Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P14780 (MMP9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 185. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Matrix metalloproteinase-9

Short name=MMP-9
EC=3.4.24.35
Alternative name(s):
92 kDa gelatinase
92 kDa type IV collagenase
Gelatinase B
Short name=GELB
Gene names
Name:MMP9
Synonyms:CLG4B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length707 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.16

Catalytic activity

Cleavage of gelatin types I and V and collagen types IV and V. Ref.16

Cofactor

Binds 2 zinc ions per subunit.

Binds 3 calcium ions per subunit.

Enzyme regulation

Inhibited by histatin-3 1/24 (histatin-5). Inhibited by ECM1. Ref.19 Ref.21

Subunit structure

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. Ref.18 Ref.21 Ref.27

Subcellular location

Secretedextracellular spaceextracellular matrix Probable.

Tissue specificity

Produced by normal alveolar macrophages and granulocytes.

Induction

Activated by 4-aminophenylmercuric acetate and phorbol ester. Up-regulated by ARHGEF4, SPATA13 and APC via the JNK signaling pathway in colorectal tumor cells. Ref.11 Ref.12 Ref.19 Ref.21 Ref.24

Domain

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.

Post-translational modification

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.

N- and O-glycosylated. Ref.9

Involvement in disease

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.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.22

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.

Miscellaneous

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

Sequence similarities

Belongs to the peptidase M10A family.

Contains 3 fibronectin type-II domains.

Contains 4 hemopexin repeats.

Ontologies

Keywords
   Biological processCollagen degradation
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityPolymorphism
   DomainRepeat
Signal
   LigandCalcium
Metal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcollagen catabolic process

Traceable author statement. Source: Reactome

embryo implantation

Inferred from electronic annotation. Source: Ensembl

extracellular matrix disassembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

leukocyte migration

Inferred from electronic annotation. Source: InterPro

macrophage differentiation

Traceable author statement PubMed 2251898. Source: UniProtKB

ossification

Inferred from electronic annotation. Source: InterPro

positive regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of keratinocyte migration

Inferred from mutant phenotype PubMed 17704059. Source: BHF-UCL

proteolysis

Inferred from direct assay Ref.1. Source: UniProtKB

skeletal system development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentextracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 2251898. Source: UniProtKB

proteinaceous extracellular matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncollagen binding

Traceable author statement PubMed 2251898. Source: UniProtKB

identical protein binding

Inferred from physical interaction PubMed 23601700. Source: IntAct

metalloendopeptidase activity

Inferred from direct assay PubMed 16192646Ref.1. Source: UniProtKB

zinc ion binding

Traceable author statement PubMed 2251898. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.1 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13
Propeptide20 – 9374Activation peptide
PRO_0000028754
Chain94 – ?67 kDa matrix metalloproteinase-9PRO_0000028755
Chain107 – 70760182 kDa matrix metalloproteinase-9
PRO_0000028756
Propeptide? – 707Removed in 64 kDa matrix metalloproteinase-9 and 67 kDa matrix metalloproteinase-9PRO_0000028757

Regions

Domain225 – 27349Fibronectin type-II 1
Domain283 – 33149Fibronectin type-II 2
Domain342 – 39049Fibronectin type-II 3
Repeat518 – 56346Hemopexin 1
Repeat564 – 60845Hemopexin 2
Repeat610 – 65748Hemopexin 3
Repeat658 – 70447Hemopexin 4
Motif97 – 1048Cysteine switch By similarity

Sites

Active site4021
Metal binding991Zinc 2; in inhibited form
Metal binding1311Calcium 1
Metal binding1651Calcium 2; via carbonyl oxygen
Metal binding1751Zinc 1; structural
Metal binding1771Zinc 1; structural
Metal binding1821Calcium 3
Metal binding1831Calcium 3; via carbonyl oxygen
Metal binding1851Calcium 3; via carbonyl oxygen
Metal binding1871Calcium 3; via carbonyl oxygen
Metal binding1901Zinc 1; structural
Metal binding1971Calcium 2; via carbonyl oxygen
Metal binding1991Calcium 2; via carbonyl oxygen
Metal binding2011Calcium 2
Metal binding2031Zinc 1; structural
Metal binding2051Calcium 3
Metal binding2061Calcium 1
Metal binding2081Calcium 1
Metal binding2081Calcium 3
Metal binding4011Zinc 2; catalytic
Metal binding4051Zinc 2; catalytic
Metal binding4111Zinc 2; catalytic
Site59 – 602Cleavage; by MMP3
Site106 – 1072Cleavage; by MMP3

Amino acid modifications

Glycosylation381N-linked (GlcNAc...) Potential
Glycosylation1201N-linked (GlcNAc...) Potential
Glycosylation1271N-linked (GlcNAc...) Potential
Disulfide bond230 ↔ 256 By similarity
Disulfide bond244 ↔ 271 By similarity
Disulfide bond288 ↔ 314 By similarity
Disulfide bond302 ↔ 329 By similarity
Disulfide bond347 ↔ 373 By similarity
Disulfide bond361 ↔ 388 By similarity
Disulfide bond516 ↔ 704

Natural variations

Natural variant201A → V. Ref.4 Ref.5 Ref.29
Corresponds to variant rs1805088 [ dbSNP | Ensembl ].
VAR_013780
Natural variant381N → S.
Corresponds to variant rs41427445 [ dbSNP | Ensembl ].
VAR_037004
Natural variant821E → K. Ref.29
Corresponds to variant rs1805089 [ dbSNP | Ensembl ].
VAR_013781
Natural variant1271N → K. Ref.4
Corresponds to variant rs3918252 [ dbSNP | Ensembl ].
VAR_020054
Natural variant2391R → H. Ref.5
Corresponds to variant rs28763886 [ dbSNP | Ensembl ].
VAR_025165
Natural variant2791Q → R Common polymorphism; may be associated with susceptibility to IDD. Ref.1 Ref.4 Ref.7 Ref.29
Corresponds to variant rs17576 [ dbSNP | Ensembl ].
VAR_013782
Natural variant5711F → V. Ref.5
Corresponds to variant rs35691798 [ dbSNP | Ensembl ].
VAR_025166
Natural variant5741R → P. Ref.1 Ref.3 Ref.4 Ref.5 Ref.7
Corresponds to variant rs2250889 [ dbSNP | Ensembl ].
VAR_024595
Natural variant6681R → Q. Ref.4 Ref.5
Corresponds to variant rs17577 [ dbSNP | Ensembl ].
VAR_014742

Experimental info

Mutagenesis4021E → Q: Loss of activity. Ref.26
Sequence conflict1101F → L in BAG35956. Ref.3

Secondary structure

............................................................................................................................... 707
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P14780 [UniParc].

Last modified November 24, 2009. Version 3.
Checksum: 2165AC8CA1466209

FASTA70778,458
        10         20         30         40         50         60 
MSLWQPLVLV LLVLGCCFAA PRQRQSTLVL FPGDLRTNLT DRQLAEEYLY RYGYTRVAEM 

        70         80         90        100        110        120 
RGESKSLGPA LLLLQKQLSL PETGELDSAT LKAMRTPRCG VPDLGRFQTF EGDLKWHHHN 

       130        140        150        160        170        180 
ITYWIQNYSE DLPRAVIDDA FARAFALWSA VTPLTFTRVY SRDADIVIQF GVAEHGDGYP 

       190        200        210        220        230        240 
FDGKDGLLAH AFPPGPGIQG DAHFDDDELW SLGKGVVVPT RFGNADGAAC HFPFIFEGRS 

       250        260        270        280        290        300 
YSACTTDGRS DGLPWCSTTA NYDTDDRFGF CPSERLYTQD GNADGKPCQF PFIFQGQSYS 

       310        320        330        340        350        360 
ACTTDGRSDG YRWCATTANY DRDKLFGFCP TRADSTVMGG NSAGELCVFP FTFLGKEYST 

       370        380        390        400        410        420 
CTSEGRGDGR LWCATTSNFD SDKKWGFCPD QGYSLFLVAA HEFGHALGLD HSSVPEALMY 

       430        440        450        460        470        480 
PMYRFTEGPP LHKDDVNGIR HLYGPRPEPE PRPPTTTTPQ PTAPPTVCPT GPPTVHPSER 

       490        500        510        520        530        540 
PTAGPTGPPS AGPTGPPTAG PSTATTVPLS PVDDACNVNI FDAIAEIGNQ LYLFKDGKYW 

       550        560        570        580        590        600 
RFSEGRGSRP QGPFLIADKW PALPRKLDSV FEERLSKKLF FFSGRQVWVY TGASVLGPRR 

       610        620        630        640        650        660 
LDKLGLGADV AQVTGALRSG RGKMLLFSGR RLWRFDVKAQ MVDPRSASEV DRMFPGVPLD 

       670        680        690        700 
THDVFQYREK AYFCQDRFYW RVSSRSELNQ VDQVGYVTYD ILQCPED 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"Crystal structure of human MMP9 in complex with a reverse hydroxamate inhibitor."
Rowsell S., Hawtin P., Minshull C.A., Jepson H., Brockbank S.M.V., Barratt D.G., Slater A.M., McPheat W.L., Waterson D., Henney A.M., Pauptit R.A.
J. Mol. Biol. 319:173-181(2002) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA34458.
RefSeqNP_004985.2. NM_004994.2.
UniGeneHs.297413.

3D structure databases

PDBe
RCSB PDB
PDBj
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/B110-444[»]
4H2EX-ray2.90A/B107-444[»]
4H3XX-ray1.76A/B107-444[»]
4H82X-ray1.90A/B/C/D110-444[»]
4HMAX-ray1.94A/B110-444[»]
ProteinModelPortalP14780.
SMRP14780. Positions 26-707.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110461. 5 interactions.
DIPDIP-29518N.
IntActP14780. 8 interactions.
MINTMINT-7709677.
STRING9606.ENSP00000361405.

Chemistry

ChEMBLCHEMBL2095216.
DrugBankDB01296. Glucosamine.
DB00786. Marimastat.
DB01017. Minocycline.
DB00641. Simvastatin.
GuidetoPHARMACOLOGY1633.

Protein family/group databases

MEROPSM10.004.

PTM databases

PhosphoSiteP14780.
UniCarbKBP14780.

Polymorphism databases

DMDM269849668.

Proteomic databases

PaxDbP14780.
PeptideAtlasP14780.
PRIDEP14780.

Protocols and materials databases

DNASU4318.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000372330; ENSP00000361405; ENSG00000100985.
GeneID4318.
KEGGhsa:4318.
UCSCuc002xqz.3. human.

Organism-specific databases

CTD4318.
GeneCardsGC20P044637.
H-InvDBHIX0015874.
HGNCHGNC:7176. MMP9.
HPACAB000348.
HPA001238.
MIM120361. gene.
603932. phenotype.
613073. phenotype.
neXtProtNX_P14780.
Orphanet1040. Metaphyseal anadysplasia.
PharmGKBPA30889.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG328372.
HOVERGENHBG052484.
InParanoidP14780.
KOK01403.
OMAEGDLKWH.
OrthoDBEOG70KGNX.
PhylomeDBP14780.
TreeFamTF315428.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_118779. Extracellular matrix organization.

Gene expression databases

BgeeP14780.
CleanExHS_MMP9.
GenevestigatorP14780.

Family and domain databases

Gene3D2.10.10.10. 3 hits.
2.110.10.10. 1 hit.
3.40.390.10. 2 hits.
InterProIPR000562. 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]
PANTHERPTHR10201. PTHR10201. 1 hit.
PTHR10201:SF30. PTHR10201:SF30. 1 hit.
PfamPF00040. fn2. 3 hits.
PF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
PF04886. PT. 1 hit.
[Graphical view]
PRINTSPR00138. MATRIXIN.
SMARTSM00059. FN2. 3 hits.
SM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
SSF57440. SSF57440. 3 hits.
PROSITEPS00546. 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]
ProtoNetSearch...

Other

EvolutionaryTraceP14780.
GeneWikiMMP9.
GenomeRNAi4318.
NextBio16989.
PROP14780.
SOURCESearch...

Entry information

Entry nameMMP9_HUMAN
AccessionPrimary (citable) accession number: P14780
Secondary accession number(s): B2R7V9 expand/collapse secondary AC list , Q3LR70, Q8N725, Q9H4Z1, Q9UCJ9, Q9UCL1, Q9UDK2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 24, 2009
Last modified: April 16, 2014
This is version 185 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM