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Protein

Matrix metalloproteinase-9

Gene

MMP9

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

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

Enzyme 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
  • metalloendopeptidase activity Source: UniProtKB
  • metallopeptidase activity Source: UniProtKB
  • serine-type endopeptidase activity Source: Reactome
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • collagen catabolic process Source: Reactome
  • embryo implantation Source: Ensembl
  • endodermal cell differentiation Source: UniProtKB
  • ephrin receptor signaling pathway Source: Reactome
  • extracellular matrix disassembly Source: Reactome
  • leukocyte migration Source: InterPro
  • macrophage differentiation Source: UniProtKB
  • negative regulation of apoptotic process Source: CACAO
  • negative regulation of cation channel activity Source: UniProtKB
  • negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway Source: CACAO
  • negative regulation of intrinsic apoptotic signaling pathway Source: CACAO
  • ossification Source: InterPro
  • positive regulation of DNA binding Source: CACAO
  • positive regulation of epidermal growth factor receptor signaling pathway Source: CACAO
  • positive regulation of keratinocyte migration Source: BHF-UCL
  • positive regulation of protein phosphorylation Source: CACAO
  • positive regulation of receptor binding Source: UniProtKB
  • positive regulation of release of cytochrome c from mitochondria Source: CACAO
  • positive regulation of vascular smooth muscle cell proliferation Source: BHF-UCL
  • proteolysis Source: UniProtKB
  • 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

BioCyciZFISH:HS02175-MONOMER.
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-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 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
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:7176. MMP9.

Subcellular locationi

GO - Cellular componenti

  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
  • proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

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
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_013782279Q → R Common polymorphism; may be associated with susceptibility to IDD. 4 PublicationsCorresponds to variant rs17576dbSNPEnsembl.1
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.
DrugBankiDB01197. Captopril.
DB01296. Glucosamine.
DB00786. Marimastat.
DB01017. Minocycline.
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...)Sequence analysis1
Glycosylationi120N-linked (GlcNAc...)Sequence analysis1
Glycosylationi127N-linked (GlcNAc...)Sequence 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.

PTM databases

iPTMnetiP14780.
PhosphoSitePlusiP14780.
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
(Microbial infection) Expression induced by M.bovis MPB83 (at protein level) (PubMed:20800577).1 Publication

Gene expression databases

BgeeiENSG00000100985.
CleanExiHS_MMP9.
GenevisibleiP14780. HS.

Organism-specific databases

HPAiCAB000348.
CAB068199.
CAB068200.
CAB068201.
HPA001238.
HPA063909.

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
TIMP1P010332EBI-1382326,EBI-712536
VCANP136113EBI-1382326,EBI-8515977

GO - Molecular functioni

  • collagen binding Source: UniProtKB

Protein-protein interaction databases

BioGridi110461. 17 interactors.
DIPiDIP-29518N.
IntActiP14780. 10 interactors.
MINTiMINT-7709677.
STRINGi9606.ENSP00000361405.

Chemistry databases

BindingDBiP14780.

Structurei

Secondary structure

1707
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi41 – 51Combined sources11
Helixi68 – 78Combined sources11
Helixi88 – 94Combined sources7
Beta strandi103 – 105Combined sources3
Beta strandi112 – 115Combined sources4
Beta strandi117 – 125Combined sources9
Beta strandi130 – 132Combined sources3
Helixi134 – 149Combined sources16
Beta strandi151 – 153Combined sources3
Beta strandi155 – 158Combined sources4
Beta strandi160 – 162Combined sources3
Beta strandi165 – 171Combined sources7
Beta strandi176 – 178Combined sources3
Beta strandi183 – 186Combined sources4
Beta strandi189 – 191Combined sources3
Beta strandi194 – 196Combined sources3
Turni197 – 200Combined sources4
Beta strandi202 – 205Combined sources4
Beta strandi213 – 216Combined sources4
Beta strandi221 – 225Combined sources5
Beta strandi232 – 238Combined sources7
Beta strandi240 – 243Combined sources4
Beta strandi255 – 261Combined sources7
Helixi262 – 265Combined sources4
Beta strandi268 – 270Combined sources3
Turni274 – 276Combined sources3
Beta strandi279 – 283Combined sources5
Beta strandi290 – 294Combined sources5
Beta strandi297 – 301Combined sources5
Beta strandi313 – 319Combined sources7
Helixi320 – 323Combined sources4
Beta strandi326 – 328Combined sources3
Helixi333 – 335Combined sources3
Turni340 – 344Combined sources5
Beta strandi349 – 353Combined sources5
Beta strandi356 – 358Combined sources3
Beta strandi372 – 378Combined sources7
Helixi379 – 382Combined sources4
Beta strandi385 – 387Combined sources3
Beta strandi392 – 394Combined sources3
Helixi395 – 406Combined sources12
Beta strandi408 – 411Combined sources4
Beta strandi420 – 422Combined sources3
Helixi433 – 443Combined sources11
Beta strandi444 – 446Combined sources3
Helixi450 – 460Combined sources11
Helixi515 – 517Combined sources3
Beta strandi522 – 527Combined sources6
Beta strandi530 – 535Combined sources6
Beta strandi538 – 542Combined sources5
Beta strandi545 – 547Combined sources3
Beta strandi551 – 555Combined sources5
Helixi556 – 559Combined sources4
Beta strandi568 – 572Combined sources5
Turni574 – 576Combined sources3
Beta strandi579 – 583Combined sources5
Beta strandi586 – 591Combined sources6
Beta strandi594 – 600Combined sources7
Helixi601 – 604Combined sources4
Beta strandi615 – 618Combined sources4
Beta strandi623 – 628Combined sources6
Beta strandi631 – 636Combined sources6
Turni637 – 640Combined sources4
Helixi644 – 646Combined sources3
Helixi650 – 653Combined sources4
Beta strandi662 – 667Combined sources6
Beta strandi670 – 675Combined sources6
Beta strandi678 – 683Combined sources6
Beta strandi690 – 696Combined sources7
Turni697 – 700Combined sources4

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/B107-461[»]
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[»]
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
Contains 3 fibronectin type-II domains.PROSITE-ProRule annotation
Contains 4 hemopexin repeats.Curated

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00760000118870.
HOVERGENiHBG052484.
InParanoidiP14780.
KOiK01403.
OMAiGFCPSER.
OrthoDBiEOG091G02JB.
PhylomeDBiP14780.
TreeFamiTF315428.

Family and domain databases

CDDicd00062. FN2. 3 hits.
cd00094. HX. 1 hit.
cd04278. ZnMc_MMP. 1 hit.
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.
IPR033739. M10A_MMP.
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.
[Graphical view]
PANTHERiPTHR10201:SF30. PTHR10201:SF30. 3 hits.
PfamiPF00040. fn2. 3 hits.
PF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 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

        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 → V.3 PublicationsCorresponds to variant rs1805088dbSNPEnsembl.1
Natural variantiVAR_03700438N → S.Corresponds to variant rs41427445dbSNPEnsembl.1
Natural variantiVAR_01378182E → K.1 PublicationCorresponds to variant rs1805089dbSNPEnsembl.1
Natural variantiVAR_020054127N → K.1 PublicationCorresponds to variant rs3918252dbSNPEnsembl.1
Natural variantiVAR_025165239R → H.1 PublicationCorresponds to variant rs28763886dbSNPEnsembl.1
Natural variantiVAR_013782279Q → R Common polymorphism; may be associated with susceptibility to IDD. 4 PublicationsCorresponds to variant rs17576dbSNPEnsembl.1
Natural variantiVAR_025166571F → V.1 PublicationCorresponds to variant rs35691798dbSNPEnsembl.1
Natural variantiVAR_024595574R → P.5 PublicationsCorresponds to variant rs2250889dbSNPEnsembl.1
Natural variantiVAR_014742668R → Q.2 PublicationsCorresponds to variant rs17577dbSNPEnsembl.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. 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.

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:
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. 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.

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/B107-461[»]
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[»]
ProteinModelPortaliP14780.
SMRiP14780.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110461. 17 interactors.
DIPiDIP-29518N.
IntActiP14780. 10 interactors.
MINTiMINT-7709677.
STRINGi9606.ENSP00000361405.

Chemistry databases

BindingDBiP14780.
ChEMBLiCHEMBL321.
DrugBankiDB01197. Captopril.
DB01296. Glucosamine.
DB00786. Marimastat.
DB01017. Minocycline.
GuidetoPHARMACOLOGYi1633.

Protein family/group databases

MEROPSiM10.004.

PTM databases

iPTMnetiP14780.
PhosphoSitePlusiP14780.
UniCarbKBiP14780.

Polymorphism and mutation databases

BioMutaiMMP9.
DMDMi269849668.

Proteomic databases

EPDiP14780.
PaxDbiP14780.
PeptideAtlasiP14780.
PRIDEiP14780.

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.
GeneCardsiMMP9.
H-InvDBHIX0015874.
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.
GeneTreeiENSGT00760000118870.
HOVERGENiHBG052484.
InParanoidiP14780.
KOiK01403.
OMAiGFCPSER.
OrthoDBiEOG091G02JB.
PhylomeDBiP14780.
TreeFamiTF315428.

Enzyme and pathway databases

BioCyciZFISH:HS02175-MONOMER.
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-6798695. Neutrophil degranulation.
SIGNORiP14780.

Miscellaneous databases

ChiTaRSiMMP9. human.
EvolutionaryTraceiP14780.
GeneWikiiMMP9.
GenomeRNAii4318.
PROiP14780.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000100985.
CleanExiHS_MMP9.
GenevisibleiP14780. HS.

Family and domain databases

CDDicd00062. FN2. 3 hits.
cd00094. HX. 1 hit.
cd04278. ZnMc_MMP. 1 hit.
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.
IPR033739. M10A_MMP.
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.
[Graphical view]
PANTHERiPTHR10201:SF30. PTHR10201:SF30. 3 hits.
PfamiPF00040. fn2. 3 hits.
PF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 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]
ProtoNetiSearch...

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: November 30, 2016
This is version 215 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.