ID FOXP1_MOUSE Reviewed; 705 AA. AC P58462; Q6P221; Q8C5V2; Q8CCD9; DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot. DT 05-DEC-2001, sequence version 1. DT 24-JAN-2024, entry version 190. DE RecName: Full=Forkhead box protein P1; DE AltName: Full=Forkhead-related transcription factor 1; GN Name=Foxp1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND FUNCTION. RC STRAIN=C57BL/6J; TISSUE=Lung; RX PubMed=11358962; DOI=10.1074/jbc.m100636200; RA Shu W., Yang H., Zhang L., Lu M.M., Morrisey E.E.; RT "Characterization of a new subfamily of winged-helix/forkhead (Fox) genes RT that are expressed in the lung and act as transcriptional repressors."; RL J. Biol. Chem. 276:27488-27497(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC STRAIN=C57BL/6J; TISSUE=Lung, and Testis; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C57BL/6J; TISSUE=Embryo; 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 [4] RP DEVELOPMENTAL STAGE. RX PubMed=14516685; DOI=10.1016/s0925-4773(03)00116-3; RA Lu M.M., Li S., Yang H., Morrisey E.E.; RT "Foxp4: a novel member of the Foxp subfamily of winged-helix genes co- RT expressed with Foxp1 and Foxp2 in pulmonary and gut tissues."; RL Mech. Dev. 119:S197-S202(2002). RN [5] RP FUNCTION, DIMERIZATION, INTERACTION WITH CTBP1, DOMAIN, AND MUTAGENESIS OF RP GLU-388 AND 410-PRO--VAL-414. RX PubMed=14701752; DOI=10.1128/mcb.24.2.809-822.2004; RA Li S., Weidenfeld J., Morrisey E.E.; RT "Transcriptional and DNA binding activity of the Foxp1/2/4 family is RT modulated by heterotypic and homotypic protein interactions."; RL Mol. Cell. Biol. 24:809-822(2004). RN [6] RP FUNCTION. RX PubMed=16819554; DOI=10.1038/ni1358; RA Hu H., Wang B., Borde M., Nardone J., Maika S., Allred L., Tucker P.W., RA Rao A.; RT "Foxp1 is an essential transcriptional regulator of B cell development."; RL Nat. Immunol. 7:819-826(2006). RN [7] RP FUNCTION. RX PubMed=18662545; DOI=10.1016/j.cell.2008.06.019; RA Dasen J.S., De Camilli A., Wang B., Tucker P.W., Jessell T.M.; RT "Hox repertoires for motor neuron diversity and connectivity gated by a RT single accessory factor, FoxP1."; RL Cell 134:304-316(2008). RN [8] RP FUNCTION. RX PubMed=18667151; DOI=10.1016/j.neuron.2008.06.025; RA Rousso D.L., Gaber Z.B., Wellik D., Morrisey E.E., Novitch B.G.; RT "Coordinated actions of the forkhead protein Foxp1 and Hox proteins in the RT columnar organization of spinal motor neurons."; RL Neuron 59:226-240(2008). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Spleen; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [10] RP FUNCTION. RX PubMed=20713518; DOI=10.1101/gad.1929210; RA Zhang Y., Li S., Yuan L., Tian Y., Weidenfeld J., Yang J., Liu F., RA Chokas A.L., Morrisey E.E.; RT "Foxp1 coordinates cardiomyocyte proliferation through both cell-autonomous RT and nonautonomous mechanisms."; RL Genes Dev. 24:1746-1757(2010). RN [11] RP FUNCTION, AND DEVELOPMENTAL STAGE. RX PubMed=20175877; DOI=10.1111/j.1471-4159.2010.06650.x; RA Konstantoulas C.J., Parmar M., Li M.; RT "FoxP1 promotes midbrain identity in embryonic stem cell-derived dopamine RT neurons by regulating Pitx3."; RL J. Neurochem. 113:836-847(2010). RN [12] RP ALTERNATIVE SPLICING (ISOFORM 5), FUNCTION (ISOFORM 5), AND TISSUE RP SPECIFICITY (ISOFORM 5). RX PubMed=21924763; DOI=10.1016/j.cell.2011.08.023; RA Gabut M., Samavarchi-Tehrani P., Wang X., Slobodeniuc V., O'Hanlon D., RA Sung H.K., Alvarez M., Talukder S., Pan Q., Mazzoni E.O., Nedelec S., RA Wichterle H., Woltjen K., Hughes T.R., Zandstra P.W., Nagy A., Wrana J.L., RA Blencowe B.J.; RT "An alternative splicing switch regulates embryonic stem cell pluripotency RT and reprogramming."; RL Cell 147:132-146(2011). RN [13] RP FUNCTION. RX PubMed=22675208; DOI=10.1242/dev.079699; RA Li S., Wang Y., Zhang Y., Lu M.M., DeMayo F.J., Dekker J.D., Tucker P.W., RA Morrisey E.E.; RT "Foxp1/4 control epithelial cell fate during lung development and RT regeneration through regulation of anterior gradient 2."; RL Development 139:2500-2509(2012). RN [14] RP FUNCTION. RX PubMed=23946441; DOI=10.1242/dev.097477; RA Leishman E., Howard J.M., Garcia G.E., Miao Q., Ku A.T., Dekker J.D., RA Tucker H., Nguyen H.; RT "Foxp1 maintains hair follicle stem cell quiescence through regulation of RT Fgf18."; RL Development 140:3809-3818(2013). RN [15] RP FUNCTION. RX PubMed=24859450; DOI=10.1038/ni.2890; RA Wang H., Geng J., Wen X., Bi E., Kossenkov A.V., Wolf A.I., Tas J., RA Choi Y.S., Takata H., Day T.J., Chang L.Y., Sprout S.L., Becker E.K., RA Willen J., Tian L., Wang X., Xiao C., Jiang P., Crotty S., Victora G.D., RA Showe L.C., Tucker H.O., Erikson J., Hu H.; RT "The transcription factor Foxp1 is a critical negative regulator of the RT differentiation of follicular helper T cells."; RL Nat. Immunol. 15:667-675(2014). CC -!- FUNCTION: Transcriptional repressor. Can act with CTBP1 to CC synergistically repress transcription but CTPBP1 is not essential CC (PubMed:11358962, PubMed:14701752). Plays an important role in the CC specification and differentiation of lung epithelium. Acts CC cooperatively with FOXP4 to regulate lung secretory epithelial cell CC fate and regeneration by restricting the goblet cell lineage program; CC the function may involve regulation of AGR2 (PubMed:11358962, CC PubMed:22675208). Essential transcriptional regulator of B-cell CC development (PubMed:16819554). Involved in regulation of cardiac muscle CC cell proliferation (PubMed:20713518). Involved in the columnar CC organization of spinal motor neurons. Promotes the formation of the CC lateral motor neuron column (LMC) and the preganglionic motor column CC (PGC) and is required for respective appropriate motor axon CC projections. The segment-appropriate generation of spinal cord motor CC columns requires cooperation with other Hox proteins (PubMed:18667151, CC PubMed:18662545). Can regulate PITX3 promoter activity; may promote CC midbrain identity in embryonic stem cell-derived dopamine neurons by CC regulating PITX3 (PubMed:20175877). Negatively regulates the CC differentiation of T follicular helper cells T(FH)s (PubMed:24859450). CC Involved in maintenance of hair follicle stem cell quiescence; the CC function probably involves regulation of FGF18 (PubMed:23946441). CC Represses transcription of various pro-apoptotic genes and cooperates CC with NF-kappa B-signaling in promoting B-cell expansion by inhibition CC of caspase-dependent apoptosis. Binds to CSF1R promoter elements and is CC involved in regulation of monocyte differentiation and macrophage CC functions; repression of CSF1R in monocytes seems to involve NCOR2 as CC corepressor. Involved in endothelial cell proliferation, tube formation CC and migration indicative for a role in angiogenesis; the role in CC neovascularization seems to implicate suppression of SEMA5B. Can CC negatively regulate androgen receptor signaling (By similarity). Acts CC as a transcriptional activator of the FBXL7 promoter; this activity is CC regulated by AURKA (By similarity). {ECO:0000250|UniProtKB:Q9H334, CC ECO:0000269|PubMed:14701752, ECO:0000269|PubMed:16819554, CC ECO:0000269|PubMed:18662545, ECO:0000269|PubMed:18667151, CC ECO:0000269|PubMed:20175877, ECO:0000269|PubMed:20713518, CC ECO:0000269|PubMed:22675208, ECO:0000269|PubMed:23946441, CC ECO:0000269|PubMed:24859450, ECO:0000305|PubMed:20175877, CC ECO:0000305|PubMed:22675208, ECO:0000305|PubMed:23946441}. CC -!- FUNCTION: [Isoform 5]: Involved in transcriptional regulation in CC embryonic stem cells (ESCs). Stimulates expression of transcription CC factors that are required for pluripotency and decreases expression of CC differentiation-associated genes. Has distinct DNA-binding specifities CC as compared to the canonical form and preferentially binds DNA with the CC sequence 5'-CGATACAA-3' (or closely related sequences) (By similarity). CC Promotes ESC self-renewal and pluripotency (PubMed:21924763). CC {ECO:0000250|UniProtKB:Q9H334, ECO:0000269|PubMed:21924763}. CC -!- SUBUNIT: Forms homodimers and heterodimers with FOXP2 and FOXP4. CC Dimerization is required for DNA-binding. Self-associates (By CC similarity). Interacts with CTBP1 (PubMed:14701752). Interacts with CC NCOR2 and AR. Interacts with FOXP2 (By similarity). Interacts with TBR1 CC (By similarity). Interacts with AURKA; this interaction facilitates the CC phosphorylation of FOXP1, which suppresses the expression of FBXL7 (By CC similarity). Interacts with ZMYM2 (By similarity). CC {ECO:0000250|UniProtKB:Q9H334, ECO:0000269|PubMed:14701752}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H334}. Note=Not CC found in the nucleolus. {ECO:0000250|UniProtKB:Q9H334}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing, Alternative initiation; Named isoforms=5; CC Name=1; Synonyms=A; CC IsoId=P58462-1; Sequence=Displayed; CC Name=2; Synonyms=B; CC IsoId=P58462-2; Sequence=VSP_001557; CC Name=3; Synonyms=C; CC IsoId=P58462-3; Sequence=VSP_018732; CC Name=4; CC IsoId=P58462-4; Sequence=VSP_026670; CC Name=5; Synonyms=FOXP1-ES; CC IsoId=P58462-5; Sequence=VSP_057342; CC -!- TISSUE SPECIFICITY: Isoform 5 is specifically expressed in embryonic CC stem cells (PubMed:21924763). Highest expression in the lung, brain, CC and spleen. Lower expression in heart, skeletal muscle, kidney, small CC intestine (isoform 3 not present) and liver. CC {ECO:0000269|PubMed:21924763}. CC -!- DEVELOPMENTAL STAGE: Expressed in developing lung, neural, intestinal CC and cardiovascular tissues. Expressed in both the airway epithelium of CC the forming lung as well as in the surrounding mesenchyme. By 16.5 dpc, CC expressed throughout the conducting airway epithelium, with highest CC expression in the distal alveolar regions. Also expressed in the CC endotheial cells of the pulmonary vasculature. During intestinal CC development, expressed in the mucosal layer but absent from the CC epithelium at 12.5 dpc. By 16.5 dpc, expressed in both the inner CC circular and outer longitudinal muscular layers of the intestine as CC well as in the epithelium of the intestine and developing stomach CC (PubMed:14516685). Expressed in 12.5 dpc midbrain dopaminergic neurons CC (PubMed:20175877). {ECO:0000269|PubMed:14516685, CC ECO:0000269|PubMed:20175877}. CC -!- DOMAIN: The leucine-zipper is required for dimerization and CC transcriptional repression. {ECO:0000269|PubMed:14701752}. CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative initiation at Met- CC 251 of isoform 1. {ECO:0000305}. CC -!- MISCELLANEOUS: [Isoform 4]: Produced by alternative splicing. CC {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; AF339103; AAK69648.1; -; mRNA. DR EMBL; AF339104; AAK69649.1; -; mRNA. DR EMBL; AF339105; AAK69650.1; -; mRNA. DR EMBL; AK033368; BAC28249.1; -; mRNA. DR EMBL; AK077062; BAC36586.1; -; mRNA. DR EMBL; BC064764; AAH64764.1; -; mRNA. DR CCDS; CCDS39578.1; -. [P58462-1] DR RefSeq; NP_001184250.1; NM_001197321.1. DR RefSeq; NP_001184251.1; NM_001197322.1. DR RefSeq; NP_444432.1; NM_053202.2. [P58462-1] DR RefSeq; XP_006505385.1; XM_006505322.1. DR RefSeq; XP_006505386.1; XM_006505323.3. DR AlphaFoldDB; P58462; -. DR SMR; P58462; -. DR BioGRID; 224357; 12. DR IntAct; P58462; 6. DR STRING; 10090.ENSMUSP00000108948; -. DR GlyGen; P58462; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; P58462; -. DR PhosphoSitePlus; P58462; -. DR EPD; P58462; -. DR MaxQB; P58462; -. DR PaxDb; 10090-ENSMUSP00000135181; -. DR PeptideAtlas; P58462; -. DR ProteomicsDB; 271596; -. [P58462-1] DR ProteomicsDB; 271597; -. [P58462-2] DR ProteomicsDB; 271598; -. [P58462-3] DR ProteomicsDB; 271599; -. [P58462-4] DR ProteomicsDB; 271600; -. [P58462-5] DR Pumba; P58462; -. DR Antibodypedia; 81597; 31 antibodies from 1 providers. DR DNASU; 108655; -. DR Ensembl; ENSMUST00000074346.12; ENSMUSP00000073953.6; ENSMUSG00000030067.18. [P58462-1] DR Ensembl; ENSMUST00000113322.9; ENSMUSP00000108948.3; ENSMUSG00000030067.18. [P58462-1] DR Ensembl; ENSMUST00000113329.10; ENSMUSP00000108955.4; ENSMUSG00000030067.18. [P58462-2] DR GeneID; 108655; -. DR KEGG; mmu:108655; -. DR UCSC; uc009dbi.2; mouse. [P58462-1] DR UCSC; uc009dbl.2; mouse. [P58462-2] DR AGR; MGI:1914004; -. DR CTD; 27086; -. DR MGI; MGI:1914004; Foxp1. DR VEuPathDB; HostDB:ENSMUSG00000030067; -. DR eggNOG; KOG4385; Eukaryota. DR GeneTree; ENSGT00940000159892; -. DR InParanoid; P58462; -. DR OrthoDB; 5385885at2759; -. DR BioGRID-ORCS; 108655; 6 hits in 79 CRISPR screens. DR ChiTaRS; Foxp1; mouse. DR PRO; PR:P58462; -. DR Proteomes; UP000000589; Chromosome 6. DR RNAct; P58462; Protein. DR Bgee; ENSMUSG00000030067; Expressed in caudate-putamen and 314 other cell types or tissues. DR ExpressionAtlas; P58462; baseline and differential. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0003682; F:chromatin binding; IDA:MGI. DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; ISO:MGI. DR GO; GO:0003677; F:DNA binding; IDA:MGI. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:MGI. DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB. DR GO; GO:0042802; F:identical protein binding; IPI:MGI. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0050681; F:nuclear androgen receptor binding; ISO:MGI. DR GO; GO:0043621; F:protein self-association; ISS:UniProtKB. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IMP:NTNU_SB. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI. DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI. DR GO; GO:0001221; F:transcription coregulator binding; IPI:UniProtKB. DR GO; GO:0055007; P:cardiac muscle cell differentiation; IMP:MGI. DR GO; GO:1904637; P:cellular response to ionomycin; ISO:MGI. DR GO; GO:0006974; P:DNA damage response; ISO:MGI. DR GO; GO:0042118; P:endothelial cell activation; ISS:UniProtKB. DR GO; GO:0007507; P:heart development; IMP:MGI. DR GO; GO:0033152; P:immunoglobulin V(D)J recombination; IMP:MGI. DR GO; GO:0098582; P:innate vocalization behavior; IMP:MGI. DR GO; GO:0030324; P:lung development; IGI:MGI. DR GO; GO:0061140; P:lung secretory cell differentiation; IGI:MGI. DR GO; GO:0042116; P:macrophage activation; ISS:UniProtKB. DR GO; GO:0042117; P:monocyte activation; ISS:UniProtKB. DR GO; GO:0008045; P:motor neuron axon guidance; IMP:UniProtKB. DR GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; ISS:UniProtKB. DR GO; GO:0002903; P:negative regulation of B cell apoptotic process; ISS:UniProtKB. DR GO; GO:0061052; P:negative regulation of cell growth involved in cardiac muscle cell development; ISO:MGI. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:MGI. DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI. DR GO; GO:1901250; P:negative regulation of lung goblet cell differentiation; IGI:MGI. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB. DR GO; GO:0036035; P:osteoclast development; ISS:UniProtKB. DR GO; GO:0030316; P:osteoclast differentiation; ISS:UniProtKB. DR GO; GO:0050861; P:positive regulation of B cell receptor signaling pathway; ISO:MGI. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IMP:UniProtKB. DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISS:UniProtKB. DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IGI:MGI. DR GO; GO:1901300; P:positive regulation of hydrogen peroxide-mediated programmed cell death; ISO:MGI. DR GO; GO:0002639; P:positive regulation of immunoglobulin production; IMP:MGI. DR GO; GO:0032745; P:positive regulation of interleukin-21 production; IDA:UniProtKB. DR GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IGI:MGI. DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISS:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:MGI. DR GO; GO:0002329; P:pre-B cell differentiation; IMP:MGI. DR GO; GO:0098900; P:regulation of action potential; IMP:MGI. DR GO; GO:0060043; P:regulation of cardiac muscle cell proliferation; IMP:MGI. DR GO; GO:2000341; P:regulation of chemokine (C-X-C motif) ligand 2 production; ISS:UniProtKB. DR GO; GO:1900424; P:regulation of defense response to bacterium; ISS:UniProtKB. DR GO; GO:1901509; P:regulation of endothelial tube morphogenesis; ISO:MGI. DR GO; GO:0010468; P:regulation of gene expression; ISO:MGI. DR GO; GO:0050727; P:regulation of inflammatory response; ISO:MGI. DR GO; GO:0032651; P:regulation of interleukin-1 beta production; ISO:MGI. DR GO; GO:0032655; P:regulation of interleukin-12 production; ISO:MGI. DR GO; GO:1901249; P:regulation of lung goblet cell differentiation; IGI:MGI. DR GO; GO:1901256; P:regulation of macrophage colony-stimulating factor production; ISS:UniProtKB. DR GO; GO:0045655; P:regulation of monocyte differentiation; ISS:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0032680; P:regulation of tumor necrosis factor production; ISS:UniProtKB. DR GO; GO:0032496; P:response to lipopolysaccharide; ISS:UniProtKB. DR GO; GO:0007519; P:skeletal muscle tissue development; IGI:MGI. DR GO; GO:0048745; P:smooth muscle tissue development; IGI:MGI. DR GO; GO:0061470; P:T follicular helper cell differentiation; IDA:UniProtKB. DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:MGI. DR GO; GO:0021517; P:ventral spinal cord development; IEP:UniProtKB. DR CDD; cd20065; FH_FOXP2; 1. DR Gene3D; 1.20.5.340; -; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR InterPro; IPR047412; FH_FOXP1_P2. DR InterPro; IPR001766; Fork_head_dom. DR InterPro; IPR032354; FOXP-CC. DR InterPro; IPR030456; TF_fork_head_CS_2. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. DR PANTHER; PTHR45796; FORKHEAD BOX P, ISOFORM C; 1. DR PANTHER; PTHR45796:SF3; FORKHEAD BOX PROTEIN P1; 1. DR Pfam; PF00250; Forkhead; 1. DR Pfam; PF16159; FOXP-CC; 1. DR PRINTS; PR00053; FORKHEAD. DR SMART; SM00339; FH; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. DR PROSITE; PS00658; FORK_HEAD_2; 1. DR PROSITE; PS50039; FORK_HEAD_3; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1. DR Genevisible; P58462; MM. PE 1: Evidence at protein level; KW Alternative initiation; Alternative splicing; DNA-binding; Isopeptide bond; KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor; KW Transcription; Transcription regulation; Ubl conjugation; Zinc; KW Zinc-finger. FT CHAIN 1..705 FT /note="Forkhead box protein P1" FT /id="PRO_0000009336" FT ZN_FING 334..359 FT /note="C2H2-type" FT DNA_BIND 493..583 FT /note="Fork-head" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089" FT REGION 1..41 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 267..286 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 291..326 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 376..397 FT /note="Leucine-zipper" FT REGION 410..414 FT /note="CTBP1-binding" FT REGION 418..450 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 639..705 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..24 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 291..314 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 418..433 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 639..653 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 113 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9H334" FT MOD_RES 681 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9H334" FT MOD_RES 686 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9H334" FT CROSSLNK 315 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9H334" FT CROSSLNK 400 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9H334" FT CROSSLNK 405 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9H334" FT CROSSLNK 470 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q9H334" FT VAR_SEQ 1..250 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:11358962" FT /id="VSP_018732" FT VAR_SEQ 1..130 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_026670" FT VAR_SEQ 539..602 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11358962" FT /id="VSP_001557" FT VAR_SEQ 540..579 FT /note="AVRHNLSLHKCFVRVENVKGAVWTVDEVEFQKRRPQKISG -> GAIRTLSL FT HKCFIRVEDEFGSFWTVDDEEFLRGRHIQRGRPRKYCPDENSDELGAH (in FT isoform 5)" FT /evidence="ECO:0000269|PubMed:21924763" FT /id="VSP_057342" FT MUTAGEN 388 FT /note="Missing: Loss of dimerization. Almost complete loss FT of DNA-binding. Reduced transcriptional repression FT activity." FT /evidence="ECO:0000269|PubMed:14701752" FT MUTAGEN 410..414 FT /note="PLNLV->AANAA: No significant effect on FT transcriptional repression activity." FT /evidence="ECO:0000269|PubMed:14701752" FT CONFLICT 61..92 FT /note="Missing (in Ref. 3; AAH64764)" FT /evidence="ECO:0000305" FT CONFLICT 199 FT /note="E -> EQ (in Ref. 2; BAC28249/BAC36586)" FT /evidence="ECO:0000305" FT CONFLICT 281 FT /note="D -> H (in Ref. 2; BAC28249)" FT /evidence="ECO:0000305" FT CONFLICT 353 FT /note="K -> T (in Ref. 2; BAC28249)" FT /evidence="ECO:0000305" FT CONFLICT 597 FT /note="L -> F (in Ref. 2; BAC28249)" FT /evidence="ECO:0000305" SQ SEQUENCE 705 AA; 78833 MW; 92962B82917CC79D CRC64; MMQESGSETK SNGSAIQNGS SGGNHLLECG ALRDTRSNGE APAVDLGAAD LAHVQQQQQQ ALQVARQLLL QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQVSG LKSPKRNDKQ PALQVPVSVA MMTPQVITPQ QMQQILQQQV LSPQQLQVLL QQQQALMLQQ QLQEFYKKQQ EQLQLQLLQQ QHAGKQPKEQ QVATQQLAFQ QQLLQMQQLQ QQHLLSLQRQ GLLTIQPGQP ALPLQPLAQG MIPTELQQLW KEVTSAHTAE ETTSSNHSSL DLTSTCVSSS APSKSSLIMN PHASTNGQLS VHTPKRESLS HEEHPHSHPL YGHGVCKWPG CEAVCDDFPA FLKHLNSEHA LDDRSTAQCR VQMQVVQQLE LQLAKDKERL QAMMTHLHVK STEPKAAPQP LNLVSSVTLS KSASEASPQS LPHTPTTPTA PLTPVTQGPS VITTTSMHTV GPIRRRYSDK YNVPISSADI AQNQEFYKNA EVRPPFTYAS LIRQAILESP EKQLTLNEIY NWFTRMFAYF RRNAATWKNA VRHNLSLHKC FVRVENVKGA VWTVDEVEFQ KRRPQKISGN PSLIKNMQSS HAYCTPLNAA LQASMAENSI PLYTTASMGN PTLGSLASAI REELNGAMEH TNSNESDSSP GRSPMQAVHP IHVKEEPLDP EEAEGPLSLV TTANHSPDFD HDRDYEDEPV NEDME //