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Q03692

- COAA1_HUMAN

UniProt

Q03692 - COAA1_HUMAN

Protein

Collagen alpha-1(X) chain

Gene

COL10A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 2 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Type X collagen is a product of hypertrophic chondrocytes and has been localized to presumptive mineralization zones of hyaline cartilage.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi634 – 6341Calcium

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. cartilage development Source: Ensembl
    2. collagen catabolic process Source: Reactome
    3. endochondral ossification Source: Ensembl
    4. extracellular matrix disassembly Source: Reactome
    5. extracellular matrix organization Source: Reactome
    6. skeletal system development Source: ProtInc

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_121139. Collagen biosynthesis and modifying enzymes.
    REACT_13552. Integrin cell surface interactions.
    REACT_150180. Assembly of collagen fibrils and other multimeric structures.
    REACT_150401. Collagen degradation.
    REACT_163874. Non-integrin membrane-ECM interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Collagen alpha-1(X) chain
    Gene namesi
    Name:COL10A1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:2185. COL10A1.

    Subcellular locationi

    GO - Cellular componenti

    1. cell cortex Source: Ensembl
    2. collagen trimer Source: ProtInc
    3. endoplasmic reticulum lumen Source: Reactome
    4. extracellular region Source: Reactome
    5. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Schmid type metaphyseal chondrodysplasia (SMCD) [MIM:156500]: Dominantly inherited disorder of the osseous skeleton. The cardinal features of the phenotype are mild short stature, coxa vara and a waddling gait. Radiography usually shows sclerosis of the ribs, flaring of the metaphyses, and a wide irregular growth plate, especially of the knees. A variant form of SMCD is spondylometaphyseal dysplasia Japanese type. It is characterized by spinal involvement comprising mild platyspondyly, vertebral body abnormalities, and end-plate irregularity.8 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti18 – 181G → E in SMCD. 2 Publications
    VAR_001838
    Natural varianti18 – 181G → R in SMCD. 2 Publications
    VAR_001839
    Natural varianti582 – 5821Y → D in SMCD. 1 Publication
    VAR_023188
    Natural varianti591 – 5911C → R in SMCD. 2 Publications
    VAR_001841
    Natural varianti595 – 5951G → E in SMCD and spondylometaphyseal dysplasia Japanese type. 3 Publications
    VAR_001842
    Natural varianti595 – 5951G → R in SMCD. 1 Publication
    VAR_023189
    Natural varianti597 – 5971Y → C in SMCD. 2 Publications
    VAR_008039
    Natural varianti597 – 5971Y → H in SMCD. 2 Publications
    VAR_001843
    Natural varianti598 – 5981Y → D in SMCD. 2 Publications
    VAR_001844
    Natural varianti600 – 6001S → P in SMCD. 2 Publications
    VAR_001845
    Natural varianti614 – 6141L → P in SMCD. 2 Publications
    VAR_001846
    Natural varianti617 – 6171N → K in SMCD. 2 Publications
    VAR_001847
    Natural varianti618 – 6181G → V in SMCD. 2 Publications
    VAR_001848
    Natural varianti644 – 6441L → R in SMCD. 2 Publications
    VAR_001849
    Natural varianti648 – 6481D → G in SMCD. 2 Publications
    VAR_001850
    Natural varianti651 – 6511W → R in SMCD. 1 Publication
    VAR_023191
    Natural varianti653 – 6531Q → P in SMCD. 1 Publication
    VAR_023192
    Natural varianti671 – 6711S → P in SMCD. 1 Publication
    VAR_023193

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi156500. phenotype.
    Orphaneti174. Metaphyseal chondrodysplasia, Schmid type.
    PharmGKBiPA26701.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 680662Collagen alpha-1(X) chainPRO_0000005770Add
    BLAST

    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.

    Keywords - PTMi

    Hydroxylation

    Proteomic databases

    PaxDbiQ03692.
    PRIDEiQ03692.

    Expressioni

    Gene expression databases

    ArrayExpressiQ03692.
    BgeeiQ03692.
    CleanExiHS_COL10A1.
    GenevestigatoriQ03692.

    Organism-specific databases

    HPAiHPA053268.

    Interactioni

    Subunit structurei

    Homotrimer.

    Protein-protein interaction databases

    BioGridi107697. 1 interaction.
    MINTiMINT-101719.
    STRINGi9606.ENSP00000243222.

    Structurei

    Secondary structure

    1
    680
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi553 – 5575
    Beta strandi560 – 5623
    Beta strandi573 – 5764
    Turni584 – 5863
    Beta strandi595 – 61622
    Beta strandi619 – 6268
    Beta strandi634 – 64411
    Beta strandi649 – 6535
    Beta strandi659 – 6635
    Beta strandi666 – 6683
    Beta strandi671 – 6799

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GR3X-ray2.00A521-680[»]
    ProteinModelPortaliQ03692.
    SMRiQ03692. Positions 549-680.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ03692.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini547 – 680134C1qPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni19 – 5638Nonhelical region (NC2)Add
    BLAST
    Regioni57 – 519463Triple-helical regionAdd
    BLAST
    Regioni520 – 680161Nonhelical region (NC1)Add
    BLAST

    Sequence similaritiesi

    Contains 1 C1q domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Collagen, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG114228.
    HOGENOMiHOG000085653.
    HOVERGENiHBG108220.
    InParanoidiQ03692.
    OMAiKGPQPNT.
    OrthoDBiEOG70ZZPW.
    PhylomeDBiQ03692.
    TreeFamiTF334029.

    Family and domain databases

    Gene3Di2.60.120.40. 1 hit.
    InterProiIPR001073. C1q.
    IPR008160. Collagen.
    IPR008983. Tumour_necrosis_fac-like_dom.
    [Graphical view]
    PfamiPF00386. C1q. 1 hit.
    PF01391. Collagen. 4 hits.
    [Graphical view]
    PRINTSiPR00007. COMPLEMNTC1Q.
    SMARTiSM00110. C1Q. 1 hit.
    [Graphical view]
    SUPFAMiSSF49842. SSF49842. 1 hit.
    PROSITEiPS50871. C1Q. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q03692-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLPQIPFLLL VSLNLVHGVF YAERYQMPTG IKGPLPNTKT QFFIPYTIKS    50
    KGIAVRGEQG TPGPPGPAGP RGHPGPSGPP GKPGYGSPGL QGEPGLPGPP 100
    GPSAVGKPGV PGLPGKPGER GPYGPKGDVG PAGLPGPRGP PGPPGIPGPA 150
    GISVPGKPGQ QGPTGAPGPR GFPGEKGAPG VPGMNGQKGE MGYGAPGRPG 200
    ERGLPGPQGP TGPSGPPGVG KRGENGVPGQ PGIKGDRGFP GEMGPIGPPG 250
    PQGPPGERGP EGIGKPGAAG APGQPGIPGT KGLPGAPGIA GPPGPPGFGK 300
    PGLPGLKGER GPAGLPGGPG AKGEQGPAGL PGKPGLTGPP GNMGPQGPKG 350
    IPGSHGLPGP KGETGPAGPA GYPGAKGERG SPGSDGKPGY PGKPGLDGPK 400
    GNPGLPGPKG DPGVGGPPGL PGPVGPAGAK GMPGHNGEAG PRGAPGIPGT 450
    RGPIGPPGIP GFPGSKGDPG SPGPPGPAGI ATKGLNGPTG PPGPPGPRGH 500
    SGEPGLPGPP GPPGPPGQAV MPEGFIKAGQ RPSLSGTPLV SANQGVTGMP 550
    VSAFTVILSK AYPAIGTPIP FDKILYNRQQ HYDPRTGIFT CQIPGIYYFS 600
    YHVHVKGTHV WVGLYKNGTP VMYTYDEYTK GYLDQASGSA IIDLTENDQV 650
    WLQLPNAESN GLYSSEYVHS SFSGFLVAPM 680
    Length:680
    Mass (Da):66,158
    Last modified:November 1, 1997 - v2
    Checksum:iE2F98E53E7882459
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti500 – 5001H → P in CAA42933. (PubMed:1764025)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti18 – 181G → E in SMCD. 2 Publications
    VAR_001838
    Natural varianti18 – 181G → R in SMCD. 2 Publications
    VAR_001839
    Natural varianti27 – 271M → T.2 Publications
    Corresponds to variant rs1064583 [ dbSNP | Ensembl ].
    VAR_023186
    Natural varianti98 – 981G → R.
    Corresponds to variant rs2243370 [ dbSNP | Ensembl ].
    VAR_048767
    Natural varianti198 – 1981R → H.1 Publication
    Corresponds to variant rs148785195 [ dbSNP | Ensembl ].
    VAR_023187
    Natural varianti545 – 5451G → R.2 Publications
    Corresponds to variant rs2228547 [ dbSNP | Ensembl ].
    VAR_001840
    Natural varianti582 – 5821Y → D in SMCD. 1 Publication
    VAR_023188
    Natural varianti591 – 5911C → R in SMCD. 2 Publications
    VAR_001841
    Natural varianti595 – 5951G → E in SMCD and spondylometaphyseal dysplasia Japanese type. 3 Publications
    VAR_001842
    Natural varianti595 – 5951G → R in SMCD. 1 Publication
    VAR_023189
    Natural varianti597 – 5971Y → C in SMCD. 2 Publications
    VAR_008039
    Natural varianti597 – 5971Y → H in SMCD. 2 Publications
    VAR_001843
    Natural varianti598 – 5981Y → D in SMCD. 2 Publications
    VAR_001844
    Natural varianti600 – 6001S → P in SMCD. 2 Publications
    VAR_001845
    Natural varianti603 – 6031V → M.1 Publication
    VAR_023190
    Natural varianti614 – 6141L → P in SMCD. 2 Publications
    VAR_001846
    Natural varianti617 – 6171N → K in SMCD. 2 Publications
    VAR_001847
    Natural varianti618 – 6181G → V in SMCD. 2 Publications
    VAR_001848
    Natural varianti644 – 6441L → R in SMCD. 2 Publications
    VAR_001849
    Natural varianti648 – 6481D → G in SMCD. 2 Publications
    VAR_001850
    Natural varianti651 – 6511W → R in SMCD. 1 Publication
    VAR_023191
    Natural varianti653 – 6531Q → P in SMCD. 1 Publication
    VAR_023192
    Natural varianti671 – 6711S → P in SMCD. 1 Publication
    VAR_023193

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60382 Genomic DNA. Translation: CAA42933.1.
    X72579, X72580 Genomic DNA. Translation: CAA51170.1.
    X98568 Genomic DNA. Translation: CAA67178.1.
    AL121963 Genomic DNA. Translation: CAB87590.1.
    CH471051 Genomic DNA. Translation: EAW48240.1.
    BC130621 mRNA. Translation: AAI30622.1.
    BC130623 mRNA. Translation: AAI30624.1.
    X65120 Genomic DNA. Translation: CAA46236.1.
    X58879 Genomic DNA. Translation: CAA41686.1.
    M74050 Genomic DNA. Translation: AAA61221.1.
    S68531 mRNA. Translation: AAC60615.1.
    CCDSiCCDS5105.1.
    PIRiS26396. CGHU1D.
    RefSeqiNP_000484.2. NM_000493.3.
    XP_006715395.1. XM_006715332.1.
    XP_006715396.1. XM_006715333.1.
    UniGeneiHs.520339.

    Genome annotation databases

    EnsembliENST00000243222; ENSP00000243222; ENSG00000123500.
    ENST00000327673; ENSP00000327368; ENSG00000123500.
    GeneIDi1300.
    KEGGihsa:1300.
    UCSCiuc003pwm.3. human.

    Polymorphism databases

    DMDMi2506306.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60382 Genomic DNA. Translation: CAA42933.1 .
    X72579 , X72580 Genomic DNA. Translation: CAA51170.1 .
    X98568 Genomic DNA. Translation: CAA67178.1 .
    AL121963 Genomic DNA. Translation: CAB87590.1 .
    CH471051 Genomic DNA. Translation: EAW48240.1 .
    BC130621 mRNA. Translation: AAI30622.1 .
    BC130623 mRNA. Translation: AAI30624.1 .
    X65120 Genomic DNA. Translation: CAA46236.1 .
    X58879 Genomic DNA. Translation: CAA41686.1 .
    M74050 Genomic DNA. Translation: AAA61221.1 .
    S68531 mRNA. Translation: AAC60615.1 .
    CCDSi CCDS5105.1.
    PIRi S26396. CGHU1D.
    RefSeqi NP_000484.2. NM_000493.3.
    XP_006715395.1. XM_006715332.1.
    XP_006715396.1. XM_006715333.1.
    UniGenei Hs.520339.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GR3 X-ray 2.00 A 521-680 [» ]
    ProteinModelPortali Q03692.
    SMRi Q03692. Positions 549-680.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107697. 1 interaction.
    MINTi MINT-101719.
    STRINGi 9606.ENSP00000243222.

    Polymorphism databases

    DMDMi 2506306.

    Proteomic databases

    PaxDbi Q03692.
    PRIDEi Q03692.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000243222 ; ENSP00000243222 ; ENSG00000123500 .
    ENST00000327673 ; ENSP00000327368 ; ENSG00000123500 .
    GeneIDi 1300.
    KEGGi hsa:1300.
    UCSCi uc003pwm.3. human.

    Organism-specific databases

    CTDi 1300.
    GeneCardsi GC06M116440.
    HGNCi HGNC:2185. COL10A1.
    HPAi HPA053268.
    MIMi 120110. gene.
    156500. phenotype.
    neXtProti NX_Q03692.
    Orphaneti 174. Metaphyseal chondrodysplasia, Schmid type.
    PharmGKBi PA26701.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG114228.
    HOGENOMi HOG000085653.
    HOVERGENi HBG108220.
    InParanoidi Q03692.
    OMAi KGPQPNT.
    OrthoDBi EOG70ZZPW.
    PhylomeDBi Q03692.
    TreeFami TF334029.

    Enzyme and pathway databases

    Reactomei REACT_121139. Collagen biosynthesis and modifying enzymes.
    REACT_13552. Integrin cell surface interactions.
    REACT_150180. Assembly of collagen fibrils and other multimeric structures.
    REACT_150401. Collagen degradation.
    REACT_163874. Non-integrin membrane-ECM interactions.

    Miscellaneous databases

    EvolutionaryTracei Q03692.
    GeneWikii Collagen,_type_X,_alpha_1.
    GenomeRNAii 1300.
    NextBioi 5279.
    PROi Q03692.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q03692.
    Bgeei Q03692.
    CleanExi HS_COL10A1.
    Genevestigatori Q03692.

    Family and domain databases

    Gene3Di 2.60.120.40. 1 hit.
    InterProi IPR001073. C1q.
    IPR008160. Collagen.
    IPR008983. Tumour_necrosis_fac-like_dom.
    [Graphical view ]
    Pfami PF00386. C1q. 1 hit.
    PF01391. Collagen. 4 hits.
    [Graphical view ]
    PRINTSi PR00007. COMPLEMNTC1Q.
    SMARTi SM00110. C1Q. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49842. SSF49842. 1 hit.
    PROSITEi PS50871. C1Q. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The human collagen X gene. Complete primary translated sequence and chromosomal localization."
      Thomas J.T., Cresswell C.J., Rash B., Nicolai H., Jones T., Solomon E., Grant M.E., Boot-Handford R.P.
      Biochem. J. 280:617-623(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-27.
    2. "Genomic organization and full-length cDNA sequence of human collagen X."
      Reichenberger E., Beier F., LuValle P., Olsen B.R., von der Mark K., Bertling W.M.
      FEBS Lett. 311:305-310(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. Beier F., Lammi M.B., von der Mark K.
      Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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].
    7. "Cloning of the human and mouse type X collagen genes and mapping of the mouse type X collagen gene to chromosome 10."
      Apte S.S., Seldin M.F., Hayashi M., Olsen B.R.
      Eur. J. Biochem. 206:217-224(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 52-680.
    8. "Cloning of human alpha 1(X) collagen DNA and localization of the COL10A1 gene to the q21-q22 region of human chromosome 6."
      Apte S., Mattei M.-G., Olsen B.R.
      FEBS Lett. 282:393-396(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE OF 561-666.
    9. "In situ hybridization studies on the expression of type X collagen in fetal human cartilage."
      Reichenberger E., Aigner T., von der Mark K., Stoeb H., Bertling W.
      Dev. Biol. 148:562-572(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 547-655.
    10. "Insight into Schmid metaphyseal chondrodysplasia from the crystal structure of the collagen X NC1 domain trimer."
      Bogin O., Kvansakul M., Rom E., Singer J., Yayon A., Hohenester E.
      Structure 10:165-173(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 521-680, CALCIUM-BINDING.
    11. "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.
    12. "Amino acid substitutions of conserved residues in the carboxyl-terminal domain of the alpha 1(X) chain of type X collagen occur in two unrelated families with metaphyseal chondrodysplasia type Schmid."
      Wallis G.A., Rash B., Sweetman W.A., Thomas J.T., Super M., Evans G., Grant M.E., Boot-Handford R.P.
      Am. J. Hum. Genet. 54:169-178(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS SMCD ASP-598 AND PRO-614.
    13. "Additional mutations of type X collagen confirm COL10A1 as the Schmid metaphyseal chondrodysplasia locus."
      McIntosh I., Abbott M.H., Warman M.L., Olsen B.R., Francomano C.A.
      Hum. Mol. Genet. 3:303-307(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SMCD ARG-591.
    14. "Type X collagen multimer assembly in vitro is prevented by a Gly618 to Val mutation in the alpha 1(X) NC1 domain resulting in Schmid metaphyseal chondrodysplasia."
      Chan D., Cole W.G., Rogers J.G., Bateman J.F.
      J. Biol. Chem. 270:4558-4562(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SMCD VAL-618.
    15. "Mutations in three subdomains of the carboxy-terminal region of collagen type X account for most of the Schmid metaphyseal dysplasias."
      Bonaventure J., Chaminade F., Maroteaux P.
      Hum. Genet. 96:58-64(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS SMCD ARG-545; GLU-595; HIS-597; LYS-617; ARG-644 AND GLY-648.
    16. "Mutations within the gene encoding the alpha 1 (X) chain of type X collagen (COL10A1) cause metaphyseal chondrodysplasia type Schmid but not several other forms of metaphyseal chondrodysplasia."
      Wallis G.A., Rash B., Sykes B., Bonaventure J., Maroteaux P., Zabel B., Wynne-Davies R., Grant M.E., Boot-Handford R.P.
      J. Med. Genet. 33:450-457(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SMCD PRO-600.
    17. "Mutations in the N-terminal globular domain of the type X collagen gene (COL10A1) in patients with schmid metaphyseal chondrodysplasia."
      Ikegawa S., Nakamura K., Nagano A., Haga N., Nakamura Y.
      Hum. Mutat. 9:131-135(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS SMCD GLU-18 AND ARG-18.
    18. "Mutation of the type X collagen gene 'COL10A1' causes spondylometaphyseal dysplasia."
      Ikegawa S., Nishimura G., Nagai T., Hasegawa T., Ohashi H., Nakamura Y.
      Am. J. Hum. Genet. 63:1659-1662(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SPONDYLOMETAPHYSEAL DYSPLASIA JAPANESE TYPE GLU-595.
    19. "Novel missense mutation resulting in the substitution of tyrosine by cysteine at codon 597 of the type X collagen gene associated with Schmid metaphyseal chondrodysplasia."
      Sawai H., Ida A., Nakata Y., Koyama K.
      J. Hum. Genet. 43:259-261(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SMCD CYS-597.
    20. "Mutations of COL10A1 in Schmid metaphyseal chondrodysplasia."
      Bateman J.F., Wilson R., Freddi S., Lamande S.R., Savarirayan R.
      Hum. Mutat. 25:525-534(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS SMCD ARG-18; GLU-18; ASP-582; ARG-591; ARG-595; GLU-595; HIS-597; CYS-597; ASP-598; PRO-600; PRO-614; LYS-617; VAL-618; ARG-644; GLY-648; ARG-651; PRO-653 AND PRO-671, VARIANTS THR-27; HIS-198; ARG-545 AND MET-603.

    Entry informationi

    Entry nameiCOAA1_HUMAN
    AccessioniPrimary (citable) accession number: Q03692
    Secondary accession number(s): A1L4P2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 146 of the entry and version 2 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

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