NP_004985.2
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NCBI GenBank Nucleotide #
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UniProt Primary Accession #
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UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
78,458 Da
NCBI Official Full Name
matrix metalloproteinase-9 preproprotein
NCBI Official Synonym Full Names
matrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase)
NCBI Protein Information
matrix metalloproteinase-9; 92 kDa gelatinase; type V collagenase; macrophage gelatinase; 92 kDa type IV collagenase; matrix metalloproteinase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase)
UniProt Protein Name
Matrix metalloproteinase-9
UniProt Synonym Protein Names
92 kDa gelatinase; 92 kDa type IV collagenase; Gelatinase B
UniProt Synonym Gene Names
UniProt Entry Name
MMP9_HUMAN
NCBI Summary for MMP-9
Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The enzyme encoded by this gene degrades type IV and V collagens. Studies in rhesus monkeys suggest that the enzyme is involved in IL-8-induced mobilization of hematopoietic progenitor cells from bone marrow, and murine studies suggest a role in tumor-associated tissue remodeling. [provided by RefSeq, Jul 2008]
UniProt Comments for MMP-9
MMP9: 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. 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. Activated by 4-aminophenylmercuric acetate and phorbol ester. Up-regulated by ARHGEF4, SPATA13 and APC via the JNK signaling pathway in colorectal tumor cells. Produced by normal alveolar macrophages and granulocytes. Inhibited by histatin-3 1/24 (histatin-5). Inhibited by ECM1. Belongs to the peptidase M10A family.
Protein type: Secreted; Protease; Motility/polarity/chemotaxis; EC 3.4.24.35; Secreted, signal peptide
Chromosomal Location of Human Ortholog: 20q13.12
Cellular Component: proteinaceous extracellular matrix; extracellular space; extracellular region
Molecular Function: collagen binding; identical protein binding; protein binding; zinc ion binding; metalloendopeptidase activity; endopeptidase activity
Biological Process: positive regulation of keratinocyte migration; axon guidance; extracellular matrix disassembly; collagen catabolic process; extracellular matrix organization and biogenesis; ossification; macrophage differentiation; positive regulation of apoptosis; ephrin receptor signaling pathway; proteolysis; leukocyte migration; skeletal development; embryo implantation
Disease: Metaphyseal Anadysplasia 2
Research Articles on MMP-9
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Products associated with MMP-9 elisa kit
Pathways associated with MMP-9 elisa kit
Diseases associated with MMP-9 elisa kit
Organs/Tissues associated with MMP-9 elisa kit
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