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)

Q99542

- MMP19_HUMAN

UniProt

Q99542 - MMP19_HUMAN

Protein

Matrix metalloproteinase-19

Gene

MMP19

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 154 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Endopeptidase that degrades various components of the extracellular matrix, such as aggrecan and cartilage oligomeric matrix protein (comp), during development, haemostasis and pathological conditions (arthritic disease). May also play a role in neovascularization or angiogenesis. Hydrolyzes collagen type IV, laminin, nidogen, nascin-C isoform, fibronectin, and type I gelatin.2 Publications

    Catalytic activityi

    Cleaves aggrecan at the 360-Ser-|-Phe-361 site.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity
    Calcium.By similarity

    Enzyme regulationi

    Strongly inhibited by TIMP-2, TIMP-3 and TIMP-4, while TIMP-1 is less efficient.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi85 – 851Zinc; in inhibited formBy similarity
    Metal bindingi212 – 2121Zinc; catalyticPROSITE-ProRule annotation
    Active sitei213 – 2131PROSITE-ProRule annotation
    Metal bindingi216 – 2161Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi222 – 2221Zinc; catalyticPROSITE-ProRule annotation

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. metalloendopeptidase activity Source: InterPro
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. cell differentiation Source: UniProtKB-KW
    3. collagen catabolic process Source: Reactome
    4. extracellular matrix disassembly Source: Reactome
    5. extracellular matrix organization Source: Reactome
    6. luteolysis Source: Ensembl
    7. ovarian follicle development Source: Ensembl
    8. ovulation from ovarian follicle Source: Ensembl
    9. proteolysis Source: UniProtKB
    10. response to cAMP Source: Ensembl
    11. response to hormone Source: Ensembl

    Keywords - Molecular functioni

    Developmental protein, Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Angiogenesis, Collagen degradation, Differentiation

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_118572. Degradation of the extracellular matrix.
    REACT_150401. Collagen degradation.

    Protein family/group databases

    MEROPSiM10.021.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Matrix metalloproteinase-19 (EC:3.4.24.-)
    Short name:
    MMP-19
    Alternative name(s):
    Matrix metalloproteinase RASI
    Matrix metalloproteinase-18
    Short name:
    MMP-18
    Gene namesi
    Name:MMP19
    Synonyms:MMP18, RASI
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:7165. MMP19.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    May play a role in pathological processes participating in rheumatoid arthritis (RA)-associated joint tissue destruction. Autoantigen anti-MMP19 are frequent in RA patients.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi88 – 881E → P: Reduced autolysis rate. 1 Publication
    Mutagenesisi90 – 901P → V: Reduced autolysis rate. 1 Publication

    Organism-specific databases

    PharmGKBiPA30876.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Propeptidei19 – 97791 PublicationPRO_0000028826Add
    BLAST
    Chaini98 – 508411Matrix metalloproteinase-19PRO_0000028827Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi289 ↔ 472By similarity
    Glycosylationi464 – 4641N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Activated by autolytic cleavage after Lys-97.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PaxDbiQ99542.
    PRIDEiQ99542.

    PTM databases

    PhosphoSiteiQ99542.

    Expressioni

    Tissue specificityi

    Expressed in mammary gland, placenta, lung, pancreas, ovary, small intestine, spleen, thymus, prostate, testis colon, heart and blood vessel walls. Not detected in brain and peripheral blood leukocytes. Also expressed in the synovial fluid of normal and rheumatoid patients.

    Gene expression databases

    ArrayExpressiQ99542.
    BgeeiQ99542.
    CleanExiHS_MMP19.
    GenevestigatoriQ99542.

    Organism-specific databases

    HPAiHPA012845.

    Interactioni

    Protein-protein interaction databases

    IntActiQ99542. 1 interaction.
    STRINGi9606.ENSP00000313437.

    Structurei

    3D structure databases

    ProteinModelPortaliQ99542.
    SMRiQ99542. Positions 38-456.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati286 – 33348Hemopexin 1Add
    BLAST
    Repeati334 – 38047Hemopexin 2Add
    BLAST
    Repeati381 – 42545Hemopexin 3Add
    BLAST
    Repeati426 – 47247Hemopexin 4Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi83 – 908Cysteine switchBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi265 – 2717Poly-Glu

    Domaini

    The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

    Sequence similaritiesi

    Belongs to the peptidase M10A family.Curated
    Contains 4 hemopexin repeats.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG295915.
    HOGENOMiHOG000217927.
    HOVERGENiHBG052484.
    InParanoidiQ99542.
    KOiK07998.
    OMAiWMHCHPQ.
    PhylomeDBiQ99542.
    TreeFamiTF315428.

    Family and domain databases

    Gene3Di1.10.101.10. 1 hit.
    2.110.10.10. 1 hit.
    3.40.390.10. 1 hit.
    InterProiIPR000585. Hemopexin-like_dom.
    IPR018487. Hemopexin-like_repeat.
    IPR024079. MetalloPept_cat_dom.
    IPR028724. MMP19.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR016293. Pept_M10A_stromelysin-type.
    IPR006026. Peptidase_Metallo.
    IPR002477. Peptidoglycan-bd-like.
    [Graphical view]
    PANTHERiPTHR10201:SF117. PTHR10201:SF117. 1 hit.
    PfamiPF00045. Hemopexin. 3 hits.
    PF00413. Peptidase_M10. 1 hit.
    PF01471. PG_binding_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001191. Peptidase_M10A_matrix. 1 hit.
    PRINTSiPR00138. MATRIXIN.
    SMARTiSM00120. HX. 4 hits.
    SM00235. ZnMc. 1 hit.
    [Graphical view]
    SUPFAMiSSF47090. SSF47090. 1 hit.
    SSF50923. SSF50923. 1 hit.
    PROSITEiPS51642. HEMOPEXIN_2. 4 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    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: Q99542-1) [UniParc]FASTAAdd to Basket

    Also known as: RASI-1, RASI-11

    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

    MNCQQLWLGF LLPMTVSGRV LGLAEVAPVD YLSQYGYLQK PLEGSNNFKP    50
    EDITEALRAF QEASELPVSG QLDDATRARM RQPRCGLEDP FNQKTLKYLL 100
    LGRWRKKHLT FRILNLPSTL PPHTARAALR QAFQDWSNVA PLTFQEVQAG 150
    AADIRLSFHG RQSSYCSNTF DGPGRVLAHA DIPELGSVHF DEDEFWTEGT 200
    YRGVNLRIIA AHEVGHALGL GHSRYSQALM APVYEGYRPH FKLHPDDVAG 250
    IQALYGKKSP VIRDEEEEET ELPTVPPVPT EPSPMPDPCS SELDAMMLGP 300
    RGKTYAFKGD YVWTVSDSGP GPLFRVSALW EGLPGNLDAA VYSPRTQWIH 350
    FFKGDKVWRY INFKMSPGFP KKLNRVEPNL DAALYWPLNQ KVFLFKGSGY 400
    WQWDELARTD FSSYPKPIKG LFTGVPNQPS AAMSWQDGRV YFFKGKVYWR 450
    LNQQLRVEKG YPRNISHNWM HCRPRTIDTT PSGGNTTPSG TGITLDTTLS 500
    ATETTFEY 508
    Length:508
    Mass (Da):57,357
    Last modified:May 1, 1997 - v1
    Checksum:iBA480549AA9A8972
    GO
    Isoform 2 (identifier: Q99542-3) [UniParc]FASTAAdd to Basket

    Also known as: RASI-9

    The sequence of this isoform differs from the canonical sequence as follows:
         1-286: Missing.
         287-298: DPCSSELDAMML → MGVTWDFSMSNG

    Show »
    Length:222
    Mass (Da):25,350
    Checksum:i594DBE2F520DC0FE
    GO
    Isoform 3 (identifier: Q99542-4) [UniParc]FASTAAdd to Basket

    Also known as: RASI-6

    The sequence of this isoform differs from the canonical sequence as follows:
         58-63: RAFQEA → SLRSAG
         64-508: Missing.

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Show »
    Length:63
    Mass (Da):6,931
    Checksum:iC134E217099633E8
    GO
    Isoform 4 (identifier: Q99542-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         174-255: Missing.
         300-387: PRGKTYAFKG...PNLDAALYWP → EAPPLQAVGR...LASNTMDSLL
         388-508: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:305
    Mass (Da):33,793
    Checksum:i70E8A1C240863A8E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti376 – 3761V → S in CAA69913. (PubMed:8920941)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti103 – 1031R → C.1 Publication
    Corresponds to variant rs17844794 [ dbSNP | Ensembl ].
    VAR_021036
    Natural varianti245 – 2451P → S.
    Corresponds to variant rs1056784 [ dbSNP | Ensembl ].
    VAR_054006
    Natural varianti488 – 4881P → T.1 Publication
    Corresponds to variant rs17118042 [ dbSNP | Ensembl ].
    VAR_021037
    Natural varianti491 – 4911T → M.1 Publication
    Corresponds to variant rs17844806 [ dbSNP | Ensembl ].
    VAR_021038

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 286286Missing in isoform 2. 1 PublicationVSP_005457Add
    BLAST
    Alternative sequencei58 – 636RAFQEA → SLRSAG in isoform 3. 1 PublicationVSP_041893
    Alternative sequencei64 – 508445Missing in isoform 3. 1 PublicationVSP_041894Add
    BLAST
    Alternative sequencei174 – 25582Missing in isoform 4. 1 PublicationVSP_054573Add
    BLAST
    Alternative sequencei287 – 29812DPCSS…DAMML → MGVTWDFSMSNG in isoform 2. 1 PublicationVSP_005458Add
    BLAST
    Alternative sequencei300 – 38788PRGKT…ALYWP → EAPPLQAVGRRWGQPADPEA WTNGSDMGLQHEQWRAPWED LCFQGGLCVDCIRFRTGPLV PSVCPLGGAPRKPGCCCLLA SNTMDSLL in isoform 4. 1 PublicationVSP_054574Add
    BLAST
    Alternative sequencei388 – 508121Missing in isoform 4. 1 PublicationVSP_054575Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y08622 mRNA. Translation: CAA69913.1.
    X92521 mRNA. Translation: CAA63299.1.
    U37791 mRNA. Translation: AAC51521.1.
    U38321 mRNA. Translation: AAB63008.1.
    U38431 mRNA. Translation: AAC99995.1. Sequence problems.
    U38322 mRNA. Translation: AAB63009.1.
    AK303202 mRNA. Translation: BAG64292.1.
    AY706993 Genomic DNA. Translation: AAT97983.1.
    AC023055 Genomic DNA. No translation available.
    BC050368 mRNA. Translation: AAH50368.1.
    CCDSiCCDS61146.1. [Q99542-5]
    CCDS8895.1. [Q99542-1]
    PIRiJC5082.
    RefSeqiNP_001259030.1. NM_001272101.1. [Q99542-5]
    NP_002420.1. NM_002429.5. [Q99542-1]
    UniGeneiHs.591033.

    Genome annotation databases

    EnsembliENST00000322569; ENSP00000313437; ENSG00000123342. [Q99542-1]
    ENST00000409200; ENSP00000386625; ENSG00000123342. [Q99542-5]
    ENST00000552872; ENSP00000446776; ENSG00000123342. [Q99542-4]
    GeneIDi4327.
    KEGGihsa:4327.
    UCSCiuc001sia.3. human. [Q99542-3]
    uc001sib.4. human. [Q99542-1]

    Polymorphism databases

    DMDMi12643345.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y08622 mRNA. Translation: CAA69913.1 .
    X92521 mRNA. Translation: CAA63299.1 .
    U37791 mRNA. Translation: AAC51521.1 .
    U38321 mRNA. Translation: AAB63008.1 .
    U38431 mRNA. Translation: AAC99995.1 . Sequence problems.
    U38322 mRNA. Translation: AAB63009.1 .
    AK303202 mRNA. Translation: BAG64292.1 .
    AY706993 Genomic DNA. Translation: AAT97983.1 .
    AC023055 Genomic DNA. No translation available.
    BC050368 mRNA. Translation: AAH50368.1 .
    CCDSi CCDS61146.1. [Q99542-5 ]
    CCDS8895.1. [Q99542-1 ]
    PIRi JC5082.
    RefSeqi NP_001259030.1. NM_001272101.1. [Q99542-5 ]
    NP_002420.1. NM_002429.5. [Q99542-1 ]
    UniGenei Hs.591033.

    3D structure databases

    ProteinModelPortali Q99542.
    SMRi Q99542. Positions 38-456.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q99542. 1 interaction.
    STRINGi 9606.ENSP00000313437.

    Chemistry

    BindingDBi Q99542.
    ChEMBLi CHEMBL1938214.

    Protein family/group databases

    MEROPSi M10.021.

    PTM databases

    PhosphoSitei Q99542.

    Polymorphism databases

    DMDMi 12643345.

    Proteomic databases

    PaxDbi Q99542.
    PRIDEi Q99542.

    Protocols and materials databases

    DNASUi 4327.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000322569 ; ENSP00000313437 ; ENSG00000123342 . [Q99542-1 ]
    ENST00000409200 ; ENSP00000386625 ; ENSG00000123342 . [Q99542-5 ]
    ENST00000552872 ; ENSP00000446776 ; ENSG00000123342 . [Q99542-4 ]
    GeneIDi 4327.
    KEGGi hsa:4327.
    UCSCi uc001sia.3. human. [Q99542-3 ]
    uc001sib.4. human. [Q99542-1 ]

    Organism-specific databases

    CTDi 4327.
    GeneCardsi GC12M056230.
    HGNCi HGNC:7165. MMP19.
    HPAi HPA012845.
    MIMi 601807. gene.
    neXtProti NX_Q99542.
    PharmGKBi PA30876.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG295915.
    HOGENOMi HOG000217927.
    HOVERGENi HBG052484.
    InParanoidi Q99542.
    KOi K07998.
    OMAi WMHCHPQ.
    PhylomeDBi Q99542.
    TreeFami TF315428.

    Enzyme and pathway databases

    Reactomei REACT_118572. Degradation of the extracellular matrix.
    REACT_150401. Collagen degradation.

    Miscellaneous databases

    GeneWikii MMP19.
    GenomeRNAii 4327.
    NextBioi 17029.
    PROi Q99542.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99542.
    Bgeei Q99542.
    CleanExi HS_MMP19.
    Genevestigatori Q99542.

    Family and domain databases

    Gene3Di 1.10.101.10. 1 hit.
    2.110.10.10. 1 hit.
    3.40.390.10. 1 hit.
    InterProi IPR000585. Hemopexin-like_dom.
    IPR018487. Hemopexin-like_repeat.
    IPR024079. MetalloPept_cat_dom.
    IPR028724. MMP19.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR016293. Pept_M10A_stromelysin-type.
    IPR006026. Peptidase_Metallo.
    IPR002477. Peptidoglycan-bd-like.
    [Graphical view ]
    PANTHERi PTHR10201:SF117. PTHR10201:SF117. 1 hit.
    Pfami PF00045. Hemopexin. 3 hits.
    PF00413. Peptidase_M10. 1 hit.
    PF01471. PG_binding_1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001191. Peptidase_M10A_matrix. 1 hit.
    PRINTSi PR00138. MATRIXIN.
    SMARTi SM00120. HX. 4 hits.
    SM00235. ZnMc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47090. SSF47090. 1 hit.
    SSF50923. SSF50923. 1 hit.
    PROSITEi PS51642. HEMOPEXIN_2. 4 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of MMP-18, a putative novel human matrix metalloproteinase."
      Cossins J., Dudgeon T.J., Catlin G., Gearing A.J.H., Clements J.M.
      Biochem. Biophys. Res. Commun. 228:494-498(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Mammary gland.
    2. "Identification and characterization of a novel human matrix metalloproteinase with unique structural characteristics, chromosomal location and tissue distribution."
      Pendas A.M., Knaeuper V.V., Puente X.S., Llano E., Mattei M.-G., Apte S., Murphy G., Lopez-Otin C.
      J. Biol. Chem. 272:4281-4286(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    3. "The matrix metalloproteinase RASI-1 is expressed in synovial blood vessels of a rheumatoid arthritis patient."
      Kolb C., Mauch S., Peter H.-H., Krawinkel U., Sedlacek R.
      Immunol. Lett. 57:83-88(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Rheumatoid arthritic synovial fluid.
    4. "Matrix metalloproteinase MMP-19 (RASI-1) is expressed on the surface of activated peripheral blood mononuclear cells and is detected as an autoantigen in rheumatoid arthritis."
      Sedlacek R., Mauch S., Kolb B., Schaetzlein C., Eibel H., Peter H.-H., Schmitt J., Krawinkel U.
      Immunobiology 198:408-423(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Rheumatoid arthritic synovial fluid.
    5. Mauch S., Sedlacek R., Krawinkel U., Schaetzlein C.
      Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
    6. "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] (ISOFORM 4).
      Tissue: Thymus.
    7. NIEHS SNPs program
      Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS CYS-103; THR-488 AND MET-491.
    8. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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).
    10. "Biochemical characterization of the catalytic domain of human matrix metalloproteinase 19. Evidence for a role as a potent basement membrane degrading enzyme."
      Stracke J.O., Hutton M., Stewart M., Pendas A.M., Smith B., Lopez-Otin C., Murphy G., Knaeuper V.
      J. Biol. Chem. 275:14809-14816(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, MUTAGENESIS.
    11. "Matrix metalloproteinases 19 and 20 cleave aggrecan and cartilage oligomeric matrix protein (COMP)."
      Stracke J.O., Fosang A.J., Last K., Mercuri F.A., Pendas A.M., Llano E., Perris R., Di Cesare P.E., Murphy G., Knaeuper V.
      FEBS Lett. 478:52-56(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.

    Entry informationi

    Entry nameiMMP19_HUMAN
    AccessioniPrimary (citable) accession number: Q99542
    Secondary accession number(s): B4E030
    , O15278, O95606, Q99580
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2001
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 154 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: 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. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3