Flightless I Homolog (FLII)

FLI; FLIL; Fli1

SPN	N830
HGNC	3750
MGI	1342286
PubMed	24055811
RGD	1307590
UniProt	Q13045
Wiki	FLII

FLII encodes a protein with a gelsolin-like actin binding domain and an N-terminal leucine-rich repeat-protein protein interaction domain. The protein is similar to a Drosophila protein involved in early embryogenesis and the structural organization of indirect flight muscle. The gene is located within the Smith-Magenis syndrome region on chromosome 17.

The amino acid sequence deduced from the FLI cDNA has 52% similarity to that of the human gelsolin protein and also has an N-terminal leucine-rich domain with 16 consecutive leucine-rich repeats. FLII gene encodes a predicted 1,269-amino acid protein. Northern blot analysis revealed FLII expression as an approximately 4.4-kb mRNA in all tissues tested, with strongest expression in skeletal muscle.

Reference

"Genomic structure, evolution, and expression of human FLII, a gelsolin and leucine-rich-repeat family member: overlap with LLGL."
Genomics 42:46-54(1997) [PubMed] [Europe PMC] [Abstract]

"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]

"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]

"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]

"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]

"The Drosophila melanogaster flightless-I gene involved in gastrulation and muscle degeneration encodes gelsolin-like and leucine-rich repeat domains and is conserved in Caenorhabditis elegans and humans."
Proc. Natl. Acad. Sci. U.S.A. 90:11386-11390(1993) [PubMed] [Europe PMC] [Abstract]

"Identification of the binding partners for flightless I, a novel protein bridging the leucine-rich repeat and the gelsolin superfamilies."
J. Biol. Chem. 273:7920-7927(1998) [PubMed] [Europe PMC] [Abstract]

"TRIP: a novel double stranded RNA binding protein which interacts with the leucine rich repeat of flightless I."
Nucleic Acids Res. 26:3460-3467(1998) [PubMed] [Europe PMC] [Abstract]

"Novel proteins interacting with the leucine-rich repeat domain of human flightless-I identified by the yeast two-hybrid system."
Genomics 58:146-157(1999) [PubMed] [Europe PMC] [Abstract]

"Developmentally essential protein flightless I is a nuclear receptor coactivator with actin binding activity."
Mol. Cell. Biol. 24:2103-2117(2004) [PubMed] [Europe PMC] [Abstract]

"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]

"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]

"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]

"A quantitative atlas of mitotic phosphorylation."
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]

"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]

"Identification of Flightless-I as a substrate of the cytokine-independent survival kinase CISK."
J. Biol. Chem. 284:14377-14385(2009) [PubMed] [Europe PMC] [Abstract]

"Modulation of TLR signaling by multiple MyD88-interacting partners including leucine-rich repeat Fli-I-interacting proteins."
J. Immunol. 182:3450-3460(2009) [PubMed] [Europe PMC] [Abstract]

"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]

"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]

"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]

"Initial characterization of the human central proteome."
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]

"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]

"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]

"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]

"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]