ID FOXP2_HUMAN Reviewed; 715 AA. AC O15409; A0AUV6; A4D0U8; A6NNW4; B4DLD9; Q6ZND1; Q75MJ3; Q8IZE0; AC Q8N0W2; Q8N6B7; Q8N6B8; Q8NFQ1; Q8NFQ2; Q8NFQ3; Q8NFQ4; Q8TD74; DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot. DT 05-DEC-2001, sequence version 2. DT 30-NOV-2016, entry version 168. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING, AND RP VARIANT 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 RP 1-415 (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 259-715 (ISOFORM 6), RP AND TISSUE 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 RT 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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., RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., RA 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., RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., RA Waterston R.H., 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., RA Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., RA Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., RA Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., RA Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., RA Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., RA Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., RA Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., RA Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., RA Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., RA Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., RA Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., RA 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., RA Mural R.J., 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RT project: 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 RT 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 RT predicts functional interaction."; RL J. Neurosci. 24:3152-3163(2004). RN [13] 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 RT variants provides novel insights into the etiology of RT neurodevelopmental disorder."; RL Hum. Mol. Genet. 25:546-557(2016). CC -!- FUNCTION: Transcriptional repressor that may play a role in the CC specification and differentiation of lung epithelium. May also CC play a role in developing neural, gastrointestinal and CC cardiovascular tissues. Can act with CTBP1 to synergistically CC repress transcription but CTPBP1 is not essential. Plays a role in CC synapse formation by regulating SRPX2 levels. Involved in neural CC mechanisms mediating the development of 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). CC {ECO:0000250|UniProtKB:P58463, ECO:0000269|PubMed:26647308}. CC -!- INTERACTION: CC Q08117:AES; NbExp=3; IntAct=EBI-983612, EBI-717810; CC P24863:CCNC; NbExp=3; IntAct=EBI-983612, EBI-395261; CC Q13363-2:CTBP1; NbExp=5; IntAct=EBI-983612, EBI-10171858; CC P56545:CTBP2; NbExp=3; IntAct=EBI-983612, EBI-741533; CC Q86V42:FAM124A; NbExp=3; IntAct=EBI-983612, EBI-744506; CC Q13526:PIN1; NbExp=5; IntAct=EBI-983612, EBI-714158; CC O00560:SDCBP; NbExp=3; IntAct=EBI-983612, EBI-727004; CC Q96A04:TSACC; NbExp=5; 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 Note=No experimental confirmation available.; CC Name=9; CC IsoId=O15409-9; Sequence=VSP_043464; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 6 are expressed in adult CC and fetal brain, caudate nucleus and lung. CC {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, CC thalamic and cerebellar expression. Highly expressed in the head CC and tail of nucleus caudatus and putamen. Restricted expression CC within the globus pallidus, with high levels in the pars interna, CC which provides the principal source of output from the basal CC ganglia to the nucleus centrum medianum thalami (CM) and the major CC motor relay nuclei of the thalamus. In the thalamus, present in CC the CM and nucleus medialis dorsalis thalami. Lower levels are CC observed in the nuclei anterior thalami, dorsal and ventral, and CC the nucleus parafascicularis thalami. Expressed in the ventrobasal CC complex comprising the nucleus ventralis posterior CC lateralis/medialis. The ventral tier of the thalamus exhibits CC strong expression, including nuclei ventralis anterior, lateralis CC and 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 CC disorder characterized by severe orofacial dyspraxia resulting in CC largely incomprehensible speech. Affected individuals have severe CC impairment in the selection and sequencing of fine orofacial CC movements which are necessary for articulation, and deficits in CC several facets of grammatical skills and language processing, such CC as the ability to break up words into their constituent phonemes. CC {ECO:0000269|PubMed:11586359}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- DISEASE: Note=A chromosomal aberration involving FOXP2 is a cause CC of severe speech and language impairment. Translocation CC t(5;7)(q22;q31.2). CC -!- SIMILARITY: Contains 1 C2H2-type zinc finger. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 fork-head DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00089}. CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Talking heads - Issue CC 51 of October 2004; CC URL="http://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. [O15409-4] DR UniGene; Hs.282787; -. 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 ProteinModelPortal; O15409; -. DR SMR; O15409; -. DR BioGrid; 125073; 28. DR DIP; DIP-29004N; -. DR IntAct; O15409; 15. DR STRING; 9606.ENSP00000386200; -. DR iPTMnet; O15409; -. DR PhosphoSitePlus; O15409; -. DR BioMuta; FOXP2; -. DR PaxDb; O15409; -. DR PeptideAtlas; O15409; -. DR PRIDE; O15409; -. DR Ensembl; ENST00000350908; ENSP00000265436; ENSG00000128573. [O15409-1] DR Ensembl; ENST00000360232; ENSP00000353367; ENSG00000128573. [O15409-6] DR Ensembl; ENST00000378237; ENSP00000367482; ENSG00000128573. [O15409-7] DR Ensembl; ENST00000393489; ENSP00000377129; ENSG00000128573. [O15409-2] DR Ensembl; ENST00000393494; ENSP00000377132; ENSG00000128573. [O15409-1] DR Ensembl; ENST00000403559; ENSP00000385069; ENSG00000128573. [O15409-9] DR Ensembl; ENST00000408937; ENSP00000386200; ENSG00000128573. [O15409-4] DR Ensembl; ENST00000412402; ENSP00000405470; ENSG00000128573. [O15409-8] DR Ensembl; ENST00000441290; ENSP00000416825; ENSG00000128573. [O15409-8] DR Ensembl; ENST00000635109; ENSP00000489457; ENSG00000128573. [O15409-8] DR GeneID; 93986; -. DR KEGG; hsa:93986; -. DR UCSC; uc003vgx.3; human. [O15409-1] DR CTD; 93986; -. DR DisGeNET; 93986; -. DR GeneCards; FOXP2; -. DR HGNC; HGNC:13875; FOXP2. DR HPA; CAB011488; -. DR HPA; HPA000382; -. DR HPA; HPA000383; -. 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; Childhood apraxia of speech. DR PharmGKB; PA28242; -. DR eggNOG; KOG4385; Eukaryota. DR eggNOG; COG5025; LUCA. DR GeneTree; ENSGT00800000124014; -. DR HOGENOM; HOG000092089; -. DR HOVERGEN; HBG051657; -. DR InParanoid; O15409; -. DR KO; K09409; -. DR OMA; PETKLCV; -. DR PhylomeDB; O15409; -. DR TreeFam; TF326978; -. DR BioCyc; ZFISH:ENSG00000128573-MONOMER; -. DR SIGNOR; O15409; -. DR ChiTaRS; FOXP2; human. DR EvolutionaryTrace; O15409; -. DR GeneWiki; FOXP2; -. DR GenomeRNAi; 93986; -. DR PRO; PR:O15409; -. DR Proteomes; UP000005640; Chromosome 7. DR Bgee; ENSG00000128573; -. DR ExpressionAtlas; O15409; baseline and differential. DR Genevisible; O15409; HS. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB. 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 core promoter proximal region sequence-specific DNA binding; IEA:Ensembl. DR GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:BHF-UCL. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:BHF-UCL. DR GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; IEA:Ensembl. DR GO; GO:0043010; P:camera-type eye development; IEA:Ensembl. DR GO; GO:0021757; P:caudate nucleus development; IMP:UniProtKB. DR GO; GO:0021549; P:cerebellum development; IEA:Ensembl. DR GO; GO:0021987; P:cerebral cortex development; IEP:BHF-UCL. DR GO; GO:0040007; P:growth; IEA:Ensembl. DR GO; GO:0048286; P:lung alveolus development; IEA:Ensembl. DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:BHF-UCL. DR GO; GO:0060501; P:positive regulation of epithelial cell proliferation involved in lung morphogenesis; IEA:Ensembl. DR GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IEA:Ensembl. DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl. DR GO; GO:0021758; P:putamen development; IMP:UniProtKB. DR GO; GO:0060013; P:righting reflex; IEA:Ensembl. DR GO; GO:0007519; P:skeletal muscle tissue development; IEA:Ensembl. DR GO; GO:0048745; P:smooth muscle tissue development; IEA:Ensembl. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0042297; P:vocal learning; IEA:Ensembl. 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; IPR011991; WHTH_DNA-bd_dom. 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 Complete proteome; Disease mutation; DNA-binding; Metal-binding; KW Nucleus; Reference proteome; Repressor; Transcription; KW Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1 715 Forkhead box protein P2. FT /FTId=PRO_0000091879. FT ZN_FING 346 371 C2H2-type. FT DNA_BIND 504 594 Fork-head. {ECO:0000255|PROSITE- FT ProRule:PRU00089}. FT REGION 388 409 Leucine-zipper. FT REGION 422 426 CTBP1-binding. {ECO:0000250}. FT COMPBIAS 53 268 Gln-rich. FT VAR_SEQ 1 92 Missing (in isoform 3). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_001558. FT VAR_SEQ 86 86 Q -> QELLPETKLCICGHSSGDGHPHNTFA (in FT isoform 4 and isoform 5). FT {ECO:0000303|Ref.3, ECO:0000303|Ref.4}. FT /FTId=VSP_011532. FT VAR_SEQ 87 87 V -> P (in isoform 8). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_011533. FT VAR_SEQ 88 715 Missing (in isoform 8). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_011534. FT VAR_SEQ 132 132 Q -> QDFLDSGLENFRAALEKN (in isoform 9). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_043464. FT VAR_SEQ 133 143 QQLQEFYKKQQ -> VMWVTCFGVLA (in isoform FT 5). {ECO:0000303|Ref.3}. FT /FTId=VSP_011535. FT VAR_SEQ 144 715 Missing (in isoform 5). FT {ECO:0000303|Ref.3}. FT /FTId=VSP_011536. FT VAR_SEQ 366 715 Missing (in isoform 7). FT {ECO:0000303|PubMed:12189486}. FT /FTId=VSP_011537. FT VAR_SEQ 423 432 LNLVSSVTMS -> VSAYCFINSK (in isoform 6). FT {ECO:0000303|PubMed:12189486}. FT /FTId=VSP_011538. FT VAR_SEQ 433 715 Missing (in isoform 6). FT {ECO:0000303|PubMed:12189486}. FT /FTId=VSP_011539. FT VARIANT 553 553 R -> H (in SPCH1; dbSNP:rs121908377). FT {ECO:0000269|PubMed:11586359}. FT /FTId=VAR_012278. FT CONFLICT 29 29 A -> V (in Ref. 2; AAM60762). FT {ECO:0000305}. FT CONFLICT 134 134 Q -> H (in Ref. 10; AAB91439). FT {ECO:0000305}. FT CONFLICT 290 304 DLTTNNSSSTTSSNT -> EEFPVQGPAAVCAGL (in FT Ref. 10; AAB91439). {ECO:0000305}. FT CONFLICT 414 414 S -> L (in Ref. 2; AAM60766). FT {ECO:0000305}. FT HELIX 509 519 {ECO:0000244|PDB:2A07}. FT HELIX 527 541 {ECO:0000244|PDB:2A07}. FT HELIX 545 558 {ECO:0000244|PDB:2A07}. FT STRAND 562 567 {ECO:0000244|PDB:2AS5}. FT STRAND 568 572 {ECO:0000244|PDB:2A07}. FT HELIX 577 583 {ECO:0000244|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 //