Version 5.4
Mus musculus Protein: Marcks
Summary
InnateDB Protein IDBP-144105.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Marcks
Protein Name myristoylated alanine rich protein kinase C substrate
Synonyms Macs; PKCSL;
Species Mus musculus
Ensembl Protein ENSMUSP00000090245
InnateDB Gene IDBG-144103 (Marcks)
Protein Structure
UniProt Annotation
Function MARCKS is the most prominent cellular substrate for protein kinase C. This protein binds calmodulin, actin, and synapsin. MARCKS is a filamentous (F) actin cross-linking protein.
Subcellular Localization Cytoplasm, cytoskeleton {ECO:0000305}. Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}.
Disease Associations
Tissue Specificity Brain, spleen, less in kidney and heart, and very low levels in liver.
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 12 experimentally validated interaction(s) in this database.
They are also associated with 17 interaction(s) predicted by orthology.
Experimentally validated
Total 12 [view]
Protein-Protein 12 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 17 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003779 actin binding
GO:0005080 protein kinase C binding
GO:0005515 protein binding
GO:0005516 calmodulin binding
Biological Process
Cellular Component
GO:0005737 cytoplasm
GO:0005813 centrosome
GO:0005938 cell cortex
GO:0016020 membrane
GO:0042585 germinal vesicle
GO:0070062 extracellular vesicular exosome
Protein Structure and Domains
PDB ID MGI:96907
InterPro IPR002101 Myristoylated alanine-rich C-kinase substrate MARCKS
PFAM PF02063
PRINTS PR00963
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt P26645
PhosphoSite PhosphoSite-P26645
TrEMBL Q05BL6
UniProt Splice Variant
Entrez Gene 17118
UniGene Mm.485179
RefSeq NP_032564
MGI ID 1IWQ
MGI Symbol Marcks
OMIM
CCDS CCDS23784
HPRD
IMGT
EMBL BC039911 BC046601 M60474
GenPept AAA39491 AAH39911 AAH46601

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