Version 5.4
Mus musculus Protein: Fnip2
Summary
InnateDB Protein IDBP-153031.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Fnip2
Protein Name folliculin interacting protein 2
Synonyms
Species Mus musculus
Ensembl Protein ENSMUSP00000075497
InnateDB Gene IDBG-153029 (Fnip2)
Protein Structure
UniProt Annotation
Function May be involved in energy and/or nutrient sensing through the AMPK and mTOR signaling pathways. May regulate phosphorylation of RPS6KB1 (By similarity). May play a role in the signal transduction pathway of apoptosis induced by O6- methylguanine-mispaired lesions. {ECO:0000250, ECO:0000269PubMed:19137017}.
Subcellular Localization Cytoplasm {ECO:0000269PubMed:19137017}. Note=Colocalizes with FLCN in the cytoplasm. {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.
Gene Ontology

Molecular Function
Accession GO Term
GO:0003674 molecular_function
Biological Process
GO:0000122 negative regulation of transcription from RNA polymerase II promoter
GO:0001932 regulation of protein phosphorylation
GO:0006468 protein phosphorylation
GO:0008630 intrinsic apoptotic signaling pathway in response to DNA damage
GO:0033138 positive regulation of peptidyl-serine phosphorylation
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005886 plasma membrane
Protein Structure and Domains
PDB ID MGI:2683054
InterPro
PFAM
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q80TD3
PhosphoSite PhosphoSite-Q80TD3
TrEMBL
UniProt Splice Variant
Entrez Gene 329679
UniGene Mm.244005
RefSeq NP_001156471
MGI ID
MGI Symbol Fnip2
OMIM
CCDS CCDS50934
HPRD
IMGT
EMBL AC113945 AC142502 AK122512
GenPept BAC65794

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