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P14780

- MMP9_HUMAN

UniProt

P14780 - MMP9_HUMAN

Protein

Matrix metalloproteinase-9

Gene

MMP9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 190 (01 Oct 2014)
      Sequence version 3 (24 Nov 2009)
      Previous versions | rss
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    Functioni

    May play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-|-Leu bond. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide.1 Publication

    Catalytic activityi

    Cleavage of gelatin types I and V and collagen types IV and V.1 Publication

    Cofactori

    Binds 2 zinc ions per subunit.
    Binds 3 calcium ions per subunit.

    Enzyme regulationi

    Inhibited by histatin-3 1/24 (histatin-5). Inhibited by ECM1.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei59 – 602Cleavage; by MMP3
    Metal bindingi99 – 991Zinc 2; in inhibited form2 Publications
    Sitei106 – 1072Cleavage; by MMP3
    Metal bindingi131 – 1311Calcium 1
    Metal bindingi165 – 1651Calcium 2; via carbonyl oxygen
    Metal bindingi175 – 1751Zinc 1; structural2 Publications
    Metal bindingi177 – 1771Zinc 1; structural2 Publications
    Metal bindingi182 – 1821Calcium 3
    Metal bindingi183 – 1831Calcium 3; via carbonyl oxygen
    Metal bindingi185 – 1851Calcium 3; via carbonyl oxygen
    Metal bindingi187 – 1871Calcium 3; via carbonyl oxygen
    Metal bindingi190 – 1901Zinc 1; structural2 Publications
    Metal bindingi197 – 1971Calcium 2; via carbonyl oxygen
    Metal bindingi199 – 1991Calcium 2; via carbonyl oxygen
    Metal bindingi201 – 2011Calcium 2
    Metal bindingi203 – 2031Zinc 1; structural2 Publications
    Metal bindingi205 – 2051Calcium 3
    Metal bindingi206 – 2061Calcium 1
    Metal bindingi208 – 2081Calcium 1
    Metal bindingi208 – 2081Calcium 3
    Metal bindingi401 – 4011Zinc 2; catalytic2 Publications
    Active sitei402 – 4021
    Metal bindingi405 – 4051Zinc 2; catalytic2 Publications
    Metal bindingi411 – 4111Zinc 2; catalytic2 Publications

    GO - Molecular functioni

    1. collagen binding Source: UniProtKB
    2. identical protein binding Source: IntAct
    3. metalloendopeptidase activity Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. collagen catabolic process Source: Reactome
    2. embryo implantation Source: Ensembl
    3. extracellular matrix disassembly Source: Reactome
    4. extracellular matrix organization Source: Reactome
    5. leukocyte migration Source: InterPro
    6. macrophage differentiation Source: UniProtKB
    7. negative regulation of cation channel activity Source: UniProt
    8. ossification Source: InterPro
    9. positive regulation of apoptotic process Source: Ensembl
    10. positive regulation of keratinocyte migration Source: BHF-UCL
    11. positive regulation of receptor binding Source: UniProt
    12. proteolysis Source: UniProtKB
    13. skeletal system development Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Collagen degradation

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_111040. Signaling by SCF-KIT.
    REACT_118572. Degradation of the extracellular matrix.
    REACT_118682. Activation of Matrix Metalloproteinases.
    REACT_150180. Assembly of collagen fibrils and other multimeric structures.
    REACT_150401. Collagen degradation.
    REACT_222620. Collagen degradation.

    Protein family/group databases

    MEROPSiM10.004.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Matrix metalloproteinase-9 (EC:3.4.24.35)
    Short name:
    MMP-9
    Alternative name(s):
    92 kDa gelatinase
    92 kDa type IV collagenase
    Gelatinase B
    Short name:
    GELB
    Cleaved into the following 2 chains:
    Gene namesi
    Name:MMP9
    Synonyms:CLG4B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:7176. MMP9.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. extracellular space Source: UniProtKB
    3. extracellular vesicular exosome Source: UniProt
    4. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Intervertebral disc disease (IDD) [MIM:603932]: A common musculo-skeletal disorder caused by degeneration of intervertebral disks of the lumbar spine. It results in low-back pain and unilateral leg pain.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti279 – 2791Q → R Common polymorphism; may be associated with susceptibility to IDD. 4 Publications
    Corresponds to variant rs17576 [ dbSNP | Ensembl ].
    VAR_013782
    Metaphyseal anadysplasia 2 (MANDP2) [MIM:613073]: A bone development disorder characterized by skeletal anomalies that resolve spontaneously with age. Clinical characteristics are evident from the first months of life and include slight shortness of stature and a mild varus deformity of the legs. Patients attain a normal stature in adolescence and show improvement or complete resolution of varus deformity of the legs and rhizomelic micromelia.
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi402 – 4021E → Q: Loss of activity. 1 Publication

    Organism-specific databases

    MIMi603932. phenotype.
    613073. phenotype.
    Orphaneti1040. Metaphyseal anadysplasia.
    PharmGKBiPA30889.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Propeptidei? – 707Removed in 64 kDa matrix metalloproteinase-9 and 67 kDa matrix metalloproteinase-9PRO_0000028757
    Signal peptidei1 – 19196 PublicationsAdd
    BLAST
    Propeptidei20 – 9374Activation peptidePRO_0000028754Add
    BLAST
    Chaini94 – ?67 kDa matrix metalloproteinase-9PRO_0000028755
    Chaini107 – 70760182 kDa matrix metalloproteinase-9PRO_0000028756Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi38 – 381N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi120 – 1201N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi127 – 1271N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi230 ↔ 256PROSITE-ProRule annotation
    Disulfide bondi244 ↔ 271PROSITE-ProRule annotation
    Disulfide bondi288 ↔ 314PROSITE-ProRule annotation
    Disulfide bondi302 ↔ 329PROSITE-ProRule annotation
    Disulfide bondi347 ↔ 373PROSITE-ProRule annotation
    Disulfide bondi361 ↔ 388PROSITE-ProRule annotation
    Disulfide bondi516 ↔ 704

    Post-translational modificationi

    Processing of the precursor yields different active forms of 64, 67 and 82 kDa. Sequentially processing by MMP3 yields the 82 kDa matrix metalloproteinase-9.3 Publications
    N- and O-glycosylated.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PaxDbiP14780.
    PeptideAtlasiP14780.
    PRIDEiP14780.

    PTM databases

    PhosphoSiteiP14780.
    UniCarbKBiP14780.

    Expressioni

    Tissue specificityi

    Produced by normal alveolar macrophages and granulocytes.

    Inductioni

    Activated by 4-aminophenylmercuric acetate and phorbol ester. Up-regulated by ARHGEF4, SPATA13 and APC via the JNK signaling pathway in colorectal tumor cells.3 Publications

    Gene expression databases

    BgeeiP14780.
    CleanExiHS_MMP9.
    GenevestigatoriP14780.

    Organism-specific databases

    HPAiCAB000348.
    HPA001238.

    Interactioni

    Subunit structurei

    Exists as monomer or homodimer; disulfide-linked. Exists also as heterodimer with a 25 kDa protein. Macrophages and transformed cell lines produce only the monomeric form. Interacts with ECM1.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-1382326,EBI-1382326
    MEP1AQ168192EBI-1382326,EBI-8153734
    MEP1BQ168202EBI-1382326,EBI-968418
    SCUBE3Q8IX302EBI-1382326,EBI-4479975
    VCANP136113EBI-1382326,EBI-8515977

    Protein-protein interaction databases

    BioGridi110461. 5 interactions.
    DIPiDIP-29518N.
    IntActiP14780. 9 interactions.
    MINTiMINT-7709677.
    STRINGi9606.ENSP00000361405.

    Structurei

    Secondary structure

    1
    707
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi41 – 5111
    Helixi68 – 7811
    Helixi88 – 947
    Beta strandi103 – 1053
    Beta strandi112 – 1154
    Beta strandi117 – 1259
    Beta strandi130 – 1323
    Helixi134 – 14916
    Beta strandi151 – 1533
    Beta strandi155 – 1584
    Beta strandi160 – 1623
    Beta strandi165 – 1717
    Beta strandi176 – 1783
    Beta strandi183 – 1864
    Beta strandi189 – 1913
    Beta strandi194 – 1963
    Turni197 – 2004
    Beta strandi202 – 2054
    Beta strandi210 – 2145
    Beta strandi221 – 2255
    Beta strandi232 – 2387
    Beta strandi240 – 2434
    Beta strandi255 – 2617
    Helixi262 – 2654
    Beta strandi268 – 2703
    Turni274 – 2763
    Beta strandi279 – 2835
    Beta strandi290 – 2945
    Beta strandi297 – 3015
    Beta strandi313 – 3197
    Helixi320 – 3234
    Beta strandi326 – 3283
    Helixi333 – 3353
    Turni340 – 3445
    Beta strandi349 – 3535
    Beta strandi356 – 3583
    Beta strandi372 – 3787
    Helixi379 – 3824
    Beta strandi385 – 3873
    Beta strandi391 – 3944
    Helixi395 – 40612
    Beta strandi420 – 4223
    Helixi433 – 44311
    Beta strandi444 – 4463
    Helixi450 – 46011
    Helixi515 – 5173
    Beta strandi522 – 5276
    Beta strandi530 – 5356
    Beta strandi538 – 5425
    Beta strandi545 – 5473
    Beta strandi551 – 5555
    Helixi556 – 5594
    Beta strandi568 – 5725
    Turni574 – 5763
    Beta strandi579 – 5835
    Beta strandi586 – 5916
    Beta strandi594 – 6007
    Helixi601 – 6044
    Beta strandi615 – 6184
    Beta strandi623 – 6286
    Beta strandi631 – 6366
    Turni637 – 6404
    Helixi644 – 6463
    Helixi650 – 6534
    Beta strandi662 – 6676
    Beta strandi670 – 6756
    Beta strandi678 – 6836
    Beta strandi690 – 6967
    Turni697 – 7004

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GKCX-ray2.30A/B107-443[»]
    1GKDX-ray2.10A/B107-443[»]
    1ITVX-ray1.95A/B513-707[»]
    1L6JX-ray2.50A20-444[»]
    1LKGmodel-A1-707[»]
    2OVXX-ray2.00A/B110-443[»]
    2OVZX-ray2.00A/B110-443[»]
    2OW0X-ray2.00A/B110-443[»]
    2OW1X-ray2.20A/B110-443[»]
    2OW2X-ray2.90A/B110-443[»]
    4H1QX-ray1.59A/B110-214[»]
    A/B391-444[»]
    4H2EX-ray2.90A/B107-461[»]
    4H3XX-ray1.76A/B107-444[»]
    4H82X-ray1.90A/B/C/D110-444[»]
    4HMAX-ray1.94A/B110-444[»]
    4JIJX-ray1.70A/B107-444[»]
    4JQGX-ray1.85A/B107-444[»]
    ProteinModelPortaliP14780.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP14780.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini225 – 27349Fibronectin type-II 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini283 – 33149Fibronectin type-II 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini342 – 39049Fibronectin type-II 3PROSITE-ProRule annotationAdd
    BLAST
    Repeati518 – 56346Hemopexin 1Add
    BLAST
    Repeati564 – 60845Hemopexin 2Add
    BLAST
    Repeati610 – 65748Hemopexin 3Add
    BLAST
    Repeati658 – 70447Hemopexin 4Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi97 – 1048Cysteine 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 3 fibronectin type-II domains.PROSITE-ProRule annotation
    Contains 4 hemopexin repeats.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG328372.
    HOVERGENiHBG052484.
    InParanoidiP14780.
    KOiK01403.
    OMAiEGDLKWH.
    OrthoDBiEOG70KGNX.
    PhylomeDBiP14780.
    TreeFamiTF315428.

    Family and domain databases

    Gene3Di2.10.10.10. 3 hits.
    2.110.10.10. 1 hit.
    3.40.390.10. 2 hits.
    InterProiIPR000562. FN_type2_col-bd.
    IPR000585. Hemopexin-like_dom.
    IPR018487. Hemopexin-like_repeat.
    IPR018486. Hemopexin_CS.
    IPR013806. Kringle-like.
    IPR024079. MetalloPept_cat_dom.
    IPR028688. MMP9.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR021158. Pept_M10A_Zn_BS.
    IPR006026. Peptidase_Metallo.
    IPR002477. Peptidoglycan-bd-like.
    IPR006970. PT.
    [Graphical view]
    PANTHERiPTHR10201:SF30. PTHR10201:SF30. 1 hit.
    PfamiPF00040. fn2. 3 hits.
    PF00045. Hemopexin. 4 hits.
    PF00413. Peptidase_M10. 1 hit.
    PF01471. PG_binding_1. 1 hit.
    PF04886. PT. 1 hit.
    [Graphical view]
    PRINTSiPR00138. MATRIXIN.
    SMARTiSM00059. FN2. 3 hits.
    SM00120. HX. 4 hits.
    SM00235. ZnMc. 1 hit.
    [Graphical view]
    SUPFAMiSSF47090. SSF47090. 1 hit.
    SSF50923. SSF50923. 1 hit.
    SSF57440. SSF57440. 3 hits.
    PROSITEiPS00546. CYSTEINE_SWITCH. 1 hit.
    PS00023. FN2_1. 3 hits.
    PS51092. FN2_2. 3 hits.
    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.

    P14780-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSLWQPLVLV LLVLGCCFAA PRQRQSTLVL FPGDLRTNLT DRQLAEEYLY    50
    RYGYTRVAEM RGESKSLGPA LLLLQKQLSL PETGELDSAT LKAMRTPRCG 100
    VPDLGRFQTF EGDLKWHHHN ITYWIQNYSE DLPRAVIDDA FARAFALWSA 150
    VTPLTFTRVY SRDADIVIQF GVAEHGDGYP FDGKDGLLAH AFPPGPGIQG 200
    DAHFDDDELW SLGKGVVVPT RFGNADGAAC HFPFIFEGRS YSACTTDGRS 250
    DGLPWCSTTA NYDTDDRFGF CPSERLYTQD GNADGKPCQF PFIFQGQSYS 300
    ACTTDGRSDG YRWCATTANY DRDKLFGFCP TRADSTVMGG NSAGELCVFP 350
    FTFLGKEYST CTSEGRGDGR LWCATTSNFD SDKKWGFCPD QGYSLFLVAA 400
    HEFGHALGLD HSSVPEALMY PMYRFTEGPP LHKDDVNGIR HLYGPRPEPE 450
    PRPPTTTTPQ PTAPPTVCPT GPPTVHPSER PTAGPTGPPS AGPTGPPTAG 500
    PSTATTVPLS PVDDACNVNI FDAIAEIGNQ LYLFKDGKYW RFSEGRGSRP 550
    QGPFLIADKW PALPRKLDSV FEERLSKKLF FFSGRQVWVY TGASVLGPRR 600
    LDKLGLGADV AQVTGALRSG RGKMLLFSGR RLWRFDVKAQ MVDPRSASEV 650
    DRMFPGVPLD THDVFQYREK AYFCQDRFYW RVSSRSELNQ VDQVGYVTYD 700
    ILQCPED 707
    Length:707
    Mass (Da):78,458
    Last modified:November 24, 2009 - v3
    Checksum:i2165AC8CA1466209
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti110 – 1101F → L in BAG35956. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti20 – 201A → V.3 Publications
    Corresponds to variant rs1805088 [ dbSNP | Ensembl ].
    VAR_013780
    Natural varianti38 – 381N → S.
    Corresponds to variant rs41427445 [ dbSNP | Ensembl ].
    VAR_037004
    Natural varianti82 – 821E → K.1 Publication
    Corresponds to variant rs1805089 [ dbSNP | Ensembl ].
    VAR_013781
    Natural varianti127 – 1271N → K.1 Publication
    Corresponds to variant rs3918252 [ dbSNP | Ensembl ].
    VAR_020054
    Natural varianti239 – 2391R → H.1 Publication
    Corresponds to variant rs28763886 [ dbSNP | Ensembl ].
    VAR_025165
    Natural varianti279 – 2791Q → R Common polymorphism; may be associated with susceptibility to IDD. 4 Publications
    Corresponds to variant rs17576 [ dbSNP | Ensembl ].
    VAR_013782
    Natural varianti571 – 5711F → V.1 Publication
    Corresponds to variant rs35691798 [ dbSNP | Ensembl ].
    VAR_025166
    Natural varianti574 – 5741R → P.5 Publications
    Corresponds to variant rs2250889 [ dbSNP | Ensembl ].
    VAR_024595
    Natural varianti668 – 6681R → Q.2 Publications
    Corresponds to variant rs17577 [ dbSNP | Ensembl ].
    VAR_014742

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05070 mRNA. Translation: AAA51539.1.
    M68343 Genomic DNA. No translation available.
    M68344 Genomic DNA. No translation available.
    M68345 Genomic DNA. No translation available.
    M68346 Genomic DNA. No translation available.
    M68347 Genomic DNA. No translation available.
    M68348 Genomic DNA. No translation available.
    M68349 Genomic DNA. No translation available.
    M68350 Genomic DNA. No translation available.
    M68351 Genomic DNA. No translation available.
    M68352 Genomic DNA. No translation available.
    M68353 Genomic DNA. No translation available.
    M68354 Genomic DNA. No translation available.
    M68355 Genomic DNA. No translation available.
    AK313137 mRNA. Translation: BAG35956.1.
    AF538844 Genomic DNA. Translation: AAM97934.1.
    DQ194553 Genomic DNA. Translation: ABA03169.1.
    AL162458 Genomic DNA. Translation: CAC10459.1.
    BC006093 mRNA. Translation: AAH06093.1.
    D10051 Genomic DNA. Translation: BAA20967.1.
    CCDSiCCDS13390.1.
    PIRiA34458.
    RefSeqiNP_004985.2. NM_004994.2.
    UniGeneiHs.297413.

    Genome annotation databases

    EnsembliENST00000372330; ENSP00000361405; ENSG00000100985.
    GeneIDi4318.
    KEGGihsa:4318.
    UCSCiuc002xqz.3. human.

    Polymorphism databases

    DMDMi269849668.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J05070 mRNA. Translation: AAA51539.1 .
    M68343 Genomic DNA. No translation available.
    M68344 Genomic DNA. No translation available.
    M68345 Genomic DNA. No translation available.
    M68346 Genomic DNA. No translation available.
    M68347 Genomic DNA. No translation available.
    M68348 Genomic DNA. No translation available.
    M68349 Genomic DNA. No translation available.
    M68350 Genomic DNA. No translation available.
    M68351 Genomic DNA. No translation available.
    M68352 Genomic DNA. No translation available.
    M68353 Genomic DNA. No translation available.
    M68354 Genomic DNA. No translation available.
    M68355 Genomic DNA. No translation available.
    AK313137 mRNA. Translation: BAG35956.1 .
    AF538844 Genomic DNA. Translation: AAM97934.1 .
    DQ194553 Genomic DNA. Translation: ABA03169.1 .
    AL162458 Genomic DNA. Translation: CAC10459.1 .
    BC006093 mRNA. Translation: AAH06093.1 .
    D10051 Genomic DNA. Translation: BAA20967.1 .
    CCDSi CCDS13390.1.
    PIRi A34458.
    RefSeqi NP_004985.2. NM_004994.2.
    UniGenei Hs.297413.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GKC X-ray 2.30 A/B 107-443 [» ]
    1GKD X-ray 2.10 A/B 107-443 [» ]
    1ITV X-ray 1.95 A/B 513-707 [» ]
    1L6J X-ray 2.50 A 20-444 [» ]
    1LKG model - A 1-707 [» ]
    2OVX X-ray 2.00 A/B 110-443 [» ]
    2OVZ X-ray 2.00 A/B 110-443 [» ]
    2OW0 X-ray 2.00 A/B 110-443 [» ]
    2OW1 X-ray 2.20 A/B 110-443 [» ]
    2OW2 X-ray 2.90 A/B 110-443 [» ]
    4H1Q X-ray 1.59 A/B 110-214 [» ]
    A/B 391-444 [» ]
    4H2E X-ray 2.90 A/B 107-461 [» ]
    4H3X X-ray 1.76 A/B 107-444 [» ]
    4H82 X-ray 1.90 A/B/C/D 110-444 [» ]
    4HMA X-ray 1.94 A/B 110-444 [» ]
    4JIJ X-ray 1.70 A/B 107-444 [» ]
    4JQG X-ray 1.85 A/B 107-444 [» ]
    ProteinModelPortali P14780.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110461. 5 interactions.
    DIPi DIP-29518N.
    IntActi P14780. 9 interactions.
    MINTi MINT-7709677.
    STRINGi 9606.ENSP00000361405.

    Chemistry

    ChEMBLi CHEMBL321.
    DrugBanki DB01296. Glucosamine.
    DB00786. Marimastat.
    DB01017. Minocycline.
    DB00641. Simvastatin.
    GuidetoPHARMACOLOGYi 1633.

    Protein family/group databases

    MEROPSi M10.004.

    PTM databases

    PhosphoSitei P14780.
    UniCarbKBi P14780.

    Polymorphism databases

    DMDMi 269849668.

    Proteomic databases

    PaxDbi P14780.
    PeptideAtlasi P14780.
    PRIDEi P14780.

    Protocols and materials databases

    DNASUi 4318.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000372330 ; ENSP00000361405 ; ENSG00000100985 .
    GeneIDi 4318.
    KEGGi hsa:4318.
    UCSCi uc002xqz.3. human.

    Organism-specific databases

    CTDi 4318.
    GeneCardsi GC20P044637.
    H-InvDB HIX0015874.
    HGNCi HGNC:7176. MMP9.
    HPAi CAB000348.
    HPA001238.
    MIMi 120361. gene.
    603932. phenotype.
    613073. phenotype.
    neXtProti NX_P14780.
    Orphaneti 1040. Metaphyseal anadysplasia.
    PharmGKBi PA30889.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG328372.
    HOVERGENi HBG052484.
    InParanoidi P14780.
    KOi K01403.
    OMAi EGDLKWH.
    OrthoDBi EOG70KGNX.
    PhylomeDBi P14780.
    TreeFami TF315428.

    Enzyme and pathway databases

    Reactomei REACT_111040. Signaling by SCF-KIT.
    REACT_118572. Degradation of the extracellular matrix.
    REACT_118682. Activation of Matrix Metalloproteinases.
    REACT_150180. Assembly of collagen fibrils and other multimeric structures.
    REACT_150401. Collagen degradation.
    REACT_222620. Collagen degradation.

    Miscellaneous databases

    EvolutionaryTracei P14780.
    GeneWikii MMP9.
    GenomeRNAii 4318.
    NextBioi 16989.
    PROi P14780.
    SOURCEi Search...

    Gene expression databases

    Bgeei P14780.
    CleanExi HS_MMP9.
    Genevestigatori P14780.

    Family and domain databases

    Gene3Di 2.10.10.10. 3 hits.
    2.110.10.10. 1 hit.
    3.40.390.10. 2 hits.
    InterProi IPR000562. FN_type2_col-bd.
    IPR000585. Hemopexin-like_dom.
    IPR018487. Hemopexin-like_repeat.
    IPR018486. Hemopexin_CS.
    IPR013806. Kringle-like.
    IPR024079. MetalloPept_cat_dom.
    IPR028688. MMP9.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR021158. Pept_M10A_Zn_BS.
    IPR006026. Peptidase_Metallo.
    IPR002477. Peptidoglycan-bd-like.
    IPR006970. PT.
    [Graphical view ]
    PANTHERi PTHR10201:SF30. PTHR10201:SF30. 1 hit.
    Pfami PF00040. fn2. 3 hits.
    PF00045. Hemopexin. 4 hits.
    PF00413. Peptidase_M10. 1 hit.
    PF01471. PG_binding_1. 1 hit.
    PF04886. PT. 1 hit.
    [Graphical view ]
    PRINTSi PR00138. MATRIXIN.
    SMARTi SM00059. FN2. 3 hits.
    SM00120. HX. 4 hits.
    SM00235. ZnMc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47090. SSF47090. 1 hit.
    SSF50923. SSF50923. 1 hit.
    SSF57440. SSF57440. 3 hits.
    PROSITEi PS00546. CYSTEINE_SWITCH. 1 hit.
    PS00023. FN2_1. 3 hits.
    PS51092. FN2_2. 3 hits.
    PS00024. HEMOPEXIN. 1 hit.
    PS51642. HEMOPEXIN_2. 4 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "SV40-transformed human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by normal human macrophages."
      Wilhelm S.M., Collier I.E., Marmer B.L., Eisen A.Z., Grant G.A., Goldberg G.I.
      J. Biol. Chem. 264:17213-17221(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-37, VARIANTS ARG-279 AND PRO-574.
    2. "Complete structure of the human gene for 92-kDa type IV collagenase. Divergent regulation of expression for the 92- and 72-kilodalton enzyme genes in HT-1080 cells."
      Huhtala P., Tuuttila A., Chow L.T., Lohi J., Keski-Oja J., Tryggvason K.
      J. Biol. Chem. 266:16485-16490(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    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], VARIANT PRO-574.
      Tissue: Umbilical cord blood.
    4. SeattleSNPs variation discovery resource
      Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-20; LYS-127; ARG-279; PRO-574 AND GLN-668.
    5. NIEHS SNPs program
      Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-20; HIS-239; VAL-571; PRO-574 AND GLN-668.
    6. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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], VARIANTS ARG-279 AND PRO-574.
      Tissue: B-cell.
    8. "Regulatory mechanism of 92 kDa type IV collagenase gene expression which is associated with invasiveness of tumor cells."
      Sato H., Seiki M.
      Oncogene 8:395-405(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
    9. "Human neutrophil gelatinase: a marker for circulating blood neutrophils. Purification and quantitation by enzyme linked immunosorbent assay."
      Kjeldsen L., Bjerrum O.W., Hovgaard D., Johnsen A.H., Sehested M., Borregaard N.
      Eur. J. Haematol. 49:180-191(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 20-39, GLYCOSYLATION.
      Tissue: Neutrophil.
    10. "The cytokine-protease connection: identification of a 96-kD THP-1 gelatinase and regulation by interleukin-1 and cytokine inducers."
      van Ranst M., Norga K., Masure S., Proost P., Vandekerckhove F., Auwerx J., van Damme J., Opdenakker G.
      Cytokine 3:231-239(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 20-37.
    11. "Matrix metalloproteinase 3 (stromelysin) activates the precursor for the human matrix metalloproteinase 9."
      Ogata Y., Enghild J.J., Nagase H.
      J. Biol. Chem. 267:3581-3584(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 20-34; 60-71 AND 107-118, INDUCTION, PROTEOLYTIC PROCESSING BY MMP3.
    12. "Matrix metalloproteinase 9 (92-kDa gelatinase/type IV collagenase) from HT 1080 human fibrosarcoma cells. Purification and activation of the precursor and enzymic properties."
      Okada Y., Gonoji Y., Naka K., Tomita K., Nakanishi I., Iwata K., Yamashita K., Hayakawa T.
      J. Biol. Chem. 267:21712-21719(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 20-32 AND 94-111, PROTEOLYTIC PROCESSING, INDUCTION.
      Tissue: Fibrosarcoma.
    13. "Proteolytic and non-proteolytic activation of human neutrophil progelatinase B."
      Sang Q.X., Birkedal-Hansen H., Van Wart H.E.
      Biochim. Biophys. Acta 1251:99-108(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 20-27; 60-67; 94-101 AND 107-113.
    14. "Purification and identification of 91-kDa neutrophil gelatinase. Release by the activating peptide interleukin-8."
      Masure S., Proost P., van Damme J., Opdenakker G.
      Eur. J. Biochem. 198:391-398(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 28-60.
      Tissue: Neutrophil.
    15. "Cytokine-mediated regulation of human leukocyte gelatinases and role in arthritis."
      Opdenakker G., Masure S., Grillet B., Van Damme J.
      Lymphokine Cytokine Res. 10:317-324(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 28-37.
    16. "Latent collagenase and gelatinase from human neutrophils and their activation."
      Tschesche H., Knaeuper V., Kraemer S., Michaelis J., Oberhoff R., Reinke H.
      Matrix Suppl. 1:245-255(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 93-115, FUNCTION, CATALYTIC ACTIVITY.
      Tissue: Blood.
    17. "Purification and characterization of human 92-kDa type IV collagenase (gelatinase B)."
      Kang K., Lee D.-H.
      Exp. Mol. Med. 28:161-165(1996)
      Cited for: CHARACTERIZATION.
    18. "Characterization of the monomeric and dimeric forms of latent and active matrix metalloproteinase-9. Differential rates for activation by stromelysin 1."
      Olson M.W., Bernardo M.M., Pietila M., Gervasi D.C., Toth M., Kotra L.P., Massova I., Mobashery S., Fridman R.
      J. Biol. Chem. 275:2661-2668(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    19. "Salivary histatin 5 is an inhibitor of both host and bacterial enzymes implicated in periodontal disease."
      Gusman H., Travis J., Helmerhorst E.J., Potempa J., Troxler R.F., Oppenheim F.G.
      Infect. Immun. 69:1402-1408(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    20. "Cleavage of metastasis suppressor gene product KiSS-1 protein/metastin by matrix metalloproteinases."
      Takino T., Koshikawa N., Miyamori H., Tanaka M., Sasaki T., Okada Y., Seiki M., Sato H.
      Oncogene 22:4617-4626(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEOLYTIC PROCESSING OF KISS1.
    21. "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 ECM1, ENZYME REGULATION.
    22. "A functional polymorphism in THBS2 that affects alternative splicing and MMP binding is associated with lumbar-disc herniation."
      Hirose Y., Chiba K., Karasugi T., Nakajima M., Kawaguchi Y., Mikami Y., Furuichi T., Mio F., Miyake A., Miyamoto T., Ozaki K., Takahashi A., Mizuta H., Kubo T., Kimura T., Tanaka T., Toyama Y., Ikegawa S.
      Am. J. Hum. Genet. 82:1122-1129(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN SUSCEPTIBILITY TO IDD.
    23. "Mutations in MMP9 and MMP13 determine the mode of inheritance and the clinical spectrum of metaphyseal anadysplasia."
      Lausch E., Keppler R., Hilbert K., Cormier-Daire V., Nikkel S., Nishimura G., Unger S., Spranger J., Superti-Furga A., Zabel B.
      Am. J. Hum. Genet. 85:168-178(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN METAPHYSEAL ANADYSPLASIA TYPE 2.
    24. "The adenomatous polyposis coli-associated exchange factors Asef and Asef2 are required for adenoma formation in Apc(Min/+)mice."
      Kawasaki Y., Tsuji S., Muroya K., Furukawa S., Shibata Y., Okuno M., Ohwada S., Akiyama T.
      EMBO Rep. 10:1355-1362(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    25. "Structure of the C-terminally truncated human ProMMP9, a gelatin-binding matrix metalloproteinase."
      Elkins P.A., Ho Y.S., Smith W.W., Janson C.A., D'Alessio K.J., McQueney M.S., Cummings M.D., Romanic A.M.
      Acta Crystallogr. D 58:1182-1192(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 20-444 IN COMPLEX WITH ZINC AND MAGNESIUM IONS.
    26. Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 107-215 IN COMPLEX WITH INHIBITOR; ZINC AND CALCIUM IONS, MUTAGENESIS OF GLU-402.
    27. "Structural basis of the adaptive molecular recognition by MMP9."
      Cha H., Kopetzki E., Huber R., Lanzendoerfer M., Brandstetter H.
      J. Mol. Biol. 320:1065-1079(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 513-707, SUBUNIT.
    28. "Theoretical model of human type IV collagenase precursor."
      Mallena S.C., Sagajkar R.D.
      Submitted (APR-2002) to the PDB data bank
      Cited for: 3D-STRUCTURE MODELING.
    29. "Genetic variation at the matrix metalloproteinase-9 locus on chromosome 20q12.2-13.1."
      Zhang B., Henney A., Eriksson P., Hamsten A., Watkins H., Ye S.
      Hum. Genet. 105:418-423(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS VAL-20; LYS-82 AND ARG-279.

    Entry informationi

    Entry nameiMMP9_HUMAN
    AccessioniPrimary (citable) accession number: P14780
    Secondary accession number(s): B2R7V9
    , Q3LR70, Q8N725, Q9H4Z1, Q9UCJ9, Q9UCL1, Q9UDK2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: November 24, 2009
    Last modified: October 1, 2014
    This is version 190 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

    Miscellaneous

    In the arthritis patient this enzyme might contribute to the pathogenesis of joint destruction and might constitute a useful marker of disease status.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: 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