FOXP1_HUMAN
ID FOXP1_HUMAN Reviewed; 677 AA.
AC Q9H334; A3QVP8; B3KV70; G5E9V8; Q8NAN6; Q9BSG9; Q9H332; Q9H333; Q9P0R1;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Forkhead box protein P1;
DE AltName: Full=Mac-1-regulated forkhead {ECO:0000303|PubMed:15286807};
DE Short=MFH {ECO:0000303|PubMed:15286807};
GN Name=FOXP1; ORFNames=HSPC215;
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), NUCLEOTIDE SEQUENCE [MRNA] OF
RP 210-677 (ISOFORM 7), AND PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Testis;
RX PubMed=11751404;
RA Banham A.H., Beasley N., Campo E., Fernandez P.L., Fidler C., Gatter K.,
RA Jones M., Mason D.Y., Prime J.E., Trougouboff P., Wood K., Cordell J.L.;
RT "The FOXP1 winged helix transcription factor is a novel candidate tumor
RT suppressor gene on chromosome 3p.";
RL Cancer Res. 61:8820-8829(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 6 AND 7), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 101-677 (ISOFORM 4).
RC TISSUE=Embryonic head, and 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC TISSUE=Lung;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 60-677, AND CHROMOSOMAL TRANSLOCATION WITH
RP PAX5.
RX PubMed=17344859; DOI=10.1038/nature05690;
RA Mullighan C.G., Goorha S., Radtke I., Miller C.B., Coustan-Smith E.,
RA Dalton J.D., Girtman K., Mathew S., Ma J., Pounds S.B., Su X., Pui C.-H.,
RA Relling M.V., Evans W.E., Shurtleff S.A., Downing J.R.;
RT "Genome-wide analysis of genetic alterations in acute lymphoblastic
RT leukaemia.";
RL Nature 446:758-764(2007).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 528-677.
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [9]
RP FUNCTION.
RX PubMed=15286807; DOI=10.1172/jci200421100;
RA Shi C., Zhang X., Chen Z., Sulaiman K., Feinberg M.W., Ballantyne C.M.,
RA Jain M.K., Simon D.I.;
RT "Integrin engagement regulates monocyte differentiation through the
RT forkhead transcription factor Foxp1.";
RL J. Clin. Invest. 114:408-418(2004).
RN [10]
RP FUNCTION, INTERACTION WITH AR, AND INDUCTION BY ANDROGEN.
RX PubMed=18640093; DOI=10.1016/j.bbrc.2008.07.056;
RA Takayama K., Horie-Inoue K., Ikeda K., Urano T., Murakami K.,
RA Hayashizaki Y., Ouchi Y., Inoue S.;
RT "FOXP1 is an androgen-responsive transcription factor that negatively
RT regulates androgen receptor signaling in prostate cancer cells.";
RL Biochem. Biophys. Res. Commun. 374:388-393(2008).
RN [11]
RP FUNCTION.
RX PubMed=18799727; DOI=10.1182/blood-2008-01-137018;
RA Shi C., Sakuma M., Mooroka T., Liscoe A., Gao H., Croce K.J., Sharma A.,
RA Kaplan D., Greaves D.R., Wang Y., Simon D.I.;
RT "Down-regulation of the forkhead transcription factor Foxp1 is required for
RT monocyte differentiation and macrophage function.";
RL Blood 112:4699-4711(2008).
RN [12]
RP FUNCTION, AND INTERACTION WITH NCOR2.
RX PubMed=18347093; DOI=10.1101/gad.1637108;
RA Jepsen K., Gleiberman A.S., Shi C., Simon D.I., Rosenfeld M.G.;
RT "Cooperative regulation in development by SMRT and FOXP1.";
RL Genes Dev. 22:740-745(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [14]
RP FUNCTION, INVOLVEMENT IN MRLIAF, AND VARIANTS ALA-215; MET-445; SER-570 AND
RP ASN-613.
RX PubMed=20950788; DOI=10.1016/j.ajhg.2010.09.017;
RA Hamdan F.F., Daoud H., Rochefort D., Piton A., Gauthier J., Langlois M.,
RA Foomani G., Dobrzeniecka S., Krebs M.O., Joober R., Lafreniere R.G.,
RA Lacaille J.C., Mottron L., Drapeau P., Beauchamp M.H., Phillips M.S.,
RA Fombonne E., Rouleau G.A., Michaud J.L.;
RT "De novo mutations in FOXP1 in cases with intellectual disability, autism,
RT and language impairment.";
RL Am. J. Hum. Genet. 87:671-678(2010).
RN [15]
RP ALTERNATIVE SPLICING (ISOFORM 8), FUNCTION (ISOFORM 8), AND TISSUE
RP SPECIFICITY (ISOFORM 8).
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 [16]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-149 (ISOFORM 4).
RC TISSUE=Kidney;
RG The Cancer Genome Anatomy Project (CGAP) at the National Cancer Institute;
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP FUNCTION.
RX PubMed=24023716; DOI=10.1371/journal.pone.0070873;
RA Grundmann S., Lindmayer C., Hans F.P., Hoefer I., Helbing T.,
RA Pasterkamp G., Bode C., de Kleijn D., Moser M.;
RT "FoxP1 stimulates angiogenesis by repressing the inhibitory guidance
RT protein semaphorin 5B in endothelial cells.";
RL PLoS ONE 8:E70873-E70873(2013).
RN [19]
RP FUNCTION.
RX PubMed=25267198; DOI=10.1182/blood-2014-01-553412;
RA van Keimpema M., Grueneberg L.J., Mokry M., van Boxtel R., Koster J.,
RA Coffer P.J., Pals S.T., Spaargaren M.;
RT "FOXP1 directly represses transcription of pro-apoptotic genes and
RT cooperates with NF-kappaB to promote survival of human B-cells.";
RL Blood 124:3431-3440(2014).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-653 AND SER-658, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [21]
RP INTERACTION WITH FOXP2 AND FOXP4, AND SUBCELLULAR LOCATION.
RX PubMed=25027557; DOI=10.1007/s12031-014-0359-7;
RA Sin C., Li H., Crawford D.A.;
RT "Transcriptional Regulation by FOXP1, FOXP2, and FOXP4 Dimerization.";
RL J. Mol. Neurosci. 55:437-448(2015).
RN [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-287; LYS-372; LYS-377 AND
RP LYS-442, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [23]
RP FUNCTION, AND INTERACTION WITH AURKA.
RX PubMed=28218735; DOI=10.1038/oncsis.2016.80;
RA Kamran M., Long Z.J., Xu D., Lv S.S., Liu B., Wang C.L., Xu J., Lam E.W.,
RA Liu Q.;
RT "Aurora kinase A regulates Survivin stability through targeting FBXL7 in
RT gastric cancer drug resistance and prognosis.";
RL Oncogenesis 6:E298-E298(2017).
RN [24]
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 [25]
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).
RN [26]
RP STRUCTURE BY NMR OF 462-548.
RX PubMed=21416545; DOI=10.1002/pro.626;
RA Chu Y.P., Chang C.H., Shiu J.H., Chang Y.T., Chen C.Y., Chuang W.J.;
RT "Solution structure and backbone dynamics of the DNA-binding domain of
RT FOXP1: insight into its domain swapping and DNA binding.";
RL Protein Sci. 20:908-924(2011).
RN [27]
RP VARIANT ALA-215.
RX PubMed=19352412; DOI=10.1038/ejhg.2009.43;
RA Vernes S.C., MacDermot K.D., Monaco A.P., Fisher S.E.;
RT "Assessing the impact of FOXP1 mutations on developmental verbal
RT dyspraxia.";
RL Eur. J. Hum. Genet. 17:1354-1358(2009).
RN [28]
RP VARIANTS PRO-5; VAL-101; ALA-215; PRO-261; SER-390 AND SER-570, AND VARIANT
RP MRLIAF THR-597.
RX PubMed=20848658; DOI=10.1002/humu.21362;
RA Horn D., Kapeller J., Rivera-Brugues N., Moog U., Lorenz-Depiereux B.,
RA Eck S., Hempel M., Wagenstaller J., Gawthrope A., Monaco A.P., Bonin M.,
RA Riess O., Wohlleber E., Illig T., Bezzina C.R., Franke A., Spranger S.,
RA Villavicencio-Lorini P., Seifert W., Rosenfeld J., Klopocki E.,
RA Rappold G.A., Strom T.M.;
RT "Identification of FOXP1 deletions in three unrelated patients with mental
RT retardation and significant speech and language deficits.";
RL Hum. Mutat. 31:E1851-E1860(2010).
RN [29]
RP VARIANTS MRLIAF GLY-465; CYS-514; ARG-534 AND THR-597, VARIANTS THR-107;
RP ALA-215 AND SER-570, CHARACTERIZATION OF VARIANTS MRLIAF GLY-465; CYS-514;
RP ARG-534 AND THR-597, CHARACTERIZATION OF VARIANTS THR-107; ALA-215 AND
RP SER-570, FUNCTION, SELF-ASSOCIATION, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH FOXP2.
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 [30]
RP VARIANT THR-107.
RX PubMed=29463886; DOI=10.1038/s41380-018-0020-x;
RA Eising E., Carrion-Castillo A., Vino A., Strand E.A., Jakielski K.J.,
RA Scerri T.S., Hildebrand M.S., Webster R., Ma A., Mazoyer B., Francks C.,
RA Bahlo M., Scheffer I.E., Morgan A.T., Shriberg L.D., Fisher S.E.;
RT "A set of regulatory genes co-expressed in embryonic human brain is
RT implicated in disrupted speech development.";
RL Mol. Psychiatry 24:1065-1078(2019).
CC -!- FUNCTION: Transcriptional repressor (PubMed:18347093, PubMed:26647308).
CC Can act with CTBP1 to synergistically repress transcription but CTPBP1
CC is not essential (By similarity). 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. Essential transcriptional
CC regulator of B-cell development. Involved in regulation of cardiac
CC muscle cell proliferation. Involved in the columnar organization of
CC spinal motor neurons. Promotes the formation of the lateral motor
CC neuron column (LMC) and the preganglionic motor column (PGC) and is
CC required for respective appropriate motor axon projections. The
CC segment-appropriate generation of spinal cord motor columns requires
CC cooperation with other Hox proteins. Can regulate PITX3 promoter
CC activity; may promote midbrain identity in embryonic stem cell-derived
CC dopamine neurons by regulating PITX3. Negatively regulates the
CC differentiation of T follicular helper cells T(FH)s. Involved in
CC maintenance of hair follicle stem cell quiescence; the function
CC probably involves regulation of FGF18 (By similarity). Represses
CC transcription of various pro-apoptotic genes and cooperates with NF-
CC kappa B-signaling in promoting B-cell expansion by inhibition of
CC caspase-dependent apoptosis (PubMed:25267198). Binds to CSF1R promoter
CC elements and is involved in regulation of monocyte differentiation and
CC macrophage functions; repression of CSF1R in monocytes seems to involve
CC NCOR2 as corepressor (PubMed:15286807, PubMed:18799727,
CC PubMed:18347093). Involved in endothelial cell proliferation, tube
CC formation and migration indicative for a role in angiogenesis; the role
CC in neovascularization seems to implicate suppression of SEMA5B
CC (PubMed:24023716). Can negatively regulate androgen receptor signaling
CC (PubMed:18640093). Acts as a transcriptional activator of the FBXL7
CC promoter; this activity is regulated by AURKA (PubMed:28218735).
CC {ECO:0000250|UniProtKB:P58462, ECO:0000269|PubMed:15286807,
CC ECO:0000269|PubMed:18640093, ECO:0000269|PubMed:18799727,
CC ECO:0000269|PubMed:24023716, ECO:0000269|PubMed:25267198,
CC ECO:0000269|PubMed:26647308, ECO:0000269|PubMed:28218735,
CC ECO:0000305|PubMed:18347093, ECO:0000305|PubMed:24023716}.
CC -!- FUNCTION: [Isoform 8]: 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)
CC (PubMed:21924763). Promotes ESC self-renewal and pluripotency (By
CC similarity). {ECO:0000250|UniProtKB:P58462,
CC ECO:0000269|PubMed:21924763}.
CC -!- SUBUNIT: Forms homodimers and heterodimers with FOXP2 and FOXP4
CC (PubMed:25027557). Dimerization is required for DNA-binding. Self-
CC associates (PubMed:26647308). Interacts with CTBP1 (By similarity).
CC Interacts with NCOR2 and AR (PubMed:18347093, PubMed:18640093).
CC Interacts with FOXP2 (PubMed:26647308). Interacts with TBR1
CC (PubMed:30250039). Interacts with AURKA; this interaction facilitates
CC the phosphorylation of FOXP1, which suppresses the expression of FBXL7
CC (PubMed:28218735). Interacts with ZMYM2 (PubMed:32891193).
CC {ECO:0000250|UniProtKB:P58462, ECO:0000269|PubMed:18347093,
CC ECO:0000269|PubMed:18640093, ECO:0000269|PubMed:25027557,
CC ECO:0000269|PubMed:26647308, ECO:0000269|PubMed:28218735,
CC ECO:0000269|PubMed:30250039, ECO:0000269|PubMed:32891193}.
CC -!- INTERACTION:
CC Q9H334; Q9H334: FOXP1; NbExp=8; IntAct=EBI-983809, EBI-983809;
CC Q9H334; O15409: FOXP2; NbExp=13; IntAct=EBI-983809, EBI-983612;
CC Q9H334; Q8IVH2: FOXP4; NbExp=6; IntAct=EBI-983809, EBI-1054619;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25027557,
CC ECO:0000269|PubMed:26647308}. Note=Not found in the nucleolus.
CC {ECO:0000269|PubMed:26647308}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q9H334-1; Sequence=Displayed;
CC Name=3;
CC IsoId=Q9H334-3; Sequence=VSP_001555, VSP_001556;
CC Name=4;
CC IsoId=Q9H334-4; Sequence=VSP_001555;
CC Name=5;
CC IsoId=Q9H334-5; Sequence=VSP_043462, VSP_043463;
CC Name=6;
CC IsoId=Q9H334-6; Sequence=VSP_001556;
CC Name=7;
CC IsoId=Q9H334-7; Sequence=VSP_046930;
CC Name=8; Synonyms=FOXP1-ES;
CC IsoId=Q9H334-8; Sequence=VSP_057341;
CC -!- TISSUE SPECIFICITY: Isoform 8 is specifically expressed in embryonic
CC stem cells. {ECO:0000269|PubMed:21924763}.
CC -!- INDUCTION: By androgen in an isoform-specific manner; expression of
CC isoform 4 is greatly induced. {ECO:0000269|PubMed:18640093}.
CC -!- DOMAIN: The leucine-zipper is required for dimerization and
CC transcriptional repression. {ECO:0000250|UniProtKB:P58462}.
CC -!- DISEASE: Note=A chromosomal aberration involving FOXP1 is found in
CC acute lymphoblastic leukemia. Translocation t(9;3)(p13;p14.1) with
CC PAX5.
CC -!- DISEASE: Intellectual disability with language impairment and autistic
CC features (MRLIAF) [MIM:613670]: A developmental disorder characterized
CC by mild to moderate intellectual disability, language impairment, and
CC autistic features. Patients show global delay, delayed walking,
CC severely delayed speech development, and behavioral abnormalities,
CC including irritability, hyperactivity, aggression, and stereotypical
CC rigid behaviors. {ECO:0000269|PubMed:20848658,
CC ECO:0000269|PubMed:20950788, ECO:0000269|PubMed:26647308}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: [Isoform 3]: Incomplete sequence. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: Incomplete sequence. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 7]: May be due to competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF36135.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAG47634.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC Sequence=ABI33105.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB55005.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/FOXP1ID40632ch3p14.html";
CC ---------------------------------------------------------------------------
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DR EMBL; AF146696; AAG47632.1; -; mRNA.
DR EMBL; AF146697; AAG47633.1; -; mRNA.
DR EMBL; AF146698; AAG47634.1; ALT_SEQ; mRNA.
DR EMBL; AF275309; AAK69408.1; -; mRNA.
DR EMBL; BT006643; AAP35289.1; -; mRNA.
DR EMBL; AK092383; BAC03875.1; -; mRNA.
DR EMBL; AK122710; BAG53682.1; -; mRNA.
DR EMBL; AC097632; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC097634; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC103586; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104442; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104645; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC138058; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471055; EAW65494.1; -; Genomic_DNA.
DR EMBL; CH471055; EAW65499.1; -; Genomic_DNA.
DR EMBL; BC005055; AAH05055.1; -; mRNA.
DR EMBL; BC054815; AAH54815.1; -; mRNA.
DR EMBL; BC071893; AAH71893.1; -; mRNA.
DR EMBL; BC080521; AAH80521.1; -; mRNA.
DR EMBL; DQ845346; ABI33105.1; ALT_INIT; mRNA.
DR EMBL; AK027264; BAB55005.1; ALT_INIT; mRNA.
DR EMBL; AF151049; AAF36135.1; ALT_FRAME; mRNA.
DR EMBL; BQ017072; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS2914.1; -. [Q9H334-1]
DR CCDS; CCDS33785.1; -. [Q9H334-5]
DR CCDS; CCDS58838.1; -. [Q9H334-6]
DR CCDS; CCDS58839.1; -. [Q9H334-7]
DR CCDS; CCDS74964.1; -. [Q9H334-8]
DR RefSeq; NP_001012523.1; NM_001012505.1. [Q9H334-5]
DR RefSeq; NP_001231737.1; NM_001244808.1. [Q9H334-7]
DR RefSeq; NP_001231739.1; NM_001244810.1. [Q9H334-8]
DR RefSeq; NP_001231741.1; NM_001244812.1. [Q9H334-6]
DR RefSeq; NP_001231743.1; NM_001244814.1. [Q9H334-1]
DR RefSeq; NP_001231744.1; NM_001244815.1.
DR RefSeq; NP_001231745.1; NM_001244816.1. [Q9H334-1]
DR RefSeq; NP_116071.2; NM_032682.5. [Q9H334-1]
DR RefSeq; XP_006713165.1; XM_006713102.2. [Q9H334-1]
DR RefSeq; XP_006713166.1; XM_006713103.2. [Q9H334-1]
DR RefSeq; XP_006713167.1; XM_006713104.2. [Q9H334-1]
DR RefSeq; XP_011531886.1; XM_011533584.2.
DR RefSeq; XP_011531887.1; XM_011533585.2. [Q9H334-1]
DR RefSeq; XP_016861654.1; XM_017006165.1. [Q9H334-1]
DR RefSeq; XP_016861655.1; XM_017006166.1.
DR RefSeq; XP_016861657.1; XM_017006168.1. [Q9H334-5]
DR PDB; 2KIU; NMR; -; A=462-548.
DR PDBsum; 2KIU; -.
DR AlphaFoldDB; Q9H334; -.
DR SMR; Q9H334; -.
DR BioGRID; 117989; 95.
DR DIP; DIP-36585N; -.
DR IntAct; Q9H334; 85.
DR MINT; Q9H334; -.
DR GlyGen; Q9H334; 9 sites, 2 O-linked glycans (9 sites).
DR iPTMnet; Q9H334; -.
DR PhosphoSitePlus; Q9H334; -.
DR BioMuta; FOXP1; -.
DR DMDM; 14548062; -.
DR EPD; Q9H334; -.
DR jPOST; Q9H334; -.
DR MassIVE; Q9H334; -.
DR MaxQB; Q9H334; -.
DR PaxDb; Q9H334; -.
DR PeptideAtlas; Q9H334; -.
DR PRIDE; Q9H334; -.
DR ProteomicsDB; 34057; -.
DR ProteomicsDB; 72684; -.
DR ProteomicsDB; 80663; -. [Q9H334-1]
DR ProteomicsDB; 80665; -. [Q9H334-3]
DR ProteomicsDB; 80666; -. [Q9H334-4]
DR ProteomicsDB; 80667; -. [Q9H334-5]
DR ABCD; Q9H334; 3 sequenced antibodies.
DR Antibodypedia; 902; 859 antibodies from 49 providers.
DR DNASU; 27086; -.
DR Ensembl; ENST00000318779.7; ENSP00000318721.3; ENSG00000114861.24. [Q9H334-5]
DR Ensembl; ENST00000318789.11; ENSP00000318902.5; ENSG00000114861.24. [Q9H334-1]
DR Ensembl; ENST00000484350.5; ENSP00000417857.1; ENSG00000114861.24. [Q9H334-6]
DR Ensembl; ENST00000493089.7; ENSP00000418524.1; ENSG00000114861.24. [Q9H334-7]
DR Ensembl; ENST00000498215.7; ENSP00000418102.1; ENSG00000114861.24. [Q9H334-1]
DR Ensembl; ENST00000648380.1; ENSP00000497344.1; ENSG00000114861.24. [Q9H334-1]
DR Ensembl; ENST00000648426.1; ENSP00000498110.1; ENSG00000114861.24. [Q9H334-8]
DR Ensembl; ENST00000648710.2; ENSP00000497430.2; ENSG00000114861.24. [Q9H334-7]
DR Ensembl; ENST00000648718.1; ENSP00000496810.1; ENSG00000114861.24. [Q9H334-7]
DR Ensembl; ENST00000649528.3; ENSP00000497369.1; ENSG00000114861.24. [Q9H334-1]
DR Ensembl; ENST00000649631.1; ENSP00000496990.1; ENSG00000114861.24. [Q9H334-1]
DR Ensembl; ENST00000650068.2; ENSP00000497454.2; ENSG00000114861.24. [Q9H334-1]
DR GeneID; 27086; -.
DR KEGG; hsa:27086; -.
DR MANE-Select; ENST00000649528.3; ENSP00000497369.1; NM_001349338.3; NP_001336267.1.
DR UCSC; uc003dol.4; human. [Q9H334-1]
DR CTD; 27086; -.
DR DisGeNET; 27086; -.
DR GeneCards; FOXP1; -.
DR HGNC; HGNC:3823; FOXP1.
DR HPA; ENSG00000114861; Low tissue specificity.
DR MalaCards; FOXP1; -.
DR MIM; 605515; gene.
DR MIM; 613670; phenotype.
DR neXtProt; NX_Q9H334; -.
DR OpenTargets; ENSG00000114861; -.
DR Orphanet; 585877; B-lymphoblastic leukemia/lymphoma with recurrent genetic abnormality.
DR Orphanet; 391372; Intellectual disability-severe speech delay-mild dysmorphism syndrome.
DR Orphanet; 52417; MALT lymphoma.
DR PharmGKB; PA28241; -.
DR VEuPathDB; HostDB:ENSG00000114861; -.
DR eggNOG; KOG4385; Eukaryota.
DR GeneTree; ENSGT00940000159892; -.
DR HOGENOM; CLU_168648_0_0_1; -.
DR InParanoid; Q9H334; -.
DR OMA; GHAYCTP; -.
DR OrthoDB; 836427at2759; -.
DR PhylomeDB; Q9H334; -.
DR TreeFam; TF326978; -.
DR PathwayCommons; Q9H334; -.
DR Reactome; R-HSA-452723; Transcriptional regulation of pluripotent stem cells. [Q9H334-8]
DR SignaLink; Q9H334; -.
DR SIGNOR; Q9H334; -.
DR BioGRID-ORCS; 27086; 14 hits in 1098 CRISPR screens.
DR ChiTaRS; FOXP1; human.
DR GeneWiki; FOXP1; -.
DR GenomeRNAi; 27086; -.
DR Pharos; Q9H334; Tbio.
DR PRO; PR:Q9H334; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9H334; protein.
DR Bgee; ENSG00000114861; Expressed in pancreatic ductal cell and 194 other tissues.
DR ExpressionAtlas; Q9H334; baseline and differential.
DR Genevisible; Q9H334; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; IDA:UniProtKB.
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:0050681; F:nuclear androgen receptor binding; IDA:UniProtKB.
DR GO; GO:0043621; F:protein self-association; IMP:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:ARUK-UCL.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR GO; GO:0042118; P:endothelial cell activation; IMP:UniProtKB.
DR GO; GO:0042116; P:macrophage activation; IDA:UniProtKB.
DR GO; GO:0042117; P:monocyte activation; IDA:UniProtKB.
DR GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0002903; P:negative regulation of B cell apoptotic process; IDA:UniProtKB.
DR GO; GO:0061052; P:negative regulation of cell growth involved in cardiac muscle cell development; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:ARUK-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:UniProtKB.
DR GO; GO:0036035; P:osteoclast development; IDA:UniProtKB.
DR GO; GO:0030316; P:osteoclast differentiation; IDA:UniProtKB.
DR GO; GO:0050861; P:positive regulation of B cell receptor signaling pathway; IMP:ARUK-UCL.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IMP:UniProtKB.
DR GO; GO:1905206; P:positive regulation of hydrogen peroxide-induced cell death; IEA:Ensembl.
DR GO; GO:0032745; P:positive regulation of interleukin-21 production; ISS:UniProtKB.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IMP:UniProtKB.
DR GO; GO:2000341; P:regulation of chemokine (C-X-C motif) ligand 2 production; IDA:UniProtKB.
DR GO; GO:1900424; P:regulation of defense response to bacterium; IDA:UniProtKB.
DR GO; GO:1901509; P:regulation of endothelial tube morphogenesis; IMP:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0050727; P:regulation of inflammatory response; IDA:UniProtKB.
DR GO; GO:0032651; P:regulation of interleukin-1 beta production; IDA:UniProtKB.
DR GO; GO:0032655; P:regulation of interleukin-12 production; IDA:UniProtKB.
DR GO; GO:1901256; P:regulation of macrophage colony-stimulating factor production; IDA:UniProtKB.
DR GO; GO:0045655; P:regulation of monocyte differentiation; IDA: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; IDA:UniProtKB.
DR GO; GO:0032496; P:response to lipopolysaccharide; IDA:UniProtKB.
DR GO; GO:0033574; P:response to testosterone; IEA:Ensembl.
DR GO; GO:0021756; P:striatum development; IEA:Ensembl.
DR GO; GO:0061470; P:T follicular helper cell differentiation; ISS: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 3D-structure; Alternative splicing; Chromosomal rearrangement;
KW Disease variant; DNA-binding; Intellectual disability; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..677
FT /note="Forkhead box protein P1"
FT /id="PRO_0000091877"
FT ZN_FING 306..331
FT /note="C2H2-type"
FT DNA_BIND 465..555
FT /note="Fork-head"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..369
FT /note="Leucine-zipper"
FT REGION 382..386
FT /note="CTBP1-binding"
FT /evidence="ECO:0000250"
FT REGION 390..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..677
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 270..286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 611..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 59..60
FT /note="Breakpoint for translocation to form PAX5-FOXP1"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 653
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 658
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CROSSLNK 287
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 372
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 377
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 442
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..60
FT /note="MMQESGTETKSNGSAIQNGSGGSNHLLECGGLREGRSNGETPAVDIGAADLA
FT HAQQQQQQ -> MFQCVFSSSVLQPHSTSCLFKHLFYHSATPASQKQPEPIYSKKTEIQ
FT RQTVRAPFAKLFIFS (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_001555"
FT VAR_SEQ 61..114
FT /note="ALQVARQLLLQQQQQQQVSGLKSPKRNDKQPALQVPVSVAMMTPQVITPQQM
FT QQ -> WHLINHQPSRSPSSWLKRLISSPWELEVLQVPLWGAVAETKMSGPVCQPNPSP
FT F (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_043462"
FT VAR_SEQ 95..170
FT /note="Missing (in isoform 3 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_001556"
FT VAR_SEQ 115..677
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_043463"
FT VAR_SEQ 450
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:11751404,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_046930"
FT VAR_SEQ 511..551
FT /note="NAVRHNLSLHKCFVRVENVKGAVWTVDEVEFQKRRPQKISG -> GAIRTNL
FT SLHKCFIRVEDEFGSFWTVDDEEFKRGRHIQRGRPRKYCPDENFDELVAH (in
FT isoform 8)"
FT /evidence="ECO:0000269|PubMed:21924763"
FT /id="VSP_057341"
FT VARIANT 5
FT /note="S -> P (in dbSNP:rs762898505)"
FT /evidence="ECO:0000269|PubMed:20848658"
FT /id="VAR_065067"
FT VARIANT 101
FT /note="M -> V (in dbSNP:rs564508875)"
FT /evidence="ECO:0000269|PubMed:20848658"
FT /id="VAR_065068"
FT VARIANT 107
FT /note="I -> T (likely benign variant; does not affect
FT nuclear localization; no loss of transcriptional repression
FT activity; no loss of ability to self-associate; no loss of
FT interaction with FOXP2)"
FT /evidence="ECO:0000269|PubMed:26647308,
FT ECO:0000269|PubMed:29463886"
FT /id="VAR_075246"
FT VARIANT 215
FT /note="P -> A (does not affect nuclear localization; no
FT loss of transcriptional repression activity; no loss of
FT ability to self-associate; no loss of interaction with
FT FOXP2; dbSNP:rs146606219)"
FT /evidence="ECO:0000269|PubMed:19352412,
FT ECO:0000269|PubMed:20848658, ECO:0000269|PubMed:20950788,
FT ECO:0000269|PubMed:26647308"
FT /id="VAR_065069"
FT VARIANT 261
FT /note="S -> P"
FT /evidence="ECO:0000269|PubMed:20848658"
FT /id="VAR_065070"
FT VARIANT 390
FT /note="T -> S (in dbSNP:rs761840006)"
FT /evidence="ECO:0000269|PubMed:20848658"
FT /id="VAR_065071"
FT VARIANT 445
FT /note="V -> M (in dbSNP:rs147756430)"
FT /evidence="ECO:0000269|PubMed:20950788"
FT /id="VAR_065072"
FT VARIANT 465
FT /note="R -> G (in MRLIAF; nuclear and cytoplasmic
FT aggregation; loss of transcriptional repression activity;
FT loss of ability to self-associate; loss of interaction with
FT FOXP2; dbSNP:rs869025202)"
FT /evidence="ECO:0000269|PubMed:26647308"
FT /id="VAR_075247"
FT VARIANT 514
FT /note="R -> C (in MRLIAF; nuclear and cytoplasmic
FT aggregation; loss of transcriptional repression activity;
FT loss of ability to self-associate; loss of interaction with
FT FOXP2; dbSNP:rs869025203)"
FT /evidence="ECO:0000269|PubMed:26647308"
FT /id="VAR_075248"
FT VARIANT 534
FT /note="W -> R (in MRLIAF; nuclear and cytoplasmic
FT aggregation; loss of transcriptional repression activity;
FT loss of ability to self-associate; loss of interaction with
FT FOXP2; dbSNP:rs587777855)"
FT /evidence="ECO:0000269|PubMed:26647308"
FT /id="VAR_075249"
FT VARIANT 570
FT /note="N -> S (does not affect nuclear localization; no
FT loss of transcriptional repression activity; no loss of
FT ability to self-associate; no loss of interaction with
FT FOXP2; dbSNP:rs140161845)"
FT /evidence="ECO:0000269|PubMed:20848658,
FT ECO:0000269|PubMed:20950788, ECO:0000269|PubMed:26647308"
FT /id="VAR_065073"
FT VARIANT 597
FT /note="N -> T (in MRLIAF; unknown pathological
FT significance; does not affect nuclear localization; no loss
FT of transcriptional repression activity; no loss of ability
FT to self-associate; no loss of interaction with FOXP2)"
FT /evidence="ECO:0000269|PubMed:20848658,
FT ECO:0000269|PubMed:26647308"
FT /id="VAR_065074"
FT VARIANT 613
FT /note="T -> N (in dbSNP:rs1318614471)"
FT /evidence="ECO:0000269|PubMed:20950788"
FT /id="VAR_065075"
FT CONFLICT 138
FT /note="L -> P (in Ref. 3; BAG53682)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="Q -> R (in Ref. 3; BAB55005)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="L -> V (in Ref. 3; BAB55005)"
FT /evidence="ECO:0000305"
FT CONFLICT 210..212
FT /note="GQP -> ARA (in Ref. 1; AAK69408)"
FT /evidence="ECO:0000305"
FT HELIX 470..479
FT /evidence="ECO:0007829|PDB:2KIU"
FT STRAND 481..486
FT /evidence="ECO:0007829|PDB:2KIU"
FT HELIX 488..498
FT /evidence="ECO:0007829|PDB:2KIU"
FT HELIX 500..502
FT /evidence="ECO:0007829|PDB:2KIU"
FT HELIX 506..519
FT /evidence="ECO:0007829|PDB:2KIU"
FT STRAND 523..526
FT /evidence="ECO:0007829|PDB:2KIU"
FT STRAND 533..536
FT /evidence="ECO:0007829|PDB:2KIU"
FT HELIX 538..543
FT /evidence="ECO:0007829|PDB:2KIU"
SQ SEQUENCE 677 AA; 75317 MW; AEE92D47BB20964B CRC64;
MMQESGTETK SNGSAIQNGS GGSNHLLECG GLREGRSNGE TPAVDIGAAD LAHAQQQQQQ
ALQVARQLLL QQQQQQQVSG LKSPKRNDKQ PALQVPVSVA MMTPQVITPQ QMQQILQQQV
LSPQQLQVLL QQQQALMLQQ QQLQEFYKKQ QEQLQLQLLQ QQHAGKQPKE QQQVATQQLA
FQQQLLQMQQ LQQQHLLSLQ RQGLLTIQPG QPALPLQPLA QGMIPTELQQ LWKEVTSAHT
AEETTGNNHS SLDLTTTCVS SSAPSKTSLI MNPHASTNGQ LSVHTPKRES LSHEEHPHSH
PLYGHGVCKW PGCEAVCEDF QSFLKHLNSE HALDDRSTAQ CRVQMQVVQQ LELQLAKDKE
RLQAMMTHLH VKSTEPKAAP QPLNLVSSVT LSKSASEASP QSLPHTPTTP TAPLTPVTQG
PSVITTTSMH TVGPIRRRYS DKYNVPISSA DIAQNQEFYK NAEVRPPFTY ASLIRQAILE
SPEKQLTLNE IYNWFTRMFA YFRRNAATWK NAVRHNLSLH KCFVRVENVK GAVWTVDEVE
FQKRRPQKIS GNPSLIKNMQ SSHAYCTPLN AALQASMAEN SIPLYTTASM GNPTLGNLAS
AIREELNGAM EHTNSNESDS SPGRSPMQAV HPVHVKEEPL DPEEAEGPLS LVTTANHSPD
FDHDRDYEDE PVNEDME
