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O15232

- MATN3_HUMAN

UniProt

O15232 - MATN3_HUMAN

Protein

Matrilin-3

Gene

MATN3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 2 (01 May 1999)
      Previous versions | rss
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    Functioni

    Major component of the extracellular matrix of cartilage and may play a role in the formation of extracellular filamentous networks.

    GO - Molecular functioni

    1. extracellular matrix structural constituent Source: ProtInc
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. extracellular matrix organization Source: Reactome
    2. skeletal system development Source: ProtInc

    Enzyme and pathway databases

    ReactomeiREACT_163906. ECM proteoglycans.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Matrilin-3
    Gene namesi
    Name:MATN3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:6909. MATN3.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. proteinaceous extracellular matrix Source: ProtInc

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Multiple epiphyseal dysplasia 5 (EDM5) [MIM:607078]: 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. Multiple epiphyseal dysplasia type 5 is relatively mild and clinically variable. It is primarily characterized by delayed and irregular ossification of the epiphyses and early-onset osteoarthritis.7 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti70 – 701R → H in EDM5. 1 Publication
    VAR_054807
    Natural varianti105 – 1051F → S in EDM5. 1 Publication
    VAR_020844
    Natural varianti120 – 1201T → M in EDM5; retained and accumulates within the cell. 3 Publications
    VAR_019882
    Natural varianti121 – 1211R → W in EDM5; retained and accumulates within the cell. 5 Publications
    VAR_013691
    Natural varianti128 – 1281A → P in EDM5; bilateral hereditary microepiphyseal dysplasia. 1 Publication
    VAR_019883
    Natural varianti134 – 1341E → K in EDM5; retained and accumulates within the cell. 1 Publication
    VAR_019884
    Natural varianti171 – 1766Missing in EDM5.
    VAR_066830
    Natural varianti173 – 1731A → D in EDM5. 1 Publication
    VAR_066831
    Natural varianti192 – 1921I → N in EDM5; retained and accumulates within the cell. 1 Publication
    VAR_019885
    Natural varianti194 – 1941V → D in EDM5; retained and accumulates within the cell. 1 Publication
    VAR_013692
    Natural varianti195 – 1951T → K in EDM5. 2 Publications
    VAR_054808
    Natural varianti209 – 2091R → P in EDM5. 1 Publication
    VAR_066832
    Natural varianti218 – 2181Y → N in EDM5. 2 Publications
    VAR_054809
    Natural varianti219 – 2191A → D in EDM5; retained and accumulates within the cell. 2 Publications
    Corresponds to variant rs28939677 [ dbSNP | Ensembl ].
    VAR_019886
    Natural varianti231 – 2311K → N in EDM5. 1 Publication
    VAR_066833
    Natural varianti245 – 2451V → M in EDM5. 1 Publication
    Corresponds to variant rs182164052 [ dbSNP | Ensembl ].
    VAR_066834
    Spondyloepimetaphyseal dysplasia MATN3-related (SEMD-MATN3) [MIM:608728]: A bone disease characterized by disproportionate early-onset dwarfism, bowing of the lower limbs, lumbar lordosis and normal hands. Skeletal abnormalities include short, wide and stocky long bones with severe epiphyseal and metaphyseal changes, hypoplastic iliac bones and flat, ovoid vertebral bodies.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti304 – 3041C → S in SEMD-MATN3. 1 Publication
    VAR_019888
    Osteoarthritis 2 (OS2) [MIM:140600]: A degenerative disease of the joints characterized by degradation of the hyaline articular cartilage and remodeling of the subchondral bone with sclerosis. Clinical symptoms include pain and joint stiffness often leading to significant disability and joint replacement. In the hand, osteoarthritis can develop in the distal interphalangeal and the first carpometacarpal (base of thumb) and proximal interphalangeal joints. Patients with osteoarthritis may have one, a few, or all of these sites affected.
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

    Keywords - Diseasei

    Disease mutation, Dwarfism

    Organism-specific databases

    MIMi140600. phenotype.
    607078. phenotype.
    608728. phenotype.
    Orphaneti93311. Multiple epiphyseal dysplasia type 5.
    156728. Spondyloepimetaphyseal dysplasia, matrilin-3 type.
    PharmGKBiPA30652.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2828Sequence AnalysisAdd
    BLAST
    Chaini29 – 486458Matrilin-3PRO_0000007657Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi268 ↔ 279PROSITE-ProRule annotation
    Disulfide bondi275 ↔ 289PROSITE-ProRule annotation
    Disulfide bondi291 ↔ 304PROSITE-ProRule annotation
    Disulfide bondi310 ↔ 321PROSITE-ProRule annotation
    Disulfide bondi317 ↔ 331PROSITE-ProRule annotation
    Disulfide bondi333 ↔ 346PROSITE-ProRule annotation
    Disulfide bondi352 ↔ 363PROSITE-ProRule annotation
    Disulfide bondi359 ↔ 373PROSITE-ProRule annotation
    Disulfide bondi375 ↔ 388PROSITE-ProRule annotation
    Disulfide bondi394 ↔ 405PROSITE-ProRule annotation
    Disulfide bondi401 ↔ 415PROSITE-ProRule annotation
    Disulfide bondi417 ↔ 430PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    MaxQBiO15232.
    PaxDbiO15232.
    PRIDEiO15232.

    PTM databases

    PhosphoSiteiO15232.

    Miscellaneous databases

    PMAP-CutDBO15232.

    Expressioni

    Tissue specificityi

    Expressed only in cartilaginous tissues, such as vertebrae, ribs and shoulders.

    Gene expression databases

    ArrayExpressiO15232.
    BgeeiO15232.
    CleanExiHS_MATN3.
    GenevestigatoriO15232.

    Interactioni

    Subunit structurei

    Can form homooligomers (monomers, dimers, trimers and tetramers) and heterooligomers with matrilin-1 By similarity. Interacts with COMP.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi110318. 3 interactions.
    IntActiO15232. 1 interaction.
    STRINGi9606.ENSP00000383894.

    Structurei

    3D structure databases

    ProteinModelPortaliO15232.
    SMRiO15232. Positions 82-245, 255-432.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini83 – 258176VWFAPROSITE-ProRule annotationAdd
    BLAST
    Domaini264 – 30542EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini306 – 34742EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini348 – 38942EGF-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini390 – 43142EGF-like 4PROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili456 – 48025By similarityAdd
    BLAST

    Sequence similaritiesi

    Contains 4 EGF-like domains.PROSITE-ProRule annotation
    Contains 1 VWFA domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, EGF-like domain, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG300624.
    HOGENOMiHOG000263415.
    HOVERGENiHBG056906.
    InParanoidiO15232.
    OMAiRFQETFC.
    OrthoDBiEOG7X9G6P.
    PhylomeDBiO15232.
    TreeFamiTF330078.

    Family and domain databases

    Gene3Di1.20.5.30. 1 hit.
    3.40.50.410. 1 hit.
    InterProiIPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR019466. Matrilin_coiled-coil_trimer.
    IPR002035. VWF_A.
    [Graphical view]
    PfamiPF10393. Matrilin_ccoil. 1 hit.
    PF00092. VWA. 1 hit.
    [Graphical view]
    SMARTiSM00181. EGF. 4 hits.
    SM00327. VWA. 1 hit.
    [Graphical view]
    SUPFAMiSSF53300. SSF53300. 1 hit.
    SSF57184. SSF57184. 1 hit.
    PROSITEiPS01186. EGF_2. 4 hits.
    PS50026. EGF_3. 4 hits.
    PS50234. VWFA. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O15232-1) [UniParc]FASTAAdd to Basket

    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

    MPRPAPARRL PGLLLLLWPL LLLPSAAPDP VARPGFRRLE TRGPGGSPGR    50
    RPSPAAPDGA PASGTSEPGR ARGAGVCKSR PLDLVFIIDS SRSVRPLEFT 100
    KVKTFVSRII DTLDIGPADT RVAVVNYAST VKIEFQLQAY TDKQSLKQAV 150
    GRITPLSTGT MSGLAIQTAM DEAFTVEAGA REPSSNIPKV AIIVTDGRPQ 200
    DQVNEVAARA QASGIELYAV GVDRADMASL KMMASEPLEE HVFYVETYGV 250
    IEKLSSRFQE TFCALDPCVL GTHQCQHVCI SDGEGKHHCE CSQGYTLNAD 300
    KKTCSALDRC ALNTHGCEHI CVNDRSGSYH CECYEGYTLN EDRKTCSAQD 350
    KCALGTHGCQ HICVNDRTGS HHCECYEGYT LNADKKTCSV RDKCALGSHG 400
    CQHICVSDGA ASYHCDCYPG YTLNEDKKTC SATEEARRLV STEDACGCEA 450
    TLAFQDKVSS YLQRLNTKLD DILEKLKINE YGQIHR 486
    Length:486
    Mass (Da):52,817
    Last modified:May 1, 1999 - v2
    Checksum:i688847BCC791B331
    GO
    Isoform 2 (identifier: O15232-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         266-307: Missing.

    Show »
    Length:444
    Mass (Da):48,317
    Checksum:i86E2198CA1627B15
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti11 – 111P → S.1 Publication
    VAR_019881
    Natural varianti70 – 701R → H in EDM5. 1 Publication
    VAR_054807
    Natural varianti105 – 1051F → S in EDM5. 1 Publication
    VAR_020844
    Natural varianti120 – 1201T → M in EDM5; retained and accumulates within the cell. 3 Publications
    VAR_019882
    Natural varianti121 – 1211R → W in EDM5; retained and accumulates within the cell. 5 Publications
    VAR_013691
    Natural varianti128 – 1281A → P in EDM5; bilateral hereditary microepiphyseal dysplasia. 1 Publication
    VAR_019883
    Natural varianti134 – 1341E → K in EDM5; retained and accumulates within the cell. 1 Publication
    VAR_019884
    Natural varianti171 – 1766Missing in EDM5.
    VAR_066830
    Natural varianti173 – 1731A → D in EDM5. 1 Publication
    VAR_066831
    Natural varianti192 – 1921I → N in EDM5; retained and accumulates within the cell. 1 Publication
    VAR_019885
    Natural varianti194 – 1941V → D in EDM5; retained and accumulates within the cell. 1 Publication
    VAR_013692
    Natural varianti195 – 1951T → K in EDM5. 2 Publications
    VAR_054808
    Natural varianti209 – 2091R → P in EDM5. 1 Publication
    VAR_066832
    Natural varianti218 – 2181Y → N in EDM5. 2 Publications
    VAR_054809
    Natural varianti219 – 2191A → D in EDM5; retained and accumulates within the cell. 2 Publications
    Corresponds to variant rs28939677 [ dbSNP | Ensembl ].
    VAR_019886
    Natural varianti231 – 2311K → N in EDM5. 1 Publication
    VAR_066833
    Natural varianti245 – 2451V → M in EDM5. 1 Publication
    Corresponds to variant rs182164052 [ dbSNP | Ensembl ].
    VAR_066834
    Natural varianti252 – 2521E → K Secreted normally as the wild-type. 3 Publications
    Corresponds to variant rs52826764 [ dbSNP | Ensembl ].
    VAR_019887
    Natural varianti303 – 3031T → M.3 Publications
    Corresponds to variant rs28939676 [ dbSNP | Ensembl ].
    VAR_015852
    Natural varianti304 – 3041C → S in SEMD-MATN3. 1 Publication
    VAR_019888

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei266 – 30742Missing in isoform 2. 1 PublicationVSP_054374Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ224741 mRNA. Translation: CAA12110.1.
    EU541440 mRNA. Translation: ACB29772.1.
    AC079145 Genomic DNA. Translation: AAX88937.1.
    CH471053 Genomic DNA. Translation: EAX00837.1.
    BC139907 mRNA. Translation: AAI39908.1.
    AJ001047 mRNA. Translation: CAA04501.1.
    Y13341 mRNA. Translation: CAA73785.1.
    CCDSiCCDS46226.1. [O15232-1]
    RefSeqiNP_002372.1. NM_002381.4. [O15232-1]
    UniGeneiHs.656199.

    Genome annotation databases

    EnsembliENST00000407540; ENSP00000383894; ENSG00000132031. [O15232-1]
    ENST00000421259; ENSP00000398753; ENSG00000132031. [O15232-2]
    GeneIDi4148.
    KEGGihsa:4148.
    UCSCiuc002rdl.3. human. [O15232-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ224741 mRNA. Translation: CAA12110.1 .
    EU541440 mRNA. Translation: ACB29772.1 .
    AC079145 Genomic DNA. Translation: AAX88937.1 .
    CH471053 Genomic DNA. Translation: EAX00837.1 .
    BC139907 mRNA. Translation: AAI39908.1 .
    AJ001047 mRNA. Translation: CAA04501.1 .
    Y13341 mRNA. Translation: CAA73785.1 .
    CCDSi CCDS46226.1. [O15232-1 ]
    RefSeqi NP_002372.1. NM_002381.4. [O15232-1 ]
    UniGenei Hs.656199.

    3D structure databases

    ProteinModelPortali O15232.
    SMRi O15232. Positions 82-245, 255-432.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110318. 3 interactions.
    IntActi O15232. 1 interaction.
    STRINGi 9606.ENSP00000383894.

    PTM databases

    PhosphoSitei O15232.

    Proteomic databases

    MaxQBi O15232.
    PaxDbi O15232.
    PRIDEi O15232.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000407540 ; ENSP00000383894 ; ENSG00000132031 . [O15232-1 ]
    ENST00000421259 ; ENSP00000398753 ; ENSG00000132031 . [O15232-2 ]
    GeneIDi 4148.
    KEGGi hsa:4148.
    UCSCi uc002rdl.3. human. [O15232-1 ]

    Organism-specific databases

    CTDi 4148.
    GeneCardsi GC02M020191.
    GeneReviewsi MATN3.
    HGNCi HGNC:6909. MATN3.
    MIMi 140600. phenotype.
    602109. gene.
    607078. phenotype.
    608728. phenotype.
    neXtProti NX_O15232.
    Orphaneti 93311. Multiple epiphyseal dysplasia type 5.
    156728. Spondyloepimetaphyseal dysplasia, matrilin-3 type.
    PharmGKBi PA30652.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG300624.
    HOGENOMi HOG000263415.
    HOVERGENi HBG056906.
    InParanoidi O15232.
    OMAi RFQETFC.
    OrthoDBi EOG7X9G6P.
    PhylomeDBi O15232.
    TreeFami TF330078.

    Enzyme and pathway databases

    Reactomei REACT_163906. ECM proteoglycans.

    Miscellaneous databases

    GeneWikii MATN3.
    GenomeRNAii 4148.
    NextBioi 16298.
    PMAP-CutDB O15232.
    PROi O15232.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O15232.
    Bgeei O15232.
    CleanExi HS_MATN3.
    Genevestigatori O15232.

    Family and domain databases

    Gene3Di 1.20.5.30. 1 hit.
    3.40.50.410. 1 hit.
    InterProi IPR000742. EG-like_dom.
    IPR013032. EGF-like_CS.
    IPR009030. Growth_fac_rcpt_N_dom.
    IPR019466. Matrilin_coiled-coil_trimer.
    IPR002035. VWF_A.
    [Graphical view ]
    Pfami PF10393. Matrilin_ccoil. 1 hit.
    PF00092. VWA. 1 hit.
    [Graphical view ]
    SMARTi SM00181. EGF. 4 hits.
    SM00327. VWA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53300. SSF53300. 1 hit.
    SSF57184. SSF57184. 1 hit.
    PROSITEi PS01186. EGF_2. 4 hits.
    PS50026. EGF_3. 4 hits.
    PS50234. VWFA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of human matrilin-3 (MATN3)."
      Belluoccio D., Schenker T., Baici A., Trueb B.
      Genomics 53:391-394(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
      Tissue: Cartilage.
    2. "Matrilin-3 increases not only upon osteoarthritis but also in cartilage-forming tumors and down-regulates SOX9 via EGF domain 1-dependent signaling."
      Vincourt J.-B., Takigawa M.
      Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    6. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 184-486 (ISOFORM 1).
    7. "Primary structure of matrilin-3, a new member of a family of extracellular matrix proteins related to cartilage matrix protein (matrilin-1) and von Willebrand factor."
      Wagener R., Kobbe B., Paulsson M.
      FEBS Lett. 413:129-134(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 177-486 (ISOFORM 1).
    8. "Interactions between the cartilage oligomeric matrix protein and matrilins. Implications for matrix assembly and the pathogenesis of chondrodysplasias."
      Mann H.H., Oezbek S., Engel J., Paulsson M., Wagener R.
      J. Biol. Chem. 279:25294-25298(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH COMP.
    9. "Mutations in the region encoding the von Willebrand factor A domain of matrilin-3 are associated with multiple epiphyseal dysplasia."
      Chapman K.L., Mortier G.R., Chapman K., Loughlin J., Grant M.E., Briggs M.D.
      Nat. Genet. 28:393-396(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS EDM5 TRP-121 AND ASP-194.
    10. Cited for: VARIANT MET-303, ASSOCIATION WITH OS2.
    11. "Familial multiple epiphyseal dysplasia due to a matrilin-3 mutation: further delineation of the phenotype including 40 years follow-up."
      Mostert A.K., Dijkstra P.F., Jansen B.R.H., van Horn J.R., de Graaf B., Heutink P., Lindhout D.
      Am. J. Med. Genet. A 120:490-497(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EDM5 PRO-128.
    12. "Novel and recurrent mutations clustered in the von Willebrand factor A domain of MATN3 in multiple epiphyseal dysplasia."
      Mabuchi A., Haga N., Maeda K., Nakashima E., Manabe N., Hiraoka H., Kitoh H., Kosaki R., Nishimura G., Ohashi H., Ikegawa S.
      Hum. Mutat. 24:439-440(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS EDM5 SER-105; MET-120 AND TRP-121, VARIANTS SER-11; LYS-252 AND MET-303.
    13. "Missense mutations in the beta strands of the single A-domain of matrilin-3 result in multiple epiphyseal dysplasia."
      Jackson G.C., Barker F.S., Jakkula E., Czarny-Ratajczak M., Maekitie O., Cole W.G., Wright M.J., Smithson S.F., Suri M., Rogala P., Mortier G.R., Baldock C., Wallace A., Elles R., Ala-Kokko L., Briggs M.D.
      J. Med. Genet. 41:52-59(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS EDM5 MET-120; TRP-121; LYS-134; ASN-192 AND ASP-219, VARIANTS LYS-252 AND MET-303.
    14. "Spondylo-epi-metaphyseal dysplasia (SEMD) matrilin 3 type: homozygote matrilin 3 mutation in a novel form of SEMD."
      Borochowitz Z.U., Scheffer D., Adir V., Dagoneau N., Munnich A., Cormier-Daire V.
      J. Med. Genet. 41:366-372(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SEMD-MATN3 SER-304.
    15. "Mutation in the von Willebrand factor-A domain is not a prerequisite for the MATN3 mutation in multiple epiphyseal dysplasia."
      Maeda K., Nakashima E., Horikoshi T., Mabuchi A., Ikegawa S.
      Am. J. Med. Genet. A 136:285-286(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT EDM5 HIS-70.
    16. "Multiple epiphyseal dysplasia mutations in MATN3 cause misfolding of the A-domain and prevent secretion of mutant matrilin-3."
      Cotterill S.L., Jackson G.C., Leighton M.P., Wagener R., Maekitie O., Cole W.G., Briggs M.D.
      Hum. Mutat. 26:557-565(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS EDM5 TRP-121; LYS-195 AND ASN-218, VARIANT LYS-252, CHARACTERIZATION OF VARIANTS MET-120; TRP-121; LYS-134; ASN-192; ASP-194 AND ASP-219, CHARACTERIZATION OF VARIANT LYS-252.
    17. "Pseudoachondroplasia and multiple epiphyseal dysplasia: A 7-year comprehensive analysis of the known disease genes identify novel and recurrent mutations and provides an accurate assessment of their relative contribution."
      Jackson G.C., Mittaz-Crettol L., Taylor J.A., Mortier G.R., Spranger J., Zabel B., Le Merrer M., Cormier-Daire V., Hall C.M., Offiah A., Wright M.J., Savarirayan R., Nishimura G., Ramsden S.C., Elles R., Bonafe L., Superti-Furga A., Unger S., Zankl A., Briggs M.D.
      Hum. Mutat. 33:144-157(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS EDM5 MET-120; TRP-121; 171-ASP--VAL-176 DEL; ASP-173; LYS-195; PRO-209; ASN-218; ASP-219; ASN-231 AND MET-245.

    Entry informationi

    Entry nameiMATN3_HUMAN
    AccessioniPrimary (citable) accession number: O15232
    Secondary accession number(s): B2CPU0, Q4ZG02
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2001
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 145 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: 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