Version 5.4
Mus musculus Protein: Ckmt2
Summary
InnateDB Protein IDBP-171649.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Ckmt2
Protein Name creatine kinase, mitochondrial 2
Synonyms 2300008A19Rik; ScCKmit;
Species Mus musculus
Ensembl Protein ENSMUSP00000022122
InnateDB Gene IDBG-171647 (Ckmt2)
Protein Structure
UniProt Annotation
Function Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa (By similarity). {ECO:0000250}.
Subcellular Localization Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Intermembrane side {ECO:0000250}.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 0 experimentally validated interaction(s) in this database.
They are also associated with 8 interaction(s) predicted by orthology.
Predicted by orthology
Total 8 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0004111 creatine kinase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
GO:0016772 transferase activity, transferring phosphorus-containing groups
Biological Process
GO:0006603 phosphocreatine metabolic process
GO:0016310 phosphorylation
Cellular Component
GO:0005739 mitochondrion
GO:0005743 mitochondrial inner membrane
Protein Structure and Domains
PDB ID MGI:1923972
InterPro IPR022413 ATP:guanido phosphotransferase, N-terminal
IPR022414 ATP:guanido phosphotransferase, catalytic domain
PFAM PF02807
PF00217
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q6P8J7
PhosphoSite PhosphoSite-Q6P8J7
TrEMBL
UniProt Splice Variant
Entrez Gene 76722
UniGene
RefSeq NP_940807
MGI ID
MGI Symbol Ckmt2
OMIM
CCDS CCDS26679
HPRD
IMGT
EMBL BC061221
GenPept AAH61221

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