Version 5.4
Mus musculus Protein: Cldn18
Summary
InnateDB Protein IDBP-193117.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Cldn18
Protein Name claudin 18
Synonyms
Species Mus musculus
Ensembl Protein ENSMUSP00000035048
InnateDB Gene IDBG-193115 (Cldn18)
Protein Structure
UniProt Annotation
Function Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium- independent cell-adhesion activity. {ECO:0000250}.
Subcellular Localization Cell junction, tight junction. Cell membrane; Multi-pass membrane protein.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 3 experimentally validated interaction(s) in this database.
They are also associated with 1 interaction(s) predicted by orthology.
Experimentally validated
Total 3 [view]
Protein-Protein 3 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 1 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0005198 structural molecule activity
GO:0042802 identical protein binding
Biological Process
GO:0016338 calcium-independent cell-cell adhesion
Cellular Component
GO:0005886 plasma membrane
GO:0005923 tight junction
GO:0016021 integral component of membrane
Protein Structure and Domains
PDB ID MGI:1929209
InterPro IPR003928 Claudin-18
IPR004031 PMP-22/EMP/MP20/Claudin superfamily
IPR006187 Claudin
PFAM PF00822
PF13903
PRINTS PR01448
PR01077
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt P56857
PhosphoSite PhosphoSite-P56857
TrEMBL
UniProt Splice Variant
Entrez Gene 56492
UniGene Mm.469796
RefSeq NP_062789
MGI ID
MGI Symbol Cldn18
OMIM
CCDS CCDS23437
HPRD
IMGT
EMBL AF221068 AF349450 AF349451 AF349453
GenPept AAF26447 AAL15635 AAL15636 AAL15638

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