MMP14 (matrix metallopeptidase 14 (membrane-inserted))

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MMP14 (matrix metallopeptidase 14 (membrane-inserted))

Written	2010-10	Cem Kuscu, Nikki Evensen, Jian Cao
		Division of Cancer Prevention, Stony Brook University, Stony Brook, New York 11794, USA

(Note : for Links provided by Atlas : click)

Identity

Alias (NCBI)	MMP-X1
	MT1-MMP
	MTMMP1
HGNC (Hugo)	MMP14
HGNC Alias symb	MT1-MMP
HGNC Alias name	membrane type 1 metalloprotease
	membrane type 1-matrix metalloproteinase
HGNC Previous name	matrix metalloproteinase 14 (membrane-inserted)
	matrix metallopeptidase 14 (membrane-inserted)
LocusID (NCBI)	4323
Atlas_Id	41391
Location	14q11.2 [Link to chromosome band 14q11]
Location_base_pair	Starts at 22836585 and ends at 22847758 bp from pter ( according to GRCh38/hg38-Dec_2013) [Mapping MMP14.png]

Fusion genes
(updated 2017)

Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)

ETNK2 (1q32.1)::MMP14 (14q11.2)	MMP14 (14q11.2)::H19 (11p15.5)	MMP14 (14q11.2)::MED23 (6q23.2)
MMP14 (14q11.2)::MMP14 (14q11.2)	PDXDC1 (16p13.11)::MMP14 (14q11.2)	SFTPA2 (10q22.3)::MMP14 (14q11.2)

DNA/RNA



Description	MMP14 spans 11009 bp on chromosome 14 in the region of q11.2. It consists of 10 exons.
Transcription	The human MMP-14 (MT1-MMP) transcript has been determined to be 3558 bp in length before splicing and 1749 bp after splicing. The start codon (ATG) of MMP-14 gene exists in the first exon and the stop codon (TGA) is present in the last and longest exon of the transcribed product of MMP-14. No TATA box, which controls the expression of 30% of all genes found in the human genome, is found in the proximal region in the MMP-14 promoter. In the promoter region, Egr-1 has been reported to be one of the most important transcription factors regulating the expression of MMP-14. MMP-14 expression is also regulated by other transcription factors, including AP-4, NF-kB, c-ETS1 and p53. However, some common transcription factors, such as AP-1, AP-2 and TGF-alpha, which play major roles in the regulation of other MMPs do not have binding sites within the promoter of MMP-14. Besides these common transcription factors, MMP-14 expression is also regulated by hypoxia inducible factor 2a (HIF-2alpha) under hypoxic conditions. Two HBSs (HIF binding site) have been identified in the proximal promoter region, the one around -125 bp relative to the transcription start site is shown to affect MMP-14 transcription. Some growth factors and cytokines, e.g IL1B, EGF, TNFalpha, bFGF, GM-CSF, SF/HGF, and TGF-beta have also been reported to induce the expression of MMP-14. Two functional SNPs in the MMP-14 promoter have been found in focal-segmental glomerulosclerosis (FSGS) disease. -378 T/C and -364 G/T alterations cause a reduction in the expression of MMP-14 and correlate with significant risk reduction of FSGS. Epigenetic regulation is also involved in the regulation of MMP-14 expression. Hypermethylation of the CpG100 island, which spans a region from the proximal promoter to the 1st intron of MMP-14, and trimethylation of Histone H3 lysine-27 (known as a repressive marker) are determined as epigenetic controls causing the transcriptional silencing of MMP-14.
Pseudogene	No pseudogenes have been identified.

Protein



	Schematic representation of the domain structures of MMP-14 (domains are not scaled).

Description	Matrix metalloproteinases (MMPs) compose one of the metzincins super family also known as zinc endopeptidases. Highly conserved motif of this family contains three histidines that bind zinc ion in the catalytic site of the protein and conserved methionine. Besides the secreted MMPs of the MMP family, six membrane type-MMPs have been identified so far, all with similar domain compositions. The best characterized MT-MMP is MMP-14 or MT1-MMP, which contains seven domains from N-terminus to C-terminus: a signal peptide leading MMP-14 into the secretory pathway; a propeptide domain maintaining MMP in a latent form; a catalytic domain responsible for enzymatic activity; a hinge region maintaining proper conformation; a hemopexin domain required for substrate reorganization; a transmembrane domain anchoring MMP into the plasma membrane; and a cytoplasmic domain required for endocytosis. MT-1, MT2-, MT3- and MT5-MMPs all contain seven similar domains, whereas MT4- and MT6-MMPs lack the transmembrane and cytoplasmic domains. Both MT4- and MT6-MMPs are linked to the cell surface through GPI-anchorage. There is a furin consensus sequence (Arg¹⁰⁸-Arg¹⁰⁹-Lys¹¹⁰-Arg¹¹¹) between MMP-14 propeptide and catalytic domains. Furin has been reported to be responsible for MMP-14 activation. However, the activation mechanism of MMP-14 is still under debate. The hemopexin-like domain of MMP-14 is the largest domain, and it provides a suitable flat surface for the protein-protein interactions with the existence of four bladed beta-propeller structures.
Expression	MMP-14 is widely expressed in human tissues. Its expression has been proven in the adult human intestine, kidney, lung, ovary, placenta, prostate, and spleen. Increase in its expression level has also been observed in the wound healing area. A Mouse embryogenesis study provides evidence for the expression of MMP-14 mainly in the muscle cells, fibroblast, chondrocytes, and neural cells. MMP-14 is upregulated in most human cancers. Both cancer and stromal cells have been reported to be upregulated in tumor tissues.
Localisation	Plasma Membrane (single-pass type I membrane protein). MMP-14 contains a 24 amino acid hydrophobic motif at the C-terminus which is responsible for plasma membrane localization of MMP-14.
Function	MMP-14 plays an important role in remodelling of extracellular matrix (ECM) and enhancing cell migration. Besides the role of MMP-14 in these pathophysiological processes, it also plays an important physiological role during development. Studies performed with MMP-14 null mice have shown the importance of its function during embryogenesis as the lack of MMP-14 caused craniofacial dysmorphism, arthritis, osteopenia, dwarfism, fibrosis of soft tissues and premature death. In the adult life, MMP-14 is also required for the wound healing process. All of these functions are related to MMP-14's cleavage or activation of the protein within its substrate profile, which includes proteins in ECM, pro-MMPs, cell-adhesion molecules, cytokines, growth factors and receptors on the cell membrane. Recent studies have also demonstrated the activation of signal transduction pathways via the cytoplasmic tail of MMP-14 important for the invasion process. Functions of MMP-14 can be summarized under the categories of activation of proMMMPs; degradation of ECM; shedding of cell surface molecules; cleavage of cytokines and growth factors; and activation of ERK cascade. I-) Activation of proMMPs and degradation of ECM Pro-MMP2 was the first identified substrate of MMP-14 and the trimolecular complex consisting of MMP-14 and proMMP2-TIMP2 has been investigated very well for many years. TIMP2 (tissue inhibitor of metalloproteinases-2) is actually the inhibitor of the MMPs. However, low concentrations of TIMP-2 aids in the activation of proMMP-2 by MMP-14 within this complex by binding to the catalytic domain of MMP-14 and the C-terminal domain of pro-MMP2. Following the formation of the triplex, a second MMP-14, which is free of TIMP-2, forms a dimer with the pre-existing MMP-14 on the cell membrane and cleaves the latent pro-MMP2 to produce active MMP2. Active MMP-2 can then participate in other events such as the degradation of collagen type-IV, a major protein component of the basement membrane, which is not cleaved by MMP-14 itself. Another substrate of MMP-14 within the MMP family is the pro-MMP-13, which also functions as a collagenase in the surrounding tissue after its activation. Besides activation of MMPs, especially pro-MMP-2, MMP-14 cleaves many proteins in the ECM and changes the composition of the matrix. Type I-Type II-Type III collagen, gelatin, fibronectin, laminin-1 and -5, fibrin and proteoglycans are the major direct targets of MMP-14 in the extracellular environment. Out of these substrates, collagen makes up a significant portion of the ECM and acts as a barrier for migratory cells. Within the collagenases, which includes MMP-1, MMP-2, MMP-8, MMP-13, only MMP-14 can stimulate invasion into collagen by epithelial cells, fibroblasts, and cancer cells. MMP-14 concentrates in the protrusions of the cells, called lamellipodia in normal cells and invadopodia in cancer cells, to induce a significant increase in cell migration and invasion by degrading components of the ECM and making a path in through the surrounding tissue. In this aspect, MMP-14 should be bound to the plasma membrane in vivo, as membrane-bound MMP-14 has been demonstrated to be more proteolytically active than the soluble recombinant MMP-14. II-) Shedding of cell surface molecules Studies underlying the mechanism of the constitutive shedding of CD44 from the human melanoma cell surface implicated the necessity of MMP-14 with the presence of ADAM-10 for this process. Especially in the hyaluronan based matrix, cleavage of CD44 at the stem region by MMP-14 sheds these molecules from the cell surface and concurrently promotes the migration of the cells from the leading edge. Another cell adhesion molecule, E-cadherin, is also cleaved by MMP-14 to disrupt contact between cells. In the ischemia-induced ARF (acute renal failure), MMP-14 expression is required for the disruption of the cadherin/catenin complex. Syndecan-1 is another cell surface molecule which is cleaved by MMP-14. III-) Cleavage of cytokines and growth factors MMP-14 indirectly plays a major role in cleavage of the cytokines and growth factors by activating pro-MMP-2 and pro-MMP13. It also makes direct contact with several chemokines and growth factors including; the neutrophil chemokine IL-8, secretory leukocyte protease inhibitor, pro-tumor necrosis factor, death receptor-6, and connective tissue growth factor. IV-) Activation of ERK cascade by the cytoplasmic tail of MMP-14 In several studies, overexpression of MMP-14 has been reported to activate the ERK cascade. It is not yet clear how MMP-14 activates ERK signalling, but overexpression of the cytoplasmic-deleted form of MMP-14 has been shown to eradicate ERK activation. Within the cytoplasmic tail, the 573YCQR576 motif has been suggested to be involved in ERK activation. In addition to ERK activation, the role of MMP-14 in the p38 and JNK pathway has also been investigated. V-) Inhibition of MMP-14 function Function of MMP-14 can be abolished either by TIMPs (Tissue Inhibitor of MetalloProteinases) or proteolytic degradation. TIMP-2, -3 and -4 but not TIMP-1 specifically inactivates the functions of MMP-14. Besides TIMPs, RECK and N-Tes can also block the activity of MMP-14 in a similar manner. For the proteolytic cleavage of MMP-14, membrane bound MMP-14 should be internalized by the clathrin-dependent and caveolae-dependent pathways. There is an AP-2 binding site in the cytoplasmic domain of MMP-14, ⁵⁷¹LLY⁵⁷³ which is required for the incorporation of MMP-14 into clathrin-coated vesicles. The palmitoylation of the C574 right after the AP-2 binding site has also been demonstrated to be an essential modification for the internalization of MMP-14.
Homology	All MT-MMPs have shown a 40-50% identity according to their amino acid sequence. In the phylogenetic tree, MMP-14 shares the highest similarity rate with MT2-MMP (MMP-15).

Implicated in

Note

Entity	Various cancers
Note	Degradation of the ECM by MMP-14 has been linked to proliferation, invasion and metastasis of cancer cells in most cancer types. The expression level of MMP-14 has also been correlated with invasiveness in many cancer cell lines, especially for breast carcinoma. Increase in the MMP-14 expression level has also been observed in a variety of human tumors, including lung, gastric, breast, colon, liver, pancreatic, thyroid, head and neck, ovarian, prostate, bladder, cervical and brain tumors. Genetic alterations, such as gene amplification or activating mutations, have not been observed for MMP-14 in these cancer types, therefore up regulation of MMP-14 has been linked to the transcriptional changes during tumor formation. Immunohistochemical and in-situ hybridization analysis have demonstrated the presence of MMP-14 in both tumor cells and stromal cells. Interestingly, most of the MMP-14 expression is produced by the stromal cells rather than the cancer cells in many tumor types, including breast and lung tumors. The possible explanation for this observation is the production of Extracellular Matrix Metalloproteinase Inducer (EMMPRIN) by the cancer cells on their cell surface. EMMPRIN stimulates the surrounding stromal cells to produce MMPs, including MMP-14. However, in some human cancers, including thyroid, brain, and head and neck cancer, a majority of the MMP-14 expression has been shown to be produced by the cancer cells rather than surrounding stromal cells. Another major role of the MMP-14 expression for tumor formation is the upregulation of VEGF production. VEGF is the key molecule for the vascularisation of tumor cells and angiogenesis. For the VEGF gene transcription, C-terminal of MMP-14 in the cytoplasmic tail has a structural region composed of ⁵⁷⁴CQRSLLDKV⁵⁸².


Entity	Atherosclerosis
Note	In the numerous stages of atherosclerosis, pro-inflammatory molecules such IL-1a, TNF-a and oxidized-LDL trigger the smooth muscle cells (SMC) and macrophages to increase their levels of MMP-14. Higher expression of MMP-14 activates its downstream molecule, pro-MMP-2, and then both MMP-14 and MMP-2 contribute to the abnormal matrix turnover, leading to the atherosclerotic plaques in the walls of arteries.


Entity	Rheumatoid disease
Note	It has been reported that fibroblasts, macrophages, and osteoclast-like cells in both the lining and sublinig layers of the rheumatoid synovial tissue have higher expression of MMP-14 and MT3-MMP. Effects of MMP-14 have been implicated in the destruction of tissue seen in arthritis. Successful suppression of the joint destruction has also been observed after treatment with one of the MMP-14 inhibitors, called FR217840.


Entity	Neurologic disease
Note	Neurons and astrocytes have been known to express MMPs and remodel the ECM after nerve injury in the body. In the case of amyotrophic lateral sclerosis, MMP-14 expression has been found to be increased in the astrocytes of affected tissues of the mouse central nervous system.


Entity	Lung disease
Note	Vascular endothelial cells and bronchial epithelial cells of the lung were injured by the high volume ventilation in the ventilator-induced lung (VIL) rat model. In the injured cells of the VIL, an increase in the MMP-14 expression has been reported. Prinomastat, an MMP-14 inhibitor, treatment of the VIL rat has also been shown to abolish the injury.


Entity	Kidney disease
Note	Data suggest that the development of crescentic glomerulonephritis, a kidney disease characterized by inflammation of the glomeruli or small blood vessels, triggered by the expression of MMP-14 in macrophages. In this disease, MMP-14 activates proMMP-2, and then they both contribute to the pathological degradation of the ECM.

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Citation

This paper should be referenced as such :

Kuscu, C ; Evensen, N ; Cao, J

MMP14 (matrix metallopeptidase 14 (membrane-inserted))

Atlas Genet Cytogenet Oncol Haematol. 2011;15(6):502-506.

Free journal version : [ pdf ] [ DOI ]

External links

	Nomenclature
HGNC (Hugo)	MMP14 7160
	Cards
Atlas	MMP14ID41391ch14q11
Entrez_Gene (NCBI)	MMP14 matrix metallopeptidase 14
Aliases	MMP-14; MMP-X1; MT-MMP; MT-MMP;
	MT1-MMP; MT1MMP; MTMMP1; WNCHRS
GeneCards (Weizmann)	MMP14
Ensembl hg19 (Hinxton)	ENSG00000157227 [Gene_View]
Ensembl hg38 (Hinxton)	ENSG00000157227 [Gene_View] ENSG00000157227 [Sequence] chr14:22836585-22847758 [Contig_View] MMP14 [Vega]
ICGC DataPortal	ENSG00000157227
TCGA cBioPortal	MMP14
AceView (NCBI)	MMP14
Genatlas (Paris)	MMP14
SOURCE (Princeton)	MMP14
Genetics Home Reference (NIH)	MMP14
	Genomic and cartography
GoldenPath hg38 (UCSC)	MMP14 - chr14:22836585-22847758 + 14q11.2 [Description] (hg38-Dec_2013)
GoldenPath hg19 (UCSC)	MMP14 - 14q11.2 [Description] (hg19-Feb_2009)
GoldenPath	MMP14 - 14q11.2 [CytoView hg19] MMP14 - 14q11.2 [CytoView hg38]
ImmunoBase	ENSG00000157227
Genome Data Viewer NCBI	MMP14 [Mapview hg19]
OMIM	277950 600754
	Gene and transcription
Genbank (Entrez)	AK291325 AK312657 BC039581 BC064803 BQ009340
RefSeq transcript (Entrez)	NM_004995
Consensus coding sequences : CCDS (NCBI)	MMP14
Gene Expression	MMP14 [ NCBI-GEO ] MMP14 [ EBI - ARRAY_EXPRESS ] MMP14 [ SEEK ] MMP14 [ MEM ]
Gene Expression Viewer (FireBrowse)	MMP14 [ Firebrowse - Broad ]
Genevisible	Expression of MMP14 in : [tissues] [cell-lines] [cancer] [perturbations]
BioGPS (Tissue expression)	4323
GTEX Portal (Tissue expression)	MMP14
Human Protein Atlas	ENSG00000157227-MMP14 [pathology] [cell] [tissue]
	Protein : pattern, domain, 3D structure
UniProt/SwissProt	P50281 [function] [subcellular_location] [family_and_domains] [pathology_and_biotech] [ptm_processing] [expression] [interaction]
NextProt	P50281 [Sequence] [Exons] [Medical] [Publications]
With graphics : InterPro	P50281
Catalytic activity : Enzyme	3.4.24.80 [ Enzyme-Expasy ] 3.4.24.80 3.4.24.80 [ IntEnz-EBI ] 3.4.24.80 [ BRENDA ] 3.4.24.80 [ KEGG ] [ MEROPS ]
PhosPhoSitePlus	P50281
Domaine pattern : Prosite (Expaxy)	CYSTEINE_SWITCH (PS00546) HEMOPEXIN (PS00024) HEMOPEXIN_2 (PS51642) ZINC_PROTEASE (PS00142)
Domains : Interpro (EBI)	Hemopexin-like_dom Hemopexin-like_dom_sf Hemopexin-like_repeat Hemopexin_CS M10A_MMP MetalloPept_cat_dom_sf Pept_M10_metallopeptidase Pept_M10A Pept_M10A_metallopeptidase_C Pept_M10A_Zn_BS Peptidase_Metallo Peptidoglycan-bd-like PGBD-like_sf PGBDSf
Domain families : Pfam (Sanger)	DUF3377 (PF11857) Hemopexin (PF00045) Peptidase_M10 (PF00413) PG_binding_1 (PF01471)
Domain families : Pfam (NCBI)	pfam11857 pfam00045 pfam00413 pfam01471
Domain families : Smart (EMBL)	HX (SM00120) ZnMc (SM00235)
Conserved Domain (NCBI)	MMP14
PDB (RSDB)	1BQQ 1BUV 2MQS 3C7X 3MA2 3X23 4P3C 4P3D 4QXU 5H0U 6CLZ 6CM1
PDB Europe	1BQQ 1BUV 2MQS 3C7X 3MA2 3X23 4P3C 4P3D 4QXU 5H0U 6CLZ 6CM1
PDB (PDBSum)	1BQQ 1BUV 2MQS 3C7X 3MA2 3X23 4P3C 4P3D 4QXU 5H0U 6CLZ 6CM1
PDB (IMB)	1BQQ 1BUV 2MQS 3C7X 3MA2 3X23 4P3C 4P3D 4QXU 5H0U 6CLZ 6CM1
Structural Biology KnowledgeBase	1BQQ 1BUV 2MQS 3C7X 3MA2 3X23 4P3C 4P3D 4QXU 5H0U 6CLZ 6CM1
SCOP (Structural Classification of Proteins)	1BQQ 1BUV 2MQS 3C7X 3MA2 3X23 4P3C 4P3D 4QXU 5H0U 6CLZ 6CM1
CATH (Classification of proteins structures)	1BQQ 1BUV 2MQS 3C7X 3MA2 3X23 4P3C 4P3D 4QXU 5H0U 6CLZ 6CM1
Superfamily	P50281
AlphaFold pdb e-kb	P50281
Human Protein Atlas [tissue]	ENSG00000157227-MMP14 [tissue]
HPRD	02856
	Protein Interaction databases
DIP (DOE-UCLA)	P50281
IntAct (EBI)	P50281
BioGRID	MMP14
STRING (EMBL)	MMP14
ZODIAC	MMP14
	Ontologies - Pathways
QuickGO	P50281
Ontology : AmiGO	skeletal system development angiogenesis ovarian follicle development response to hypoxia endothelial cell proliferation endochondral ossification endopeptidase activity metalloendopeptidase activity metalloendopeptidase activity integrin binding protein binding extracellular space nucleus cytoplasm Golgi lumen cytosol plasma membrane plasma membrane integral component of plasma membrane focal adhesion proteolysis proteolysis response to oxidative stress zinc ion binding male gonad development response to mechanical stimulus positive regulation of myotube differentiation positive regulation of protein processing response to organic cyclic compound protein processing extracellular matrix disassembly extracellular matrix organization positive regulation of cell growth lung development positive regulation of cell migration collagen catabolic process collagen catabolic process extracellular matrix cytoplasmic vesicle zymogen activation zymogen activation endodermal cell differentiation chondrocyte proliferation melanosome astrocyte cell migration response to estrogen macropinosome intermediate filament cytoskeleton positive regulation of B cell differentiation negative regulation of Notch signaling pathway embryonic cranial skeleton morphogenesis branching morphogenesis of an epithelial tube tissue remodeling cell motility negative regulation of focal adhesion assembly head development metalloaminopeptidase activity metalloaminopeptidase activity craniofacial suture morphogenesis regulation of protein localization to plasma membrane positive regulation of macrophage migration response to odorant
Ontology : EGO-EBI	skeletal system development angiogenesis ovarian follicle development response to hypoxia endothelial cell proliferation endochondral ossification endopeptidase activity metalloendopeptidase activity metalloendopeptidase activity integrin binding protein binding extracellular space nucleus cytoplasm Golgi lumen cytosol plasma membrane plasma membrane integral component of plasma membrane focal adhesion proteolysis proteolysis response to oxidative stress zinc ion binding male gonad development response to mechanical stimulus positive regulation of myotube differentiation positive regulation of protein processing response to organic cyclic compound protein processing extracellular matrix disassembly extracellular matrix organization positive regulation of cell growth lung development positive regulation of cell migration collagen catabolic process collagen catabolic process extracellular matrix cytoplasmic vesicle zymogen activation zymogen activation endodermal cell differentiation chondrocyte proliferation melanosome astrocyte cell migration response to estrogen macropinosome intermediate filament cytoskeleton positive regulation of B cell differentiation negative regulation of Notch signaling pathway embryonic cranial skeleton morphogenesis branching morphogenesis of an epithelial tube tissue remodeling cell motility negative regulation of focal adhesion assembly head development metalloaminopeptidase activity metalloaminopeptidase activity craniofacial suture morphogenesis regulation of protein localization to plasma membrane positive regulation of macrophage migration response to odorant
Pathways : BIOCARTA	Inhibition of Matrix Metalloproteinases [Genes]
Pathways : KEGG	TNF signaling pathway GnRH signaling pathway
REACTOME	P50281 [protein]
REACTOME Pathways	R-HSA-1592389 [pathway]
NDEx Network	MMP14
Atlas of Cancer Signalling Network	MMP14
Wikipedia pathways	MMP14
	Orthology - Evolution
OrthoDB	4323
GeneTree (enSembl)	ENSG00000157227
Phylogenetic Trees/Animal Genes : TreeFam	MMP14
Homologs : HomoloGene	MMP14
Homology/Alignments : Family Browser (UCSC)	MMP14
	Gene fusions - Rearrangements
Fusion : Mitelman	MMP14::H19 [14q11.2/11p15.5]
Fusion : Mitelman	PDXDC1::MMP14 [16p13.11/14q11.2]
Fusion : Quiver	MMP14
	Polymorphisms : SNP and Copy number variants
NCBI Variation Viewer	MMP14 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)	MMP14
dbVar	MMP14
ClinVar	MMP14
Monarch	MMP14
1000_Genomes	MMP14
Exome Variant Server	MMP14
GNOMAD Browser	ENSG00000157227
Varsome Browser	MMP14
ACMG	MMP14 variants
Varity	P50281
Genomic Variants (DGV)	MMP14 [DGVbeta]
DECIPHER	MMP14 [patients] [syndromes] [variants] [genes]
CONAN: Copy Number Analysis	MMP14
	Mutations
ICGC Data Portal	MMP14
TCGA Data Portal	MMP14
Broad Tumor Portal	MMP14
OASIS Portal	MMP14 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMIC	MMP14 [overview] [genome browser] [tissue] [distribution]
Somatic Mutations in Cancer : COSMIC3D	MMP14
Mutations and Diseases : HGMD	MMP14
LOVD (Leiden Open Variation Database)	[gene] [transcripts] [variants]
BioMuta	MMP14
DgiDB (Drug Gene Interaction Database)	MMP14
DoCM (Curated mutations)	MMP14
CIViC (Clinical Interpretations of Variants in Cancer)	MMP14
NCG (London)	MMP14
Cancer3D	MMP14
Impact of mutations	[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
	Diseases
OMIM	277950 600754
Orphanet	3042 11654
DisGeNET	MMP14
Medgen	MMP14
Genetic Testing Registry	MMP14
NextProt	P50281 [Medical]
GENETests	MMP14
Target Validation	MMP14
Huge Navigator	MMP14 [HugePedia]
ClinGen	MMP14
	Clinical trials, drugs, therapy
MyCancerGenome	MMP14
Protein Interactions : CTD	MMP14
Pharm GKB Gene	PA30872
Pharos	P50281
Clinical trial	MMP14
	Miscellaneous
canSAR (ICR)	MMP14
Harmonizome	MMP14
DataMed Index	MMP14
	Probes
	Litterature
PubMed	499 Pubmed reference(s) in Entrez
GeneRIFs	Gene References Into Functions (Entrez)
EVEX	MMP14

REVIEW articles	automatic search in PubMed
Last year publications	automatic search in PubMed

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indexed on : Fri Oct 8 21:22:48 CEST 2021

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