FOXP2_HUMAN
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 03-AUG-2022, entry version 206.
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";
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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. [O15409-4]
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; 40.
DR DIP; DIP-29004N; -.
DR IntAct; O15409; 31.
DR MINT; O15409; -.
DR STRING; 9606.ENSP00000386200; -.
DR iPTMnet; O15409; -.
DR PhosphoSitePlus; O15409; -.
DR BioMuta; FOXP2; -.
DR jPOST; O15409; -.
DR MassIVE; O15409; -.
DR MaxQB; O15409; -.
DR PaxDb; O15409; -.
DR PeptideAtlas; O15409; -.
DR PRIDE; 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 Antibodypedia; 672; 475 antibodies from 40 providers.
DR DNASU; 93986; -.
DR Ensembl; ENST00000350908.9; ENSP00000265436.7; ENSG00000128573.27. [O15409-1]
DR Ensembl; ENST00000360232.8; ENSP00000353367.4; ENSG00000128573.27. [O15409-6]
DR Ensembl; ENST00000378237.7; ENSP00000367482.3; ENSG00000128573.27. [O15409-7]
DR Ensembl; ENST00000393489.8; ENSP00000377129.4; ENSG00000128573.27. [O15409-8]
DR Ensembl; ENST00000393494.6; ENSP00000377132.2; ENSG00000128573.27. [O15409-1]
DR Ensembl; ENST00000403559.8; ENSP00000385069.4; ENSG00000128573.27. [O15409-9]
DR Ensembl; ENST00000408937.7; ENSP00000386200.3; ENSG00000128573.27. [O15409-4]
DR Ensembl; ENST00000412402.5; ENSP00000405470.1; ENSG00000128573.27. [O15409-8]
DR Ensembl; ENST00000441290.6; ENSP00000416825.1; ENSG00000128573.27. [O15409-8]
DR Ensembl; ENST00000635109.1; ENSP00000489457.1; ENSG00000128573.27. [O15409-8]
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 CTD; 93986; -.
DR DisGeNET; 93986; -.
DR GeneCards; FOXP2; -.
DR GeneReviews; FOXP2; -.
DR HGNC; HGNC:13875; FOXP2.
DR HPA; ENSG00000128573; Low tissue specificity.
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; REYPESH; -.
DR PhylomeDB; O15409; -.
DR TreeFam; TF326978; -.
DR PathwayCommons; O15409; -.
DR SignaLink; O15409; -.
DR SIGNOR; O15409; -.
DR BioGRID-ORCS; 93986; 14 hits in 1092 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 178 other tissues.
DR ExpressionAtlas; O15409; baseline and differential.
DR Genevisible; O15409; HS.
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:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; 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; cd00059; FH; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR IDEAL; IID00429; -.
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 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
