HUMAN:MMP9

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	has_direct_input:(UniProtKB:P37840) occurs_in:(GO:0005576)	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
edit table

Notes

References

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

↑ ^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
↑ 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
↑ Glavey, SV et al. (2017) Proteomic characterization of human multiple myeloma bone marrow extracellular matrix. Leukemia 31 2426-2434 PubMed GONUTS page
↑ 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
↑ ^5.0 ^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
↑ 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
↑ 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
↑ 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
↑ ^9.0 ^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
↑ Sung, JY et al. (2005) Proteolytic cleavage of extracellular secreted {alpha}-synuclein via matrix metalloproteinases. J. Biol. Chem. 280 25216-24 PubMed GONUTS page
↑ ^11.0 ^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
↑ 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
↑ 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
↑ ^14.0 ^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
↑ 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
↑ ^16.0 ^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
↑ 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
↑ ^18.0 ^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
↑ 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
↑ 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
↑ 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
↑ 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
↑ 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
↑ 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
↑ Xi, P et al. (2013) DDRGK1 regulates NF-κB activity by modulating IκBα stability. PLoS ONE 8 e64231 PubMed GONUTS page

[PMID:22984561-1] 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

[PMID:22024282-2] 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

[PMID:28344315-3] Glavey, SV et al. (2017) Proteomic characterization of human multiple myeloma bone marrow extracellular matrix. Leukemia 31 2426-2434 PubMed GONUTS page

[PMID:28280358-4] 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

[PMID:26514923-5] 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

[PMID:27068509-6] 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

[PMID:18667463-7] 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

[PMID:25645918-8] 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

[PMID:24236012-9] 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

[PMID:15863497-10] Sung, JY et al. (2005) Proteolytic cleavage of extracellular secreted {alpha}-synuclein via matrix metalloproteinases. J. Biol. Chem. 280 25216-24 PubMed GONUTS page

[PMID:19022250-11] 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

[PMID:23533145-12] 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

[PMID:23154389-13] 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

[PMID:24164424-14] 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

[PMID:17704059-15] 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

[PMID:2551898-16] 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

[PMID:16192646-17] 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

[PMID:21873635-18] 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

[PMID:17428795-19] 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

[PMID:9789069-20] 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

[PMID:23601700-21] 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

[PMID:18077379-22] 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

[PMID:17937912-23] 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

[PMID:25049354-24] 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

[PMID:23675531-25] Xi, P et al. (2013) DDRGK1 regulates NF-κB activity by modulating IκBα stability. PLoS ONE 8 e64231 PubMed GONUTS page

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

[9]

[10]

[11]

[12]

[13]

[14]

[15]

[16]

[17]

[18]

[19]

[20]

[21]

[22]

[23]

[24]

[25]

HUMAN:MMP9

Contents

Annotations

Notes

References

c

e

f

h

i

l

m

n

o

p

r

s

t

v

z

Navigation menu

Personal tools

Namespaces

Variants

Views

More

Search

Navigation

Cacao

Links

Tools