FOXP1_MOUSE
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 03-AUG-2022, entry version 182.
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; 11.
DR IntAct; P58462; 6.
DR STRING; 10090.ENSMUSP00000135181; -.
DR iPTMnet; P58462; -.
DR PhosphoSitePlus; P58462; -.
DR EPD; P58462; -.
DR MaxQB; P58462; -.
DR PaxDb; P58462; -.
DR PeptideAtlas; P58462; -.
DR PRIDE; 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 DNASU; 108655; -.
DR Ensembl; ENSMUST00000074346; ENSMUSP00000073953; ENSMUSG00000030067. [P58462-1]
DR Ensembl; ENSMUST00000113322; ENSMUSP00000108948; ENSMUSG00000030067. [P58462-1]
DR Ensembl; ENSMUST00000113329; ENSMUSP00000108955; ENSMUSG00000030067. [P58462-2]
DR GeneID; 108655; -.
DR KEGG; mmu:108655; -.
DR UCSC; uc009dbi.2; mouse. [P58462-1]
DR UCSC; uc009dbl.2; mouse. [P58462-2]
DR CTD; 27086; -.
DR MGI; MGI:1914004; Foxp1.
DR VEuPathDB; HostDB:ENSMUSG00000030067; -.
DR eggNOG; KOG4385; Eukaryota.
DR GeneTree; ENSGT00940000159892; -.
DR InParanoid; P58462; -.
DR OrthoDB; 836427at2759; -.
DR BioGRID-ORCS; 108655; 6 hits in 73 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 312 other tissues.
DR ExpressionAtlas; P58462; baseline and differential.
DR Genevisible; P58462; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
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:0006974; P:cellular response to DNA damage stimulus; ISO:MGI.
DR GO; GO:1904637; P:cellular response to ionomycin; 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: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:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
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: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:1905206; P:positive regulation of hydrogen peroxide-induced 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:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
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; cd00059; FH; 1.
DR Gene3D; 1.10.10.10; -; 1.
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 Pfam; PF00250; Forkhead; 1.
DR Pfam; PF16159; FOXP-CC; 1.
DR PRINTS; PR00053; FORKHEAD.
DR SMART; SM00339; FH; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS00658; FORK_HEAD_2; 1.
DR PROSITE; PS50039; FORK_HEAD_3; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
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
