ID FOXP2_HUMAN Reviewed; 715 AA. AC O15409; A0AUV6; A4D0U8; A6NNW4; B4DLD9; Q6ZND1; Q75MJ3; Q8IZE0; Q8N0W2; AC Q8N6B7; Q8N6B8; Q8NFQ1; Q8NFQ2; Q8NFQ3; Q8NFQ4; Q8TD74; DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot. DT 05-DEC-2001, sequence version 2. DT 27-MAR-2024, entry version 215. DE RecName: Full=Forkhead box protein P2; DE AltName: Full=CAG repeat protein 44; DE AltName: Full=Trinucleotide repeat-containing gene 10 protein; GN Name=FOXP2; Synonyms=CAGH44, TNRC10; 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), ALTERNATIVE SPLICING, AND VARIANT RP SPCH1 HIS-553. RX PubMed=11586359; DOI=10.1038/35097076; RA Lai C.S.L., Fisher S.E., Hurst J.A., Vargha-Khadem F., Monaco A.P.; RT "A forkhead-domain gene is mutated in a severe speech and language RT disorder."; RL Nature 413:519-523(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), NUCLEOTIDE SEQUENCE [MRNA] OF 1-415 RP (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 259-715 (ISOFORM 6), AND TISSUE RP SPECIFICITY. RC TISSUE=Brain, Corpus striatum, Fetal brain, and Frontal cortex; RX PubMed=12189486; DOI=10.1007/s00439-002-0768-5; RA Bruce H.A., Margolis R.L.; RT "FOXP2: novel exons, splice variants, and CAG repeat length stability."; RL Hum. Genet. 111:136-144(2002). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5). RA Vincent J.B., Scherer S.W.; RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Brain; RA Guo J.H., Chen L., Yu L.; RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 8 AND 9). RC TISSUE=Tongue; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12690205; DOI=10.1126/science.1083423; RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D., RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., RA Adams M.D., Tsui L.-C.; RT "Human chromosome 7: DNA sequence and biology."; RL Science 300:767-772(2003). RN [8] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Brain; 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 [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-304 (ISOFORM 1). RC TISSUE=Brain cortex; RX PubMed=9225980; DOI=10.1007/s004390050476; RA Margolis R.L., Abraham M.R., Gatchell S.B., Li S.-H., Kidwai A.S., RA Breschel T.S., Stine O.C., Callahan C., McInnis M.G., Ross C.A.; RT "cDNAs with long CAG trinucleotide repeats from human brain."; RL Hum. Genet. 100:114-122(1997). RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 113-329. RX PubMed=12192408; DOI=10.1038/nature01025; RA Enard W., Przeworski M., Fisher S.E., Lai C.S.L., Wiebe V., Kitano T., RA Monaco A.P., Paeaebo S.; RT "Molecular evolution of FOXP2, a gene involved in speech and language."; RL Nature 418:869-872(2002). RN [12] RP DEVELOPMENTAL STAGE. RX PubMed=15056695; DOI=10.1523/jneurosci.5589-03.2004; RA Teramitsu I., Kudo L.C., London S.E., Geschwind D.H., White S.A.; RT "Parallel FoxP1 and FoxP2 expression in songbird and human brain predicts RT functional interaction."; RL J. Neurosci. 24:3152-3163(2004). RN [13] RP INTERACTION WITH TBR1, AND CHARACTERIZATION OF VARIANT SPCH1 HIS-553. RX PubMed=25232744; DOI=10.1038/ncomms5954; RA Deriziotis P., O'Roak B.J., Graham S.A., Estruch S.B., Dimitropoulou D., RA Bernier R.A., Gerdts J., Shendure J., Eichler E.E., Fisher S.E.; RT "De novo TBR1 mutations in sporadic autism disrupt protein functions."; RL Nat. Commun. 5:4954-4954(2014). RN [14] RP INTERACTION WITH FOXP1. RX PubMed=26647308; DOI=10.1093/hmg/ddv495; RA Sollis E., Graham S.A., Vino A., Froehlich H., Vreeburg M., RA Dimitropoulou D., Gilissen C., Pfundt R., Rappold G.A., Brunner H.G., RA Deriziotis P., Fisher S.E.; RT "Identification and functional characterization of de novo FOXP1 variants RT provides novel insights into the etiology of neurodevelopmental disorder."; RL Hum. Mol. Genet. 25:546-557(2016). RN [15] RP INTERACTION WITH TBR1. RX PubMed=30250039; DOI=10.1038/s41598-018-32053-6; RA den Hoed J., Sollis E., Venselaar H., Estruch S.B., Deriziotis P., RA Fisher S.E.; RT "Functional characterization of TBR1 variants in neurodevelopmental RT disorder."; RL Sci. Rep. 8:14279-14279(2018). RN [16] RP INTERACTION WITH ZMYM2. RX PubMed=32891193; DOI=10.1016/j.ajhg.2020.08.013; RA Connaughton D.M., Dai R., Owen D.J., Marquez J., Mann N., RA Graham-Paquin A.L., Nakayama M., Coyaud E., Laurent E.M.N., RA St-Germain J.R., Blok L.S., Vino A., Klaembt V., Deutsch K., Wu C.W., RA Kolvenbach C.M., Kause F., Ottlewski I., Schneider R., Kitzler T.M., RA Majmundar A.J., Buerger F., Onuchic-Whitford A.C., Youying M., Kolb A., RA Salmanullah D., Chen E., van der Ven A.T., Rao J., Ityel H., Seltzsam S., RA Rieke J.M., Chen J., Vivante A., Hwang D.Y., Kohl S., Dworschak G.C., RA Hermle T., Alders M., Bartolomaeus T., Bauer S.B., Baum M.A., RA Brilstra E.H., Challman T.D., Zyskind J., Costin C.E., Dipple K.M., RA Duijkers F.A., Ferguson M., Fitzpatrick D.R., Fick R., Glass I.A., RA Hulick P.J., Kline A.D., Krey I., Kumar S., Lu W., Marco E.J., RA Wentzensen I.M., Mefford H.C., Platzer K., Povolotskaya I.S., Savatt J.M., RA Shcherbakova N.V., Senguttuvan P., Squire A.E., Stein D.R., Thiffault I., RA Voinova V.Y., Somers M.J.G., Ferguson M.A., Traum A.Z., Daouk G.H., RA Daga A., Rodig N.M., Terhal P.A., van Binsbergen E., Eid L.A., Tasic V., RA Rasouly H.M., Lim T.Y., Ahram D.F., Gharavi A.G., Reutter H.M., Rehm H.L., RA MacArthur D.G., Lek M., Laricchia K.M., Lifton R.P., Xu H., Mane S.M., RA Sanna-Cherchi S., Sharrocks A.D., Raught B., Fisher S.E., Bouchard M., RA Khokha M.K., Shril S., Hildebrandt F.; RT "Mutations of the transcriptional corepressor ZMYM2 cause syndromic urinary RT tract malformations."; RL Am. J. Hum. Genet. 107:727-742(2020). CC -!- FUNCTION: Transcriptional repressor that may play a role in the CC specification and differentiation of lung epithelium. May also play a CC role in developing neural, gastrointestinal and cardiovascular tissues. CC Can act with CTBP1 to synergistically repress transcription but CTPBP1 CC is not essential. Plays a role in synapse formation by regulating SRPX2 CC levels. Involved in neural mechanisms mediating the development of CC speech and language. CC -!- SUBUNIT: Forms homodimers and heterodimers with FOXP1 and FOXP4. CC Dimerization is required for DNA-binding. Interacts with CTBP1 (By CC similarity). Interacts with FOXP1 (PubMed:26647308). Isoform 1 and CC isoform 3 interact with TBR1 (PubMed:25232744, PubMed:30250039). CC Interacts with ZMYM2 (PubMed:32891193). {ECO:0000250|UniProtKB:P58463, CC ECO:0000269|PubMed:25232744, ECO:0000269|PubMed:26647308, CC ECO:0000269|PubMed:30250039, ECO:0000269|PubMed:32891193}. CC -!- INTERACTION: CC O15409; P24863: CCNC; NbExp=3; IntAct=EBI-983612, EBI-395261; CC O15409; Q00526: CDK3; NbExp=3; IntAct=EBI-983612, EBI-1245761; CC O15409; Q13363-2: CTBP1; NbExp=7; IntAct=EBI-983612, EBI-10171858; CC O15409; P56545: CTBP2; NbExp=4; IntAct=EBI-983612, EBI-741533; CC O15409; P56545-3: CTBP2; NbExp=3; IntAct=EBI-983612, EBI-10171902; CC O15409; Q86V42: FAM124A; NbExp=3; IntAct=EBI-983612, EBI-744506; CC O15409; Q9H334: FOXP1; NbExp=13; IntAct=EBI-983612, EBI-983809; CC O15409; O15409: FOXP2; NbExp=5; IntAct=EBI-983612, EBI-983612; CC O15409; Q8IVH2: FOXP4; NbExp=6; IntAct=EBI-983612, EBI-1054619; CC O15409; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-983612, EBI-739832; CC O15409; Q13526: PIN1; NbExp=6; IntAct=EBI-983612, EBI-714158; CC O15409; O00560: SDCBP; NbExp=3; IntAct=EBI-983612, EBI-727004; CC O15409; Q08117: TLE5; NbExp=3; IntAct=EBI-983612, EBI-717810; CC O15409; Q08117-2: TLE5; NbExp=3; IntAct=EBI-983612, EBI-11741437; CC O15409; Q96A04: TSACC; NbExp=6; IntAct=EBI-983612, EBI-740411; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=9; CC Name=1; Synonyms=I; CC IsoId=O15409-1; Sequence=Displayed; CC Name=2; Synonyms=II; CC IsoId=O15409-3; Sequence=Not described; CC Name=3; Synonyms=III, IV; CC IsoId=O15409-2; Sequence=VSP_001558; CC Name=4; CC IsoId=O15409-4; Sequence=VSP_011532; CC Name=5; CC IsoId=O15409-5; Sequence=VSP_011532, VSP_011535, VSP_011536; CC Name=6; Synonyms=FOXP2-S; CC IsoId=O15409-6; Sequence=VSP_011538, VSP_011539; CC Name=7; CC IsoId=O15409-7; Sequence=VSP_011537; CC Name=8; CC IsoId=O15409-8; Sequence=VSP_011533, VSP_011534; CC Name=9; CC IsoId=O15409-9; Sequence=VSP_043464; CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 6 are expressed in adult and CC fetal brain, caudate nucleus and lung. {ECO:0000269|PubMed:12189486}. CC -!- DEVELOPMENTAL STAGE: Expressed in the brain at 15 and 22 weeks of CC gestation, with a pattern of strong cortical, basal ganglia, thalamic CC and cerebellar expression. Highly expressed in the head and tail of CC nucleus caudatus and putamen. Restricted expression within the globus CC pallidus, with high levels in the pars interna, which provides the CC principal source of output from the basal ganglia to the nucleus CC centrum medianum thalami (CM) and the major motor relay nuclei of the CC thalamus. In the thalamus, present in the CM and nucleus medialis CC dorsalis thalami. Lower levels are observed in the nuclei anterior CC thalami, dorsal and ventral, and the nucleus parafascicularis thalami. CC Expressed in the ventrobasal complex comprising the nucleus ventralis CC posterior lateralis/medialis. The ventral tier of the thalamus exhibits CC strong expression, including nuclei ventralis anterior, lateralis and CC posterior lateralis pars oralis. Also expressed in the nucleus CC subthalamicus bilaterally and in the nucleus ruber. CC {ECO:0000269|PubMed:15056695}. CC -!- DOMAIN: The leucine-zipper is required for dimerization and CC transcriptional repression. {ECO:0000250}. CC -!- DISEASE: Speech-language disorder 1 (SPCH1) [MIM:602081]: A disorder CC characterized by severe orofacial dyspraxia resulting in largely CC incomprehensible speech. Affected individuals have severe impairment in CC the selection and sequencing of fine orofacial movements which are CC necessary for articulation, and deficits in several facets of CC grammatical skills and language processing, such as the ability to CC break up words into their constituent phonemes. CC {ECO:0000269|PubMed:11586359, ECO:0000269|PubMed:25232744}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: Note=A chromosomal aberration involving FOXP2 is a cause of CC severe speech and language impairment. Translocation t(5;7)(q22;q31.2). CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Talking heads - Issue 51 of CC October 2004; CC URL="https://web.expasy.org/spotlight/back_issues/051"; CC -!- WEB RESOURCE: Name=Wikipedia; Note=FOXP2 entry; CC URL="https://en.wikipedia.org/wiki/FOXP2"; 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; AF337817; AAL10762.1; -; mRNA. DR EMBL; AF467252; AAM60762.1; -; mRNA. DR EMBL; AF467253; AAM60763.1; -; mRNA. DR EMBL; AF467254; AAM60764.1; -; mRNA. DR EMBL; AF467255; AAM60765.1; -; mRNA. DR EMBL; AF467256; AAM60766.1; -; mRNA. DR EMBL; AF467257; AAM60767.1; -; mRNA. DR EMBL; AF493430; AAM13672.1; -; mRNA. DR EMBL; AY144615; AAN60016.1; -; mRNA. DR EMBL; AK131266; BAD18444.1; ALT_SEQ; mRNA. DR EMBL; AK296957; BAG59501.1; -; mRNA. DR EMBL; AC003992; AAS07399.1; -; Genomic_DNA. DR EMBL; AC020606; AAS07502.1; -; Genomic_DNA. DR EMBL; AC073626; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC074000; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC092148; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC092606; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH236947; EAL24367.1; -; Genomic_DNA. DR EMBL; CH236947; EAL24369.1; -; Genomic_DNA. DR EMBL; CH471070; EAW83484.1; -; Genomic_DNA. DR EMBL; CH471070; EAW83486.1; -; Genomic_DNA. DR EMBL; BC126104; AAI26105.1; -; mRNA. DR EMBL; BC143866; AAI43867.1; -; mRNA. DR EMBL; U80741; AAB91439.1; -; mRNA. DR EMBL; AF515031; AAN03389.1; -; Genomic_DNA. DR EMBL; AF515032; AAN03390.1; -; Genomic_DNA. DR EMBL; AF515033; AAN03391.1; -; Genomic_DNA. DR EMBL; AF515034; AAN03392.1; -; Genomic_DNA. DR EMBL; AF515035; AAN03393.1; -; Genomic_DNA. DR EMBL; AF515036; AAN03394.1; -; Genomic_DNA. DR EMBL; AF515037; AAN03395.1; -; Genomic_DNA. DR EMBL; AF515038; AAN03396.1; -; Genomic_DNA. DR EMBL; AF515039; AAN03397.1; -; Genomic_DNA. DR EMBL; AF515040; AAN03398.1; -; Genomic_DNA. DR EMBL; AF515041; AAN03399.1; -; Genomic_DNA. DR EMBL; AF515042; AAN03400.1; -; Genomic_DNA. DR EMBL; AF515043; AAN03401.1; -; Genomic_DNA. DR EMBL; AF515044; AAN03402.1; -; Genomic_DNA. DR EMBL; AF515045; AAN03403.1; -; Genomic_DNA. DR EMBL; AF515046; AAN03404.1; -; Genomic_DNA. DR EMBL; AF515047; AAN03405.1; -; Genomic_DNA. DR EMBL; AF515048; AAN03406.1; -; Genomic_DNA. DR EMBL; AF515049; AAN03407.1; -; Genomic_DNA. DR EMBL; AF515050; AAN03408.1; -; Genomic_DNA. DR CCDS; CCDS43635.1; -. [O15409-4] DR CCDS; CCDS55154.1; -. [O15409-9] DR CCDS; CCDS5760.1; -. [O15409-1] DR CCDS; CCDS5761.2; -. [O15409-6] DR RefSeq; NP_001166237.1; NM_001172766.2. DR RefSeq; NP_001166238.1; NM_001172767.2. DR RefSeq; NP_055306.1; NM_014491.3. [O15409-1] DR RefSeq; NP_683696.2; NM_148898.3. [O15409-4] DR RefSeq; NP_683697.2; NM_148899.3. [O15409-6] DR RefSeq; NP_683698.2; NM_148900.3. [O15409-9] DR RefSeq; XP_016868290.1; XM_017012801.1. DR PDB; 2A07; X-ray; 1.90 A; F/G/H/I/J/K=502-594. DR PDB; 2AS5; X-ray; 2.70 A; F/G=502-594. DR PDBsum; 2A07; -. DR PDBsum; 2AS5; -. DR AlphaFoldDB; O15409; -. DR SMR; O15409; -. DR BioGRID; 125073; 41. DR DIP; DIP-29004N; -. DR IntAct; O15409; 31. DR MINT; O15409; -. DR STRING; 9606.ENSP00000386200; -. DR GlyGen; O15409; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O15409; -. DR PhosphoSitePlus; O15409; -. DR BioMuta; FOXP2; -. DR jPOST; O15409; -. DR MassIVE; O15409; -. DR MaxQB; O15409; -. DR PaxDb; 9606-ENSP00000386200; -. DR PeptideAtlas; O15409; -. DR ProteomicsDB; 48644; -. [O15409-1] DR ProteomicsDB; 48645; -. [O15409-2] DR ProteomicsDB; 48646; -. [O15409-4] DR ProteomicsDB; 48647; -. [O15409-5] DR ProteomicsDB; 48648; -. [O15409-6] DR ProteomicsDB; 48649; -. [O15409-7] DR ProteomicsDB; 48650; -. [O15409-8] DR ProteomicsDB; 48651; -. [O15409-9] DR Pumba; O15409; -. DR Antibodypedia; 672; 511 antibodies from 40 providers. DR DNASU; 93986; -. DR Ensembl; ENST00000350908.9; ENSP00000265436.7; ENSG00000128573.28. [O15409-1] DR Ensembl; ENST00000360232.8; ENSP00000353367.4; ENSG00000128573.28. [O15409-6] DR Ensembl; ENST00000378237.7; ENSP00000367482.3; ENSG00000128573.28. [O15409-7] DR Ensembl; ENST00000393489.8; ENSP00000377129.4; ENSG00000128573.28. [O15409-8] DR Ensembl; ENST00000393494.6; ENSP00000377132.2; ENSG00000128573.28. [O15409-1] DR Ensembl; ENST00000403559.9; ENSP00000385069.4; ENSG00000128573.28. [O15409-9] DR Ensembl; ENST00000408937.7; ENSP00000386200.3; ENSG00000128573.28. [O15409-4] DR Ensembl; ENST00000412402.5; ENSP00000405470.1; ENSG00000128573.28. [O15409-8] DR Ensembl; ENST00000441290.6; ENSP00000416825.1; ENSG00000128573.28. [O15409-8] DR Ensembl; ENST00000635109.1; ENSP00000489457.1; ENSG00000128573.28. [O15409-8] DR Ensembl; ENST00000703613.1; ENSP00000515397.1; ENSG00000128573.28. [O15409-9] DR Ensembl; ENST00000703614.1; ENSP00000515398.1; ENSG00000128573.28. [O15409-1] DR GeneID; 93986; -. DR KEGG; hsa:93986; -. DR MANE-Select; ENST00000350908.9; ENSP00000265436.7; NM_014491.4; NP_055306.1. DR UCSC; uc003vgx.3; human. [O15409-1] DR AGR; HGNC:13875; -. DR CTD; 93986; -. DR DisGeNET; 93986; -. DR GeneCards; FOXP2; -. DR GeneReviews; FOXP2; -. DR HGNC; HGNC:13875; FOXP2. DR HPA; ENSG00000128573; Tissue enhanced (intestine). DR MalaCards; FOXP2; -. DR MIM; 602081; phenotype. DR MIM; 605317; gene. DR neXtProt; NX_O15409; -. DR OpenTargets; ENSG00000128573; -. DR Orphanet; 251061; 7q31 microdeletion syndrome. DR Orphanet; 209908; Isolated childhood apraxia of speech. DR PharmGKB; PA28242; -. DR VEuPathDB; HostDB:ENSG00000128573; -. DR eggNOG; KOG4385; Eukaryota. DR GeneTree; ENSGT00940000155480; -. DR HOGENOM; CLU_2557677_0_0_1; -. DR InParanoid; O15409; -. DR OMA; XHLNNEH; -. DR OrthoDB; 5385885at2759; -. DR PhylomeDB; O15409; -. DR TreeFam; TF326978; -. DR PathwayCommons; O15409; -. DR SignaLink; O15409; -. DR SIGNOR; O15409; -. DR BioGRID-ORCS; 93986; 15 hits in 1171 CRISPR screens. DR ChiTaRS; FOXP2; human. DR EvolutionaryTrace; O15409; -. DR GeneWiki; FOXP2; -. DR GenomeRNAi; 93986; -. DR Pharos; O15409; Tbio. DR PRO; PR:O15409; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; O15409; Protein. DR Bgee; ENSG00000128573; Expressed in buccal mucosa cell and 180 other cell types or tissues. DR ExpressionAtlas; O15409; baseline and differential. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:BHF-UCL. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB. DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:BHF-UCL. DR GO; GO:0021757; P:caudate nucleus development; IMP:UniProtKB. DR GO; GO:0021987; P:cerebral cortex development; IEP:BHF-UCL. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:BHF-UCL. DR GO; GO:0021758; P:putamen development; IMP:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. 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 IDEAL; IID00429; -. 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:SF1; FORKHEAD BOX PROTEIN P2; 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; O15409; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Chromosomal rearrangement; KW Disease variant; DNA-binding; Metal-binding; Nucleus; Reference proteome; KW Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1..715 FT /note="Forkhead box protein P2" FT /id="PRO_0000091879" FT ZN_FING 346..371 FT /note="C2H2-type" FT DNA_BIND 504..594 FT /note="Fork-head" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089" FT REGION 1..46 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 281..339 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 388..409 FT /note="Leucine-zipper" FT REGION 422..426 FT /note="CTBP1-binding" FT /evidence="ECO:0000250" FT REGION 438..465 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 649..668 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 678..715 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 288..327 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 650..665 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 701..715 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 1..92 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_001558" FT VAR_SEQ 86 FT /note="Q -> QELLPETKLCICGHSSGDGHPHNTFA (in isoform 4 and FT isoform 5)" FT /evidence="ECO:0000303|Ref.3, ECO:0000303|Ref.4" FT /id="VSP_011532" FT VAR_SEQ 87 FT /note="V -> P (in isoform 8)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_011533" FT VAR_SEQ 88..715 FT /note="Missing (in isoform 8)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_011534" FT VAR_SEQ 132 FT /note="Q -> QDFLDSGLENFRAALEKN (in isoform 9)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043464" FT VAR_SEQ 133..143 FT /note="QQLQEFYKKQQ -> VMWVTCFGVLA (in isoform 5)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_011535" FT VAR_SEQ 144..715 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_011536" FT VAR_SEQ 366..715 FT /note="Missing (in isoform 7)" FT /evidence="ECO:0000303|PubMed:12189486" FT /id="VSP_011537" FT VAR_SEQ 423..432 FT /note="LNLVSSVTMS -> VSAYCFINSK (in isoform 6)" FT /evidence="ECO:0000303|PubMed:12189486" FT /id="VSP_011538" FT VAR_SEQ 433..715 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:12189486" FT /id="VSP_011539" FT VARIANT 553 FT /note="R -> H (in SPCH1; reduced interaction with TBR1; FT dbSNP:rs121908377)" FT /evidence="ECO:0000269|PubMed:11586359, FT ECO:0000269|PubMed:25232744" FT /id="VAR_012278" FT CONFLICT 29 FT /note="A -> V (in Ref. 2; AAM60762)" FT /evidence="ECO:0000305" FT CONFLICT 134 FT /note="Q -> H (in Ref. 10; AAB91439)" FT /evidence="ECO:0000305" FT CONFLICT 290..304 FT /note="DLTTNNSSSTTSSNT -> EEFPVQGPAAVCAGL (in Ref. 10; FT AAB91439)" FT /evidence="ECO:0000305" FT CONFLICT 414 FT /note="S -> L (in Ref. 2; AAM60766)" FT /evidence="ECO:0000305" FT HELIX 509..519 FT /evidence="ECO:0007829|PDB:2A07" FT HELIX 527..541 FT /evidence="ECO:0007829|PDB:2A07" FT HELIX 545..558 FT /evidence="ECO:0007829|PDB:2A07" FT STRAND 562..567 FT /evidence="ECO:0007829|PDB:2AS5" FT STRAND 568..572 FT /evidence="ECO:0007829|PDB:2A07" FT HELIX 577..583 FT /evidence="ECO:0007829|PDB:2A07" SQ SEQUENCE 715 AA; 79919 MW; 4F9FBDB6D90516E0 CRC64; MMQESATETI SNSSMNQNGM STLSSQLDAG SRDGRSSGDT SSEVSTVELL HLQQQQALQA ARQLLLQQQT SGLKSPKSSD KQRPLQVPVS VAMMTPQVIT PQQMQQILQQ QVLSPQQLQA LLQQQQAVML QQQQLQEFYK KQQEQLHLQL LQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QHPGKQAKEQ QQQQQQQQQL AAQQLVFQQQ LLQMQQLQQQ QHLLSLQRQG LISIPPGQAA LPVQSLPQAG LSPAEIQQLW KEVTGVHSME DNGIKHGGLD LTTNNSSSTT SSNTSKASPP ITHHSIVNGQ SSVLSARRDS SSHEETGASH TLYGHGVCKW PGCESICEDF GQFLKHLNNE HALDDRSTAQ CRVQMQVVQQ LEIQLSKERE RLQAMMTHLH MRPSEPKPSP KPLNLVSSVT MSKNMLETSP QSLPQTPTTP TAPVTPITQG PSVITPASVP NVGAIRRRHS DKYNIPMSSE IAPNYEFYKN ADVRPPFTYA TLIRQAIMES SDRQLTLNEI YSWFTRTFAY FRRNAATWKN AVRHNLSLHK CFVRVENVKG AVWTVDEVEY QKRRSQKITG SPTLVKNIPT SLGYGAALNA SLQAALAESS LPLLSNPGLI NNASSGLLQA VHEDLNGSLD HIDSNGNSSP GCSPQPHIHS IHVKEEPVIA EDEDCPMSLV TTANHSPELE DDREIEEEPL SEDLE //