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MMP2 (human)

Overview MMP2 Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3beta in vitro. Interacts (via the C-terminal hemopexin-like domains- containing region) with the integrin alpha-V/beta-3; the interaction promotes vascular invasion in angiogenic vessels and melamoma cells. Interacts (via the C-terminal PEX domain) with TIMP2 (via the C-terminal); the interaction inhibits the degradation activity. Interacts with GSK3B. Aspirin appears to inhibit expression. Produced by normal skin fibroblasts. PEX is expressed in a number of tumors including gliomas, breast and prostate. Inhibited by histatin-3 1/24 (histatin-5). Belongs to the peptidase M10A family. Note: This description may include information from UniProtKB. Protein type: EC 3.4.24.24; Protease; Apoptosis; Motility/polarity/chemotaxis; Secreted, signal peptide; Secreted; Cell development/differentiation Cellular Component: extracellular space; proteinaceous extracellular matrix; sarcomere; plasma membrane; extracellular region; nucleus Molecular Function: protein binding; zinc ion binding; metalloendopeptidase activity; serine-type endopeptidase activity Biological Process: collagen catabolic process; extracellular matrix disassembly; extracellular matrix organization and biogenesis; intramembranous ossification; response to hypoxia; angiogenesis; proteolysis; blood vessel maturation; embryo implantation Reference #:  P08253 (UniProtKB) Alt. Names/Synonyms: 72 kDa gelatinase; 72 kDa type IV collagenase; CLG4; CLG4A; collagenase type IV-A; Gelatinase A; matrix metallopeptidase 2 (gelatinase A, 72kDa gelatinase, 72kDa type IV collagenase); Matrix metalloproteinase-2; matrix metalloproteinase-II; MMP-2; MMP-II; MMP2; MONA; neutrophil gelatinase; PEX; TBE-1 Gene Symbols: MMP2 Molecular weight: 73,882 Da Basal Isoelectric point: 5.26  Predict pI for various phosphorylation states CST Pathways:  Angiogenesis  |  GPCRs Signaling to MAPK/Erk Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below MMP2 1CK7 - A=30-660 (human) 1CXW - A=278-336 (human) 1EAK - A/B/C/D=32-452 (human) 1GEN - A=443-660 (human) 1GXD - A/B=30-660 (human) 1HOV - A=110-256 (human) 1J7M - A=337-394 (human) 1KS0 - A=223-282 (human) 1QIB - A=115-260 (human) 1RTG - A=451-660 (human) 3AYU - A=394-450 (human)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 1CK7 1CXW 1EAK 1GEN 1GXD 1HOV 1J7M 1KS0 1QIB 1RTG 3AYU  |  ENZYME  |  Phospho3D  |  DISEASE 120360 259600  |  Source  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene

	Modification Sites and Domains

	Modification Sites in Parent Protein, Orthologs, and Isoforms

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human
0	1		T11-p	LMARGALtGPLRALC
1	0		S160-p	DVTPLRFsRIHDGEA
0	1		S246-p	FNGKEYNsCTDtGRS
1	0		T250-p	EYNsCTDtGRSDGFL
0	1		Y360-p	FTFLGNKyEsCtsAG
0	1		S362-p	FLGNKyEsCtsAGRs
0	2		T364-p	GNKyEsCtsAGRsDG
1	1		S365-p	NKyEsCtsAGRsDGK
0	1		S369-p	sCtsAGRsDGKMWCA
1	0		T377-p	DGKMWCAttANYDDD
1	0		T378-p	GKMWCAttANYDDDR

	mouse
A11	RVAWGALAGPLRVLC
S160	DVTPLRFSRIHDGEA
S246	FNGREYSSCTDTGRS
T250	EYSSCTDTGRSDGFL
Y360	FTFLGNKYESCTSAG
S362	FLGNKYESCTSAGRN
T364	GNKYESCTSAGRNDG
S365	NKYESCTSAGRNDGK
N369	SCTSAGRNDGKVWCA
T377	DGKVWCATTTNYDDD
T378	GKVWCATTTNYDDDR

	rat
V11	RLVWGVLVGPLRVLC
S160	DVTPLRFSRIHDGEA
S246	FNGREYSSCTDTGRS
T250	EYSSCTDTGRSDGFL
Y360	FTFLGNKYESCTSAG
S362	FLGNKYESCTSAGRN
T364	GNKYESCTSAGRNDG
S365	NKYESCTSAGRNDGK
N369	SCTSAGRNDGKVWCA
T377	DGKVWCATTTNYDDD
T378	GKVWCATTTNYDDDR

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