Version 5.4
Homo sapiens Protein: LMLN
Summary
InnateDB Protein IDBP-473937.4
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol LMLN
Protein Name leishmanolysin-like (metallopeptidase M8 family)
Synonyms
Species Homo sapiens
Ensembl Protein ENSP00000418324
InnateDB Gene IDBG-71932 (LMLN)
Protein Structure
UniProt Annotation
Function Metalloprotease essential for the coordination of mitotic progression, and also plays a role in cell migration. {ECO:0000250}.
Subcellular Localization Cytoplasm. Lipid droplet. Note=Found in ring-like structures resembling invadopodia. In migrating cells it relocalizes from internal structures to the leading edge of cells.
Disease Associations
Tissue Specificity Expressed in all cell lines analyzed. {ECO:0000269PubMed:19706689}.
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 0 experimentally validated interaction(s) in this database.
Gene Ontology

Molecular Function
Accession GO Term
GO:0004222 metalloendopeptidase activity
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis
GO:0007067 mitotic nuclear division
GO:0007155 cell adhesion
Cellular Component
GO:0005737 cytoplasm
GO:0005811 lipid particle
GO:0005925 focal adhesion
GO:0016020 membrane
Protein Structure and Domains
PDB ID
InterPro IPR001577 Peptidase M8, leishmanolysin
PFAM PF01457
PRINTS PR00782
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q96KR4
PhosphoSite PhosphoSite-Q96KR4
TrEMBL
UniProt Splice Variant
Entrez Gene 89782
UniGene Hs.708456
RefSeq
HUGO HGNC:15991
OMIM 609380
CCDS
HPRD 07023
IMGT
EMBL AC135893 AJ312398 AJ312399 AM920777 AM920778
GenPept CAC42882 CAC42883 CAP49203 CAP49204

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