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P20849

- CO9A1_HUMAN

UniProt

P20849 - CO9A1_HUMAN

Protein

Collagen alpha-1(IX) chain

Gene

COL9A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 169 (01 Oct 2014)
      Sequence version 3 (18 May 2010)
      Previous versions | rss
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    Functioni

    Structural component of hyaline cartilage and vitreous of the eye.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi213 – 2131Zinc
    Metal bindingi215 – 2151Zinc
    Metal bindingi253 – 2531Zinc

    GO - Molecular functioni

    1. extracellular matrix structural constituent conferring tensile strength Source: BHF-UCL
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. axon guidance Source: Reactome
    2. collagen catabolic process Source: Reactome
    3. extracellular matrix disassembly Source: Reactome
    4. extracellular matrix organization Source: Reactome
    5. growth plate cartilage development Source: Ensembl
    6. organ morphogenesis Source: ProtInc
    7. tissue homeostasis Source: Ensembl

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_121139. Collagen biosynthesis and modifying enzymes.
    REACT_13552. Integrin cell surface interactions.
    REACT_150401. Collagen degradation.
    REACT_163906. ECM proteoglycans.
    REACT_16888. Signaling by PDGF.
    REACT_18312. NCAM1 interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Collagen alpha-1(IX) chain
    Gene namesi
    Name:COL9A1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:2217. COL9A1.

    Subcellular locationi

    GO - Cellular componenti

    1. collagen type IX trimer Source: UniProtKB
    2. endoplasmic reticulum lumen Source: Reactome
    3. extracellular region Source: Reactome

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Multiple epiphyseal dysplasia 6 (EDM6) [MIM:614135]: A generalized skeletal dysplasia associated with significant morbidity. Joint pain, joint deformity, waddling gait, and short stature are the main clinical signs and symptoms. Radiological examination of the skeleton shows delayed, irregular mineralization of the epiphyseal ossification centers and of the centers of the carpal and tarsal bones. Multiple epiphyseal dysplasia is broadly categorized into the more severe Fairbank and the milder Ribbing types. The Fairbank type is characterized by shortness of stature, short and stubby fingers, small epiphyses in several joints, including the knee, ankle, hand, and hip. The Ribbing type is confined predominantly to the hip joints and is characterized by hands that are normal and stature that is normal or near-normal.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Stickler syndrome 4 (STL4) [MIM:614134]: An autosomal recessive form of Stickler syndrome, an inherited disorder that associates ocular signs with more or less complete forms of Pierre Robin sequence, bone disorders and sensorineural deafness. Ocular disorders may include juvenile cataract, myopia, strabismus, vitreoretinal or chorioretinal degeneration, retinal detachment, and chronic uveitis. Robin sequence includes an opening in the roof of the mouth (a cleft palate), a large tongue (macroglossia), and a small lower jaw (micrognathia). Bones are affected by slight platyspondylisis and large, often defective epiphyses. Juvenile joint laxity is followed by early signs of arthrosis. The degree of hearing loss varies among affected individuals and may become more severe over time. Syndrome expressivity is variable.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Deafness, Stickler syndrome

    Organism-specific databases

    MIMi614134. phenotype.
    614135. phenotype.
    Orphaneti250984. Autosomal recessive Stickler syndrome.
    166002. Multiple epiphyseal dysplasia due to collagen 9 anomaly.
    PharmGKBiPA26733.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Add
    BLAST
    Chaini24 – 921898Collagen alpha-1(IX) chainPRO_0000005765Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi44 ↔ 2421 Publication
    Glycosylationi171 – 1711N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi198 ↔ 2521 Publication
    Disulfide bondi411 – 411Interchain1 Publication
    Disulfide bondi415 – 415Interchain1 Publication

    Post-translational modificationi

    Covalently linked to the telopeptides of type II collagen by lysine-derived cross-links.
    Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Hydroxylation

    Proteomic databases

    PaxDbiP20849.
    PRIDEiP20849.

    PTM databases

    PhosphoSiteiP20849.

    Expressioni

    Gene expression databases

    ArrayExpressiP20849.
    BgeeiP20849.
    GenevestigatoriP20849.

    Interactioni

    Subunit structurei

    Heterotrimer of an alpha 1(IX), an alpha 2(IX) and an alpha 3(IX) chain.

    Protein-protein interaction databases

    BioGridi107694. 2 interactions.

    Structurei

    Secondary structure

    1
    921
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi56 – 583
    Helixi59 – 624
    Helixi65 – 695
    Turni70 – 723
    Beta strandi76 – 783
    Beta strandi85 – 895
    Beta strandi96 – 983
    Helixi99 – 1024
    Beta strandi109 – 11810
    Helixi121 – 1255
    Beta strandi127 – 1348
    Beta strandi140 – 1478
    Helixi148 – 1503
    Beta strandi152 – 1598
    Beta strandi164 – 1696
    Helixi173 – 1753
    Beta strandi177 – 1793
    Beta strandi181 – 1888
    Beta strandi191 – 1966
    Beta strandi199 – 2057
    Beta strandi215 – 22511
    Beta strandi233 – 24210
    Helixi246 – 2494

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2UURX-ray1.80A24-268[»]
    ProteinModelPortaliP20849.
    SMRiP20849. Positions 42-256.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP20849.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini50 – 244195Laminin G-likeAdd
    BLAST
    Domaini269 – 32456Collagen-like 1Add
    BLAST
    Domaini325 – 35632Collagen-like 2Add
    BLAST
    Domaini358 – 40346Collagen-like 3Add
    BLAST
    Domaini416 – 47257Collagen-like 4Add
    BLAST
    Domaini473 – 51644Collagen-like 5Add
    BLAST
    Domaini587 – 64357Collagen-like 6Add
    BLAST
    Domaini655 – 71258Collagen-like 7Add
    BLAST
    Domaini713 – 75543Collagen-like 8Add
    BLAST
    Domaini790 – 84758Collagen-like 9Add
    BLAST
    Domaini848 – 89952Collagen-like 10Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni24 – 268245Nonhelical region (NC4)Add
    BLAST
    Regioni269 – 405137Triple-helical region (COL3)Add
    BLAST
    Regioni406 – 41712Nonhelical region (NC3)Add
    BLAST
    Regioni418 – 756339Triple-helical region (COL2)Add
    BLAST
    Regioni757 – 78630Nonhelical region (NC2)Add
    BLAST
    Regioni787 – 901115Triple-helical region (COL1)Add
    BLAST
    Regioni902 – 92120Nonhelical region (NC1)Add
    BLAST

    Domaini

    Each subunit is composed of three triple-helical domains interspersed with non-collagenous domains. The globular domain at the N-terminus of type IX collagen molecules represents the NC4 domain which may participate in electrostatic interactions with polyanionic glycosaminoglycans in cartilage.

    Sequence similaritiesi

    Contains 10 collagen-like domains.Curated
    Contains 1 laminin G-like domain.Curated

    Keywords - Domaini

    Collagen, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG12793.
    HOVERGENiHBG004933.
    InParanoidiP20849.
    KOiK08131.
    OMAiGFCEPAS.
    OrthoDBiEOG7VHSXW.
    PhylomeDBiP20849.
    TreeFamiTF332900.

    Family and domain databases

    Gene3Di2.60.120.200. 1 hit.
    InterProiIPR008160. Collagen.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR001791. Laminin_G.
    [Graphical view]
    PfamiPF01391. Collagen. 10 hits.
    [Graphical view]
    SMARTiSM00210. TSPN. 1 hit.
    [Graphical view]
    SUPFAMiSSF49899. SSF49899. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 1 (identifier: P20849-1) [UniParc]FASTAAdd to Basket

    Also known as: Long

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MKTCWKIPVF FFVCSFLEPW ASAAVKRRPR FPVNSNSNGG NELCPKIRIG    50
    QDDLPGFDLI SQFQVDKAAS RRAIQRVVGS ATLQVAYKLG NNVDFRIPTR 100
    NLYPSGLPEE YSFLTTFRMT GSTLKKNWNI WQIQDSSGKE QVGIKINGQT 150
    QSVVFSYKGL DGSLQTAAFS NLSSLFDSQW HKIMIGVERS SATLFVDCNR 200
    IESLPIKPRG PIDIDGFAVL GKLADNPQVS VPFELQWMLI HCDPLRPRRE 250
    TCHELPARIT PSQTTDERGP PGEQGPPGPP GPPGVPGIDG IDGDRGPKGP 300
    PGPPGPAGEP GKPGAPGKPG TPGADGLTGP DGSPGSIGSK GQKGEPGVPG 350
    SRGFPGRGIP GPPGPPGTAG LPGELGRVGP VGDPGRRGPP GPPGPPGPRG 400
    TIGFHDGDPL CPNACPPGRS GYPGLPGMRG HKGAKGEIGE PGRQGHKGEE 450
    GDQGELGEVG AQGPPGAQGL RGITGIVGDK GEKGARGLDG EPGPQGLPGA 500
    PGDQGQRGPP GEAGPKGDRG AEGARGIPGL PGPKGDTGLP GVDGRDGIPG 550
    MPGTKGEPGK PGPPGDAGLQ GLPGVPGIPG AKGVAGEKGS TGAPGKPGQM 600
    GNSGKPGQQG PPGEVGPRGP QGLPGSRGEL GPVGSPGLPG KLGSLGSPGL 650
    PGLPGPPGLP GMKGDRGVVG EPGPKGEQGA SGEEGEAGER GELGDIGLPG 700
    PKGSAGNPGE PGLRGPEGSR GLPGVEGPRG PPGPRGVQGE QGATGLPGVQ 750
    GPPGRAPTDQ HIKQVCMRVI QEHFAEMAAS LKRPDSGATG LPGRPGPPGP 800
    PGPPGENGFP GQMGIRGLPG IKGPPGALGL RGPKGDLGEK GERGPPGRGP 850
    NGLPGAIGLP GDPGPASYGR NGRDGERGPP GVAGIPGVPG PPGPPGLPGF 900
    CEPASCTMQA GQRAFNKGPD P 921
    Length:921
    Mass (Da):91,869
    Last modified:May 18, 2010 - v3
    Checksum:iA69BF076127283D0
    GO
    Isoform 2 (identifier: P20849-2) [UniParc]FASTAAdd to Basket

    Also known as: Short

    The sequence of this isoform differs from the canonical sequence as follows:
         1-243: Missing.
         244-267: PLRPRRETCHELPARITPSQTTDE → MAWTARDRGALGLLLLGLCLCAAQ

    Show »
    Length:678
    Mass (Da):64,372
    Checksum:iAD0E99997DF2896E
    GO
    Isoform 3 (identifier: P20849-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         326-328: GLT → TSP
         329-921: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:328
    Mass (Da):35,509
    Checksum:iBDD662939FECAD21
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti279 – 2802PP → AS in CAA38276. (PubMed:2209617)Curated
    Sequence conflicti279 – 2802PP → AS in CAA38277. (PubMed:2209617)Curated
    Sequence conflicti476 – 4761I → L in CAA38276. (PubMed:2209617)Curated
    Sequence conflicti570 – 5701Q → H in AAC33527. (PubMed:9707347)Curated
    Sequence conflicti570 – 5701Q → H in AAC33528. (PubMed:9707347)Curated
    Sequence conflicti910 – 92112AGQRA…KGPDP → LVSEHLTKGLTLERLTAAWL SA in AAA53475. (PubMed:2209617)CuratedAdd
    BLAST

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti339 – 3391S → P.1 Publication
    Corresponds to variant rs592121 [ dbSNP | Ensembl ].
    VAR_026463
    Natural varianti621 – 6211Q → R.2 Publications
    Corresponds to variant rs1135056 [ dbSNP | Ensembl ].
    VAR_026464
    Natural varianti684 – 6841E → K.
    Corresponds to variant rs35470562 [ dbSNP | Ensembl ].
    VAR_055668
    Natural varianti767 – 7671M → V.
    Corresponds to variant rs6910140 [ dbSNP | Ensembl ].
    VAR_055669
    Natural varianti870 – 8701R → K.3 Publications
    Corresponds to variant rs1056921 [ dbSNP | Ensembl ].
    VAR_023326
    Natural varianti882 – 8821V → L.3 Publications
    Corresponds to variant rs1056923 [ dbSNP | Ensembl ].
    VAR_023327

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 243243Missing in isoform 2. 2 PublicationsVSP_001141Add
    BLAST
    Alternative sequencei244 – 26724PLRPR…QTTDE → MAWTARDRGALGLLLLGLCL CAAQ in isoform 2. 2 PublicationsVSP_001142Add
    BLAST
    Alternative sequencei326 – 3283GLT → TSP in isoform 3. 1 PublicationVSP_015250
    Alternative sequencei329 – 921593Missing in isoform 3. 1 PublicationVSP_015251Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X54412 mRNA. Translation: CAA38276.1.
    X54413 mRNA. Translation: CAA38277.1.
    AF036130
    , AF036110, AF036111, AF036112, AF036113, AF036114, AF036115, AF036116, AF036117, AF036118, AF036119, AF036120, AF036121, AF036122, AF036123, AF036124, AF036125, AF036126, AF036127, AF036128, AF036129 Genomic DNA. Translation: AAC33527.1.
    AF036130
    , AF036112, AF036113, AF036114, AF036115, AF036116, AF036117, AF036118, AF036119, AF036120, AF036121, AF036122, AF036123, AF036124, AF036125, AF036126, AF036127, AF036128, AF036129 Genomic DNA. Translation: AAC33528.1.
    AL080275, AL160262 Genomic DNA. Translation: CAI19590.1.
    AL080275 Genomic DNA. Translation: CAI19591.1.
    AL160262, AL080275 Genomic DNA. Translation: CAI42321.1.
    BC015409 mRNA. Translation: AAH15409.1.
    BC063646 mRNA. Translation: AAH63646.1.
    M32137, M32133 Genomic DNA. Translation: AAA53474.1.
    M32137, M32135 Genomic DNA. Translation: AAA53475.1.
    CCDSiCCDS47447.1. [P20849-2]
    CCDS4971.1. [P20849-1]
    PIRiS13580.
    S13581.
    RefSeqiNP_001842.3. NM_001851.4. [P20849-1]
    NP_511040.2. NM_078485.3. [P20849-2]
    UniGeneiHs.590892.

    Genome annotation databases

    EnsembliENST00000320755; ENSP00000315252; ENSG00000112280. [P20849-2]
    ENST00000357250; ENSP00000349790; ENSG00000112280. [P20849-1]
    ENST00000370496; ENSP00000359527; ENSG00000112280. [P20849-3]
    GeneIDi1297.
    KEGGihsa:1297.
    UCSCiuc003pff.4. human. [P20849-2]
    uc003pfg.4. human. [P20849-1]

    Polymorphism databases

    DMDMi296439373.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X54412 mRNA. Translation: CAA38276.1 .
    X54413 mRNA. Translation: CAA38277.1 .
    AF036130
    , AF036110 , AF036111 , AF036112 , AF036113 , AF036114 , AF036115 , AF036116 , AF036117 , AF036118 , AF036119 , AF036120 , AF036121 , AF036122 , AF036123 , AF036124 , AF036125 , AF036126 , AF036127 , AF036128 , AF036129 Genomic DNA. Translation: AAC33527.1 .
    AF036130
    , AF036112 , AF036113 , AF036114 , AF036115 , AF036116 , AF036117 , AF036118 , AF036119 , AF036120 , AF036121 , AF036122 , AF036123 , AF036124 , AF036125 , AF036126 , AF036127 , AF036128 , AF036129 Genomic DNA. Translation: AAC33528.1 .
    AL080275 , AL160262 Genomic DNA. Translation: CAI19590.1 .
    AL080275 Genomic DNA. Translation: CAI19591.1 .
    AL160262 , AL080275 Genomic DNA. Translation: CAI42321.1 .
    BC015409 mRNA. Translation: AAH15409.1 .
    BC063646 mRNA. Translation: AAH63646.1 .
    M32137 , M32133 Genomic DNA. Translation: AAA53474.1 .
    M32137 , M32135 Genomic DNA. Translation: AAA53475.1 .
    CCDSi CCDS47447.1. [P20849-2 ]
    CCDS4971.1. [P20849-1 ]
    PIRi S13580.
    S13581.
    RefSeqi NP_001842.3. NM_001851.4. [P20849-1 ]
    NP_511040.2. NM_078485.3. [P20849-2 ]
    UniGenei Hs.590892.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2UUR X-ray 1.80 A 24-268 [» ]
    ProteinModelPortali P20849.
    SMRi P20849. Positions 42-256.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107694. 2 interactions.

    PTM databases

    PhosphoSitei P20849.

    Polymorphism databases

    DMDMi 296439373.

    Proteomic databases

    PaxDbi P20849.
    PRIDEi P20849.

    Protocols and materials databases

    DNASUi 1297.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000320755 ; ENSP00000315252 ; ENSG00000112280 . [P20849-2 ]
    ENST00000357250 ; ENSP00000349790 ; ENSG00000112280 . [P20849-1 ]
    ENST00000370496 ; ENSP00000359527 ; ENSG00000112280 . [P20849-3 ]
    GeneIDi 1297.
    KEGGi hsa:1297.
    UCSCi uc003pff.4. human. [P20849-2 ]
    uc003pfg.4. human. [P20849-1 ]

    Organism-specific databases

    CTDi 1297.
    GeneCardsi GC06M070924.
    GeneReviewsi COL9A1.
    HGNCi HGNC:2217. COL9A1.
    MIMi 120210. gene.
    614134. phenotype.
    614135. phenotype.
    neXtProti NX_P20849.
    Orphaneti 250984. Autosomal recessive Stickler syndrome.
    166002. Multiple epiphyseal dysplasia due to collagen 9 anomaly.
    PharmGKBi PA26733.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG12793.
    HOVERGENi HBG004933.
    InParanoidi P20849.
    KOi K08131.
    OMAi GFCEPAS.
    OrthoDBi EOG7VHSXW.
    PhylomeDBi P20849.
    TreeFami TF332900.

    Enzyme and pathway databases

    Reactomei REACT_121139. Collagen biosynthesis and modifying enzymes.
    REACT_13552. Integrin cell surface interactions.
    REACT_150401. Collagen degradation.
    REACT_163906. ECM proteoglycans.
    REACT_16888. Signaling by PDGF.
    REACT_18312. NCAM1 interactions.

    Miscellaneous databases

    ChiTaRSi COL9A1. human.
    EvolutionaryTracei P20849.
    GeneWikii Collagen,_type_IX,_alpha_1.
    GenomeRNAii 1297.
    NextBioi 5265.
    PROi P20849.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P20849.
    Bgeei P20849.
    Genevestigatori P20849.

    Family and domain databases

    Gene3Di 2.60.120.200. 1 hit.
    InterProi IPR008160. Collagen.
    IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR001791. Laminin_G.
    [Graphical view ]
    Pfami PF01391. Collagen. 10 hits.
    [Graphical view ]
    SMARTi SM00210. TSPN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49899. SSF49899. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "The complete primary structure of two distinct forms of human alpha 1 (IX) collagen chains."
      Muragaki Y., Kimura T., Ninomiya Y., Olsen B.R.
      Eur. J. Biochem. 192:703-708(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, VARIANTS LYS-870 AND LEU-882.
    2. "Human COL9A1 and COL9A2 genes. Two genes of 90 and 15 kb code for similar polypeptides of the same collagen molecule."
      Pihlajamaa T., Vuoristo M.M., Annunen S., Peraelae M., Prockop D.J., Ala-Kokko L.
      Matrix Biol. 17:237-241(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING, VARIANTS ARG-621; LYS-870 AND LEU-882.
    3. "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].
    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] (ISOFORMS 2 AND 3).
      Tissue: Brain and Mammary gland.
    5. "Collagen type IX from human cartilage: a structural profile of intermolecular cross-linking sites."
      Diab M., Wu J.J., Eyre D.R.
      Biochem. J. 314:327-332(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 405-417 (ISOFORMS 1/2).
    6. "Molecular cloning of rat and human type IX collagen cDNA and localization of the alpha 1(IX) gene on the human chromosome 6."
      Kimura T., Mattei M.-G., Stevens J.W., Goldring M.B., Ninomiya Y., Olsen B.R.
      Eur. J. Biochem. 179:71-78(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 580-820 AND 835-884, VARIANTS LYS-870 AND LEU-882.
    7. "The alpha 1 (IX) collagen gene gives rise to two different transcripts in both mouse embryonic and human fetal RNA."
      Muragaki Y., Nishimura I., Henney A., Ninomiya Y., Olsen B.R.
      Proc. Natl. Acad. Sci. U.S.A. 87:2400-2404(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
    8. "Crystal structure of the N-terminal NC4 domain of collagen IX, a zinc binding member of the laminin-neurexin-sex hormone binding globulin (LNS) domain family."
      Leppanen V.M., Tossavainen H., Permi P., Lehtio L., Ronnholm G., Goldman A., Kilpelainen I., Pihlajamaa T.
      J. Biol. Chem. 282:23219-23230(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 24-268, DISULFIDE BONDS, ZINC-BINDING SITES.
    9. Cited for: VARIANTS PRO-339 AND ARG-621, INVOLVEMENT IN EDM6.
    10. Cited for: INVOLVEMENT IN STL4.

    Entry informationi

    Entry nameiCO9A1_HUMAN
    AccessioniPrimary (citable) accession number: P20849
    Secondary accession number(s): Q13699
    , Q13700, Q5TF52, Q6P467, Q96BM8, Q99225, Q9H151, Q9H152, Q9Y6P2, Q9Y6P3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1991
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 169 of the entry and version 3 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, Direct protein sequencing, 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

    Dasty 3