Version 5.4
Homo sapiens Gene: MMP27
Summary
InnateDB Gene IDBG-69142.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol MMP27
Gene Name matrix metallopeptidase 27
Synonyms
Species Homo sapiens
Ensembl Gene ENSG00000137675
Encoded Proteins
IDBP-69144
matrix metallopeptidase 27
Protein Structure
Useful resources Stemformatics EHFPI ImmGen
Entrez Gene
Summary 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. [provided by RefSeq, Jul 2008]
Gene Information
Type Protein coding
Genomic Location Chromosome 11:102691487-102705806
Strand Reverse strand
Band q22.2
Transcripts
ENST00000260229 ENSP00000260229
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 1 experimentally validated interaction(s) in this database.
Experimentally validated
Total 1 [view]
Protein-Protein 1 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0004222 metalloendopeptidase activity
GO:0005509 calcium ion binding
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
Biological Process
GO:0006508 proteolysis
GO:0030574 collagen catabolic process
Cellular Component
GO:0005578 proteinaceous extracellular matrix
GO:0031012 extracellular matrix
Orthologs
Species
Mus musculus
Bos taurus
Gene ID
Gene Order
ENSMUSG00000070323
View Gene Order
ENSBTAG00000040567
Not yet available
Cross-References
SwissProt
TrEMBL
UniProt Splice Variant
Entrez Gene
UniGene Hs.534479
RefSeq NM_022122
HUGO
OMIM
CCDS CCDS8319
HPRD 07025
IMGT
EMBL
GenPept
RNA Seq Atlas

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca