FLII_HUMAN
ID FLII_HUMAN Reviewed; 1269 AA.
AC Q13045; B4DIL0; F5H407; J3QLG3;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 2.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Protein flightless-1 homolog;
GN Name=FLII; Synonyms=FLIL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9177775; DOI=10.1006/geno.1997.4709;
RA Campbell H.D., Fountain S., Young I.G., Claudianos C., Hoheisel J.D.,
RA Chen K.-S., Lupski J.R.;
RT "Genomic structure, evolution, and expression of human FLII, a gelsolin and
RT leucine-rich-repeat family member: overlap with LLGL.";
RL Genomics 42:46-54(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 1-11, AND ACETYLATION AT MET-1.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-1269 (ISOFORM 1).
RC TISSUE=Hippocampus;
RX PubMed=8248259; DOI=10.1073/pnas.90.23.11386;
RA Campbell H.D., Schimansky T., Claudianos C., Ozsarac N., Kasprzak A.B.,
RA Cotsell J.N., Young I.G., de Couet H.G., Miklos G.L.G.;
RT "The Drosophila melanogaster flightless-I gene involved in gastrulation and
RT muscle degeneration encodes gelsolin-like and leucine-rich repeat domains
RT and is conserved in Caenorhabditis elegans and humans.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:11386-11390(1993).
RN [7]
RP INTERACTION WITH ACTIN AND LRRFIP1, AND TISSUE SPECIFICITY.
RX PubMed=9525888; DOI=10.1074/jbc.273.14.7920;
RA Liu Y.-T., Yin H.L.;
RT "Identification of the binding partners for flightless I, a novel protein
RT bridging the leucine-rich repeat and the gelsolin superfamilies.";
RL J. Biol. Chem. 273:7920-7927(1998).
RN [8]
RP INTERACTION WITH LRRFIP1.
RX PubMed=9671805; DOI=10.1093/nar/26.15.3460;
RA Wilson S.A., Brown E.C., Kingsman A.J., Kingsman S.M.;
RT "TRIP: a novel double stranded RNA binding protein which interacts with the
RT leucine rich repeat of flightless I.";
RL Nucleic Acids Res. 26:3460-3467(1998).
RN [9]
RP INTERACTION WITH LRRFIP1 AND LRRFIP2.
RC TISSUE=Skeletal muscle;
RX PubMed=10366446; DOI=10.1006/geno.1999.5817;
RA Fong K.S.K., de Couet H.G.;
RT "Novel proteins interacting with the leucine-rich repeat domain of human
RT flightless-I identified by the yeast two-hybrid system.";
RL Genomics 58:146-157(1999).
RN [10]
RP FUNCTION, INTERACTION WITH CARM1; ESR1; THRB; NCOA2 AND ACTL6A, AND
RP MUTAGENESIS OF GLU-586 AND GLY-603.
RX PubMed=14966289; DOI=10.1128/mcb.24.5.2103-2117.2004;
RA Lee Y.-H., Campbell H.D., Stallcup M.R.;
RT "Developmentally essential protein flightless I is a nuclear receptor
RT coactivator with actin binding activity.";
RL Mol. Cell. Biol. 24:2103-2117(2004).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-856, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406 AND SER-856, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-856, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-856, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP PHOSPHORYLATION AT SER-436 AND THR-818, AND INTERACTION WITH SGK3.
RX PubMed=19293151; DOI=10.1074/jbc.m807770200;
RA Xu J., Liao L., Qin J., Xu J., Liu D., Songyang Z.;
RT "Identification of Flightless-I as a substrate of the cytokine-independent
RT survival kinase CISK.";
RL J. Biol. Chem. 284:14377-14385(2009).
RN [17]
RP INTERACTION WITH LRRFIP1; LRRFIP2 AND MYD88.
RX PubMed=19265123; DOI=10.4049/jimmunol.0802260;
RA Dai P., Jeong S.Y., Yu Y., Leng T., Wu W., Xie L., Chen X.;
RT "Modulation of TLR signaling by multiple MyD88-interacting partners
RT including leucine-rich repeat Fli-I-interacting proteins.";
RL J. Immunol. 182:3450-3460(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-856, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-21, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406; SER-436 AND SER-856, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-436 AND SER-856, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406; SER-856 AND SER-860, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-436 AND SER-856, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: May play a role as coactivator in transcriptional activation
CC by hormone-activated nuclear receptors (NR) and acts in cooperation
CC with NCOA2 and CARM1. Involved in estrogen hormone signaling. Involved
CC in early embryonic development (By similarity). May play a role in
CC regulation of cytoskeletal rearrangements involved in cytokinesis and
CC cell migration, by inhibiting Rac1-dependent paxillin phosphorylation.
CC {ECO:0000250, ECO:0000269|PubMed:14966289}.
CC -!- SUBUNIT: Interacts with actin, ACTL6A, NCOA2, CARM1 and MYD88.
CC Interacts with LRRFIP1 and LRRFIP2. Upon LPS stimulation, LRRFIP2
CC competes for MYD88-binding. LRRFIP1 constitutively blocks the
CC interaction with MyD88, even in the absence of LPS. Interacts with the
CC nuclear receptors ESR1 and THRB. Interacts with SGK3.
CC {ECO:0000269|PubMed:10366446, ECO:0000269|PubMed:14966289,
CC ECO:0000269|PubMed:19265123, ECO:0000269|PubMed:19293151,
CC ECO:0000269|PubMed:9525888, ECO:0000269|PubMed:9671805}.
CC -!- INTERACTION:
CC Q13045; Q32MZ4: LRRFIP1; NbExp=2; IntAct=EBI-351549, EBI-1369100;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center,
CC centrosome {ECO:0000250}. Cell junction, focal adhesion {ECO:0000250}.
CC Note=Colocalizes to actin-rich structures in blastocysts and, together
CC with HRAS, RHOA and CDC42, in migrating fibroblasts. Localizes to
CC centrosomes (By similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q13045-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13045-2; Sequence=VSP_044686, VSP_044687;
CC Name=3;
CC IsoId=Q13045-3; Sequence=VSP_046887;
CC -!- TISSUE SPECIFICITY: Strongest expression in skeletal muscle with high
CC expression also in the heart and lung. {ECO:0000269|PubMed:9525888}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAG58522.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U80184; AAC02796.1; -; Genomic_DNA.
DR EMBL; AK295655; BAG58522.1; ALT_INIT; mRNA.
DR EMBL; AC127537; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC025300; AAH25300.1; -; mRNA.
DR EMBL; U01184; AAC03568.1; -; mRNA.
DR CCDS; CCDS11192.1; -. [Q13045-1]
DR CCDS; CCDS58521.1; -. [Q13045-3]
DR CCDS; CCDS58522.1; -. [Q13045-2]
DR PIR; A49674; A49674.
DR RefSeq; NP_001243193.1; NM_001256264.1. [Q13045-3]
DR RefSeq; NP_001243194.1; NM_001256265.1. [Q13045-2]
DR RefSeq; NP_002009.1; NM_002018.3. [Q13045-1]
DR AlphaFoldDB; Q13045; -.
DR SMR; Q13045; -.
DR BioGRID; 108603; 195.
DR IntAct; Q13045; 70.
DR MINT; Q13045; -.
DR STRING; 9606.ENSP00000324573; -.
DR iPTMnet; Q13045; -.
DR MetOSite; Q13045; -.
DR PhosphoSitePlus; Q13045; -.
DR SwissPalm; Q13045; -.
DR BioMuta; FLII; -.
DR DMDM; 18202493; -.
DR EPD; Q13045; -.
DR jPOST; Q13045; -.
DR MassIVE; Q13045; -.
DR MaxQB; Q13045; -.
DR PaxDb; Q13045; -.
DR PeptideAtlas; Q13045; -.
DR PRIDE; Q13045; -.
DR ProteomicsDB; 26432; -.
DR ProteomicsDB; 59121; -. [Q13045-1]
DR Antibodypedia; 1881; 178 antibodies from 32 providers.
DR DNASU; 2314; -.
DR Ensembl; ENST00000327031.9; ENSP00000324573.4; ENSG00000177731.16. [Q13045-1]
DR Ensembl; ENST00000545457.6; ENSP00000438536.2; ENSG00000177731.16. [Q13045-2]
DR Ensembl; ENST00000579294.5; ENSP00000463534.1; ENSG00000177731.16. [Q13045-3]
DR Ensembl; ENST00000638207.2; ENSP00000491480.1; ENSG00000284571.2. [Q13045-1]
DR Ensembl; ENST00000638404.1; ENSP00000492392.1; ENSG00000284571.2. [Q13045-2]
DR Ensembl; ENST00000638812.1; ENSP00000491660.1; ENSG00000284571.2. [Q13045-3]
DR GeneID; 2314; -.
DR KEGG; hsa:2314; -.
DR MANE-Select; ENST00000327031.9; ENSP00000324573.4; NM_002018.4; NP_002009.1.
DR UCSC; uc002gsr.3; human. [Q13045-1]
DR CTD; 2314; -.
DR DisGeNET; 2314; -.
DR GeneCards; FLII; -.
DR HGNC; HGNC:3750; FLII.
DR HPA; ENSG00000177731; Tissue enhanced (skeletal).
DR MalaCards; FLII; -.
DR MIM; 600362; gene.
DR neXtProt; NX_Q13045; -.
DR OpenTargets; ENSG00000177731; -.
DR Orphanet; 819; Smith-Magenis syndrome.
DR PharmGKB; PA28171; -.
DR VEuPathDB; HostDB:ENSG00000177731; -.
DR eggNOG; KOG0444; Eukaryota.
DR GeneTree; ENSGT00940000156643; -.
DR HOGENOM; CLU_002568_1_0_1; -.
DR InParanoid; Q13045; -.
DR OMA; CFHGWSA; -.
DR OrthoDB; 1376537at2759; -.
DR PhylomeDB; Q13045; -.
DR TreeFam; TF313468; -.
DR PathwayCommons; Q13045; -.
DR SignaLink; Q13045; -.
DR SIGNOR; Q13045; -.
DR BioGRID-ORCS; 2314; 213 hits in 1082 CRISPR screens.
DR ChiTaRS; FLII; human.
DR GeneWiki; FLII; -.
DR GenomeRNAi; 2314; -.
DR Pharos; Q13045; Tbio.
DR PRO; PR:Q13045; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q13045; protein.
DR Bgee; ENSG00000177731; Expressed in lower esophagus mucosa and 90 other tissues.
DR ExpressionAtlas; Q13045; baseline and differential.
DR Genevisible; Q13045; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005903; C:brush border; IEA:Ensembl.
DR GO; GO:0034451; C:centriolar satellite; IDA:HPA.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003779; F:actin binding; IDA:HGNC.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0051014; P:actin filament severing; IBA:GO_Central.
DR GO; GO:0008154; P:actin polymerization or depolymerization; IBA:GO_Central.
DR GO; GO:0051016; P:barbed-end actin filament capping; IBA:GO_Central.
DR GO; GO:0030239; P:myofibril assembly; IBA:GO_Central.
DR Gene3D; 3.40.20.10; -; 6.
DR Gene3D; 3.80.10.10; -; 3.
DR InterPro; IPR029006; ADF-H/Gelsolin-like_dom_sf.
DR InterPro; IPR029919; FliI.
DR InterPro; IPR007123; Gelsolin-like_dom.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR025875; Leu-rich_rpt_4.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR007122; Villin/Gelsolin.
DR PANTHER; PTHR11977; PTHR11977; 1.
DR PANTHER; PTHR11977:SF85; PTHR11977:SF85; 1.
DR Pfam; PF00626; Gelsolin; 4.
DR Pfam; PF12799; LRR_4; 1.
DR Pfam; PF13855; LRR_8; 3.
DR PRINTS; PR00597; GELSOLIN.
DR SMART; SM00262; GEL; 6.
DR SMART; SM00369; LRR_TYP; 9.
DR PROSITE; PS51450; LRR; 11.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Activator; Alternative splicing; Cell junction;
KW Cytoplasm; Cytoskeleton; Developmental protein; Direct protein sequencing;
KW Leucine-rich repeat; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation.
FT CHAIN 1..1269
FT /note="Protein flightless-1 homolog"
FT /id="PRO_0000218750"
FT REPEAT 7..32
FT /note="LRR 1"
FT REPEAT 33..55
FT /note="LRR 2"
FT REPEAT 56..78
FT /note="LRR 3"
FT REPEAT 80..103
FT /note="LRR 4"
FT REPEAT 104..126
FT /note="LRR 5"
FT REPEAT 127..149
FT /note="LRR 6"
FT REPEAT 150..173
FT /note="LRR 7"
FT REPEAT 175..196
FT /note="LRR 8"
FT REPEAT 197..222
FT /note="LRR 9"
FT REPEAT 223..245
FT /note="LRR 10"
FT REPEAT 247..268
FT /note="LRR 11"
FT REPEAT 269..291
FT /note="LRR 12"
FT REPEAT 293..316
FT /note="LRR 13"
FT REPEAT 318..339
FT /note="LRR 14"
FT REPEAT 340..363
FT /note="LRR 15"
FT REPEAT 501..559
FT /note="Gelsolin-like 1"
FT REPEAT 640..670
FT /note="Gelsolin-like 2"
FT REPEAT 755..798
FT /note="Gelsolin-like 3"
FT REPEAT 1068..1115
FT /note="Gelsolin-like 4"
FT REPEAT 1176..1218
FT /note="Gelsolin-like 5"
FT REGION 1..427
FT /note="Interaction with LRRFIP1 and LRRFIP2"
FT REGION 452..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..827
FT /note="Interaction with ACTL6A"
FT /evidence="ECO:0000269|PubMed:14966289"
FT REGION 951..975
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:12665801,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 21
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 406
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 436
FT /note="Phosphoserine; by SGK3"
FT /evidence="ECO:0000269|PubMed:19293151,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 818
FT /note="Phosphothreonine; by SGK3"
FT /evidence="ECO:0000269|PubMed:19293151"
FT MOD_RES 856
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 860
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..21
FT /note="MEATGVLPFVRGVDLSGNDFK -> MDLRGLRPVP (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_046887"
FT VAR_SEQ 138..191
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044686"
FT VAR_SEQ 416
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044687"
FT VARIANT 1243
FT /note="R -> H (in dbSNP:rs8821)"
FT /id="VAR_029258"
FT MUTAGEN 586
FT /note="E->K: No change in ESR1 binding but reduced binding
FT to ACTL6A and reduced coactivator function."
FT /evidence="ECO:0000269|PubMed:14966289"
FT MUTAGEN 603
FT /note="G->S: No change in binding to ACTL6A or in
FT coactivator function."
FT /evidence="ECO:0000269|PubMed:14966289"
FT CONFLICT 1
FT /note="M -> V (in Ref. 2; BAG58522)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="Y -> N (in Ref. 2; BAG58522)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1269 AA; 144751 MW; 29AC7C07738B7B47 CRC64;
MEATGVLPFV RGVDLSGNDF KGGYFPENVK AMTSLRWLKL NRTGLCYLPE ELAALQKLEH
LSVSHNNLTT LHGELSSLPS LRAIVARANS LKNSGVPDDI FKLDDLSVLD LSHNQLTECP
RELENAKNML VLNLSHNSID TIPNQLFINL TDLLYLDLSE NRLESLPPQM RRLVHLQTLV
LNGNPLLHAQ LRQLPAMTAL QTLHLRSTQR TQSNLPTSLE GLSNLADVDL SCNDLTRVPE
CLYTLPSLRR LNLSSNQITE LSLCIDQWVH VETLNLSRNQ LTSLPSAICK LSKLKKLYLN
SNKLDFDGLP SGIGKLTNLE EFMAANNNLE LVPESLCRCP KLRKLVLNKN HLVTLPEAIH
FLTEIEVLDV RENPNLVMPP KPADRAAEWY NIDFSLQNQL RLAGASPATV AAAAAAGSGP
KDPMARKMRL RRRKDSAQDD QAKQVLKGMS DVAQEKNKKQ EESADARAPS GKVRRWDQGL
EKPRLDYSEF FTEDVGQLPG LTIWQIENFV PVLVEEAFHG KFYEADCYIV LKTFLDDSGS
LNWEIYYWIG GEATLDKKAC SAIHAVNLRN YLGAECRTVR EEMGDESEEF LQVFDNDISY
IEGGTASGFY TVEDTHYVTR MYRVYGKKNI KLEPVPLKGT SLDPRFVFLL DRGLDIYVWR
GAQATLSSTT KARLFAEKIN KNERKGKAEI TLLVQGQELP EFWEALGGEP SEIKKHVPED
FWPPQPKLYK VGLGLGYLEL PQINYKLSVE HKQRPKVELM PRMRLLQSLL DTRCVYILDC
WSDVFIWLGR KSPRLVRAAA LKLGQELCGM LHRPRHATVS RSLEGTEAQV FKAKFKNWDD
VLTVDYTRNA EAVLQSPGLS GKVKRDAEKK DQMKADLTAL FLPRQPPMSL AEAEQLMEEW
NEDLDGMEGF VLEGKKFARL PEEEFGHFYT QDCYVFLCRY WVPVEYEEEE KKEDKEEKAE
GKEGEEATAE AEEKQPEEDF QCIVYFWQGR EASNMGWLTF TFSLQKKFES LFPGKLEVVR
MTQQQENPKF LSHFKRKFII HRGKRKAVQG AQQPSLYQIR TNGSALCTRC IQINTDSSLL
NSEFCFILKV PFESEDNQGI VYAWVGRASD PDEAKLAEDI LNTMFDTSYS KQVINEGEEP
ENFFWVGIGA QKPYDDDAEY MKHTRLFRCS NEKGYFAVTE KCSDFCQDDL ADDDIMLLDN
GQEVYMWVGT QTSQVEIKLS LKACQVYIQH MRSKEHERPR RLRLVRKGNE QHAFTRCFHA
WSAFCKALA
