Go Annotations as Summary Text (Tabular View) (GO Graph)

GO curators for mouse genes have assigned the following annotations to the gene product of Flna. (This text reflects annotations as of Wednesday, January 23, 2013.)

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Summary from NCBI RefSeq

[Summary is not available for the mouse gene. This summary is for the human ortholog.] The protein encoded by this gene is an actin-binding protein that crosslinks actin filaments and links actin filaments to membrane glycoproteins. The encoded protein is involved in remodeling the cytoskeleton to effect changes in cell shape and migration. This protein interacts with integrins, transmembrane receptor complexes, and second messengers. Defects in this gene are a cause of several syndromes, including periventricular nodular heterotopias (PVNH1, PVNH4), otopalatodigital syndromes (OPD1, OPD2), frontometaphyseal dysplasia (FMD), Melnick-Needles syndrome (MNS), and X-linked congenital idiopathic intestinal pseudoobstruction (CIIPX). Two transcript variants encoding different isoforms have been found for this gene.[provided by RefSeq, Mar 2009]

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Summary text based on GO annotations supported by experimental evidence in mouse

• Researchers have inferred from direct assay, that the gene product of Flna
  • participates in the following biological processes:
    • early endosome to late endosome transport ^[4]
  • performs the following molecular functions:
    • protein kinase C binding ^[7]
  • is located in the following cellular components:
    • trans-Golgi network ^[4]
• The gene product of Flna has been shown to bind to the gene products of Amot, Flnb, Furin, Myoz1, Plcg2. ^{[1, 2, 4, 5, 6]}
• Researchers have inferred, based on genetic interactions, that the gene product of Flna
  • participates in the following biological processes:
    • actin cytoskeleton organization based on interactions with Fam101b ^[3]
    • epithelial to mesenchymal transition based on interactions with Fam101b ^[3]

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Summary text based on GO annotations supported by experimental evidence in other organisms

• From comparative sequence analysis (see table for details), MGI curators have determined that the gene product of Flna:
  • participates in the following biological processes:
    • actin crosslink formation
    • actin cytoskeleton reorganization
    • adenylate cyclase-inhibiting dopamine receptor signaling pathway
    • cilium assembly
    • cytoplasmic sequestering of protein
    • establishment of protein localization
    • negative regulation of protein catabolic process
    • negative regulation of sequence-specific DNA binding transcription factor activity
    • positive regulation of I-kappaB kinase/NF-kappaB cascade
    • positive regulation of transcription factor import into nucleus
    • protein localization to cell surface
    • protein stabilization
    • receptor clustering
    • spindle assembly involved in mitosis
  • performs the following molecular functions:
    • actin filament binding
    • Fc-gamma receptor I complex binding
    • glycoprotein binding
    • protein homodimerization activity
    • Rac GTPase binding
    • Ral GTPase binding
    • Rho GTPase binding
    • signal transducer activity
    • small GTPase binding
    • transcription factor binding
  • is located in the following cellular components:
    • actin cytoskeleton
    • actin filament
    • cortical cytoskeleton
    • cytoplasm
    • cytosol
    • extracellular vesicular exosome
    • Myb complex
    • nucleus
    • plasma membrane

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Summary text for additional MGI annotations

• Automated translation to GO terms of SwissProt keywords that describe Flna indicates that it:
  • participates in the following biological processes:
    • cell projection organization
  • is located in the following cellular components:
    • cytoskeleton

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References

1. Ernkvist M et al. (2009) The Amot/Patj/Syx signaling complex spatially controls RhoA GTPase activity in migrating endothelial cells. Blood, 113:244-53. (PubMed:18824598)
2. Frey N et al. (2000) Calsarcins, a novel family of sarcomeric calcineurin-binding proteins Proc Natl Acad Sci U S A, 97:14632-7. (PubMed:11114196)
3. Gay O et al. (2011) RefilinB (FAM101B) targets FilaminA to organize perinuclear actin networks and regulates nuclear shape. Proc Natl Acad Sci U S A, 108:11464-9. (PubMed:21709252)
4. Liu G et al. (1997) Cytoskeletal protein ABP-280 directs the intracellular trafficking of furin and modulates proprotein processing in the endocytic pathway. J Cell Biol, 139:1719-33. (PubMed:9412467)
5. Papin J et al. (2004) Bioinformatics and cellular signaling. Curr Opin Biotechnol, 15:78-81. (PubMed:15102471)
6. Sheen VL et al. (2002) Filamin A and Filamin B are co-expressed within neurons during periods of neuronal migration and can physically interact. Hum Mol Genet, 11:2845-54. (PubMed:12393796)
7. Tigges U et al. (2003) The F-actin cross-linking and focal adhesion protein filamin A is a ligand and in vivo substrate for protein kinase C alpha. J Biol Chem, 278:23561-9. (PubMed:12704190)

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Gene Ontology Evidence Code Abbreviations:

EXP Inferred from experiment

IC Inferred by curator

IDA Inferred from direct assay

IEA Inferred from electronic annotation

IGI Inferred from genetic interaction

IMP Inferred from mutant phenotype

IPI Inferred from physical interaction

ISS Inferred from sequence or structural similarity

ISO Inferred from sequence orthology

ISA Inferred from sequence alignment

ISM Inferred from sequence model

NAS Non-traceable author statement

ND No biological data available

RCA Reviewed computational analysis

TAS Traceable author statement

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