ID FLI1_HUMAN Reviewed; 452 AA. AC Q01543; B2R8H2; B4DFV4; B4DTC6; G3V183; Q14319; Q92480; Q9UE07; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 27-MAR-2024, entry version 234. DE RecName: Full=Friend leukemia integration 1 transcription factor; DE AltName: Full=Proto-oncogene Fli-1; DE AltName: Full=Transcription factor ERGB; GN Name=FLI1; 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 [MRNA] (ISOFORM 1), AND CHROMOSOMAL TRANSLOCATION. RC TISSUE=Bone marrow; RX PubMed=1522903; DOI=10.1038/359162a0; RA Delattre O., Zucman J., Plougastel B., Desmaze C., Melot T., Peter M., RA Kovar H., Joubert I., de Jong P., Rouleau G., Aurias A., Thomas G.; RT "Gene fusion with an ETS DNA-binding domain caused by chromosome RT translocation in human tumours."; RL Nature 359:162-165(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=1445800; RA Watson D.K., Smyth F.E., Thompson D.M., Cheng J.Q., Testa J.R., Papas T.S., RA Seth A.; RT "The ERGB/Fli-1 gene: isolation and characterization of a new member of the RT family of human ETS transcription factors."; RL Cell Growth Differ. 3:705-713(1992). RN [3] RP SEQUENCE REVISION. RA Watson D.; RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=1394211; RA Prasad D.D., Rao V.N., Reddy E.S.; RT "Structure and expression of human Fli-1 gene."; RL Cancer Res. 52:5833-5837(1992). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Blood; RX PubMed=8439553; DOI=10.1016/0167-4781(93)90283-j; RA Hromas R., May W., Denny C., Raskind W., Moore J., Maki R.A., Beck E., RA Klemsz M.J.; RT "Human FLI-1 localizes to chromosome 11q24 and has an aberrant transcript RT in neuroepithelioma."; RL Biochim. Biophys. Acta 1172:155-158(1993). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND CHROMOSOMAL RP TRANSLOCATION. RX PubMed=1765382; DOI=10.1016/0888-7543(91)90124-w; RA Baud V., Lipinski M., Rassart E., Poliquin L., Bergeron D.; RT "The human homolog of the mouse common viral integration region, FLI1, maps RT to 11q23-q24."; RL Genomics 11:223-224(1991). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Ubhi B.T.S., Rainey D.R., Meredith D.M.; RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4). RC TISSUE=Amygdala, Placenta, and Thymus; 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 [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16554811; DOI=10.1038/nature04632; RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G., RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., RA Hattori M., Rogers J., Lander E.S., Sakaki Y.; RT "Human chromosome 11 DNA sequence and analysis including novel gene RT identification."; RL Nature 440:497-500(2006). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lymph; 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 [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 58-452. RX PubMed=9751743; DOI=10.1073/pnas.95.20.11786; RA Zucman-Rossi J., Legoix P., Victor J.M., Lopez B., Thomas G.; RT "Chromosome translocation based on illegitimate recombination in human RT tumors."; RL Proc. Natl. Acad. Sci. U.S.A. 95:11786-11791(1998). RN [13] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 278-301. RC TISSUE=Placenta; RX PubMed=7542907; DOI=10.1002/gcc.2870130209; RA Bhagirath T., Abe S., Nojima T., Yoshida M.C.; RT "Molecular analysis of a t(11;22) translocation junction in a case of RT Ewing's sarcoma."; RL Genes Chromosomes Cancer 13:126-132(1995). RN [14] RP IDENTIFICATION BY 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 [15] RP FUNCTION, INVOLVEMENT IN BDPLT21, VARIANTS BDPLT21 TRP-337 AND CYS-343, AND RP CHARACTERIZATION OF VARIANTS BDPLT21 TRP-337 AND CYS-343. RX PubMed=24100448; DOI=10.1182/blood-2013-06-506873; RG UK Genotyping and Phenotyping of Platelets Study Group; RA Stockley J., Morgan N.V., Bem D., Lowe G.C., Lordkipanidze M., Dawood B., RA Simpson M.A., Macfarlane K., Horner K., Leo V.C., Talks K., Motwani J., RA Wilde J.T., Collins P.W., Makris M., Watson S.P., Daly M.E.; RT "Enrichment of FLI1 and RUNX1 mutations in families with excessive bleeding RT and platelet dense granule secretion defects."; RL Blood 122:4090-4093(2013). RN [16] RP FUNCTION, INVOLVEMENT IN BDPLT21, VARIANT BDPLT21 TRP-324, AND RP CHARACTERIZATION OF VARIANT BDPLT21 TRP-324. RX PubMed=26316623; DOI=10.1182/blood-2015-06-650887; RA Stevenson W.S., Rabbolini D.J., Beutler L., Chen Q., Gabrielli S., RA Mackay J.P., Brighton T.A., Ward C.M., Morel-Kopp M.C.; RT "Paris-Trousseau thrombocytopenia is phenocopied by the autosomal recessive RT inheritance of a DNA-binding domain mutation in FLI1."; RL Blood 126:2027-2030(2015). RN [17] RP FUNCTION, SUBCELLULAR LOCATION, INVOLVEMENT IN BDPLT21, VARIANTS BDPLT21 RP GLN-337 AND GLU-345, AND CHARACTERIZATION OF VARIANTS BDPLT21 GLN-337 AND RP GLU-345. RX PubMed=28255014; DOI=10.3324/haematol.2016.153577; RA Saultier P., Vidal L., Canault M., Bernot D., Falaise C., Pouymayou C., RA Bordet J.C., Saut N., Rostan A., Baccini V., Peiretti F., Favier M., RA Lucca P., Deleuze J.F., Olaso R., Boland A., Morange P.E., Gachet C., RA Malergue F., Faure S., Eckly A., Tregouet D.A., Poggi M., Alessi M.C.; RT "Macrothrombocytopenia and dense granule deficiency associated with FLI1 RT variants: ultrastructural and pathogenic features."; RL Haematologica 102:1006-1016(2017). RN [18] RP STRUCTURE BY NMR OF 276-373. RX PubMed=7773776; DOI=10.1038/nsb1294-871; RA Liang H., Mao X., Olejniczak E.T., Nettesheim D.G., Yu L., Meadows R.P., RA Thompson C.B., Fesik S.W.; RT "Solution structure of the ets domain of Fli-1 when bound to DNA."; RL Nat. Struct. Biol. 1:871-875(1994). RN [19] RP STRUCTURE BY NMR OF 114-198. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the SAM_pnt-domain of the human Friend leukemia RT integration 1 transcription factor."; RL Submitted (NOV-2005) to the PDB data bank. CC -!- FUNCTION: Sequence-specific transcriptional activator (PubMed:24100448, CC PubMed:26316623, PubMed:28255014). Recognizes the DNA sequence 5'- CC C[CA]GGAAGT-3'. {ECO:0000269|PubMed:24100448, CC ECO:0000269|PubMed:26316623, ECO:0000269|PubMed:28255014}. CC -!- SUBUNIT: Can form homodimers or heterodimers with ETV6/TEL1. CC -!- INTERACTION: CC Q01543; P56545-3: CTBP2; NbExp=3; IntAct=EBI-2271018, EBI-10171902; CC Q01543; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-2271018, EBI-747107; CC Q01543; P84022: SMAD3; NbExp=3; IntAct=EBI-2271018, EBI-347161; CC Q01543; O94993: SOX30; NbExp=3; IntAct=EBI-2271018, EBI-742973; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28255014}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q01543-1; Sequence=Displayed; CC Name=2; CC IsoId=Q01543-2; Sequence=VSP_001478; CC Name=3; CC IsoId=Q01543-3; Sequence=VSP_045276; CC Name=4; CC IsoId=Q01543-4; Sequence=VSP_046943; CC -!- DISEASE: Ewing sarcoma (ES) [MIM:612219]: A highly malignant, CC metastatic, primitive small round cell tumor of bone and soft tissue CC that affects children and adolescents. It belongs to the Ewing sarcoma CC family of tumors, a group of morphologically heterogeneous neoplasms CC that share the same cytogenetic features. They are considered neural CC tumors derived from cells of the neural crest. Ewing sarcoma represents CC the less differentiated form of the tumors. CC {ECO:0000269|PubMed:1522903, ECO:0000269|PubMed:1765382}. Note=The gene CC represented in this entry is involved in disease pathogenesis. A CC chromosomal aberration involving FLI1 is found in patients with Erwing CC sarcoma. Translocation t(11;22)(q24;q12) with EWSR1. CC {ECO:0000269|PubMed:1522903, ECO:0000269|PubMed:1765382}. CC -!- DISEASE: Bleeding disorder, platelet-type, 21 (BDPLT21) [MIM:617443]: A CC disorder characterized by increased bleeding tendency due to platelet CC dysfunction. Clinical features include epistaxis, hematomas, bleeding CC after tooth extraction, and menorrhagia. BDPLT21 patients may have mild CC to moderate thrombocytopenia. {ECO:0000269|PubMed:24100448, CC ECO:0000269|PubMed:26316623, ECO:0000269|PubMed:28255014}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- MISCELLANEOUS: Located on a fragment of chromosome 11 flanked on the CC centromeric side by the acute lymphoblastic leukemia-associated CC t(4;11)(q21;q23) translocation breakpoint and on the telomeric side by CC the Ewing- and neuroepithelioma-associated t(11;22) (q24;q12) CC breakpoint. CC -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/79/FLI1"; 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; X67001; CAA47399.1; -; mRNA. DR EMBL; M98833; AAA35812.2; -; mRNA. DR EMBL; S45205; AAB23637.1; -; mRNA. DR EMBL; M93255; AAA58479.1; -; mRNA. DR EMBL; M93255; AAA58480.1; -; mRNA. DR EMBL; AY029368; AAK50443.1; -; mRNA. DR EMBL; AK294279; BAG57565.1; -; mRNA. DR EMBL; AK300153; BAG61938.1; -; mRNA. DR EMBL; AK313370; BAG36169.1; -; mRNA. DR EMBL; AP001122; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471065; EAW67715.1; -; Genomic_DNA. DR EMBL; CH471065; EAW67718.1; -; Genomic_DNA. DR EMBL; BC001670; AAH01670.1; -; mRNA. DR EMBL; BC010115; AAH10115.1; -; mRNA. DR EMBL; Y17293; CAA76731.1; -; Genomic_DNA. DR EMBL; D38408; BAA07463.1; ALT_TERM; Genomic_DNA. DR CCDS; CCDS44768.1; -. [Q01543-1] DR CCDS; CCDS53725.1; -. [Q01543-3] DR CCDS; CCDS59230.1; -. [Q01543-4] DR CCDS; CCDS59231.1; -. [Q01543-2] DR PIR; I37565; I37565. DR PIR; S29844; S29844. DR RefSeq; NP_001161153.1; NM_001167681.2. [Q01543-3] DR RefSeq; NP_001257939.1; NM_001271010.1. [Q01543-2] DR RefSeq; NP_001257941.1; NM_001271012.1. [Q01543-4] DR RefSeq; NP_002008.2; NM_002017.4. [Q01543-1] DR RefSeq; XP_011541003.1; XM_011542701.2. [Q01543-3] DR RefSeq; XP_016872894.1; XM_017017405.1. [Q01543-3] DR RefSeq; XP_016872895.1; XM_017017406.1. [Q01543-3] DR PDB; 1FLI; NMR; -; A=276-373. DR PDB; 1X66; NMR; -; A=114-198. DR PDB; 2YTU; NMR; -; A=100-220. DR PDB; 5E8G; X-ray; 2.70 A; A/B/C/D=276-399. DR PDB; 5E8I; X-ray; 3.45 A; A/D/G/J=276-399. DR PDB; 5JVT; X-ray; 3.10 A; A/D/G=276-375. DR PDB; 6VG2; X-ray; 3.90 A; A/D=276-375. DR PDB; 6VG8; X-ray; 4.31 A; A=276-375. DR PDB; 6VGD; X-ray; 4.20 A; A=276-375. DR PDBsum; 1FLI; -. DR PDBsum; 1X66; -. DR PDBsum; 2YTU; -. DR PDBsum; 5E8G; -. DR PDBsum; 5E8I; -. DR PDBsum; 5JVT; -. DR PDBsum; 6VG2; -. DR PDBsum; 6VG8; -. DR PDBsum; 6VGD; -. DR AlphaFoldDB; Q01543; -. DR BMRB; Q01543; -. DR SMR; Q01543; -. DR BioGRID; 108602; 51. DR CORUM; Q01543; -. DR IntAct; Q01543; 17. DR MINT; Q01543; -. DR STRING; 9606.ENSP00000433488; -. DR BindingDB; Q01543; -. DR GlyCosmos; Q01543; 14 sites, 2 glycans. DR GlyGen; Q01543; 14 sites, 2 O-linked glycans (14 sites). DR iPTMnet; Q01543; -. DR MetOSite; Q01543; -. DR PhosphoSitePlus; Q01543; -. DR BioMuta; FLI1; -. DR DMDM; 399496; -. DR EPD; Q01543; -. DR jPOST; Q01543; -. DR MassIVE; Q01543; -. DR MaxQB; Q01543; -. DR PaxDb; 9606-ENSP00000433488; -. DR PeptideAtlas; Q01543; -. DR ProteomicsDB; 32288; -. DR ProteomicsDB; 4083; -. DR ProteomicsDB; 57969; -. [Q01543-1] DR ProteomicsDB; 57970; -. [Q01543-2] DR Pumba; Q01543; -. DR Antibodypedia; 9350; 780 antibodies from 43 providers. DR DNASU; 2313; -. DR Ensembl; ENST00000281428.12; ENSP00000281428.8; ENSG00000151702.18. [Q01543-2] DR Ensembl; ENST00000344954.10; ENSP00000339627.7; ENSG00000151702.18. [Q01543-4] DR Ensembl; ENST00000527786.7; ENSP00000433488.2; ENSG00000151702.18. [Q01543-1] DR Ensembl; ENST00000534087.3; ENSP00000432950.1; ENSG00000151702.18. [Q01543-3] DR GeneID; 2313; -. DR KEGG; hsa:2313; -. DR MANE-Select; ENST00000527786.7; ENSP00000433488.2; NM_002017.5; NP_002008.2. DR UCSC; uc009zci.4; human. [Q01543-1] DR AGR; HGNC:3749; -. DR CTD; 2313; -. DR DisGeNET; 2313; -. DR GeneCards; FLI1; -. DR HGNC; HGNC:3749; FLI1. DR HPA; ENSG00000151702; Tissue enhanced (lymphoid). DR MalaCards; FLI1; -. DR MIM; 193067; gene. DR MIM; 612219; phenotype. DR MIM; 617443; phenotype. DR neXtProt; NX_Q01543; -. DR OpenTargets; ENSG00000151702; -. DR Orphanet; 370334; Extraskeletal Ewing sarcoma. DR Orphanet; 248340; Isolated delta-storage pool disease. DR Orphanet; 2308; Jacobsen syndrome. DR Orphanet; 851; Paris-Trousseau thrombocytopenia. DR Orphanet; 370348; Peripheral primitive neuroectodermal tumor. DR Orphanet; 319; Skeletal Ewing sarcoma. DR PharmGKB; PA28170; -. DR VEuPathDB; HostDB:ENSG00000151702; -. DR eggNOG; KOG3806; Eukaryota. DR GeneTree; ENSGT00940000158261; -. DR HOGENOM; CLU_933700_0_0_1; -. DR InParanoid; Q01543; -. DR OMA; AXSLLAY; -. DR OrthoDB; 2882052at2759; -. DR PhylomeDB; Q01543; -. DR TreeFam; TF350537; -. DR PathwayCommons; Q01543; -. DR Reactome; R-HSA-9616222; Transcriptional regulation of granulopoiesis. DR SignaLink; Q01543; -. DR SIGNOR; Q01543; -. DR BioGRID-ORCS; 2313; 61 hits in 1178 CRISPR screens. DR ChiTaRS; FLI1; human. DR EvolutionaryTrace; Q01543; -. DR GeneWiki; FLI1; -. DR GenomeRNAi; 2313; -. DR Pharos; Q01543; Tbio. DR PRO; PR:Q01543; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; Q01543; Protein. DR Bgee; ENSG00000151702; Expressed in monocyte and 167 other cell types or tissues. DR ExpressionAtlas; Q01543; baseline and differential. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl. DR GO; GO:0003677; F:DNA binding; TAS:ProtInc. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl. DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL. DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:ARUK-UCL. DR GO; GO:0009887; P:animal organ morphogenesis; TAS:ProtInc. DR GO; GO:0008015; P:blood circulation; IEA:Ensembl. DR GO; GO:0007599; P:hemostasis; TAS:ProtInc. DR GO; GO:0035855; P:megakaryocyte development; IEA:Ensembl. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR CDD; cd08541; SAM_PNT-FLI-1; 1. DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR InterPro; IPR000418; Ets_dom. DR InterPro; IPR046328; ETS_fam. DR InterPro; IPR003118; Pointed_dom. DR InterPro; IPR013761; SAM/pointed_sf. DR InterPro; IPR035573; SAM_PNT-FLI-1. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. DR PANTHER; PTHR11849; ETS; 1. DR PANTHER; PTHR11849:SF161; FRIEND LEUKEMIA INTEGRATION 1 TRANSCRIPTION FACTOR; 1. DR Pfam; PF00178; Ets; 1. DR Pfam; PF02198; SAM_PNT; 1. DR PRINTS; PR00454; ETSDOMAIN. DR SMART; SM00413; ETS; 1. DR SMART; SM00251; SAM_PNT; 1. DR SUPFAM; SSF47769; SAM/Pointed domain; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. DR PROSITE; PS00345; ETS_DOMAIN_1; 1. DR PROSITE; PS00346; ETS_DOMAIN_2; 1. DR PROSITE; PS50061; ETS_DOMAIN_3; 1. DR PROSITE; PS51433; PNT; 1. DR Genevisible; Q01543; HS. PE 1: Evidence at protein level; KW 3D-structure; Activator; Alternative splicing; Chromosomal rearrangement; KW Disease variant; DNA-binding; Nucleus; Phosphoprotein; Proto-oncogene; KW Reference proteome; Transcription; Transcription regulation. FT CHAIN 1..452 FT /note="Friend leukemia integration 1 transcription factor" FT /id="PRO_0000204124" FT DOMAIN 112..198 FT /note="PNT" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00762" FT DNA_BIND 281..361 FT /note="ETS" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00237" FT REGION 209..271 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 433..452 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 228..271 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 39 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P26323" FT VAR_SEQ 1..197 FT /note="MDGTIKEALSVVSDDQSLFDSAYGAAAHLPKADMTASGSPDYGQPHKINPLP FT PQQEWINQPVRVNVKREYDHMNGSRESPVDCSVSKCSKLVGGGESNPMNYNSYMDEKNG FT PPPPNMTTNERRVIVPADPTLWTQEHVRQWLEWAIKEYSLMEIDTSFFQNMDGKELCKM FT NKEDFLRATTLYNTEVLLSHLSYLRES -> MDPG (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_046943" FT VAR_SEQ 1..76 FT /note="MDGTIKEALSVVSDDQSLFDSAYGAAAHLPKADMTASGSPDYGQPHKINPLP FT PQQEWINQPVRVNVKREYDHMNGS -> MEGGLAGERA (in isoform 2)" FT /evidence="ECO:0000303|PubMed:1765382, FT ECO:0000303|PubMed:8439553" FT /id="VSP_001478" FT VAR_SEQ 1..33 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045276" FT VARIANT 324 FT /note="R -> W (in BDPLT21; decreased function in positive FT regulation of DNA-templated transcription; FT dbSNP:rs773148506)" FT /evidence="ECO:0000269|PubMed:26316623" FT /id="VAR_078929" FT VARIANT 337 FT /note="R -> Q (in BDPLT21; loss of function in positive FT regulation of DNA-templated transcription; decreased FT localization to nucleus; no effect on protein abundance; FT dbSNP:rs1064797086)" FT /evidence="ECO:0000269|PubMed:28255014" FT /id="VAR_078930" FT VARIANT 337 FT /note="R -> W (in BDPLT21; loss of function in positive FT regulation of DNA-templated transcription; FT dbSNP:rs1064797083)" FT /evidence="ECO:0000269|PubMed:24100448" FT /id="VAR_078931" FT VARIANT 343 FT /note="Y -> C (in BDPLT21; loss of function in positive FT regulation of DNA-templated transcription; FT dbSNP:rs1064797084)" FT /evidence="ECO:0000269|PubMed:24100448" FT /id="VAR_078932" FT VARIANT 345 FT /note="K -> E (in BDPLT21; loss of function in positive FT regulation of DNA-templated transcription; decreased FT localization to nucleus; no effect on protein abundance; FT dbSNP:rs1064797087)" FT /evidence="ECO:0000269|PubMed:28255014" FT /id="VAR_078933" FT CONFLICT 69 FT /note="E -> V (in Ref. 5; AAA58479)" FT /evidence="ECO:0000305" FT CONFLICT 77 FT /note="Missing (in Ref. 5; AAA58479)" FT /evidence="ECO:0000305" FT CONFLICT 130 FT /note="P -> A (in Ref. 5; AAA58479/AAA58480)" FT /evidence="ECO:0000305" FT CONFLICT 133 FT /note="W -> V (in Ref. 5; AAA58479/AAA58480)" FT /evidence="ECO:0000305" FT CONFLICT 294 FT /note="S -> N (in Ref. 8; BAG61938)" FT /evidence="ECO:0000305" FT CONFLICT 323 FT /note="E -> Q (in Ref. 4; AAB23637 and 5; FT AAA58479/AAA58480)" FT /evidence="ECO:0000305" FT CONFLICT 426 FT /note="Missing (in Ref. 5; AAA58479/AAA58480)" FT /evidence="ECO:0000305" FT STRAND 112..114 FT /evidence="ECO:0007829|PDB:2YTU" FT STRAND 120..122 FT /evidence="ECO:0007829|PDB:1X66" FT HELIX 130..132 FT /evidence="ECO:0007829|PDB:1X66" FT HELIX 137..148 FT /evidence="ECO:0007829|PDB:1X66" FT HELIX 156..159 FT /evidence="ECO:0007829|PDB:1X66" FT HELIX 164..169 FT /evidence="ECO:0007829|PDB:1X66" FT HELIX 172..176 FT /evidence="ECO:0007829|PDB:1X66" FT HELIX 181..195 FT /evidence="ECO:0007829|PDB:1X66" FT HELIX 283..291 FT /evidence="ECO:0007829|PDB:5E8G" FT HELIX 294..296 FT /evidence="ECO:0007829|PDB:5E8G" FT TURN 297..299 FT /evidence="ECO:0007829|PDB:5E8G" FT STRAND 300..302 FT /evidence="ECO:0007829|PDB:5E8I" FT STRAND 308..310 FT /evidence="ECO:0007829|PDB:5E8G" FT HELIX 314..324 FT /evidence="ECO:0007829|PDB:5E8G" FT HELIX 332..344 FT /evidence="ECO:0007829|PDB:5E8G" FT STRAND 347..350 FT /evidence="ECO:0007829|PDB:5E8G" FT STRAND 352..360 FT /evidence="ECO:0007829|PDB:5E8G" FT HELIX 362..368 FT /evidence="ECO:0007829|PDB:5E8G" SQ SEQUENCE 452 AA; 50982 MW; 9C2AAEEAF683F3FA CRC64; MDGTIKEALS VVSDDQSLFD SAYGAAAHLP KADMTASGSP DYGQPHKINP LPPQQEWINQ PVRVNVKREY DHMNGSRESP VDCSVSKCSK LVGGGESNPM NYNSYMDEKN GPPPPNMTTN ERRVIVPADP TLWTQEHVRQ WLEWAIKEYS LMEIDTSFFQ NMDGKELCKM NKEDFLRATT LYNTEVLLSH LSYLRESSLL AYNTTSHTDQ SSRLSVKEDP SYDSVRRGAW GNNMNSGLNK SPPLGGAQTI SKNTEQRPQP DPYQILGPTS SRLANPGSGQ IQLWQFLLEL LSDSANASCI TWEGTNGEFK MTDPDEVARR WGERKSKPNM NYDKLSRALR YYYDKNIMTK VHGKRYAYKF DFHGIAQALQ PHPTESSMYK YPSDISYMPS YHAHQQKVNF VPPHPSSMPV TSSSFFGAAS QYWTSPTGGI YPNPNVPRHP NTHVPSHLGS YY //