Gene Symbol | MMP16 |
Entrez ID | 4325 |
Uniprot ID | P51512 |
Description | matrix metallopeptidase 16 |
Chromosomal Location | chr8: 88,032,009-88,328,025 |
Ontology | GO ID | GO Term | Definition | Evidence |
---|---|---|---|---|
BP |
GO:0001958 |
endochondral ossification |
Replacement ossification wherein bone tissue replaces cartilage. |
IEA |
BP |
GO:0006508 |
proteolysis |
The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. |
IDA|TAS |
BP |
GO:0016485 |
protein processing |
Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a protein. Protein maturation is the process leading to the attainment of the full functional capacity of a protein. |
IDA |
BP |
GO:0019538 |
protein metabolic process |
The chemical reactions and pathways involving a specific protein, rather than of proteins in general. Includes protein modification. |
TAS |
BP |
GO:0022617 |
extracellular matrix disassembly |
A process that results in the breakdown of the extracellular matrix. |
TAS |
BP |
GO:0030574 |
collagen catabolic process |
The proteolytic chemical reactions and pathways resulting in the breakdown of collagen in the extracellular matrix, usually carried out by proteases secreted by nearby cells. |
IEA |
BP |
GO:0035988 |
chondrocyte proliferation |
The multiplication or reproduction of chondrocytes by cell division, resulting in the expansion of their population. A chondrocyte is a polymorphic cell that forms cartilage. |
IEA |
BP |
GO:0043085 |
positive regulation of catalytic activity |
Any process that activates or increases the activity of an enzyme. |
IEA |
BP |
GO:0048701 |
embryonic cranial skeleton morphogenesis |
The process in which the anatomical structures of the cranial skeleton are generated and organized during the embryonic phase. |
IEA |
BP |
GO:0097094 |
craniofacial suture morphogenesis |
The process in which any suture between cranial and/or facial bones is generated and organized. |
IEA |
CC |
GO:0005578 |
proteinaceous extracellular matrix |
A layer consisting mainly of proteins (especially collagen) and glycosaminoglycans (mostly as proteoglycans) that forms a sheet underlying or overlying cells such as endothelial and epithelial cells. The proteins are secreted by cells in the vicinity. An example of this component is found in Mus musculus. |
IEA |
CC |
GO:0005796 |
Golgi lumen |
The volume enclosed by the membranes of any cisterna or subcompartment of the Golgi apparatus, including the cis- and trans-Golgi networks. |
TAS |
CC |
GO:0005886 |
plasma membrane |
The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
TAS |
CC |
GO:0005887 |
integral component of plasma membrane |
The component of the plasma membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
IDA |
CC |
GO:0009986 |
cell surface |
The external part of the cell wall and/or plasma membrane. |
IEA |
MF |
GO:0004222 |
metalloendopeptidase activity |
Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions. |
IDA |
MF |
GO:0005509 |
calcium ion binding |
Interacting selectively and non-covalently with calcium ions (Ca2+). |
IEA |
MF |
GO:0008047 |
enzyme activator activity |
Binds to and increases the activity of an enzyme. |
TAS |
MF |
GO:0008270 |
zinc ion binding |
Interacting selectively and non-covalently with zinc (Zn) ions. |
IDA |
MF |
GO:0070006 |
metalloaminopeptidase activity |
Catalysis of the hydrolysis of N-terminal amino acid residues from a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions. |
IDA|TAS |
Domain ID | Description |
---|---|
IPR000585 |
Hemopexin-like domain |
IPR001818 |
Peptidase M10, metallopeptidase |
IPR002477 |
Peptidoglycan binding-like |
IPR006026 |
Peptidase, metallopeptidase |
IPR016293 |
Peptidase M10A, stromelysin-type |
IPR018486 |
Hemopexin, conserved site |
IPR018487 |
Hemopexin-like repeats |
IPR021158 |
Peptidase M10A, cysteine switch, zinc binding site |
IPR021190 |
Peptidase M10A |
IPR021805 |
Peptidase M10A, matrix metallopeptidase, C-terminal |
IPR024079 |
Metallopeptidase, catalytic domain |
IPR028697 |
Matrix metalloproteinase-16 |
IPR033739 |
Peptidase M10A, catalytic domain |
Pathway ID | Pathway Term | Pathway Source |
---|---|---|
hsa05206 |
MicroRNAs in cancer |
KEGG |
WP129 |
Matrix Metalloproteinases |
WikiPathways |
Tissue | Cell Type |
---|---|
esophagus |
squamous epithelial cells |
oral mucosa |
squamous epithelial cells |
placenta |
trophoblastic cells |
rectum |
glandular cells |
smooth muscle |
smooth muscle cells |
Pubmed ID | Author | Year | Title |
---|---|---|---|
12734205 |
Wood et al. |
2003 |
The Molecular Phenotype of Polycystic Ovary Syndrome (PCOS) Theca Cells and New Candidate PCOS Genes Defined by Microarray Analysis |
22617121 |
Ouandaogo et al. |
2012 |
Differences in transcriptomic profiles of human cumulus cells isolated from oocytes at GV, MI and MII stages after in vivo andin vitro oocyte maturation |
Gene Symbol | Entrez ID | Uniprot ID | Score |
---|---|---|---|
LRP1 |
4035 |
Q07954 |
0.52 |
KISS1 |
3814 |
Q15726 |
0.55 |