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MMP26 (matrix metallopeptidase 26)

Written2012-08Suzan M Semaan, Zhiyong Wang, Mark D Roycik, Xuexun Fang, Qing-Xiang Amy Sang
Department of Chemistry, Biochemistry, Institute of Molecular Biophysics, Tallahassee, Florida 32306-4390, USA (SMS, MDR, QXAS); Key Laboratory for Molecular Enzymology, Enzyme Engineering of the Ministry of Education Jilin University, Changchun, 130012, China (ZW, XF)

(Note : for Links provided by Atlas : click)

Identity

Alias_namesmatrix metalloproteinase 26
Alias_symbol (synonym)endometase
MGC126590
MGC126592
Other alias
HGNC (Hugo) MMP26
LocusID (NCBI) 56547
Atlas_Id 41403
Location 11p15.4  [Link to chromosome band 11p15]
Location_base_pair Starts at 4988191 and ends at 4992429 bp from pter ( according to hg19-Feb_2009)  [Mapping MMP26.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)

DNA/RNA

 
  Containing 6 exons spanning 4,24 kb, MMP-26 is found at chromosome 11p15.4.
Description This gene can be found at chromosome 11p15.4, and contains 6 exons spanning 4,24 kb.
Transcription MMP-26 has 998 mRNA nucleotides and no transcript variant. The transcription of this gene is regulated by three elements, estrogen-responsive element (ERE), T-cell factor-4 (TCF-4), and activator protein-1 (AP-1), due to the highly unusual poly (A) site located upstream of its promoter. Further regulation of TCF-4 is accomplished by the β-catenin/epithelial-cadherin (E-cadherin) pathway and suggests that MMP-26 is specifically expressed in cells of epithelial origin. The gene for MMP-26 has one transcriptional start site and a consensus TATA-box, located 35 and 60 nucleotides upstream of the translational start site respectively.

Protein

 
  Schematic of MMP-26 (wild type). Pre-, signal peptide of MMP-26 (residues 1-17); Pro-, pro-peptide of MMP-26 (residues 18-90); and Cat-, catalytic domain of MMP-26 (residues 91-261).
Description MMP-26 is the smallest member of the matrix metalloproteinase (MMP) family of zinc-dependent endopeptidases. Synthesized as a zymogen, the nascent form is composed of three domains: (1) "pre" domain, N-terminal signal sequence, which directs the protein into the endoplasmic reticulum; (2) an unconventional "pro" domain, which maintains enzyme-latency; and (3) a catalytic domain, which contains the conserved zinc-binding region for proteolysis. The MMP-26 pro-enzyme starts at residue 18, with the full length of the protein spanning 261 amino acids. The full-length enzyme has a theoretical molecular weight of 28 kDa that is truncated to 19 kDa upon activation (cleavage of the pro-domain). Among the MMPs, only MMP-26 has a "cysteine-switch" sequence that contains a histidine residue instead of the usual arginine residue (PH81CGVPDGSD) in the pro-peptide domain and has a zinc-binding motif (V205ATHEIGHSLGLQH) in the catalytic domain. Additionally, MMP-26 lacks the hinge region and hemopexin-like domain that is common to other family members. MMP-26 has two calcium binding sites: (1) a high-affinity site required for enzymatic activity, protein stability, and protection from denaturation; and (2) a low-affinity site primarily important for protein folding, tertiary structure, and native conformation. The protein also contains three possible N-linked glycosylation sites (N64, N133, N221).
Expression MMP-26 has been found strictly expressed in normal tissues of the placenta and moderately expressed in the uterus. However, MMP-26 expression is also associated with human cancer cells, especially in estrogen receptor (ER)-α positive breast cancer cells and cancerous cells of the ovary and endometrium. The expression of MMP-26 in cancerous breast, colon, lung, brain, head and neck, prostate, and melanoma tissues was significantly elevated when compared with parallel normal tissues, while not significantly elevated in kidney cancer, ovarian cancer, and non-Hodgkin's lymphoma.
Localisation Intracellular (endoplasmic reticulum-retained), secreted, pericellular, and extracellular.
Function MMP-26 cleaves many extracellular matrix and plasma proteins including: (1) amino terminus of estrogen receptor β; (2) α1-antitrypsin; (3) insulin-like growth factor-binding protein 1 (IGFBP-1); (4) fibronectin; (5) vitronectin; (6) fibrinogen; (7) gelatins of types I-IV; (8) gelatinase B (MMP-9); (9) α2-macroglobulin; and (10) type IV collagen. MMP-26 digests one peptide substrate of tumor necrosis factor-α converting enzyme (TACE/ADAM17) and four peptide substrates of MMPs. MMP-26 activates MMP-9 by cleavage of the pre-proenzyme (Ala93-Met94 site) and produces activated MMP-9 products that are more stable than those activated by MMP-7. MMP-26 also forms a complex with tissue inhibitors of metalloproteinases 4 (TIMP-4). MMP-26 is inhibited by GM6001 and TIMPs -2 (1,60 nM) and -4 (0,62 nM), exhibiting an inhibition profile most similar to those of MMPs with intermediate S1' pockets (His-233). MMP-26 can auto-digest itself during the folding process and is also capable of self-activation with its catalytic activity affected by detergents.
Homology Belongs to matrix metalloproteinase (MMP) family and exhibits a similar domain structure to that of matrilysin (MMP-7) but is most homologous to metalloelastase (MMP-12) with ~52% identity.

Implicated in

Note
  
Entity Breast cancer
Note MMP-26 is not expressed in normal mammary epithelium, is strongly upregulated in ductal carcinoma in situ (DCIS), and decreases throughout further disease progression (stages I to III). Co-expression of MMP-26 and TIMP-4 or MMP-9 has been detected in DCIS. Estrogen receptor-β (ER-β), not ER-α, is a substrate of MMP-26 in vivo and in vitro, indicating a novel regulation loop between estrogen and ER and modification of the ER-α/ER-β ratio. Additionally, silencing MMP-26 expression in the human breast cancer cell line MDA-MB-231 up-regulated the expression of five proteins (heat shock protein 90, glucose-regulated protein 78, annexin V, tropomyosin, peroxiredoxin II) and down-regulated the expression of four proteins (α-tubulin, cystatin SA-III, breast cancer metastasis suppressor 1 (BRMS1), and β-actin).
Prognosis MMP-26 expression is associated with ER+ human breast cancer and has positive correlation with patient survival in DCIS.
  
  
Entity Endometrial cancer, ovarian cancer
Note MMP-26 mRNA is localized in the epithelial component of normal, hyperplastic, premalignant, and malignant samples of endometrial tissue and in situ hybridization indicates maximal levels in normal tissue (midcycle) and in endometrial hyperplasia (with and without atypia). Endometrial carcinomas exhibit greater expression compared to benign endometrium from the postmenopausal period, but not from the secretory phase of the menstrual cycle. Expression progressively decreases with loss of histological differentiation in malignant samples. Increased staining intensity correlates with grade III tumors and with the depth of myometrial invasion in tumors histologically characterized as endometrioid adenocarcinoma. Relating to ovarian cancer, MMP-26 is expressed in normal tissue as well as ovarian tumors with expression increasing with increased tumor stage. Invading ovarian tumor cells display the strongest expression of MMP-26, and progression of ovarian cancer is correlated with MMP-26 co-expression with TIMP-3, and TIMP-4.
  
  
Entity Prostate cancer, prostatitis, benign prostate hyperplasia (BPH), and high-grade prostatic intraepithelial neoplasia (HGPIN)
Note Protein levels in human prostate carcinomas from multiple patients were significantly higher than those in prostatitis, benign prostate hyperplasia (BPH), and normal prostate glandular tissue. MMP-26 and TIMP-4 expression was found higher in HGPIN and cancer when compared to non-neoplastic acini.
Prognosis For the progression of high-grade prostatic intraepithelial neoplasia (HGPIN) to invasive adenocarcinoma, it is crucial to disrupt the continuity of the basal cell layer and basement membrane. MMP-26 may play an integral role during this conversion and may serve as a marker for earlier diagnoses.
Oncogenesis MMP-26, by cleaving basement membrane proteins and activating pro-MMP-9, promotes invasion of human prostate cancer cells.
  
  
Entity Squamous cell carcinomas (SCC)
Note Squamous cell cancers can be recognized as an uncontrolled wound healing process. MMP-26 expression is present in migrating keratinocytes (KC) of healing wounds compared with normal intact skin cells. Furthermore, expression was not found to be present in proliferating Ki-67-positive KC but co-localized with tumor suppressor p16. MMP-26 was also detected in squamous cell cancer (SCC) grades I and II, but was not present in grade III. In another study, high-grade SCC shows a statistically significant higher expression of MMP-26 and is associated with morphological scores of malignancy. MMP-26 is suggested to contribute to more aggressive behavior of SCCs in organ transplant recipients. In SCC of the esophagus (ESCC), MMP-26 was upregulated in incipient invasion and its expression associated with regions of low differentiation being more sporadic at the invasive front. MMP-26, nuclear β-catenin, and active MMP-9 expression correlate in ESCC tissue, which was found significantly correlated with depth of invasion, lymph node and distant metastasis, advances in pTNM stage, and recurrence.
Disease Oral squamous cell carcinomas, Esophageal squamous cell carcinoma.
Prognosis Lack of MMP-26 in SCC could be a marker of aggressive growth. Another report questions the usefulness of MMP-26 as an indicator of the metastatic potential of SCCs of the tongue. MMP-26 positive ESCC patients showed significantly shorter overall and disease-free survival periods than those did with MMP-26-negative cancers.
  
  
Entity Lung cancer
Note Expression of MMP-26 is significantly higher in non-small cell lung cancer (NSCLC) than in atypical hyperplasia and normal lung tissue and correlates with carcinogenesis, lymph node metastasis, clinical stage, and prognosis. Silencing of MMP-26 significantly reduced invasiveness of A549 cells in Transwell invasion assays, suggesting MMP-26 to play an important role in local invasion, at least in part through coordination with MMP-9.
Disease Non-small Cell Lung Cancer (NSCLC).
Prognosis MMP-26 may be used as a tumor marker in monitoring progression and predicting prognosis of NSCLC since disease-free and overall survival are shorter in NSCLC patients with high expression of MMP-26.
  
  
Entity Glioblastoma multiforme (brain tumor)
Note Overexpression of MMP-26 in U251 cells resulted in a significantly higher cell-spreading ratio when compared to parental U251 cells. The relative migration distance on Matrigel was also significantly greater. Boyden Chamber assays further indicated an enhanced invasive ability of MMP-26 overexpressed U251 cells. The microvessel density of tumor tissues derived from MMP-26 transfected cells was also greater when compared to the parental cell line.
Oncogenesis MMP-26 contributes to U251 cell invasion and migration in vitro and plays an important role in local invasion and angiogenesis.
  
  
Entity Merkel cell carcinoma (cutaneous tumor)
Note MMP-26 expression was positive in stromal cells and was associated with tumors greater than or equal to 2-cm in diameter.
Prognosis Stroma expression is associated with larger tumors with poor prognosis.
  
  
Entity Pancreatic cancer, pancreatic adenocarcinoma
Note Patients with metastatic cancer cells in lymph nodes had increased expression of MMP-26 in tumor samples. In a pancreatic cell line (PANC-1) MMP-26 was neither expressed basally nor induced by TNF-α, TGFβ1, EGF, or interferon γ.
  
  
Entity Colon cancer
Note Unlike classical MMPs, MMP-26 is expressed in the normal intestine and was detected in migrating enterocytes. Staining for MMP-26 revealed a meshwork-like pattern between cancer islets and suggested to be involved in enterocyte migration.
  

To be noted

No intracellular substrates of MMP-26 identified in disease with its high expression except for ER-β in breast cancer. No homologous analog of MMP-26 found in rodents.

Bibliography

Matrix metalloproteinases 21 and 26 are differentially expressed in esophageal squamous cell cancer.
Ahokas K, Karjalainen-Lindsberg ML, Sihvo E, Isaka K, Salo J, Saarialho-Kere U.
Tumour Biol. 2006;27(3):133-41. Epub 2006 Apr 20.
PMID 16641547
 
Matrilysin-2 (matrix metalloproteinase-26) is upregulated in keratinocytes during wound repair and early skin carcinogenesis.
Ahokas K, Skoog T, Suomela S, Jeskanen L, Impola U, Isaka K, Saarialho-Kere U.
J Invest Dermatol. 2005 Apr;124(4):849-56.
PMID 15816845
 
Immunohistochemical expression of matrix metalloproteinases in squamous cell carcinoma of the tongue and lower lip.
Barros SS, Henriques AC, Pereira KM, de Medeiros AM, Galvao HC, Freitas Rde A.
Arch Oral Biol. 2011 Aug;56(8):752-60. Epub 2011 Jan 21.
PMID 21255765
 
Increased expression of matrix metalloproteinases-21 and -26 and TIMP-4 in pancreatic adenocarcinoma.
Bister V, Skoog T, Virolainen S, Kiviluoto T, Puolakkainen P, Saarialho-Kere U.
Mod Pathol. 2007 Nov;20(11):1128-40. Epub 2007 Sep 14.
PMID 17873896
 
Differential expression of three matrix metalloproteinases, MMP-19, MMP-26, and MMP-28, in normal and inflamed intestine and colon cancer.
Bister VO, Salmela MT, Karjalainen-Lindsberg ML, Uria J, Lohi J, Puolakkainen P, Lopez-Otin C, Saarialho-Kere U.
Dig Dis Sci. 2004 Apr;49(4):653-61.
PMID 15185874
 
Expression of Matrix Metalloproteinase-26 promotes human glioma U251 cell invasion in vitro and in vivo.
Deng Y, Li W, Li Y, Yang H, Xu H, Liang S, Zhang L, Li Y.
Oncol Rep. 2010 Jan;23(1):69-78.
PMID 19956866
 
Matrix metalloproteinase-26 is expressed in human endometrium but not in endometrial carcinoma.
Isaka K, Nishi H, Nakai H, Nakada T, Feng Li Y, Ebihara Y, Takayama M.
Cancer. 2003 Jan 1;97(1):79-89.
PMID 12491508
 
Matrix metalloproteinase-26 is present more frequently in squamous cell carcinomas of immunosuppressed compared with immunocompetent patients.
Kuivanen T, Jeskanen L, Kyllonen L, Isaka K, Saarialho-Kere U.
J Cutan Pathol. 2009 Sep;36(9):929-36.
PMID 19674198
 
Coordinated peak expression of MMP-26 and TIMP-4 in preinvasive human prostate tumor.
Lee S, Desai KK, Iczkowski KA, Newcomer RG, Wu KJ, Zhao YG, Tan WW, Roycik MD, Sang QX.
Cell Res. 2006 Sep;16(9):750-8.
PMID 16940965
 
Calcium regulates tertiary structure and enzymatic activity of human endometase/matrilysin-2 and its role in promoting human breast cancer cell invasion.
Lee S, Park HI, Sang QX.
Biochem J. 2007 Apr 1;403(1):31-42.
PMID 17176253
 
Protein Signatures in Human MDA-MB-231 Breast Cancer Cells Indicating a More Invasive Phenotype Following Knockdown of Human Endometase/Matrilysin-2 by siRNA.
Lee S, Terry D, Hurst DR, Welch DR, Sang QX.
J Cancer. 2011 Mar 16;2:165-76.
PMID 21475635
 
Expression and clinical significance of matrix metalloproteinase (MMP)-26 protein in non-small cell lung cancer.
Li L, Mei TH, Zhou XD, Zhang XG.
Ai Zheng. 2009 Jan;28(1):60-3. Epub 2009 Jan 16.
PMID 19448419
 
Matrix metalloproteinase-26 is associated with estrogen-dependent malignancies and targets alpha1-antitrypsin serpin.
Li W, Savinov AY, Rozanov DV, Golubkov VS, Hedayat H, Postnova TI, Golubkova NV, Linli Y, Krajewski S, Strongin AY.
Cancer Res. 2004 Dec 1;64(23):8657-65.
PMID 15574774
 
Promoter characterization of the novel human matrix metalloproteinase-26 gene: regulation by the T-cell factor-4 implies specific expression of the gene in cancer cells of epithelial origin.
Marchenko GN, Marchenko ND, Leng J, Strongin AY.
Biochem J. 2002 Apr 15;363(Pt 2):253-62.
PMID 11931652
 
Beta-catenin regulates the gene of MMP-26, a novel metalloproteinase expressed both in carcinomas and normal epithelial cells.
Marchenko ND, Marchenko GN, Weinreb RN, Lindsey JD, Kyshtoobayeva A, Crawford HC, Strongin AY.
Int J Biochem Cell Biol. 2004 May;36(5):942-56.
PMID 15006646
 
The intermediate S1' pocket of the endometase/matrilysin-2 active site revealed by enzyme inhibition kinetic studies, protein sequence analyses, and homology modeling.
Park HI, Jin Y, Hurst DR, Monroe CA, Lee S, Schwartz MA, Sang QX.
J Biol Chem. 2003 Dec 19;278(51):51646-53. Epub 2003 Oct 7.
PMID 14532275
 
Effects of detergents on catalytic activity of human endometase/matrilysin 2, a putative cancer biomarker.
Park HI, Lee S, Ullah A, Cao Q, Sang QX.
Anal Biochem. 2010 Jan 15;396(2):262-8. Epub 2009 Oct 8.
PMID 19818727
 
Identification and characterization of human endometase (Matrix metalloproteinase-26) from endometrial tumor.
Park HI, Ni J, Gerkema FE, Liu D, Belozerov VE, Sang QX.
J Biol Chem. 2000 Jul 7;275(27):20540-4.
PMID 10801841
 
Peptide substrate specificities and protein cleavage sites of human endometase/matrilysin-2/matrix metalloproteinase-26.
Park HI, Turk BE, Gerkema FE, Cantley LC, Sang QX.
J Biol Chem. 2002 Sep 20;277(38):35168-75. Epub 2002 Jul 15.
PMID 12119297
 
Matrix metalloproteinase-26 (matrilysin-2) expression is high in endometrial hyperplasia and decreases with loss of histological differentiation in endometrial cancer.
Pilka R, Norata GD, Domanski H, Andersson C, Hansson S, Eriksson P, Casslen B.
Gynecol Oncol. 2004 Sep;94(3):661-70.
PMID 15350356
 
Human and mouse proteases: a comparative genomic approach.
Puente XS, Sanchez LM, Overall CM, Lopez-Otin C.
Nat Rev Genet. 2003 Jul;4(7):544-58. (REVIEW)
PMID 12838346
 
Expression of matrix metalloproteinase-26 and tissue inhibitors of metalloproteinase-3 and -4 in normal ovary and ovarian carcinoma.
Ripley D, Tunuguntla R, Susi L, Chegini N.
Int J Gynecol Cancer. 2006 Sep-Oct;16(5):1794-800.
PMID 17009974
 
Matrix metalloproteinase 26 proteolysis of the NH2-terminal domain of the estrogen receptor beta correlates with the survival of breast cancer patients.
Savinov AY, Remacle AG, Golubkov VS, Krajewska M, Kennedy S, Duffy MJ, Rozanov DV, Krajewski S, Strongin AY.
Cancer Res. 2006 Mar 1;66(5):2716-24.
PMID 16510592
 
Mislocalization and unconventional functions of cellular MMPs in cancer.
Strongin AY.
Cancer Metastasis Rev. 2006 Mar;25(1):87-98. (REVIEW)
PMID 16680575
 
Expression of MMP-10, MMP-21, MMP-26, and MMP-28 in Merkel cell carcinoma.
Suomela S, Koljonen V, Skoog T, Kukko H, Bohling T, Saarialho-Kere U.
Virchows Arch. 2009 Dec;455(6):495-503. Epub 2009 Nov 17.
PMID 19921252
 
Human chromosome 11 DNA sequence and analysis including novel gene identification.
Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y.
Nature. 2006 Mar 23;440(7083):497-500.
PMID 16554811
 
Expression of matrix metalloproteinase-26 and tissue inhibitors of metalloproteinases TIMP-3 and -4 in benign endometrium and endometrial cancer.
Tunuguntla R, Ripley D, Sang QX, Chegini N.
Gynecol Oncol. 2003 Jun;89(3):453-9.
PMID 12798711
 
Matrilysin-2, a new matrix metalloproteinase expressed in human tumors and showing the minimal domain organization required for secretion, latency, and activity.
Uria JA, Lopez-Otin C.
Cancer Res. 2000 Sep 1;60(17):4745-51.
PMID 10987280
 
Association of matrilysin-2 (MMP-26) expression with tumor progression and activation of MMP-9 in esophageal squamous cell carcinoma.
Yamamoto H, Vinitketkumnuen A, Adachi Y, Taniguchi H, Hirata T, Miyamoto N, Nosho K, Imsumran A, Fujita M, Hosokawa M, Hinoda Y, Imai K.
Carcinogenesis. 2004 Dec;25(12):2353-60. Epub 2004 Aug 27.
PMID 15333466
 
Non-small cell lung cancer invasion and metastasis promoted by MMP-26.
Zhang Y, Zhao H, Wang Y, Lin Y, Tan Y, Fang X, Zheng L.
Mol Med Report. 2011 Nov-Dec;4(6):1201-9. doi: 10.3892/mmr.2011.540. Epub 2011 Jul 26.
PMID 21805034
 
Expression of matrix metalloproteinase-26 in multiple human cancer tissues and smooth muscle cells.
Zhao YG, Xiao AZ, Ni J, Man YG, Sang QX.
Ai Zheng. 2009 Nov;28(11):1168-75.
PMID 19895737
 
Matrilysins may not predict the metastatic potential in squamous cell carcinoma of the tongue.
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Acta Odontol Scand. 2010 Jul;68(4):228-31.
PMID 20491537
 
Cloning of MMP-26. A novel matrilysin-like proteinase.
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Eur J Biochem. 2000 Jun;267(11):3323-9.
PMID 10824119
 

Citation

This paper should be referenced as such :
Semaan, SM ; Wang, Z ; Roycik, MD ; Fang, X ; Sang, QXA
MMP26 (matrix metallopeptidase 26)
Atlas Genet Cytogenet Oncol Haematol. 2013;17(2):110-114.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/MMP26ID41403ch11p15.html

External links

Nomenclature
HGNC (Hugo)MMP26   14249
Cards
AtlasMMP26ID41403ch11p15
Entrez_Gene (NCBI)MMP26  56547  matrix metallopeptidase 26
Aliases
GeneCards (Weizmann)MMP26
Ensembl hg19 (Hinxton)ENSG00000167346 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000167346 [Gene_View]  chr11:4988191-4992429 [Contig_View]  MMP26 [Vega]
ICGC DataPortalENSG00000167346
TCGA cBioPortalMMP26
AceView (NCBI)MMP26
Genatlas (Paris)MMP26
WikiGenes56547
SOURCE (Princeton)MMP26
Genetics Home Reference (NIH)MMP26
Genomic and cartography
GoldenPath hg38 (UCSC)MMP26  -     chr11:4988191-4992429 +  11p15.4   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)MMP26  -     11p15.4   [Description]    (hg19-Feb_2009)
EnsemblMMP26 - 11p15.4 [CytoView hg19]  MMP26 - 11p15.4 [CytoView hg38]
Mapping of homologs : NCBIMMP26 [Mapview hg19]  MMP26 [Mapview hg38]
OMIM605470   
Gene and transcription
Genbank (Entrez)AF230354 AF248646 AF291664 AJ251531 BC101541
RefSeq transcript (Entrez)NM_021801
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)MMP26
Cluster EST : UnigeneHs.204732 [ NCBI ]
CGAP (NCI)Hs.204732
Alternative Splicing GalleryENSG00000167346
Gene ExpressionMMP26 [ NCBI-GEO ]   MMP26 [ EBI - ARRAY_EXPRESS ]   MMP26 [ SEEK ]   MMP26 [ MEM ]
Gene Expression Viewer (FireBrowse)MMP26 [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevestigatorExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)56547
GTEX Portal (Tissue expression)MMP26
Human Protein AtlasENSG00000167346-MMP26 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ9NRE1   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ9NRE1  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ9NRE1
Splice isoforms : SwissVarQ9NRE1
Catalytic activity : Enzyme3.4.24.- [ Enzyme-Expasy ]   3.4.24.-3.4.24.- [ IntEnz-EBI ]   3.4.24.- [ BRENDA ]   3.4.24.- [ KEGG ]   
PhosPhoSitePlusQ9NRE1
Domaine pattern : Prosite (Expaxy)ZINC_PROTEASE (PS00142)   
Domains : Interpro (EBI)M10A_MMP    MetalloPept_cat_dom    MMP26    Pept_M10_metallopeptidase    Pept_M10A    Peptidase_Metallo   
Domain families : Pfam (Sanger)Peptidase_M10 (PF00413)   
Domain families : Pfam (NCBI)pfam00413   
Domain families : Smart (EMBL)ZnMc (SM00235)  
Conserved Domain (NCBI)MMP26
DMDM Disease mutations56547
Blocks (Seattle)MMP26
SuperfamilyQ9NRE1
Human Protein Atlas [tissue]ENSG00000167346-MMP26 [tissue]
Peptide AtlasQ9NRE1
HPRD05683
IPIIPI00299784   
Protein Interaction databases
DIP (DOE-UCLA)Q9NRE1
IntAct (EBI)Q9NRE1
FunCoupENSG00000167346
BioGRIDMMP26
STRING (EMBL)MMP26
ZODIACMMP26
Ontologies - Pathways
QuickGOQ9NRE1
Ontology : AmiGOmetalloendopeptidase activity  proteinaceous extracellular matrix  proteolysis  zinc ion binding  collagen catabolic process  negative regulation of inflammatory response  
Ontology : EGO-EBImetalloendopeptidase activity  proteinaceous extracellular matrix  proteolysis  zinc ion binding  collagen catabolic process  negative regulation of inflammatory response  
NDEx NetworkMMP26
Atlas of Cancer Signalling NetworkMMP26
Wikipedia pathwaysMMP26
Orthology - Evolution
OrthoDB56547
GeneTree (enSembl)ENSG00000167346
Phylogenetic Trees/Animal Genes : TreeFamMMP26
HOVERGENQ9NRE1
HOGENOMQ9NRE1
Homologs : HomoloGeneMMP26
Homology/Alignments : Family Browser (UCSC)MMP26
Gene fusions - Rearrangements
Fusion : QuiverMMP26
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerMMP26 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)MMP26
dbVarMMP26
ClinVarMMP26
1000_GenomesMMP26 
Exome Variant ServerMMP26
ExAC (Exome Aggregation Consortium)ENSG00000167346
GNOMAD BrowserENSG00000167346
Genetic variants : HAPMAP56547
Genomic Variants (DGV)MMP26 [DGVbeta]
DECIPHERMMP26 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisMMP26 
Mutations
ICGC Data PortalMMP26 
TCGA Data PortalMMP26 
Broad Tumor PortalMMP26
OASIS PortalMMP26 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICMMP26  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDMMP26
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch MMP26
DgiDB (Drug Gene Interaction Database)MMP26
DoCM (Curated mutations)MMP26 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)MMP26 (select a term)
intoGenMMP26
NCG5 (London)MMP26
Cancer3DMMP26(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM605470   
Orphanet
DisGeNETMMP26
MedgenMMP26
Genetic Testing Registry MMP26
NextProtQ9NRE1 [Medical]
TSGene56547
GENETestsMMP26
Target ValidationMMP26
Huge Navigator MMP26 [HugePedia]
snp3D : Map Gene to Disease56547
BioCentury BCIQMMP26
ClinGenMMP26
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD56547
Chemical/Pharm GKB GenePA30883
Clinical trialMMP26
Miscellaneous
canSAR (ICR)MMP26 (select the gene name)
Other databaseMEROPS The Peptidase Database
Probes
Litterature
PubMed55 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineMMP26
EVEXMMP26
GoPubMedMMP26
iHOPMMP26
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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