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P50281

- MMP14_HUMAN

UniProt

P50281 - MMP14_HUMAN

Protein

Matrix metalloproteinase-14

Gene

MMP14

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 153 (01 Oct 2014)
      Sequence version 3 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    Seems to specifically activate progelatinase A. May thus trigger invasion by tumor cells by activating progelatinase A on the tumor cell surface. May be involved in actin cytoskeleton reorganization by cleaving PTK7. Acts as a positive regulator of cell growth and migration via activation of MMP15. Involved in the formation of the fibrovascular tissues in association with pro-MMP2.3 Publications

    Catalytic activityi

    Endopeptidase activity. Activates progelatinase A by cleavage of the propeptide at 37-Asn-|-Leu-38. Other bonds hydrolyzed include 35-Gly-|-Ile-36 in the propeptide of collagenase 3, and 341-Asn-|-Phe-342, 441-Asp-|-Leu-442 and 354-Gln-|-Thr-355 in the aggrecan interglobular domain.

    Cofactori

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi93 – 931Zinc; in inhibited formBy similarity
    Metal bindingi239 – 2391Zinc; catalytic
    Active sitei240 – 2401PROSITE-ProRule annotation
    Metal bindingi243 – 2431Zinc; catalytic
    Metal bindingi249 – 2491Zinc; catalytic

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. metalloendopeptidase activity Source: ProtInc
    3. peptidase activator activity Source: Ensembl
    4. protein binding Source: UniProtKB
    5. sequence-specific DNA binding transcription factor activity Source: Ensembl
    6. zinc ion binding Source: ProtInc

    GO - Biological processi

    1. angiogenesis Source: Ensembl
    2. astrocyte cell migration Source: Ensembl
    3. branching morphogenesis of an epithelial tube Source: Ensembl
    4. collagen catabolic process Source: Reactome
    5. endothelial cell proliferation Source: Ensembl
    6. extracellular matrix disassembly Source: Reactome
    7. extracellular matrix organization Source: Reactome
    8. lung development Source: Ensembl
    9. male gonad development Source: Ensembl
    10. negative regulation of focal adhesion assembly Source: Ensembl
    11. ossification Source: Ensembl
    12. ovarian follicle development Source: Ensembl
    13. positive regulation of cell growth Source: UniProtKB
    14. positive regulation of cell migration Source: UniProtKB
    15. proteolysis Source: ProtInc
    16. response to estrogen Source: Ensembl
    17. response to hypoxia Source: Ensembl
    18. response to mechanical stimulus Source: Ensembl
    19. response to oxidative stress Source: Ensembl
    20. tissue remodeling Source: Ensembl
    21. zymogen activation Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciMetaCyc:ENSG00000157227-MONOMER.
    BRENDAi3.4.24.7. 2681.
    ReactomeiREACT_118572. Degradation of the extracellular matrix.
    REACT_118682. Activation of Matrix Metalloproteinases.
    REACT_150401. Collagen degradation.

    Protein family/group databases

    MEROPSiM10.014.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Matrix metalloproteinase-14 (EC:3.4.24.80)
    Short name:
    MMP-14
    Alternative name(s):
    MMP-X1
    Membrane-type matrix metalloproteinase 1
    Short name:
    MT-MMP 1
    Short name:
    MTMMP1
    Membrane-type-1 matrix metalloproteinase
    Short name:
    MT1-MMP
    Short name:
    MT1MMP
    Gene namesi
    Name:MMP14
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:7160. MMP14.

    Subcellular locationi

    Membrane Curated; Single-pass type I membrane protein Curated. Melanosome. Cytoplasm
    Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Forms a complex with BST2 and localizes to the cytoplasm.

    GO - Cellular componenti

    1. extracellular matrix Source: InterPro
    2. Golgi lumen Source: Reactome
    3. integral component of plasma membrane Source: ProtInc
    4. melanosome Source: UniProtKB-SubCell
    5. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Winchester syndrome (WNCHRS) [MIM:277950]: A disease characterized by severe osteolysis in the hands and feet, generalized osteoporosis, bone thinning, and absence of subcutaneous nodules. Various additional features include coarse face, corneal opacities, gum hypertrophy, and EKG changes.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti17 – 171T → R in WNCHRS; results in increased MMP14 proteosomal degradation and reduced protein localization to cell membrane. 1 Publication
    VAR_070567

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi277950. phenotype.
    Orphaneti85196. Nodulosis-arthropathy-osteolysis syndrome.
    3460. Torg-Winchester syndrome.
    PharmGKBiPA30872.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Propeptidei21 – 11191Activation peptide1 PublicationPRO_0000028798Add
    BLAST
    Chaini112 – 582471Matrix metalloproteinase-14PRO_0000028799Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi319 ↔ 508By similarity

    Post-translational modificationi

    The precursor is cleaved by a furin endopeptidase.By similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Zymogen

    Proteomic databases

    MaxQBiP50281.
    PaxDbiP50281.
    PRIDEiP50281.

    PTM databases

    PhosphoSiteiP50281.

    Expressioni

    Tissue specificityi

    Expressed in stromal cells of colon, breast, and head and neck. Expressed in lung tumors.1 Publication

    Inductioni

    Up-regulated by NANOS1.1 Publication

    Gene expression databases

    ArrayExpressiP50281.
    BgeeiP50281.
    CleanExiHS_MMP14.
    GenevestigatoriP50281.

    Organism-specific databases

    HPAiCAB009918.

    Interactioni

    Subunit structurei

    Interacts (via C-terminal cytoplasmic tail) with BST2.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ADI1Q9BV574EBI-992788,EBI-992807
    BCAR1P569453EBI-992788,EBI-702093
    Gorasp2Q9R06414EBI-992788,EBI-4422912From a different organism.
    LIMK1P536674EBI-992788,EBI-444403
    TIMP2P160352EBI-992788,EBI-1033507

    Protein-protein interaction databases

    BioGridi110466. 9 interactions.
    DIPiDIP-35111N.
    IntActiP50281. 16 interactions.
    MINTiMINT-246780.
    STRINGi9606.ENSP00000308208.

    Structurei

    Secondary structure

    1
    582
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi120 – 1289
    Turni133 – 1353
    Helixi137 – 15418
    Beta strandi158 – 1614
    Helixi164 – 1685
    Beta strandi171 – 1733
    Beta strandi176 – 1827
    Beta strandi187 – 1904
    Beta strandi194 – 2029
    Turni208 – 2114
    Beta strandi213 – 2164
    Beta strandi230 – 2323
    Helixi233 – 24412
    Beta strandi258 – 2603
    Helixi273 – 28311
    Helixi318 – 3203
    Beta strandi324 – 3296
    Beta strandi332 – 3376
    Beta strandi340 – 3456
    Beta strandi354 – 3563
    Helixi357 – 3604
    Beta strandi370 – 3734
    Beta strandi379 – 3835
    Beta strandi386 – 3916
    Beta strandi400 – 4023
    Helixi403 – 4053
    Beta strandi416 – 4205
    Turni422 – 4243
    Beta strandi427 – 4315
    Beta strandi434 – 4396
    Turni440 – 4434
    Beta strandi450 – 4523
    Helixi453 – 4553
    Beta strandi464 – 4685
    Beta strandi472 – 4798
    Beta strandi482 – 4876
    Turni488 – 4914
    Helixi501 – 5044

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BQQX-ray2.75M114-287[»]
    1BUVX-ray2.75M114-287[»]
    3C7XX-ray1.70A316-511[»]
    3MA2X-ray2.05A/D112-292[»]
    ProteinModelPortaliP50281.
    SMRiP50281. Positions 65-511.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP50281.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini112 – 541430ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini563 – 58220CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei542 – 56221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati316 – 36449Hemopexin 1Add
    BLAST
    Repeati365 – 41046Hemopexin 2Add
    BLAST
    Repeati412 – 46049Hemopexin 3Add
    BLAST
    Repeati461 – 50848Hemopexin 4Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi91 – 988Cysteine switchBy similarity

    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, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG295915.
    HOGENOMiHOG000217928.
    HOVERGENiHBG052484.
    InParanoidiP50281.
    KOiK07763.
    OMAiWMGCPSG.
    OrthoDBiEOG7XPZ57.
    PhylomeDBiP50281.
    TreeFamiTF352396.

    Family and domain databases

    Gene3Di2.110.10.10. 1 hit.
    3.40.390.10. 1 hit.
    InterProiIPR000585. Hemopexin-like_dom.
    IPR018487. Hemopexin-like_repeat.
    IPR018486. Hemopexin_CS.
    IPR024079. MetalloPept_cat_dom.
    IPR028693. MMP14.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR021805. Pept_M10A_metallopeptidase_C.
    IPR016293. Pept_M10A_stromelysin-type.
    IPR021158. Pept_M10A_Zn_BS.
    IPR006026. Peptidase_Metallo.
    IPR002477. Peptidoglycan-bd-like.
    [Graphical view]
    PANTHERiPTHR10201:SF24. PTHR10201:SF24. 1 hit.
    PfamiPF11857. DUF3377. 1 hit.
    PF00045. Hemopexin. 4 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.
    PROSITEiPS00546. CYSTEINE_SWITCH. 1 hit.
    PS00024. HEMOPEXIN. 1 hit.
    PS51642. HEMOPEXIN_2. 4 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P50281-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSPAPRPPRC LLLPLLTLGT ALASLGSAQS SSFSPEAWLQ QYGYLPPGDL    50
    RTHTQRSPQS LSAAIAAMQK FYGLQVTGKA DADTMKAMRR PRCGVPDKFG 100
    AEIKANVRRK RYAIQGLKWQ HNEITFCIQN YTPKVGEYAT YEAIRKAFRV 150
    WESATPLRFR EVPYAYIREG HEKQADIMIF FAEGFHGDST PFDGEGGFLA 200
    HAYFPGPNIG GDTHFDSAEP WTVRNEDLNG NDIFLVAVHE LGHALGLEHS 250
    SDPSAIMAPF YQWMDTENFV LPDDDRRGIQ QLYGGESGFP TKMPPQPRTT 300
    SRPSVPDKPK NPTYGPNICD GNFDTVAMLR GEMFVFKERW FWRVRNNQVM 350
    DGYPMPIGQF WRGLPASINT AYERKDGKFV FFKGDKHWVF DEASLEPGYP 400
    KHIKELGRGL PTDKIDAALF WMPNGKTYFF RGNKYYRFNE ELRAVDSEYP 450
    KNIKVWEGIP ESPRGSFMGS DEVFTYFYKG NKYWKFNNQK LKVEPGYPKS 500
    ALRDWMGCPS GGRPDEGTEE ETEVIIIEVD EEGGGAVSAA AVVLPVLLLL 550
    LVLAVGLAVF FFRRHGTPRR LLYCQRSLLD KV 582
    Length:582
    Mass (Da):65,894
    Last modified:January 11, 2011 - v3
    Checksum:i3722DE286A4BBCDE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti338 – 3381E → K in BAA05519. (PubMed:8015608)Curated
    Sequence conflicti500 – 5001S → P in CAA62432. (PubMed:8706726)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti4 – 41A → T.1 Publication
    Corresponds to variant rs17882219 [ dbSNP | Ensembl ].
    VAR_021029
    Natural varianti6 – 61R → K.1 Publication
    Corresponds to variant rs17884647 [ dbSNP | Ensembl ].
    VAR_021030
    Natural varianti8 – 81P → S.7 Publications
    Corresponds to variant rs1042703 [ dbSNP | Ensembl ].
    VAR_021031
    Natural varianti17 – 171T → R in WNCHRS; results in increased MMP14 proteosomal degradation and reduced protein localization to cell membrane. 1 Publication
    VAR_070567
    Natural varianti233 – 2331I → V.1 Publication
    Corresponds to variant rs17884841 [ dbSNP | Ensembl ].
    VAR_021032
    Natural varianti273 – 2731D → N.1 Publication
    Corresponds to variant rs1042704 [ dbSNP | Ensembl ].
    VAR_021033
    Natural varianti302 – 3021R → W.1 Publication
    Corresponds to variant rs17884719 [ dbSNP | Ensembl ].
    VAR_021034
    Natural varianti355 – 3551M → I.1 Publication
    Corresponds to variant rs17880989 [ dbSNP | Ensembl ].
    VAR_021035
    Natural varianti431 – 4311R → H.
    Corresponds to variant rs3751489 [ dbSNP | Ensembl ].
    VAR_031267

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D26512 mRNA. Translation: BAA05519.1.
    X83535 mRNA. Translation: CAA58519.1.
    Z48481 mRNA. Translation: CAA88372.1.
    U41078 mRNA. Translation: AAA83770.1.
    X90925 mRNA. Translation: CAA62432.1.
    AK291325 mRNA. Translation: BAF84014.1.
    AY795074 Genomic DNA. Translation: AAV40837.1.
    AL135998 Genomic DNA. No translation available.
    BC064803 mRNA. Translation: AAH64803.1.
    CCDSiCCDS9577.1.
    PIRiI38028.
    RefSeqiNP_004986.1. NM_004995.3.
    UniGeneiHs.2399.

    Genome annotation databases

    EnsembliENST00000311852; ENSP00000308208; ENSG00000157227.
    GeneIDi4323.
    KEGGihsa:4323.
    UCSCiuc001whc.3. human.

    Polymorphism databases

    DMDMi317373419.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs
    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D26512 mRNA. Translation: BAA05519.1 .
    X83535 mRNA. Translation: CAA58519.1 .
    Z48481 mRNA. Translation: CAA88372.1 .
    U41078 mRNA. Translation: AAA83770.1 .
    X90925 mRNA. Translation: CAA62432.1 .
    AK291325 mRNA. Translation: BAF84014.1 .
    AY795074 Genomic DNA. Translation: AAV40837.1 .
    AL135998 Genomic DNA. No translation available.
    BC064803 mRNA. Translation: AAH64803.1 .
    CCDSi CCDS9577.1.
    PIRi I38028.
    RefSeqi NP_004986.1. NM_004995.3.
    UniGenei Hs.2399.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BQQ X-ray 2.75 M 114-287 [» ]
    1BUV X-ray 2.75 M 114-287 [» ]
    3C7X X-ray 1.70 A 316-511 [» ]
    3MA2 X-ray 2.05 A/D 112-292 [» ]
    ProteinModelPortali P50281.
    SMRi P50281. Positions 65-511.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110466. 9 interactions.
    DIPi DIP-35111N.
    IntActi P50281. 16 interactions.
    MINTi MINT-246780.
    STRINGi 9606.ENSP00000308208.

    Chemistry

    BindingDBi P50281.
    ChEMBLi CHEMBL3869.

    Protein family/group databases

    MEROPSi M10.014.

    PTM databases

    PhosphoSitei P50281.

    Polymorphism databases

    DMDMi 317373419.

    Proteomic databases

    MaxQBi P50281.
    PaxDbi P50281.
    PRIDEi P50281.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000311852 ; ENSP00000308208 ; ENSG00000157227 .
    GeneIDi 4323.
    KEGGi hsa:4323.
    UCSCi uc001whc.3. human.

    Organism-specific databases

    CTDi 4323.
    GeneCardsi GC14P023305.
    H-InvDB HIX0202102.
    HGNCi HGNC:7160. MMP14.
    HPAi CAB009918.
    MIMi 277950. phenotype.
    600754. gene.
    neXtProti NX_P50281.
    Orphaneti 85196. Nodulosis-arthropathy-osteolysis syndrome.
    3460. Torg-Winchester syndrome.
    PharmGKBi PA30872.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG295915.
    HOGENOMi HOG000217928.
    HOVERGENi HBG052484.
    InParanoidi P50281.
    KOi K07763.
    OMAi WMGCPSG.
    OrthoDBi EOG7XPZ57.
    PhylomeDBi P50281.
    TreeFami TF352396.

    Enzyme and pathway databases

    BioCyci MetaCyc:ENSG00000157227-MONOMER.
    BRENDAi 3.4.24.7. 2681.
    Reactomei REACT_118572. Degradation of the extracellular matrix.
    REACT_118682. Activation of Matrix Metalloproteinases.
    REACT_150401. Collagen degradation.

    Miscellaneous databases

    ChiTaRSi MMP14. human.
    EvolutionaryTracei P50281.
    GeneWikii MMP14.
    GenomeRNAii 4323.
    NextBioi 17009.
    PROi P50281.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P50281.
    Bgeei P50281.
    CleanExi HS_MMP14.
    Genevestigatori P50281.

    Family and domain databases

    Gene3Di 2.110.10.10. 1 hit.
    3.40.390.10. 1 hit.
    InterProi IPR000585. Hemopexin-like_dom.
    IPR018487. Hemopexin-like_repeat.
    IPR018486. Hemopexin_CS.
    IPR024079. MetalloPept_cat_dom.
    IPR028693. MMP14.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR021805. Pept_M10A_metallopeptidase_C.
    IPR016293. Pept_M10A_stromelysin-type.
    IPR021158. Pept_M10A_Zn_BS.
    IPR006026. Peptidase_Metallo.
    IPR002477. Peptidoglycan-bd-like.
    [Graphical view ]
    PANTHERi PTHR10201:SF24. PTHR10201:SF24. 1 hit.
    Pfami PF11857. DUF3377. 1 hit.
    PF00045. Hemopexin. 4 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 PS00546. CYSTEINE_SWITCH. 1 hit.
    PS00024. HEMOPEXIN. 1 hit.
    PS51642. HEMOPEXIN_2. 4 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A matrix metalloproteinase expressed on the surface of invasive tumour cells."
      Sato H., Takino T., Okada Y., Cao J., Shinagawa A., Yamamoto E., Seiki M.
      Nature 370:61-65(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-8.
      Tissue: Placenta.
    2. "Cloning of a human gene potentially encoding a novel matrix metalloproteinase having a C-terminal transmembrane domain."
      Takino T., Sato H., Yamamoto E., Seiki M.
      Gene 155:293-298(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-8.
      Tissue: Placenta.
    3. "Membrane-type matrix metalloproteinase (MT-MMP) gene is expressed in stromal cells of human colon, breast, and head and neck carcinomas."
      Okada A., Bellocq J.-P., Rouyer N., Chenard M.P., Rio M.C., Chambon P., Basset P.
      Proc. Natl. Acad. Sci. U.S.A. 92:2730-2734(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-8.
    4. "cDNA sequence and mRNA tissue distribution of a novel human matrix metalloproteinase with a potential transmembrane segment."
      Will H., Hinzmann B.
      Eur. J. Biochem. 231:602-608(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-8.
      Tissue: Lung.
    5. Luo G.-X., Reisfeld R.A., Strongin A.Y.
      Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    6. "Regulation of membrane-type matrix metalloproteinase-1 expression by growth factors and phorbol 12-myristate 13-acetate."
      Lohi J.L., Westermarck J., Kaehaeri V.M., Keski-Oja J.
      Eur. J. Biochem. 239:239-247(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    7. "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], VARIANT SER-8.
      Tissue: Tongue.
    8. NIEHS SNPs program
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-4; LYS-6; SER-8; VAL-233; ASN-273; TRP-302 AND ILE-355.
    9. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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], VARIANT SER-8.
      Tissue: Skin.
    11. "Activation of a recombinant membrane type 1-matrix metalloproteinase (MT1-MMP) by furin and its interaction with tissue inhibitor of metalloproteinases (TIMP)-2."
      Sato H., Kinoshita T., Takino T., Nakayama K., Seiki M.
      FEBS Lett. 393:101-104(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 112-116.
    12. "Production and activation of matrix metalloproteinase-2 in proliferative diabetic retinopathy."
      Noda K., Ishida S., Inoue M., Obata K., Oguchi Y., Okada Y., Ikeda E.
      Invest. Ophthalmol. Vis. Sci. 44:2163-2170(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN THE FORMATION OF THE FIBROVASCULAR TISSUES.
    13. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
      Tissue: Melanoma.
    14. "The E-cadherin-repressed hNanos1 gene induces tumor cell invasion by upregulating MT1-MMP expression."
      Bonnomet A., Polette M., Strumane K., Gilles C., Dalstein V., Kileztky C., Berx G., van Roy F., Birembaut P., Nawrocki-Raby B.
      Oncogene 27:3692-3699(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION, TISSUE SPECIFICITY.
    15. "The Wnt/planar cell polarity protein-tyrosine kinase-7 (PTK7) is a highly efficient proteolytic target of membrane type-1 matrix metalloproteinase: implications in cancer and embryogenesis."
      Golubkov V.S., Chekanov A.V., Cieplak P., Aleshin A.E., Chernov A.V., Zhu W., Radichev I.A., Zhang D., Dong P.D., Strongin A.Y.
      J. Biol. Chem. 285:35740-35749(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "BST-2 binding with cellular MT1-MMP blocks cell growth and migration via decreasing MMP2 activity."
      Gu G., Zhao D., Yin Z., Liu P.
      J. Cell. Biochem. 113:1013-1021(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH BST2.
    17. "Crystal structure of the complex formed by the membrane type 1-matrix metalloproteinase with the tissue inhibitor of metalloproteinases-2, the soluble progelatinase A receptor."
      Fernandez-Catalan C., Bode W., Huber R., Turk D., Calvete J.J., Lichte A., Tschesche H., Maskos K.
      EMBO J. 17:5238-5248(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 114-287 IN COMPLEX WITH TIMP2.
    18. "Mutation of membrane type-1 metalloproteinase, MT1-MMP, causes the multicentric osteolysis and arthritis disease Winchester syndrome."
      Evans B.R., Mosig R.A., Lobl M., Martignetti C.R., Camacho C., Grum-Tokars V., Glucksman M.J., Martignetti J.A.
      Am. J. Hum. Genet. 91:572-576(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT WNCHRS ARG-17, CHARACTERIZATION OF VARIANT WNCHRS ARG-17.

    Entry informationi

    Entry nameiMMP14_HUMAN
    AccessioniPrimary (citable) accession number: P50281
    Secondary accession number(s): A8K5L0, Q6GSF3, Q92678
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 153 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 14
      Human chromosome 14: 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. Peptidase families
      Classification of peptidase families and list of entries
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3