes across an ethnically diverse population."
      Chan T.F., Poon A., Basu A., Addleman N.R., Chen J., Phong A., Byers P.H., Klein T.E., Kwok P.Y.
      Genomics 91:307-314(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS SER-528; ALA-549 AND THR-564.
    65. "Mutation and polymorphism spectrum in osteogenesis imperfecta type II: implications for genotype-phenotype relationships."
      Bodian D.L., Chan T.F., Poon A., Schwarze U., Yang K., Byers P.H., Kwok P.Y., Klein T.E.
      Hum. Mol. Genet. 18:463-471(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS OI2 CYS-234; ARG-283; GLU-397; CYS-454; LEU-457; 461-PRO--GLY-466 DEL; GLU-526; VAL-562; 705-ALA--PRO-707 DEL; ARG-739; VAL-748; ASP-790; PRO-798 INS; 806-PRO--GLY-811 DEL; VAL-856; SER-949; ASP-955; GLU-1027 AND 1058-PRO--ALA-1062 DEL, VARIANT ALA-549.
    66. Cited for: VARIANT THR-1119, CHARACTERIZATION OF VARIANT THR-1119.
    67. Cited for: VARIANT HIS-1067.

    Entry informationi

    Entry nameiCO1A2_HUMAN
    AccessioniPrimary (citable) accession number: P08123
    Secondary accession number(s): P02464
    , Q13897, Q13997, Q13998, Q14038, Q14057, Q15177, Q15947, Q16480, Q16511, Q7Z5S6, Q9UEB6, Q9UEF9, Q9UM83, Q9UMI1, Q9UML5, Q9UMM6, Q9UPH0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 173 of the entry and version 7 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3