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Protein

Matrix metalloproteinase-9

Gene

MMP9

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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

Miscellaneous

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

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Zn2+Note: Binds 2 Zn2+ ions per subunit.
  • Ca2+Note: Binds 3 Ca2+ ions per subunit.

Activity regulationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi99Zinc 2; in inhibited form2 Publications1
Metal bindingi131Calcium 11
Metal bindingi165Calcium 2; via carbonyl oxygen1
Metal bindingi175Zinc 1; structural2 Publications1
Metal bindingi177Zinc 1; structural2 Publications1
Metal bindingi182Calcium 31
Metal bindingi183Calcium 3; via carbonyl oxygen1
Metal bindingi185Calcium 3; via carbonyl oxygen1
Metal bindingi187Calcium 3; via carbonyl oxygen1
Metal bindingi190Zinc 1; structural2 Publications1
Metal bindingi197Calcium 2; via carbonyl oxygen1
Metal bindingi199Calcium 2; via carbonyl oxygen1
Metal bindingi201Calcium 21
Metal bindingi203Zinc 1; structural2 Publications1
Metal bindingi205Calcium 31
Metal bindingi206Calcium 11
Metal bindingi208Calcium 11
Metal bindingi208Calcium 31
Metal bindingi401Zinc 2; catalytic2 Publications1
Active sitei4021
Metal bindingi405Zinc 2; catalytic2 Publications1
Metal bindingi411Zinc 2; catalytic2 Publications1

GO - Molecular functioni

  • collagen binding Source: UniProtKB
  • endopeptidase activity Source: ParkinsonsUK-UCL
  • identical protein binding Source: IntAct
  • metalloendopeptidase activity Source: UniProtKB
  • metallopeptidase activity Source: UniProtKB
  • serine-type endopeptidase activity Source: Reactome
  • zinc ion binding Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Metalloprotease, Protease
Biological processCollagen degradation
LigandCalcium, Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.24.35 2681
ReactomeiR-HSA-1433557 Signaling by SCF-KIT
R-HSA-1442490 Collagen degradation
R-HSA-1474228 Degradation of the extracellular matrix
R-HSA-1592389 Activation of Matrix Metalloproteinases
R-HSA-2022090 Assembly of collagen fibrils and other multimeric structures
R-HSA-3928665 EPH-ephrin mediated repulsion of cells
R-HSA-6785807 Interleukin-4 and Interleukin-13 signaling
R-HSA-6798695 Neutrophil degranulation
SIGNORiP14780

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 collagenase1 Publication
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
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

EuPathDBiHostDB:ENSG00000100985.7
HGNCiHGNC:7176 MMP9
MIMi120361 gene
neXtProtiNX_P14780

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Intervertebral disc disease (IDD)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA common musculo-skeletal disorder caused by degeneration of intervertebral disks of the lumbar spine. It results in low-back pain and unilateral leg pain.
See also OMIM:603932
Metaphyseal anadysplasia 2 (MANDP2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:613073

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi402E → Q: Loss of activity. 1 Publication1

Organism-specific databases

DisGeNETi4318
MalaCardsiMMP9
MIMi603932 phenotype
613073 phenotype
OpenTargetsiENSG00000100985
Orphaneti1040 Metaphyseal anadysplasia
PharmGKBiPA30889

Chemistry databases

ChEMBLiCHEMBL321
DrugBankiDB03683 2-{[Formyl(Hydroxy)Amino]Methyl}-4-Methylpentanoic Acid
DB05387 AE-941
DB01197 Captopril
DB01296 Glucosamine
DB00786 Marimastat
DB01017 Minocycline
DB05495 PG-530742
GuidetoPHARMACOLOGYi1633

Polymorphism and mutation databases

BioMutaiMMP9
DMDMi269849668

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_0000028757? – 707Removed in 64 kDa matrix metalloproteinase-9 and 67 kDa matrix metalloproteinase-9
Signal peptidei1 – 196 PublicationsAdd BLAST19
PropeptideiPRO_000002875420 – 93Activation peptideAdd BLAST74
ChainiPRO_000002875594 – ?67 kDa matrix metalloproteinase-9
ChainiPRO_0000028756107 – 70782 kDa matrix metalloproteinase-9Add BLAST601

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi38N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi120N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi127N-linked (GlcNAc...) asparagineSequence analysis1
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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei59 – 60Cleavage; by MMP32
Sitei106 – 107Cleavage; by MMP32

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

EPDiP14780
PaxDbiP14780
PeptideAtlasiP14780
PRIDEiP14780
ProteomicsDBi53082

PTM databases

GlyConnecti1494
6
iPTMnetiP14780
PhosphoSitePlusiP14780
UniCarbKBiP14780

Expressioni

Tissue specificityi

Detected in neutrophils (at protein level) (PubMed:7683678). Produced by normal alveolar macrophages and granulocytes.1 Publication

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
(Microbial infection) Expression induced by M.bovis MPB83 (at protein level) (PubMed:20800577).1 Publication

Gene expression databases

BgeeiENSG00000100985 Expressed in 154 organ(s), highest expression level in tibia
CleanExiHS_MMP9
GenevisibleiP14780 HS

Organism-specific databases

HPAiCAB000348
CAB068199
CAB068200
CAB068201
HPA001238
HPA063909

Interactioni

Subunit structurei

Exists as monomer or homodimer; disulfide-linked (PubMed:1281792, PubMed:7683678). Exists also as heterodimer with LCN2 (PubMed:1281792, PubMed:7683678). Macrophages and transformed cell lines produce only the monomeric form. Interacts with ECM1 (PubMed:16512877).7 Publications

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi110461, 18 interactors
CORUMiP14780
DIPiDIP-29518N
IntActiP14780, 11 interactors
MINTiP14780
STRINGi9606.ENSP00000361405

Chemistry databases

BindingDBiP14780

Structurei

Secondary structure

1707
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP14780
SMRiP14780
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14780

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini225 – 273Fibronectin type-II 1PROSITE-ProRule annotationAdd BLAST49
Domaini283 – 331Fibronectin type-II 2PROSITE-ProRule annotationAdd BLAST49
Domaini342 – 390Fibronectin type-II 3PROSITE-ProRule annotationAdd BLAST49
Repeati518 – 563Hemopexin 1Add BLAST46
Repeati564 – 608Hemopexin 2Add BLAST45
Repeati610 – 657Hemopexin 3Add BLAST48
Repeati658 – 704Hemopexin 4Add BLAST47

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi97 – 104Cysteine switchBy similarity8

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

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG1565 Eukaryota
ENOG410XQ5D LUCA
GeneTreeiENSGT00910000144034
HOVERGENiHBG052484
InParanoidiP14780
KOiK01403
OMAiGFCPSER
OrthoDBiEOG091G02JB
PhylomeDBiP14780
TreeFamiTF315428

Family and domain databases

CDDicd00062 FN2, 3 hits
cd00094 HX, 1 hit
cd04278 ZnMc_MMP, 1 hit
Gene3Di1.10.101.10, 1 hit
2.10.10.10, 3 hits
2.110.10.10, 1 hit
3.40.390.10, 1 hit
InterProiView protein in InterPro
IPR000562 FN_type2_dom
IPR036943 FN_type2_sf
IPR000585 Hemopexin-like_dom
IPR036375 Hemopexin-like_dom_sf
IPR018487 Hemopexin-like_repeat
IPR018486 Hemopexin_CS
IPR013806 Kringle-like
IPR033739 M10A_MMP
IPR024079 MetalloPept_cat_dom_sf
IPR028688 MMP9
IPR001818 Pept_M10_metallopeptidase
IPR021190 Pept_M10A
IPR021158 Pept_M10A_Zn_BS
IPR006026 Peptidase_Metallo
IPR002477 Peptidoglycan-bd-like
IPR036365 PGBD-like_sf
IPR036366 PGBDSf
PANTHERiPTHR10201:SF30 PTHR10201:SF30, 1 hit
PfamiView protein in Pfam
PF00040 fn2, 3 hits
PF00045 Hemopexin, 4 hits
PF00413 Peptidase_M10, 1 hit
PF01471 PG_binding_1, 1 hit
PIRSFiPIRSF001191 Peptidase_M10A_matrix, 1 hit
PRINTSiPR00138 MATRIXIN
SMARTiView protein in SMART
SM00059 FN2, 3 hits
SM00120 HX, 4 hits
SM00235 ZnMc, 1 hit
SUPFAMiSSF47090 SSF47090, 1 hit
SSF50923 SSF50923, 1 hit
SSF57440 SSF57440, 3 hits
PROSITEiView protein in PROSITE
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

Sequencei

Sequence statusi: Complete.

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

P14780-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSLWQPLVLV LLVLGCCFAA PRQRQSTLVL FPGDLRTNLT DRQLAEEYLY
60 70 80 90 100
RYGYTRVAEM RGESKSLGPA LLLLQKQLSL PETGELDSAT LKAMRTPRCG
110 120 130 140 150
VPDLGRFQTF EGDLKWHHHN ITYWIQNYSE DLPRAVIDDA FARAFALWSA
160 170 180 190 200
VTPLTFTRVY SRDADIVIQF GVAEHGDGYP FDGKDGLLAH AFPPGPGIQG
210 220 230 240 250
DAHFDDDELW SLGKGVVVPT RFGNADGAAC HFPFIFEGRS YSACTTDGRS
260 270 280 290 300
DGLPWCSTTA NYDTDDRFGF CPSERLYTQD GNADGKPCQF PFIFQGQSYS
310 320 330 340 350
ACTTDGRSDG YRWCATTANY DRDKLFGFCP TRADSTVMGG NSAGELCVFP
360 370 380 390 400
FTFLGKEYST CTSEGRGDGR LWCATTSNFD SDKKWGFCPD QGYSLFLVAA
410 420 430 440 450
HEFGHALGLD HSSVPEALMY PMYRFTEGPP LHKDDVNGIR HLYGPRPEPE
460 470 480 490 500
PRPPTTTTPQ PTAPPTVCPT GPPTVHPSER PTAGPTGPPS AGPTGPPTAG
510 520 530 540 550
PSTATTVPLS PVDDACNVNI FDAIAEIGNQ LYLFKDGKYW RFSEGRGSRP
560 570 580 590 600
QGPFLIADKW PALPRKLDSV FEERLSKKLF FFSGRQVWVY TGASVLGPRR
610 620 630 640 650
LDKLGLGADV AQVTGALRSG RGKMLLFSGR RLWRFDVKAQ MVDPRSASEV
660 670 680 690 700
DRMFPGVPLD THDVFQYREK AYFCQDRFYW RVSSRSELNQ VDQVGYVTYD

ILQCPED
Length:707
Mass (Da):78,458
Last modified:November 24, 2009 - v3
Checksum:i2165AC8CA1466209
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti110F → L in BAG35956 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01378020A → V3 PublicationsCorresponds to variant dbSNP:rs1805088EnsemblClinVar.1
Natural variantiVAR_03700438N → S. Corresponds to variant dbSNP:rs41427445Ensembl.1
Natural variantiVAR_01378182E → K1 PublicationCorresponds to variant dbSNP:rs1805089Ensembl.1
Natural variantiVAR_020054127N → K1 PublicationCorresponds to variant dbSNP:rs3918252Ensembl.1
Natural variantiVAR_025165239R → H1 PublicationCorresponds to variant dbSNP:rs28763886EnsemblClinVar.1
Natural variantiVAR_013782279Q → R Common polymorphism; may be associated with susceptibility to IDD. 4 PublicationsCorresponds to variant dbSNP:rs17576EnsemblClinVar.1
Natural variantiVAR_025166571F → V1 PublicationCorresponds to variant dbSNP:rs35691798Ensembl.1
Natural variantiVAR_024595574R → P5 PublicationsCorresponds to variant dbSNP:rs2250889EnsemblClinVar.1
Natural variantiVAR_014742668R → Q2 PublicationsCorresponds to variant dbSNP:rs17577EnsemblClinVar.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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 No translation available.
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

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Cross-referencesi

Web resourcesi

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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 No translation available.
BC006093 mRNA Translation: AAH06093.1
D10051 Genomic DNA Translation: BAA20967.1
CCDSiCCDS13390.1
PIRiA34458
RefSeqiNP_004985.2, NM_004994.2
UniGeneiHs.297413

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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/B107-216[»]
A/B392-444[»]
4H3XX-ray1.76A/B107-216[»]
A/B392-444[»]
4H82X-ray1.90A/B/C/D110-444[»]
4HMAX-ray1.94A/B110-214[»]
A/B391-444[»]
4JIJX-ray1.70A/B107-444[»]
4JQGX-ray1.85A/B107-444[»]
4WZVX-ray1.65A/B110-444[»]
4XCTX-ray1.30A113-444[»]
5CUHX-ray1.83A/B107-444[»]
5I12X-ray1.59A113-444[»]
5TH6X-ray1.70A/B/C/D40-443[»]
5TH9X-ray3.00A/B/C40-443[»]
5UE3X-ray1.60A/B35-445[»]
5UE4X-ray1.80A/B35-445[»]
6ESMX-ray1.10A110-227[»]
ProteinModelPortaliP14780
SMRiP14780
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110461, 18 interactors
CORUMiP14780
DIPiDIP-29518N
IntActiP14780, 11 interactors
MINTiP14780
STRINGi9606.ENSP00000361405

Chemistry databases

BindingDBiP14780
ChEMBLiCHEMBL321
DrugBankiDB03683 2-{[Formyl(Hydroxy)Amino]Methyl}-4-Methylpentanoic Acid
DB05387 AE-941
DB01197 Captopril
DB01296 Glucosamine
DB00786 Marimastat
DB01017 Minocycline
DB05495 PG-530742
GuidetoPHARMACOLOGYi1633

Protein family/group databases

MEROPSiM10.004

PTM databases

GlyConnecti1494
6
iPTMnetiP14780
PhosphoSitePlusiP14780
UniCarbKBiP14780

Polymorphism and mutation databases

BioMutaiMMP9
DMDMi269849668

Proteomic databases

EPDiP14780
PaxDbiP14780
PeptideAtlasiP14780
PRIDEiP14780
ProteomicsDBi53082

Protocols and materials databases

DNASUi4318
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi4318
DisGeNETi4318
EuPathDBiHostDB:ENSG00000100985.7
GeneCardsiMMP9
H-InvDBiHIX0015874
HGNCiHGNC:7176 MMP9
HPAiCAB000348
CAB068199
CAB068200
CAB068201
HPA001238
HPA063909
MalaCardsiMMP9
MIMi120361 gene
603932 phenotype
613073 phenotype
neXtProtiNX_P14780
OpenTargetsiENSG00000100985
Orphaneti1040 Metaphyseal anadysplasia
PharmGKBiPA30889
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1565 Eukaryota
ENOG410XQ5D LUCA
GeneTreeiENSGT00910000144034
HOVERGENiHBG052484
InParanoidiP14780
KOiK01403
OMAiGFCPSER
OrthoDBiEOG091G02JB
PhylomeDBiP14780
TreeFamiTF315428

Enzyme and pathway databases

BRENDAi3.4.24.35 2681
ReactomeiR-HSA-1433557 Signaling by SCF-KIT
R-HSA-1442490 Collagen degradation
R-HSA-1474228 Degradation of the extracellular matrix
R-HSA-1592389 Activation of Matrix Metalloproteinases
R-HSA-2022090 Assembly of collagen fibrils and other multimeric structures
R-HSA-3928665 EPH-ephrin mediated repulsion of cells
R-HSA-6785807 Interleukin-4 and Interleukin-13 signaling
R-HSA-6798695 Neutrophil degranulation
SIGNORiP14780

Miscellaneous databases

ChiTaRSiMMP9 human
EvolutionaryTraceiP14780
GeneWikiiMMP9
GenomeRNAii4318
PROiPR:P14780
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000100985 Expressed in 154 organ(s), highest expression level in tibia
CleanExiHS_MMP9
GenevisibleiP14780 HS

Family and domain databases

CDDicd00062 FN2, 3 hits
cd00094 HX, 1 hit
cd04278 ZnMc_MMP, 1 hit
Gene3Di1.10.101.10, 1 hit
2.10.10.10, 3 hits
2.110.10.10, 1 hit
3.40.390.10, 1 hit
InterProiView protein in InterPro
IPR000562 FN_type2_dom
IPR036943 FN_type2_sf
IPR000585 Hemopexin-like_dom
IPR036375 Hemopexin-like_dom_sf
IPR018487 Hemopexin-like_repeat
IPR018486 Hemopexin_CS
IPR013806 Kringle-like
IPR033739 M10A_MMP
IPR024079 MetalloPept_cat_dom_sf
IPR028688 MMP9
IPR001818 Pept_M10_metallopeptidase
IPR021190 Pept_M10A
IPR021158 Pept_M10A_Zn_BS
IPR006026 Peptidase_Metallo
IPR002477 Peptidoglycan-bd-like
IPR036365 PGBD-like_sf
IPR036366 PGBDSf
PANTHERiPTHR10201:SF30 PTHR10201:SF30, 1 hit
PfamiView protein in Pfam
PF00040 fn2, 3 hits
PF00045 Hemopexin, 4 hits
PF00413 Peptidase_M10, 1 hit
PF01471 PG_binding_1, 1 hit
PIRSFiPIRSF001191 Peptidase_M10A_matrix, 1 hit
PRINTSiPR00138 MATRIXIN
SMARTiView protein in SMART
SM00059 FN2, 3 hits
SM00120 HX, 4 hits
SM00235 ZnMc, 1 hit
SUPFAMiSSF47090 SSF47090, 1 hit
SSF50923 SSF50923, 1 hit
SSF57440 SSF57440, 3 hits
PROSITEiView protein in PROSITE
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
ProtoNetiSearch...

Entry informationi

Entry nameiMMP9_HUMAN
AccessioniPrimary (citable) accession number: P14780
Secondary accession number(s): B2R7V9
, Q3LR70, Q8N725, Q9H4Z1, Q9UCJ9, Q9UCL1, Q9UDK2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 24, 2009
Last modified: November 7, 2018
This is version 233 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  7. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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