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HUMAN:MMP9

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Species (Taxon ID) Homo sapiens (Human). (9606)
Gene Name(s) MMP9 (synonyms: CLG4B)
Protein Name(s) Matrix metalloproteinase-9

MMP-9 92 kDa gelatinase 92 kDa type IV collagenase Gelatinase B GELB 67 kDa matrix metalloproteinase-9 82 kDa matrix metalloproteinase-9

External Links
UniProt P14780
EMBL J05070
M68343
M68344
M68345
M68346
M68347
M68348
M68349
M68350
M68351
M68352
M68353
M68354
M68355
AK313137
AF538844
DQ194553
AL162458
BC006093
D10051
CCDS CCDS13390.1
PIR A34458
RefSeq NP_004985.2
UniGene Hs.297413
PDB 1GKC
1GKD
1ITV
1L6J
1LKG
2OVX
2OVZ
2OW0
2OW1
2OW2
4H1Q
4H2E
4H3X
4H82
4HMA
4JIJ
4JQG
PDBsum 1GKC
1GKD
1ITV
1L6J
1LKG
2OVX
2OVZ
2OW0
2OW1
2OW2
4H1Q
4H2E
4H3X
4H82
4HMA
4JIJ
4JQG
ProteinModelPortal P14780
SMR P14780
BioGrid 110461
DIP DIP-29518N
IntAct P14780
MINT MINT-7709677
STRING 9606.ENSP00000361405
BindingDB P14780
ChEMBL CHEMBL2095216
DrugBank DB01197
DB01296
DB00786
DB01017
GuidetoPHARMACOLOGY 1633
MEROPS M10.004
PhosphoSite P14780
UniCarbKB P14780
DMDM 269849668
PaxDb P14780
PeptideAtlas P14780
PRIDE P14780
DNASU 4318
Ensembl ENST00000372330
GeneID 4318
KEGG hsa:4318
UCSC uc002xqz.3
CTD 4318
GeneCards GC20P044637
H-InvDB HIX0015874
HGNC HGNC:7176
HPA CAB000348
HPA001238
MIM 120361
603932
613073
neXtProt NX_P14780
Orphanet 1040
PharmGKB PA30889
eggNOG NOG328372
GeneTree ENSGT00760000119132
HOVERGEN HBG052484
InParanoid P14780
KO K01403
OMA EGDLKWH
OrthoDB EOG70KGNX
PhylomeDB P14780
TreeFam TF315428
Reactome REACT_111040
REACT_118572
REACT_118682
REACT_150180
REACT_150401
REACT_228189
ChiTaRS MMP9
EvolutionaryTrace P14780
GeneWiki MMP9
GenomeRNAi 4318
NextBio 16989
PRO PR:P14780
Proteomes UP000005640
Bgee P14780
CleanEx HS_MMP9
Genevestigator P14780
GO GO:0005576
GO:0005615
GO:0070062
GO:0005578
GO:0005518
GO:0004175
GO:0042802
GO:0004222
GO:0008270
GO:0030574
GO:0007566
GO:0035987
GO:0022617
GO:0030198
GO:0050900
GO:0030225
GO:2001258
GO:0001503
GO:0043065
GO:0051549
GO:1900122
GO:0006508
GO:0001501
Gene3D 2.10.10.10
2.110.10.10
3.40.390.10
InterPro IPR000562
IPR000585
IPR018487
IPR018486
IPR013806
IPR024079
IPR028688
IPR001818
IPR021190
IPR021158
IPR006026
IPR002477
IPR006970
PANTHER PTHR10201:SF30
Pfam PF00040
PF00045
PF00413
PF01471
PF04886
PRINTS PR00138
SMART SM00059
SM00120
SM00235
SUPFAM SSF47090
SSF50923
SSF57440
PROSITE PS00546
PS00023
PS51092
PS00024
PS51642
PS00142

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0045742

positive regulation of epidermal growth factor receptor signaling pathway

PMID:22984561[1]

ECO:0000315

P

Figure 4A shows that silencing uPAR and MMP-9 significantly inhibits the phosphorylation of the EGFR pathway.

complete
CACAO 5037

GO:0001934

positive regulation of protein phosphorylation

PMID:22984561[1]

ECO:0000315

P

Figure 4B shows, through pUM transfection, that silencing uPAR and MMP-9 significantly lowers the amount of phosphorylated STAT protein in the nucleus.

complete
CACAO 5186

GO:0043388

positive regulation of DNA binding

PMID:22984561[1]

ECO:0000314

P

Figure 4C shows (through EMSA) that downregulation of uPAR and MMP-9 significantly inhibits binding activity of nuclear extract to STAT3 DNA probe.

complete
CACAO 5187

GO:0008633

activation of pro-apoptotic gene products

PMID:22984561[1]

ECO:0000315

P

Figure 2

complete
CACAO 5199

GO:0001934

positive regulation of protein phosphorylation

PMID:22984561[1]

ECO:0000315

P

Figure 4B shows, through pUM transfection, that silencing uPAR and MMP-9 significantly lowers the amount of phosphorylated STAT protein in the nucleus.

complete
CACAO 5306

GO:0043066

negative regulation of apoptotic process

PMID:22984561[1]

ECO:0000315

P

Figure 1C and 1D show, through the Apo BrdU Assay and the Annexin-V assay, that inhibition of uPAR and MMP-9 induce apoptosis in Daoy and D283 cells.

complete
CACAO 5686

GO:2001243

negative regulation of intrinsic apoptotic signaling pathway

PMID:22984561[1]

ECO:0000315

P

Figure 2 shows that downregulation of uPAR and MMP9 increases levels of gene products that induce apoptosis, showing that normal function negatively regulates apoptotic signaling pathways.

complete
CACAO 5772

GO:0090200

positive regulation of release of cytochrome c from mitochondria

PMID:22984561[1]

ECO:0000315

P

Fig. 2 shows that downregulation of uPAR and MMP9 in Medulloblastoma cells causes a decrease in the amount of cytosolic cytochrome c, indicating a positive regulation of release of cytochrome c from mitochondria.

complete
CACAO 5878

GO:2001268

negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway

PMID:22984561[1]

ECO:0000315

P

Fig. 3 showed that down regulation of uPAR and MMP9 in Daoy and D283 cells activates caspase activity.

complete
CACAO 6191

GO:0008237

metalloendopeptidase activity

PMID:22024282[2]

ECO:0000315

F

Figure 4a-c MMP-9 induces cleavage of CD44 into the extracellular domain and the intracellular domain in 4910 and 5310 xenograft cells. The interaction of MMP-9 with CD44 induced CD44 cleavage which was inhibited by both transcriptional knockdown of MMP-9 and with MMP-9 specific inhibitor. Further, supplementation of purified and activated human MMP-9 (hMMP-9) in MMP-9-knockdown cells resumed CD44 cleavage and migration. Additionally, activated hMMP-9 protein induced cleavage of recombinant human CD44.

complete
CACAO 12123

part_of

GO:0062023

collagen-containing extracellular matrix

PMID:28344315[3]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

part_of:(UBERON:0002371)

Seeded From UniProt

complete

involved_in

GO:1904645

response to amyloid-beta

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P41245

P

occurs_in:(CL:0000129)

Seeded From UniProt

complete

involved_in

GO:0030335

positive regulation of cell migration

PMID:28280358[4]

ECO:0000316

genetic interaction evidence used in manual assertion

RNAcentral:URS000029D9F1_9606

P

Seeded From UniProt

complete

involved_in

GO:2000697

negative regulation of epithelial cell differentiation involved in kidney development

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:P41245

P

occurs_in:(CL:0002570)

Seeded From UniProt

complete

involved_in

GO:0034614

cellular response to reactive oxygen species

PMID:26514923[5]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0071276

cellular response to cadmium ion

PMID:26514923[5]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0008237

metallopeptidase activity

PMID:26514923[5]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0005576

extracellular region

PMID:27068509[6]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

part_of:(UBERON:0007318)

Seeded From UniProt

complete

involved_in

GO:1904707

positive regulation of vascular smooth muscle cell proliferation

PMID:18667463[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

occurs_in:(UBERON:0002012)

Seeded From UniProt

complete

part_of

GO:0005615

extracellular space

PMID:25645918[8]

ECO:0000314

direct assay evidence used in manual assertion

C

part_of:(UBERON:0007311)

Seeded From UniProt

complete

part_of

GO:0005615

extracellular space

PMID:24236012[9]

ECO:0000314

direct assay evidence used in manual assertion

C

part_of:(CL:0000235)

Seeded From UniProt

complete

enables

GO:0008237

metallopeptidase activity

PMID:24236012[9]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:2001268

negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway

PMID:22984561[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0043066

negative regulation of apoptotic process

PMID:22984561[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0001934

positive regulation of protein phosphorylation

PMID:22984561[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0090200

positive regulation of release of cytochrome c from mitochondria

PMID:22984561[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:2001243

negative regulation of intrinsic apoptotic signaling pathway

PMID:22984561[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0043388

positive regulation of DNA binding

PMID:22984561[1]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0045742

positive regulation of epidermal growth factor receptor signaling pathway

PMID:22984561[1]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

PMID:15863497[10]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

PMID:19022250[11]

ECO:0000314

direct assay evidence used in manual assertion

P

has_input:(UniProtKB:P37840)

Seeded From UniProt

complete

enables

GO:0004175

endopeptidase activity

PMID:19022250[11]

ECO:0000314

direct assay evidence used in manual assertion

F

has_direct_input:(UniProtKB:P37840)

Seeded From UniProt

complete

part_of

GO:0070062

extracellular exosome

PMID:23533145[12]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0035987

endodermal cell differentiation

PMID:23154389[13]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:2001258

negative regulation of cation channel activity

PMID:24164424[14]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:1900122

positive regulation of receptor binding

PMID:24164424[14]

ECO:0000314

direct assay evidence used in manual assertion

P

has_input:(UniProtKB:Q16281)

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

PMID:24164424[14]

ECO:0000314

direct assay evidence used in manual assertion

P

has_input:(UniProtKB:Q16281)|has_input:(UniProtKB:P29973)

Seeded From UniProt

complete

enables

GO:0004222

metalloendopeptidase activity

PMID:24164424[14]

ECO:0000314

direct assay evidence used in manual assertion

F

has_input:(UniProtKB:Q16281)|has_input:(UniProtKB:P29973)

Seeded From UniProt

complete

involved_in

GO:0051549

positive regulation of keratinocyte migration

PMID:17704059[15]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

PMID:2551898[16]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005615

extracellular space

PMID:2551898[16]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004222

metalloendopeptidase activity

PMID:2551898[16]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004222

metalloendopeptidase activity

PMID:16192646[17]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0030574

collagen catabolic process

PMID:21873635[18]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:101900
MGI:MGI:1276107
MGI:MGI:1340026
MGI:MGI:97008
MGI:MGI:97009
MGI:MGI:97011
PANTHER:PTN001303987
RGD:621316
RGD:621320
UniProtKB:P45452

P

Seeded From UniProt

complete

involved_in

GO:0030198

extracellular matrix organization

PMID:21873635[18]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

FB:FBgn0033438
FB:FBgn0035049
MGI:MGI:1340026
MGI:MGI:1353466
MGI:MGI:97008
MGI:MGI:97011
PANTHER:PTN001303987
UniProtKB:P45452
WB:WBGene00006987
ZFIN:ZDB-GENE-040426-2132

P

Seeded From UniProt

complete

part_of

GO:0005615

extracellular space

PMID:21873635[18]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:97005
MGI:MGI:97009
PANTHER:PTN000810753
RGD:3100
RGD:620196
RGD:621316
RGD:621317
RGD:621320
RGD:631408
UniProtKB:B5DFD5
UniProtKB:P02790
UniProtKB:P08253
UniProtKB:P14780
UniProtKB:P22894
UniProtKB:P39900
UniProtKB:P50281
UniProtKB:Q90611

C

Seeded From UniProt

complete

enables

GO:0004222

metalloendopeptidase activity

PMID:21873635[18]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

FB:FBgn0033438
MGI:MGI:101900
MGI:MGI:1340026
MGI:MGI:1341867
MGI:MGI:97009
MGI:MGI:97011
PANTHER:PTN001303987
RGD:620196
TAIR:locus:2020548
TAIR:locus:2025891
TAIR:locus:2032467
TAIR:locus:2055605
TAIR:locus:2130928
UniProtKB:O60882
UniProtKB:O75900
UniProtKB:P03956
UniProtKB:P14780
UniProtKB:P39900
UniProtKB:P45452
UniProtKB:P51512
UniProtKB:Q90611
UniProtKB:Q99542

F

Seeded From UniProt

complete

enables

GO:0004252

serine-type endopeptidase activity

PMID:17428795[19]

ECO:0000269

experimental evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004222

metalloendopeptidase activity

PMID:9789069[20]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:23601700[21]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P14780

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:18077379[22]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P14780

F

Seeded From UniProt

complete

enables

GO:0042802

identical protein binding

PMID:17937912[23]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P14780

F

Seeded From UniProt

complete

involved_in

GO:2000697

negative regulation of epithelial cell differentiation involved in kidney development

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P41245
ensembl:ENSMUSP00000017881

P

Seeded From UniProt

complete

involved_in

GO:1904645

response to amyloid-beta

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P41245
ensembl:ENSMUSP00000017881

P

Seeded From UniProt

complete

involved_in

GO:0043065

positive regulation of apoptotic process

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P41245
ensembl:ENSMUSP00000017881

P

Seeded From UniProt

complete

involved_in

GO:0030574

collagen catabolic process

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P41245
ensembl:ENSMUSP00000017881

P

Seeded From UniProt

complete

involved_in

GO:0030198

extracellular matrix organization

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P41245
ensembl:ENSMUSP00000017881

P

Seeded From UniProt

complete

enables

GO:0008237

metallopeptidase activity

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P41245
ensembl:ENSMUSP00000017881

F

Seeded From UniProt

complete

enables

GO:0008233

peptidase activity

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P41245
ensembl:ENSMUSP00000017881

F

Seeded From UniProt

complete

involved_in

GO:0007566

embryo implantation

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P41245
ensembl:ENSMUSP00000017881

P

Seeded From UniProt

complete

enables

GO:0004222

metalloendopeptidase activity

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P41245
ensembl:ENSMUSP00000017881

F

Seeded From UniProt

complete

involved_in

GO:0001501

skeletal system development

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P41245
ensembl:ENSMUSP00000017881

P

Seeded From UniProt

complete

involved_in

GO:0001503

ossification

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR028688

P

Seeded From UniProt

complete

enables

GO:0004222

metalloendopeptidase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001818
InterPro:IPR021158
InterPro:IPR021190
InterPro:IPR028688

F

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001818
InterPro:IPR006026
InterPro:IPR021158
InterPro:IPR021190
InterPro:IPR028688

P

Seeded From UniProt

complete

enables

GO:0008237

metallopeptidase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR006026
InterPro:IPR024079
InterPro:IPR033739

F

Seeded From UniProt

complete

enables

GO:0008270

zinc ion binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001818
InterPro:IPR006026
InterPro:IPR021158
InterPro:IPR021190
InterPro:IPR033739

F

Seeded From UniProt

complete

involved_in

GO:0030574

collagen catabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR028688

P

Seeded From UniProt

complete

part_of

GO:0031012

extracellular matrix

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001818
InterPro:IPR021158
InterPro:IPR021190

C

Seeded From UniProt

complete

involved_in

GO:0050900

leukocyte migration

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR028688

P

Seeded From UniProt

complete

involved_in

GO:0150077

regulation of neuroinflammatory response

PMID:25049354[24]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

  • occurs_in:(CL:0000129)
  • regulates_o_occurs_in:(CL:0000129)

Seeded From UniProt

complete

involved_in

GO:0030335

positive regulation of cell migration

PMID:23675531[25]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0030225

macrophage differentiation

PMID:2551898[16]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0008270

zinc ion binding

PMID:2551898[16]

ECO:0000304

author statement supported by traceable reference used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0005518

collagen binding

PMID:2551898[16]

ECO:0000304

author statement supported by traceable reference used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:1904813

ficolin-1-rich granule lumen

Reactome:R-HSA-6800434

ECO:0000304

author statement supported by traceable reference used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:1904724

tertiary granule lumen

Reactome:R-HSA-6798745

ECO:0000304

author statement supported by traceable reference used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0048013

ephrin receptor signaling pathway

Reactome:R-HSA-2682334

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0043312

neutrophil degranulation

Reactome:R-HSA-6798695

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0030574

collagen catabolic process

Reactome:R-HSA-1442490

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0022617

extracellular matrix disassembly

Reactome:R-HSA-1474228

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0019221

cytokine-mediated signaling pathway

Reactome:R-HSA-6785807

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005576

extracellular region

Reactome:R-NUL-3814821
Reactome:R-NUL-2533972
Reactome:R-NUL-2484948
Reactome:R-NUL-2484927
Reactome:R-NUL-2484859
Reactome:R-HSA-8943959
Reactome:R-HSA-6800434
Reactome:R-HSA-6798745
Reactome:R-HSA-6789615
Reactome:R-HSA-3928657
Reactome:R-HSA-3827958
Reactome:R-HSA-2485148
Reactome:R-HSA-2168923
Reactome:R-HSA-1604722
Reactome:R-HSA-1604690
Reactome:R-HSA-1602454
Reactome:R-HSA-1592436
Reactome:R-HSA-1566962
Reactome:R-HSA-1564164
Reactome:R-HSA-1564142
Reactome:R-HSA-1564112
Reactome:R-HSA-1474213
Reactome:R-HSA-1454791
Reactome:R-HSA-1454757
Reactome:R-HSA-1433374

ECO:0000304

author statement supported by traceable reference used in manual assertion

























C

Seeded From UniProt

complete

enables

GO:0004222

metalloendopeptidase activity

Reactome:R-NUL-2484927

ECO:0000304

author statement supported by traceable reference used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008233

peptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0645

F

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

part_of

GO:0005576

extracellular region

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0964

C

Seeded From UniProt

complete

enables

GO:0008237

metallopeptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0482

F

Seeded From UniProt

complete

involved_in

GO:0030574

collagen catabolic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0177

P

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0645

P

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.00 1.01 1.02 1.03 1.04 1.05 1.06 1.07 1.08 1.09 1.10 1.11 1.12 1.13 1.14 1.15 Kotipatruni, RR et al. (2012) Apoptosis induced by knockdown of uPAR and MMP-9 is mediated by inactivation of EGFR/STAT3 signaling in medulloblastoma. PLoS ONE 7 e44798 PubMed GONUTS page
  2. Chetty, C et al. (2012) MMP-9 induces CD44 cleavage and CD44 mediated cell migration in glioblastoma xenograft cells. Cell. Signal. 24 549-59 PubMed GONUTS page
  3. Glavey, SV et al. (2017) Proteomic characterization of human multiple myeloma bone marrow extracellular matrix. Leukemia 31 2426-2434 PubMed GONUTS page
  4. Luan, W et al. (2017) miR-204-5p acts as a tumor suppressor by targeting matrix metalloproteinases-9 and B-cell lymphoma-2 in malignant melanoma. Onco Targets Ther 10 1237-1246 PubMed GONUTS page
  5. 5.0 5.1 5.2 Lian, S et al. (2015) Cadmium induces matrix metalloproteinase-9 expression via ROS-dependent EGFR, NF-кB, and AP-1 pathways in human endothelial cells. Toxicology 338 104-16 PubMed GONUTS page
  6. Barallobre-Barreiro, J et al. (2016) Extracellular matrix remodelling in response to venous hypertension: proteomics of human varicose veins. Cardiovasc. Res. 110 419-30 PubMed GONUTS page
  7. El-Bizri, N et al. (2008) SM22alpha-targeted deletion of bone morphogenetic protein receptor 1A in mice impairs cardiac and vascular development, and influences organogenesis. Development 135 2981-91 PubMed GONUTS page
  8. Thaysen-Andersen, M et al. (2015) Human neutrophils secrete bioactive paucimannosidic proteins from azurophilic granules into pathogen-infected sputum. J. Biol. Chem. 290 8789-802 PubMed GONUTS page
  9. 9.0 9.1 De Clercq, S et al. (2013) L-plastin nanobodies perturb matrix degradation, podosome formation, stability and lifetime in THP-1 macrophages. PLoS ONE 8 e78108 PubMed GONUTS page
  10. Sung, JY et al. (2005) Proteolytic cleavage of extracellular secreted {alpha}-synuclein via matrix metalloproteinases. J. Biol. Chem. 280 25216-24 PubMed GONUTS page
  11. 11.0 11.1 Levin, J et al. (2009) Increased alpha-synuclein aggregation following limited cleavage by certain matrix metalloproteinases. Exp. Neurol. 215 201-8 PubMed GONUTS page
  12. Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page
  13. Brafman, DA et al. (2013) Regulation of endodermal differentiation of human embryonic stem cells through integrin-ECM interactions. Cell Death Differ. 20 369-81 PubMed GONUTS page
  14. 14.0 14.1 14.2 14.3 Meighan, SE et al. (2013) Cyclic nucleotide-gated channel subunit glycosylation regulates matrix metalloproteinase-dependent changes in channel gating. Biochemistry 52 8352-62 PubMed GONUTS page
  15. Zigrino, P et al. (2007) Role of ADAM-9 disintegrin-cysteine-rich domains in human keratinocyte migration. J. Biol. Chem. 282 30785-93 PubMed GONUTS page
  16. 16.0 16.1 16.2 16.3 16.4 16.5 Wilhelm, SM et al. (1989) SV40-transformed human lung fibroblasts secrete a 92-kDa type IV collagenase which is identical to that secreted by normal human macrophages. J. Biol. Chem. 264 17213-21 PubMed GONUTS page
  17. Stenman, M et al. (2005) Trypsin-2 degrades human type II collagen and is expressed and activated in mesenchymally transformed rheumatoid arthritis synovitis tissue. Am. J. Pathol. 167 1119-24 PubMed GONUTS page
  18. 18.0 18.1 18.2 18.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  19. Litterst, C et al. (2007) Ligand binding and calcium influx induce distinct ectodomain/gamma-secretase-processing pathways of EphB2 receptor. J. Biol. Chem. 282 16155-63 PubMed GONUTS page
  20. Takahashi, C et al. (1998) Regulation of matrix metalloproteinase-9 and inhibition of tumor invasion by the membrane-anchored glycoprotein RECK. Proc. Natl. Acad. Sci. U.S.A. 95 13221-6 PubMed GONUTS page
  21. Malla, N et al. (2013) In vitro reconstitution of complexes between pro-matrix metalloproteinase-9 and the proteoglycans serglycin and versican. FEBS J. 280 2870-87 PubMed GONUTS page
  22. Ardi, VC et al. (2007) Human neutrophils uniquely release TIMP-free MMP-9 to provide a potent catalytic stimulator of angiogenesis. Proc. Natl. Acad. Sci. U.S.A. 104 20262-7 PubMed GONUTS page
  23. Rosenblum, G et al. (2007) Insights into the structure and domain flexibility of full-length pro-matrix metalloproteinase-9/gelatinase B. Structure 15 1227-36 PubMed GONUTS page
  24. Lee, EJ et al. (2014) Matrix metalloproteinase-8 plays a pivotal role in neuroinflammation by modulating TNF-α activation. J. Immunol. 193 2384-93 PubMed GONUTS page
  25. Xi, P et al. (2013) DDRGK1 regulates NF-κB activity by modulating IκBα stability. PLoS ONE 8 e64231 PubMed GONUTS page