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P14780

- MMP9_HUMAN

UniProt

P14780 - MMP9_HUMAN

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Protein
Matrix metalloproteinase-9
Gene
MMP9, CLG4B
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 form
Sitei106 – 1072Cleavage; by MMP3
Metal bindingi131 – 1311Calcium 1
Metal bindingi165 – 1651Calcium 2; via carbonyl oxygen
Metal bindingi175 – 1751Zinc 1; structural
Metal bindingi177 – 1771Zinc 1; structural
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; structural
Metal bindingi197 – 1971Calcium 2; via carbonyl oxygen
Metal bindingi199 – 1991Calcium 2; via carbonyl oxygen
Metal bindingi201 – 2011Calcium 2
Metal bindingi203 – 2031Zinc 1; structural
Metal bindingi205 – 2051Calcium 3
Metal bindingi206 – 2061Calcium 1
Metal bindingi208 – 2081Calcium 1
Metal bindingi208 – 2081Calcium 3
Metal bindingi401 – 4011Zinc 2; catalytic
Active sitei402 – 4021
Metal bindingi405 – 4051Zinc 2; catalytic
Metal bindingi411 – 4111Zinc 2; catalytic

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
Complete GO annotation...

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
Complete GO annotation...

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.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.1 Publication
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 Publications
Add
BLAST
Propeptidei20 – 9374Activation peptide
PRO_0000028754Add
BLAST
Chaini94 – ?67 kDa matrix metalloproteinase-9PRO_0000028755
Chaini107 – 70760182 kDa matrix metalloproteinase-9
PRO_0000028756Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi38 – 381N-linked (GlcNAc...) Reviewed prediction
Glycosylationi120 – 1201N-linked (GlcNAc...) Reviewed prediction
Glycosylationi127 – 1271N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi230 ↔ 256 By similarity
Disulfide bondi244 ↔ 271 By similarity
Disulfide bondi288 ↔ 314 By similarity
Disulfide bondi302 ↔ 329 By similarity
Disulfide bondi347 ↔ 373 By similarity
Disulfide bondi361 ↔ 388 By similarity
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.
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.5 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 ECM1.3 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. 8 interactions.
MINTiMINT-7709677.
STRINGi9606.ENSP00000361405.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP14780.

Family & Domainsi

Domains and Repeats

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi97 – 1048Cysteine switch By 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.
Contains 4 hemopexin repeats.

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

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti110 – 1101F → L in BAG35956. 1 Publication

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. 8 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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 189 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

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