Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q16610

- ECM1_HUMAN

UniProt

Q16610 - ECM1_HUMAN

Protein

Extracellular matrix protein 1

Gene

ECM1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (07 Jun 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Involved in endochondral bone formation as negative regulator of bone mineralization. Stimulates the proliferation of endothelial cells and promotes angiogenesis. Inhibits MMP9 proteolytic activity.3 Publications

    GO - Molecular functioni

    1. enzyme binding Source: UniProtKB
    2. laminin binding Source: UniProtKB
    3. protease binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein C-terminus binding Source: UniProtKB
    6. signal transducer activity Source: UniProtKB

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. biomineral tissue development Source: UniProtKB-KW
    3. inflammatory response Source: Ensembl
    4. negative regulation of bone mineralization Source: UniProtKB
    5. negative regulation of cytokine-mediated signaling pathway Source: Ensembl
    6. negative regulation of peptidase activity Source: UniProtKB
    7. ossification Source: UniProtKB-KW
    8. positive regulation of angiogenesis Source: UniProtKB
    9. positive regulation of endothelial cell proliferation Source: UniProtKB
    10. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    11. regulation of T cell migration Source: Ensembl
    12. regulation of transcription from RNA polymerase II promoter Source: Ensembl
    13. regulation of type 2 immune response Source: Ensembl
    14. signal transduction Source: GOC

    Keywords - Biological processi

    Angiogenesis, Biomineralization, Mineral balance, Osteogenesis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Extracellular matrix protein 1
    Alternative name(s):
    Secretory component p85
    Gene namesi
    Name:ECM1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:3153. ECM1.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular matrix Source: UniProtKB
    2. extracellular space Source: Ensembl
    3. extracellular vesicular exosome Source: UniProt
    4. proteinaceous extracellular matrix Source: UniProtKB

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Lipoid proteinosis (LiP) [MIM:247100]: Rare autosomal recessive disorder characterized by generalized thickening of skin, mucosae and certain viscera. Classical features include beaded eyelid papules and laryngeal infiltration leading to hoarseness. Histologically, there is widespread deposition of hyaline material and disruption/reduplication of basement membrane.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti167 – 1671F → I in LiP. 1 Publication
    VAR_018691

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi247100. phenotype.
    Orphaneti530. Lipoid proteinosis.
    PharmGKBiPA27598.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919By similarityAdd
    BLAST
    Chaini20 – 540521Extracellular matrix protein 1PRO_0000021146Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi354 – 3541N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi444 – 4441N-linked (GlcNAc...) (complex)2 Publications
    Glycosylationi530 – 5301N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiQ16610.
    PaxDbiQ16610.
    PRIDEiQ16610.

    PTM databases

    PhosphoSiteiQ16610.

    Expressioni

    Tissue specificityi

    Expressed in breast cancer tissues. Little or no expression observed in normal breast tissues. Expressed in skin; wide expression is observed throughout the dermis with minimal expression in the epidermis.2 Publications

    Gene expression databases

    ArrayExpressiQ16610.
    BgeeiQ16610.
    CleanExiHS_ECM1.
    GenevestigatoriQ16610.

    Organism-specific databases

    HPAiHPA027241.

    Interactioni

    Subunit structurei

    Interacts (via C-terminus) with HSPG2 (via C-terminus). Interacts with EFEMP1/FBLN3 and LAMB3. Interacts with MMP9.3 Publications

    Protein-protein interaction databases

    BioGridi108222. 8 interactions.
    IntActiQ16610. 10 interactions.
    MINTiMINT-2858262.

    Structurei

    3D structure databases

    ProteinModelPortaliQ16610.
    SMRiQ16610. Positions 194-279, 334-361, 442-500.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati150 – 2791301Add
    BLAST
    Repeati283 – 4051232Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni150 – 4052562 X approximate repeatsAdd
    BLAST

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG45869.
    HOVERGENiHBG005561.
    OMAiCCHYPPS.
    OrthoDBiEOG7KWSHX.
    PhylomeDBiQ16610.
    TreeFamiTF330786.

    Family and domain databases

    InterProiIPR008605. ECM1.
    IPR020858. Serum_albumin-like.
    [Graphical view]
    PfamiPF05782. ECM1. 1 hit.
    [Graphical view]
    SUPFAMiSSF48552. SSF48552. 2 hits.

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q16610-1) [UniParc]FASTAAdd to Basket

    Also known as: 1a

    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

    MGTTARAALV LTYLAVASAA SEGGFTATGQ RQLRPEHFQE VGYAAPPSPP    50
    LSRSLPMDHP DSSQHGPPFE GQSQVQPPPS QEATPLQQEK LLPAQLPAEK 100
    EVGPPLPQEA VPLQKELPSL QHPNEQKEGT PAPFGDQSHP EPESWNAAQH 150
    CQQDRSQGGW GHRLDGFPPG RPSPDNLNQI CLPNRQHVVY GPWNLPQSSY 200
    SHLTRQGETL NFLEIGYSRC CHCRSHTNRL ECAKLVWEEA MSRFCEAEFS 250
    VKTRPHWCCT RQGEARFSCF QEEAPQPHYQ LRACPSHQPD ISSGLELPFP 300
    PGVPTLDNIK NICHLRRFRS VPRNLPATDP LQRELLALIQ LEREFQRCCR 350
    QGNNHTCTWK AWEDTLDKYC DREYAVKTHH HLCCRHPPSP TRDECFARRA 400
    PYPNYDRDIL TIDIGRVTPN LMGHLCGNQR VLTKHKHIPG LIHNMTARCC 450
    DLPFPEQACC AEEEKLTFIN DLCGPRRNIW RDPALCCYLS PGDEQVNCFN 500
    INYLRNVALV SGDTENAKGQ GEQGSTGGTN ISSTSEPKEE 540
    Length:540
    Mass (Da):60,674
    Last modified:June 7, 2004 - v2
    Checksum:iEA575895CDE068BE
    GO
    Isoform 2 (identifier: Q16610-2) [UniParc]FASTAAdd to Basket

    Also known as: 1b

    The sequence of this isoform differs from the canonical sequence as follows:
         237-361: Missing.

    Show »
    Length:415
    Mass (Da):46,099
    Checksum:iE6878AE9DEF1D5AC
    GO
    Isoform 3 (identifier: Q16610-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-71: Missing.
         72-81: QSQVQPPPSQ → MALPLRDRVK
         237-241: WEEAM → VRLGS
         242-540: Missing.

    Show »
    Length:170
    Mass (Da):19,069
    Checksum:i4C3B05692F1D1C8C
    GO
    Isoform 4 (identifier: Q16610-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         74-74: Q → GKEGRGPRPHSQPWLGERVGCSHIPPSI

    Note: May be due to intron retention.

    Show »
    Length:567
    Mass (Da):63,563
    Checksum:iFBCFB0E51CE13735
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti78 – 847Missing in BAG63622. (PubMed:14702039)Curated
    Sequence conflicti520 – 5201Q → R in BAF85124. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti130 – 1301T → M.3 Publications
    Corresponds to variant rs3737240 [ dbSNP | Ensembl ].
    VAR_018690
    Natural varianti167 – 1671F → I in LiP. 1 Publication
    VAR_018691
    Natural varianti415 – 4151G → S.4 Publications
    Corresponds to variant rs13294 [ dbSNP | Ensembl ].
    VAR_014761
    Natural varianti528 – 5281G → R.
    Corresponds to variant rs1050901 [ dbSNP | Ensembl ].
    VAR_014762
    Natural varianti535 – 5351S → F.
    Corresponds to variant rs1050904 [ dbSNP | Ensembl ].
    VAR_014763

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7171Missing in isoform 3. 1 PublicationVSP_036411Add
    BLAST
    Alternative sequencei72 – 8110QSQVQPPPSQ → MALPLRDRVK in isoform 3. 1 PublicationVSP_036412
    Alternative sequencei74 – 741Q → GKEGRGPRPHSQPWLGERVG CSHIPPSI in isoform 4. 1 PublicationVSP_036413
    Alternative sequencei237 – 361125Missing in isoform 2. 1 PublicationVSP_036414Add
    BLAST
    Alternative sequencei237 – 2415WEEAM → VRLGS in isoform 3. 1 PublicationVSP_036415
    Alternative sequencei242 – 540299Missing in isoform 3. 1 PublicationVSP_036416Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U68186 mRNA. Translation: AAB88081.1.
    U68187 mRNA. Translation: AAB88082.1.
    U65932 mRNA. Translation: AAB05933.1.
    U65938
    , U65933, U65934, U65935, U65936, U65937 Genomic DNA. Translation: AAB05934.1.
    AK097046 mRNA. Translation: BAG53412.1.
    AK292435 mRNA. Translation: BAF85124.1.
    AK301369 mRNA. Translation: BAG62911.1.
    AK302279 mRNA. Translation: BAG63622.1.
    AL356356 Genomic DNA. Translation: CAI15491.1.
    AL356356 Genomic DNA. Translation: CAI15492.1.
    AL356356 Genomic DNA. Translation: CAI15493.1.
    CH471121 Genomic DNA. Translation: EAW53544.1.
    CH471121 Genomic DNA. Translation: EAW53545.1.
    CH471121 Genomic DNA. Translation: EAW53546.1.
    BC023505 mRNA. Translation: AAH23505.1.
    CCDSiCCDS55632.1. [Q16610-4]
    CCDS953.1. [Q16610-1]
    CCDS954.1. [Q16610-2]
    RefSeqiNP_001189787.1. NM_001202858.1. [Q16610-4]
    NP_004416.2. NM_004425.3. [Q16610-1]
    NP_073155.2. NM_022664.2. [Q16610-2]
    UniGeneiHs.81071.

    Genome annotation databases

    EnsembliENST00000346569; ENSP00000271630; ENSG00000143369. [Q16610-2]
    ENST00000369047; ENSP00000358043; ENSG00000143369. [Q16610-1]
    ENST00000369049; ENSP00000358045; ENSG00000143369. [Q16610-4]
    GeneIDi1893.
    KEGGihsa:1893.
    UCSCiuc001eus.3. human. [Q16610-1]
    uc001eut.3. human. [Q16610-2]
    uc001euv.3. human. [Q16610-4]
    uc010pce.2. human. [Q16610-3]

    Polymorphism databases

    DMDMi48429255.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U68186 mRNA. Translation: AAB88081.1 .
    U68187 mRNA. Translation: AAB88082.1 .
    U65932 mRNA. Translation: AAB05933.1 .
    U65938
    , U65933 , U65934 , U65935 , U65936 , U65937 Genomic DNA. Translation: AAB05934.1 .
    AK097046 mRNA. Translation: BAG53412.1 .
    AK292435 mRNA. Translation: BAF85124.1 .
    AK301369 mRNA. Translation: BAG62911.1 .
    AK302279 mRNA. Translation: BAG63622.1 .
    AL356356 Genomic DNA. Translation: CAI15491.1 .
    AL356356 Genomic DNA. Translation: CAI15492.1 .
    AL356356 Genomic DNA. Translation: CAI15493.1 .
    CH471121 Genomic DNA. Translation: EAW53544.1 .
    CH471121 Genomic DNA. Translation: EAW53545.1 .
    CH471121 Genomic DNA. Translation: EAW53546.1 .
    BC023505 mRNA. Translation: AAH23505.1 .
    CCDSi CCDS55632.1. [Q16610-4 ]
    CCDS953.1. [Q16610-1 ]
    CCDS954.1. [Q16610-2 ]
    RefSeqi NP_001189787.1. NM_001202858.1. [Q16610-4 ]
    NP_004416.2. NM_004425.3. [Q16610-1 ]
    NP_073155.2. NM_022664.2. [Q16610-2 ]
    UniGenei Hs.81071.

    3D structure databases

    ProteinModelPortali Q16610.
    SMRi Q16610. Positions 194-279, 334-361, 442-500.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108222. 8 interactions.
    IntActi Q16610. 10 interactions.
    MINTi MINT-2858262.

    PTM databases

    PhosphoSitei Q16610.

    Polymorphism databases

    DMDMi 48429255.

    Proteomic databases

    MaxQBi Q16610.
    PaxDbi Q16610.
    PRIDEi Q16610.

    Protocols and materials databases

    DNASUi 1893.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000346569 ; ENSP00000271630 ; ENSG00000143369 . [Q16610-2 ]
    ENST00000369047 ; ENSP00000358043 ; ENSG00000143369 . [Q16610-1 ]
    ENST00000369049 ; ENSP00000358045 ; ENSG00000143369 . [Q16610-4 ]
    GeneIDi 1893.
    KEGGi hsa:1893.
    UCSCi uc001eus.3. human. [Q16610-1 ]
    uc001eut.3. human. [Q16610-2 ]
    uc001euv.3. human. [Q16610-4 ]
    uc010pce.2. human. [Q16610-3 ]

    Organism-specific databases

    CTDi 1893.
    GeneCardsi GC01P150480.
    HGNCi HGNC:3153. ECM1.
    HPAi HPA027241.
    MIMi 247100. phenotype.
    602201. gene.
    neXtProti NX_Q16610.
    Orphaneti 530. Lipoid proteinosis.
    PharmGKBi PA27598.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG45869.
    HOVERGENi HBG005561.
    OMAi CCHYPPS.
    OrthoDBi EOG7KWSHX.
    PhylomeDBi Q16610.
    TreeFami TF330786.

    Miscellaneous databases

    ChiTaRSi ECM1. human.
    GeneWikii ECM1.
    GenomeRNAii 1893.
    NextBioi 7719.
    PROi Q16610.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q16610.
    Bgeei Q16610.
    CleanExi HS_ECM1.
    Genevestigatori Q16610.

    Family and domain databases

    InterProi IPR008605. ECM1.
    IPR020858. Serum_albumin-like.
    [Graphical view ]
    Pfami PF05782. ECM1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48552. SSF48552. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "The human extracellular matrix gene 1 (ECM1): genomic structure, cDNA cloning, expression pattern, and chromosomal localization."
      Smits P., Ni J., Feng P., Wauters J., van Hul W., Boutaibi M.E., Dillon P.J., Merregaert J.
      Genomics 45:487-495(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), VARIANT SER-415.
    2. "Characterization of the human extracellular matrix protein 1 gene on chromosome 1q21."
      Johnson M.R., Wilkin D.J., Vos H.L., Ortiz de Luna R.I., Dehejia A.M., Polymeropoulos M.H., Francomano C.A.
      Matrix Biol. 16:289-292(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4), VARIANTS MET-130 AND SER-415.
      Tissue: Synovial cell and Testis.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [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] (ISOFORM 1), VARIANTS MET-130 AND SER-415.
      Tissue: Skin.
    7. "Recombinant human extracellular matrix protein 1 inhibits alkaline phosphatase activity and mineralization of mouse embryonic metatarsals in vitro."
      Deckers M.M.L., Smits P., Karperien M., Ni J., Tylzanowski P., Feng P., Parmelee D., Zhang J., Bouffard E., Gentz R., Loewik C.W.G.M., Merregaert J.
      Bone 28:14-20(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN BONE FORMATION.
    8. "Extracellular matrix protein 1 (ECM1) has angiogenic properties and is expressed by breast tumor cells."
      Han Z., Ni J., Smits P., Underhill C.B., Xie B., Chen Y., Liu N., Tylzanowski P., Parmelee D., Feng P., Ding I., Gao F., Gentz R., Huylebroeck D., Merregaert J., Zhang L.
      FASEB J. 15:988-994(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ANGIOGENESIS, TISSUE SPECIFICITY.
    9. Cited for: INVOLVEMENT IN LIPOID PROTEINOSIS.
    10. "Perlecan protein core interacts with extracellular matrix protein 1 (ECM1), a glycoprotein involved in bone formation and angiogenesis."
      Mongiat M., Fu J., Oldershaw R., Greenhalgh R., Gown A.M., Iozzo R.V.
      J. Biol. Chem. 278:17491-17499(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HSPG2, TISSUE SPECIFICITY.
    11. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-444.
      Tissue: Plasma.
    12. "Extracellular matrix protein 1 inhibits the activity of matrix metalloproteinase 9 through high-affinity protein/protein interactions."
      Fujimoto N., Terlizzi J., Aho S., Brittingham R., Fertala A., Oyama N., McGrath J.A., Uitto J.
      Exp. Dermatol. 15:300-307(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MMP9, FUNCTION.
    13. "ECM1 interacts with fibulin-3 and the beta 3 chain of laminin 332 through its serum albumin subdomain-like 2 domain."
      Sercu S., Lambeir A.M., Steenackers E., El Ghalbzouri A., Geentjens K., Sasaki T., Oyama N., Merregaert J.
      Matrix Biol. 28:160-169(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EFEMP1 AND LAMB3.
    14. Cited for: GLYCOSYLATION AT ASN-444.
    15. Cited for: VARIANT LIP ILE-167, VARIANTS MET-130 AND SER-415.

    Entry informationi

    Entry nameiECM1_HUMAN
    AccessioniPrimary (citable) accession number: Q16610
    Secondary accession number(s): A8K8S0
    , B4DW49, B4DY60, O43266, Q5T5G4, Q5T5G5, Q5T5G6, Q8IZ60
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: June 7, 2004
    Last modified: October 1, 2014
    This is version 124 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 1
      Human chromosome 1: 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

    External Data

    Dasty 3