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P51512

- MMP16_HUMAN

UniProt

P51512 - MMP16_HUMAN

Protein

Matrix metalloproteinase-16

Gene

MMP16

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 2 (15 Jul 1998)
      Previous versions | rss
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    Functioni

    Endopeptidase that degrades various components of the extracellular matrix, such as collagen type III and fibronectin. Activates progelatinase A. Involved in the matrix remodeling of blood vessels. Isoform short cleaves fibronectin and also collagen type III, but at lower rate. It has no effect on type I, II, IV and V collagen. However, upon interaction with CSPG4, it may be involved in degradation and invasion of type I collagen by melanoma cells.1 Publication

    Cofactori

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

    Enzyme regulationi

    TIMP-2 shows little inhibitory activity compared to TIMP-1. TIMP-1 seems to have less binding affinity than TIMP-2 for the short isoform.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi101 – 1011Zinc 1; in inhibited formBy similarity
    Metal bindingi183 – 1831Calcium 1; via carbonyl oxygen
    Metal bindingi193 – 1931Zinc 1
    Metal bindingi195 – 1951Zinc 1
    Metal bindingi200 – 2001Calcium 2
    Metal bindingi201 – 2011Calcium 2; via carbonyl oxygen
    Metal bindingi203 – 2031Calcium 2; via carbonyl oxygen
    Metal bindingi205 – 2051Calcium 2; via carbonyl oxygen
    Metal bindingi215 – 2151Calcium 1; via carbonyl oxygen
    Metal bindingi217 – 2171Calcium 1; via carbonyl oxygen
    Metal bindingi219 – 2191Calcium 1
    Metal bindingi223 – 2231Calcium 2
    Metal bindingi226 – 2261Calcium 2
    Metal bindingi246 – 2461Zinc 2; catalytic
    Active sitei247 – 2471
    Metal bindingi250 – 2501Zinc 2; catalytic
    Metal bindingi256 – 2561Zinc 2; catalytic

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. enzyme activator activity Source: ProtInc
    3. metalloendopeptidase activity Source: ProtInc
    4. zinc ion binding Source: ProtInc

    GO - Biological processi

    1. collagen catabolic process Source: UniProtKB-KW
    2. extracellular matrix disassembly Source: Reactome
    3. extracellular matrix organization Source: Reactome
    4. positive regulation of catalytic activity Source: GOC

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Collagen degradation

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_118682. Activation of Matrix Metalloproteinases.

    Protein family/group databases

    MEROPSiM10.016.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Matrix metalloproteinase-16 (EC:3.4.24.-)
    Short name:
    MMP-16
    Alternative name(s):
    MMP-X2
    Membrane-type matrix metalloproteinase 3
    Short name:
    MT-MMP 3
    Short name:
    MTMMP3
    Membrane-type-3 matrix metalloproteinase
    Short name:
    MT3-MMP
    Short name:
    MT3MMP
    Gene namesi
    Name:MMP16
    Synonyms:MMPX2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:7162. MMP16.

    Subcellular locationi

    Isoform Long : Cell membrane Curated; Single-pass type I membrane protein Curated; Extracellular side Curated
    Note: Localized at the cell surface of melanoma cells.
    Isoform Short : Secretedextracellular spaceextracellular matrix. Cell surface
    Note: Localized at the cell surface of melanoma cells.

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cell membrane, Extracellular matrix, Membrane, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30874.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3131Sequence AnalysisAdd
    BLAST
    Propeptidei32 – 11988By similarityPRO_0000028812Add
    BLAST
    Chaini120 – 607488Matrix metalloproteinase-16PRO_0000028813Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi83 – 831N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi343 ↔ 532By similarity

    Post-translational modificationi

    The precursor is cleaved by a furin endopeptidase.By similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PaxDbiP51512.
    PRIDEiP51512.

    PTM databases

    PhosphoSiteiP51512.

    Miscellaneous databases

    PMAP-CutDBP51512.

    Expressioni

    Tissue specificityi

    Expressed in heart, brain, placenta, ovary and small intestine. Isoform Short is found in the ovary.

    Developmental stagei

    Expressed in tissues undergoing reconstruction. Present in fetal tissues, especially in brain. Expression seems to decline with advanced development.

    Gene expression databases

    ArrayExpressiP51512.
    BgeeiP51512.
    CleanExiHS_MMP16.
    GenevestigatoriP51512.

    Organism-specific databases

    HPAiHPA023693.

    Interactioni

    Subunit structurei

    Interacts with CSPG4 through CSPG4 chondroitin sulfate glycosaminoglycan.2 Publications

    Protein-protein interaction databases

    IntActiP51512. 1 interaction.
    MINTiMINT-4722491.
    STRINGi9606.ENSP00000286614.

    Structurei

    Secondary structure

    1
    607
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi128 – 1369
    Turni141 – 1433
    Helixi145 – 16016
    Beta strandi166 – 1694
    Beta strandi177 – 1793
    Beta strandi183 – 1919
    Beta strandi194 – 1963
    Beta strandi201 – 2044
    Beta strandi207 – 2093
    Turni215 – 2184
    Beta strandi220 – 2234
    Beta strandi228 – 2314
    Beta strandi234 – 2396
    Helixi240 – 25112
    Beta strandi265 – 2673
    Helixi280 – 29011

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1RM8X-ray1.80A124-292[»]
    ProteinModelPortaliP51512.
    SMRiP51512. Positions 69-561.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP51512.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini120 – 564445ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini586 – 60722CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei565 – 58521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati340 – 38849Hemopexin 1Add
    BLAST
    Repeati389 – 43446Hemopexin 2Add
    BLAST
    Repeati436 – 48449Hemopexin 3Add
    BLAST
    Repeati485 – 53248Hemopexin 4Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi99 – 1068Cysteine 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.
    InParanoidiP51512.
    KOiK07996.
    OMAiVPPHRSV.
    OrthoDBiEOG7XPZ57.
    PhylomeDBiP51512.
    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.
    IPR028697. MMP16.
    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:SF26. PTHR10201:SF26. 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]

    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 Long (identifier: P51512-1) [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

    MILLTFSTGR RLDFVHHSGV FFLQTLLWIL CATVCGTEQY FNVEVWLQKY    50
    GYLPPTDPRM SVLRSAETMQ SALAAMQQFY GINMTGKVDR NTIDWMKKPR 100
    CGVPDQTRGS SKFHIRRKRY ALTGQKWQHK HITYSIKNVT PKVGDPETRK 150
    AIRRAFDVWQ NVTPLTFEEV PYSELENGKR DVDITIIFAS GFHGDSSPFD 200
    GEGGFLAHAY FPGPGIGGDT HFDSDEPWTL GNPNHDGNDL FLVAVHELGH 250
    ALGLEHSNDP TAIMAPFYQY METDNFKLPN DDLQGIQKIY GPPDKIPPPT 300
    RPLPTVPPHR SIPPADPRKN DRPKPPRPPT GRPSYPGAKP NICDGNFNTL 350
    AILRREMFVF KDQWFWRVRN NRVMDGYPMQ ITYFWRGLPP SIDAVYENSD 400
    GNFVFFKGNK YWVFKDTTLQ PGYPHDLITL GSGIPPHGID SAIWWEDVGK 450
    TYFFKGDRYW RYSEEMKTMD PGYPKPITVW KGIPESPQGA FVHKENGFTY 500
    FYKGKEYWKF NNQILKVEPG YPRSILKDFM GCDGPTDRVK EGHSPPDDVD 550
    IVIKLDNTAS TVKAIAIVIP CILALCLLVL VYTVFQFKRK GTPRHILYCK 600
    RSMQEWV 607
    Length:607
    Mass (Da):69,521
    Last modified:July 15, 1998 - v2
    Checksum:i30D6247D9CB21663
    GO
    Isoform Short (identifier: P51512-2) [UniParc]FASTAAdd to Basket

    Also known as: SM3

    The sequence of this isoform differs from the canonical sequence as follows:
         408-457: GNKYWVFKDT...VGKTYFFKGD → VKGDTLSVIQ...TYEELSSITY
         458-607: Missing.

    Show »
    Length:457
    Mass (Da):52,515
    Checksum:i94184CDA9F76C5EB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti521 – 5211Y → H in BAA23742. (PubMed:7559440)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei408 – 45750GNKYW…FFKGD → VKGDTLSVIQDGWLYKYHWK WILEQRQSVPVLSRQTEKHK TYEELSSITY in isoform Short. 1 PublicationVSP_005453Add
    BLAST
    Alternative sequencei458 – 607150Missing in isoform Short. 1 PublicationVSP_005454Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB009303 mRNA. Translation: BAA23742.1.
    D83646 mRNA. Translation: BAA12022.1.
    D83647 mRNA. Translation: BAA12023.1.
    D85511 mRNA. Translation: BAA22226.1.
    DQ003082 Genomic DNA. Translation: AAX84515.1.
    AK314274 mRNA. Translation: BAG36934.1.
    CH471060 Genomic DNA. Translation: EAW91651.1.
    BC069500 mRNA. Translation: AAH69500.1.
    BC075004 mRNA. Translation: AAH75004.1.
    BC075005 mRNA. Translation: AAH75005.1.
    CCDSiCCDS6246.1. [P51512-1]
    RefSeqiNP_005932.2. NM_005941.4. [P51512-1]
    UniGeneiHs.492187.
    Hs.546267.

    Genome annotation databases

    EnsembliENST00000286614; ENSP00000286614; ENSG00000156103. [P51512-1]
    GeneIDi4325.
    KEGGihsa:4325.
    UCSCiuc003yeb.4. human. [P51512-1]

    Polymorphism databases

    DMDMi3041669.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB009303 mRNA. Translation: BAA23742.1 .
    D83646 mRNA. Translation: BAA12022.1 .
    D83647 mRNA. Translation: BAA12023.1 .
    D85511 mRNA. Translation: BAA22226.1 .
    DQ003082 Genomic DNA. Translation: AAX84515.1 .
    AK314274 mRNA. Translation: BAG36934.1 .
    CH471060 Genomic DNA. Translation: EAW91651.1 .
    BC069500 mRNA. Translation: AAH69500.1 .
    BC075004 mRNA. Translation: AAH75004.1 .
    BC075005 mRNA. Translation: AAH75005.1 .
    CCDSi CCDS6246.1. [P51512-1 ]
    RefSeqi NP_005932.2. NM_005941.4. [P51512-1 ]
    UniGenei Hs.492187.
    Hs.546267.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1RM8 X-ray 1.80 A 124-292 [» ]
    ProteinModelPortali P51512.
    SMRi P51512. Positions 69-561.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P51512. 1 interaction.
    MINTi MINT-4722491.
    STRINGi 9606.ENSP00000286614.

    Chemistry

    BindingDBi P51512.
    ChEMBLi CHEMBL2200.

    Protein family/group databases

    MEROPSi M10.016.

    PTM databases

    PhosphoSitei P51512.

    Polymorphism databases

    DMDMi 3041669.

    Proteomic databases

    PaxDbi P51512.
    PRIDEi P51512.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000286614 ; ENSP00000286614 ; ENSG00000156103 . [P51512-1 ]
    GeneIDi 4325.
    KEGGi hsa:4325.
    UCSCi uc003yeb.4. human. [P51512-1 ]

    Organism-specific databases

    CTDi 4325.
    GeneCardsi GC08M089044.
    HGNCi HGNC:7162. MMP16.
    HPAi HPA023693.
    MIMi 602262. gene.
    neXtProti NX_P51512.
    PharmGKBi PA30874.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG295915.
    HOGENOMi HOG000217928.
    HOVERGENi HBG052484.
    InParanoidi P51512.
    KOi K07996.
    OMAi VPPHRSV.
    OrthoDBi EOG7XPZ57.
    PhylomeDBi P51512.
    TreeFami TF352396.

    Enzyme and pathway databases

    Reactomei REACT_118682. Activation of Matrix Metalloproteinases.

    Miscellaneous databases

    EvolutionaryTracei P51512.
    GeneWikii MMP16.
    GenomeRNAii 4325.
    NextBioi 17017.
    PMAP-CutDB P51512.
    PROi P51512.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P51512.
    Bgeei P51512.
    CleanExi HS_MMP16.
    Genevestigatori P51512.

    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.
    IPR028697. MMP16.
    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:SF26. PTHR10201:SF26. 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. "Identification of the second membrane-type matrix metalloproteinase (MT-MMP-2) gene from a human placenta cDNA library. MT-MMPs form a unique membrane-type subclass in the MMP family."
      Takino T., Sato H., Shinagawa A., Seiki M.
      J. Biol. Chem. 270:23013-23020(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
      Tissue: Placenta.
    2. Seiki M.
      Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "Identification of soluble type of membrane-type matrix metalloproteinase-3 formed by alternatively spliced mRNA."
      Matsumoto S., Katoh M., Saito S., Watanabe T., Masuho Y.
      Biochim. Biophys. Acta 1354:159-170(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
      Tissue: Ovary.
    4. "Expression of three membrane-type matrix metalloproteinases (MT-MMPs) in rat vascular smooth muscle cells and characterization of MT3-MMPs with and without transmembrane domain."
      Shofuda K., Yasumitsu H., Nishihashi A., Miki K., Miyazaki K.
      J. Biol. Chem. 272:9749-9754(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
      Tissue: Fetal brain.
    5. NIEHS SNPs program
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    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 LONG).
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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 LONG).
      Tissue: Brain.
    9. "Melanoma chondroitin sulfate proteoglycan regulates matrix metalloproteinase-dependent human melanoma invasion into type I collagen."
      Iida J., Pei D., Kang T., Simpson M.A., Herlyn M., Furcht L.T., McCarthy J.B.
      J. Biol. Chem. 276:18786-18794(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CSPG4, SUBCELLULAR LOCATION, FUNCTION.
    10. "Crystal structure of the catalytic domain of MMP-16/MT3-MMP: characterization of MT-MMP specific features."
      Lang R., Braun M., Sounni N.E., Noel A., Frankenne F., Foidart J.M., Bode W., Maskos K.
      J. Mol. Biol. 336:213-225(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 124-292 IN COMPLEX WITH INHIBITOR, ZINC-BINDING SITES, CALCIUM-BINDING SITES.

    Entry informationi

    Entry nameiMMP16_HUMAN
    AccessioniPrimary (citable) accession number: P51512
    Secondary accession number(s): B2RAN7, Q14824, Q52H48
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: July 15, 1998
    Last modified: October 1, 2014
    This is version 153 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. Peptidase families
      Classification of peptidase families and list of entries
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3