Version 5.4
Homo sapiens Protein: MTMR9
Summary
InnateDB Protein IDBP-7197.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol MTMR9
Protein Name myotubularin related protein 9
Synonyms
Species Homo sapiens
Ensembl Protein ENSP00000221086
InnateDB Gene IDBG-7193 (MTMR9)
Protein Structure
UniProt Annotation
Function Probable pseudophosphatase. Contains a Gly residue instead of a conserved Cys residue in the dsPTPase catalytic loop which renders it catalytically inactive as a phosphatase (Potential). {ECO:0000305}.
Subcellular Localization Cytoplasm {ECO:0000269PubMed:16787938}.
Disease Associations
Tissue Specificity Expressed in many tissues.
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 15 experimentally validated interaction(s) in this database.
Experimentally validated
Total 15 [view]
Protein-Protein 15 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0005515 protein binding
GO:0016791 phosphatase activity
GO:0030234 enzyme regulator activity
Biological Process
GO:0016311 dephosphorylation
GO:0050790 regulation of catalytic activity
Cellular Component
GO:0005737 cytoplasm
Protein Structure and Domains
PDB ID
InterPro IPR010569 Myotubularin-like phosphatase domain
IPR029021 Protein-tyrosine phosphatase-like
PFAM PF06602
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q96QG7
PhosphoSite PhosphoSite-Q96QG7
TrEMBL Q9Y4N6
UniProt Splice Variant
Entrez Gene 66036
UniGene Hs.639224
RefSeq NP_056273
HUGO HGNC:14596
OMIM 606260
CCDS CCDS5979
HPRD 09377
IMGT
EMBL AF131216 AJ297823 AJ297824 AK000444 AK294463 AL080178 BC022003 BC034990 BC093788 BC101623
GenPept AAH22003 AAH34990 AAH93788 AAI01624 BAA91170 BAH11777 CAB45763 CAC51114 CAC51115

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