FOXA1_HUMAN
ID FOXA1_HUMAN Reviewed; 472 AA.
AC P55317; B2R9H6; B7ZAP5; Q9H2A0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Hepatocyte nuclear factor 3-alpha;
DE Short=HNF-3-alpha;
DE Short=HNF-3A;
DE AltName: Full=Forkhead box protein A1;
DE AltName: Full=Transcription factor 3A;
DE Short=TCF-3A;
GN Name=FOXA1; Synonyms=HNF3A, TCF3A;
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), AND VARIANTS ALA-72; MET-124 INS
RP AND ARG-185.
RC TISSUE=Lung;
RX PubMed=8652662; DOI=10.1016/0167-4781(96)00058-9;
RA Bingle C.D., Gowan S.;
RT "Molecular cloning of the forkhead transcription factor HNF-3 alpha from a
RT human pulmonary adenocarcinoma cell line.";
RL Biochim. Biophys. Acta 1307:17-20(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ALA-72; THR-83; MET-124
RP INS; ARG-185 AND ASN-448.
RX PubMed=10899756; DOI=10.1159/000022943;
RA Navas M.A., Vaisse C., Boger S., Heimesaat M., Kollee L.A., Stoffel M.;
RT "The human HNF-3 genes: cloning, partial sequence and mutation screening in
RT patients with impaired glucose homeostasis.";
RL Hum. Hered. 50:370-381(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Yu L., Takeda J.;
RT "Genetic variation in the HNF-3alpha gene.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Mammary gland, and Trachea;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [8]
RP TISSUE SPECIFICITY.
RX PubMed=12234996;
RA Lin L., Miller C.T., Contreras J.I., Prescott M.S., Dagenais S.L., Wu R.,
RA Yee J., Orringer M.B., Misek D.E., Hanash S.M., Glover T.W., Beer D.G.;
RT "The hepatocyte nuclear factor 3 alpha gene, HNF3alpha (FOXA1), on
RT chromosome band 14q13 is amplified and overexpressed in esophageal and lung
RT adenocarcinomas.";
RL Cancer Res. 62:5273-5279(2002).
RN [9]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=15987773; DOI=10.1242/dev.01917;
RA Gao N., Ishii K., Mirosevich J., Kuwajima S., Oppenheimer S.R.,
RA Roberts R.L., Jiang M., Yu X., Shappell S.B., Caprioli R.M., Stoffel M.,
RA Hayward S.W., Matusik R.J.;
RT "Forkhead box A1 regulates prostate ductal morphogenesis and promotes
RT epithelial cell maturation.";
RL Development 132:3431-3443(2005).
RN [10]
RP FUNCTION.
RX PubMed=16087863; DOI=10.1073/pnas.0505575102;
RA Laganiere J., Deblois G., Lefebvre C., Bataille A.R., Robert F.,
RA Giguere V.;
RT "Location analysis of estrogen receptor alpha target promoters reveals that
RT FOXA1 defines a domain of the estrogen response.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11651-11656(2005).
RN [11]
RP FUNCTION IN CELL CYCLE REGULATION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=16331276; DOI=10.1038/sj.onc.1209170;
RA Williamson E.A., Wolf I., O'Kelly J., Bose S., Tanosaki S., Koeffler H.P.;
RT "BRCA1 and FOXA1 proteins coregulate the expression of the cell cycle-
RT dependent kinase inhibitor p27(Kip1).";
RL Oncogene 25:1391-1399(2006).
RN [12]
RP INTERACTION WITH NKX2-1.
RX PubMed=17220277; DOI=10.1128/mcb.01133-06;
RA Minoo P., Hu L., Xing Y., Zhu N.L., Chen H., Li M., Borok Z., Li C.;
RT "Physical and functional interactions between homeodomain NKX2.1 and winged
RT helix/forkhead FOXA1 in lung epithelial cells.";
RL Mol. Cell. Biol. 27:2155-2165(2007).
RN [13]
RP FUNCTION IN CELL TYPE-SPECIFIC TRANSCRIPTION, AND DIFFERENTIAL RECRUITMENT
RP TO CHROMATIN.
RX PubMed=18358809; DOI=10.1016/j.cell.2008.01.018;
RA Lupien M., Eeckhoute J., Meyer C.A., Wang Q., Zhang Y., Li W.,
RA Carroll J.S., Liu X.S., Brown M.;
RT "FoxA1 translates epigenetic signatures into enhancer-driven lineage-
RT specific transcription.";
RL Cell 132:958-970(2008).
RN [14]
RP FUNCTION IN REGULATION OF APOPTOSIS.
RX PubMed=19127412; DOI=10.1007/s12192-008-0095-4;
RA Song L., Wei X., Zhang B., Luo X., Liu J., Feng Y., Xiao X.;
RT "Role of Foxa1 in regulation of bcl2 expression during oxidative-stress-
RT induced apoptosis in A549 type II pneumocytes.";
RL Cell Stress Chaperones 14:417-425(2009).
RN [15]
RP INTERACTION WITH FOXA2.
RX PubMed=19919681; DOI=10.1186/gb-2009-10-11-r129;
RA Motallebipour M., Ameur A., Reddy Bysani M.S., Patra K., Wallerman O.,
RA Mangion J., Barker M.A., McKernan K.J., Komorowski J., Wadelius C.;
RT "Differential binding and co-binding pattern of FOXA1 and FOXA3 and their
RT relation to H3K4me3 in HepG2 cells revealed by ChIP-seq.";
RL Genome Biol. 10:R129.0-R129.0(2009).
RN [16]
RP FUNCTION IN ESR1-MEDIATED TRANSCRIPTION REPRESSION, DIFFERENTIAL
RP RECRUITMENT TO CHROMATIN, AND INTERACTION WITH HDAC7.
RX PubMed=19917725; DOI=10.1128/mcb.00907-09;
RA Malik S., Jiang S., Garee J.P., Verdin E., Lee A.V., O'Malley B.W.,
RA Zhang M., Belaguli N.S., Oesterreich S.;
RT "Histone deacetylase 7 and FoxA1 in estrogen-mediated repression of RPRM.";
RL Mol. Cell. Biol. 30:399-412(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307 AND SER-331, 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).
CC -!- FUNCTION: Transcription factor that is involved in embryonic
CC development, establishment of tissue-specific gene expression and
CC regulation of gene expression in differentiated tissues. Is thought to
CC act as a 'pioneer' factor opening the compacted chromatin for other
CC proteins through interactions with nucleosomal core histones and
CC thereby replacing linker histones at target enhancer and/or promoter
CC sites. Binds DNA with the consensus sequence 5'-
CC [AC]A[AT]T[AG]TT[GT][AG][CT]T[CT]-3' (By similarity). Proposed to play
CC a role in translating the epigenetic signatures into cell type-specific
CC enhancer-driven transcriptional programs. Its differential recruitment
CC to chromatin is dependent on distribution of histone H3 methylated at
CC 'Lys-5' (H3K4me2) in estrogen-regulated genes. Involved in the
CC development of multiple endoderm-derived organ systems such as liver,
CC pancreas, lung and prostate; FOXA1 and FOXA2 seem to have at least in
CC part redundant roles (By similarity). Modulates the transcriptional
CC activity of nuclear hormone receptors. Is involved in ESR1-mediated
CC transcription; required for ESR1 binding to the NKX2-1 promoter in
CC breast cancer cells; binds to the RPRM promoter and is required for the
CC estrogen-induced repression of RPRM. Involved in regulation of
CC apoptosis by inhibiting the expression of BCL2. Involved in cell cycle
CC regulation by activating expression of CDKN1B, alone or in conjunction
CC with BRCA1. Originally described as a transcription activator for a
CC number of liver genes such as AFP, albumin, tyrosine aminotransferase,
CC PEPCK, etc. Interacts with the cis-acting regulatory regions of these
CC genes. Involved in glucose homeostasis. {ECO:0000250,
CC ECO:0000269|PubMed:16087863, ECO:0000269|PubMed:16331276,
CC ECO:0000269|PubMed:18358809, ECO:0000269|PubMed:19127412,
CC ECO:0000269|PubMed:19917725}.
CC -!- SUBUNIT: Binds DNA as a monomer (By similarity). Interacts with FOXA2.
CC Interacts with NKX2-1. Interacts with HDAC7. Interacts with the histone
CC H3-H4 heterodimer. Associates with nucleosomes containing histone H2A.
CC Interacts with AR. Interacts with NR0B2 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P55317; P10275: AR; NbExp=4; IntAct=EBI-3918034, EBI-608057;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089,
CC ECO:0000269|PubMed:15987773, ECO:0000269|PubMed:16331276}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P55317-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P55317-2; Sequence=VSP_055094;
CC -!- TISSUE SPECIFICITY: Highly expressed in prostate and ESR1-positive
CC breast tumors. Overexpressed in esophageal and lung adenocarcinomas.
CC {ECO:0000269|PubMed:12234996, ECO:0000269|PubMed:15987773,
CC ECO:0000269|PubMed:16331276}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Hepatocyte nuclear factors entry;
CC URL="https://en.wikipedia.org/wiki/Hepatocyte_nuclear_factors";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/FOXA1ID44403ch14q21.html";
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DR EMBL; U39840; AAB06493.1; -; mRNA.
DR EMBL; AF176112; AAD51979.1; -; Genomic_DNA.
DR EMBL; AF176111; AAD51979.1; JOINED; Genomic_DNA.
DR EMBL; AF303743; AAG40847.1; -; Genomic_DNA.
DR EMBL; AF303742; AAG40847.1; JOINED; Genomic_DNA.
DR EMBL; AK313785; BAG36523.1; -; mRNA.
DR EMBL; AK316360; BAH14731.1; -; mRNA.
DR EMBL; AL121790; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471078; EAW65844.1; -; Genomic_DNA.
DR EMBL; BC033890; AAH33890.1; -; mRNA.
DR CCDS; CCDS9665.1; -. [P55317-1]
DR PIR; S70357; S70357.
DR RefSeq; NP_004487.2; NM_004496.3. [P55317-1]
DR RefSeq; XP_016876735.1; XM_017021246.1. [P55317-2]
DR AlphaFoldDB; P55317; -.
DR SMR; P55317; -.
DR BioGRID; 109411; 297.
DR DIP; DIP-57138N; -.
DR ELM; P55317; -.
DR IntAct; P55317; 43.
DR MINT; P55317; -.
DR STRING; 9606.ENSP00000250448; -.
DR GlyGen; P55317; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P55317; -.
DR PhosphoSitePlus; P55317; -.
DR SwissPalm; P55317; -.
DR BioMuta; FOXA1; -.
DR DMDM; 296434509; -.
DR EPD; P55317; -.
DR jPOST; P55317; -.
DR MassIVE; P55317; -.
DR MaxQB; P55317; -.
DR PaxDb; P55317; -.
DR PeptideAtlas; P55317; -.
DR PRIDE; P55317; -.
DR ProteomicsDB; 56845; -. [P55317-1]
DR ProteomicsDB; 7076; -.
DR Antibodypedia; 23304; 1476 antibodies from 43 providers.
DR DNASU; 3169; -.
DR Ensembl; ENST00000250448.5; ENSP00000250448.3; ENSG00000129514.8. [P55317-1]
DR GeneID; 3169; -.
DR KEGG; hsa:3169; -.
DR MANE-Select; ENST00000250448.5; ENSP00000250448.3; NM_004496.5; NP_004487.2.
DR UCSC; uc001wuf.5; human. [P55317-1]
DR CTD; 3169; -.
DR DisGeNET; 3169; -.
DR GeneCards; FOXA1; -.
DR HGNC; HGNC:5021; FOXA1.
DR HPA; ENSG00000129514; Tissue enhanced (prostate, stomach).
DR MIM; 602294; gene.
DR neXtProt; NX_P55317; -.
DR OpenTargets; ENSG00000129514; -.
DR PharmGKB; PA201090; -.
DR VEuPathDB; HostDB:ENSG00000129514; -.
DR eggNOG; KOG3563; Eukaryota.
DR GeneTree; ENSGT00940000162043; -.
DR HOGENOM; CLU_027910_4_1_1; -.
DR InParanoid; P55317; -.
DR OMA; FKCEKQA; -.
DR OrthoDB; 1181467at2759; -.
DR PhylomeDB; P55317; -.
DR TreeFam; TF316127; -.
DR PathwayCommons; P55317; -.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR SignaLink; P55317; -.
DR SIGNOR; P55317; -.
DR BioGRID-ORCS; 3169; 60 hits in 1107 CRISPR screens.
DR ChiTaRS; FOXA1; human.
DR GeneWiki; FOXA1; -.
DR GenomeRNAi; 3169; -.
DR Pharos; P55317; Tbio.
DR PRO; PR:P55317; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P55317; protein.
DR Bgee; ENSG00000129514; Expressed in endometrium epithelium and 105 other tissues.
DR ExpressionAtlas; P55317; baseline and differential.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0005902; C:microvillus; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISS:BHF-UCL.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0019904; F:protein domain specific binding; IEA:InterPro.
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:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0061144; P:alveolar secondary septum development; IEA:Ensembl.
DR GO; GO:0048646; P:anatomical structure formation involved in morphogenesis; IEA:Ensembl.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR GO; GO:0071542; P:dopaminergic neuron differentiation; TAS:ParkinsonsUK-UCL.
DR GO; GO:0021904; P:dorsal/ventral neural tube patterning; IEA:Ensembl.
DR GO; GO:0060743; P:epithelial cell maturation involved in prostate gland development; IEA:Ensembl.
DR GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IEA:Ensembl.
DR GO; GO:0060738; P:epithelial-mesenchymal signaling involved in prostate gland development; IEA:Ensembl.
DR GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR GO; GO:0042445; P:hormone metabolic process; IEA:Ensembl.
DR GO; GO:0060487; P:lung epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; IMP:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0048665; P:neuron fate specification; IEA:Ensembl.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:2000049; P:positive regulation of cell-cell adhesion mediated by cadherin; IC:BHF-UCL.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IMP:UniProtKB.
DR GO; GO:1904340; P:positive regulation of dopaminergic neuron differentiation; IEA:Ensembl.
DR GO; GO:0033148; P:positive regulation of intracellular estrogen receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0060740; P:prostate gland epithelium morphogenesis; IEA:Ensembl.
DR GO; GO:0060741; P:prostate gland stromal morphogenesis; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:1902691; P:respiratory basal cell differentiation; IEA:Ensembl.
DR GO; GO:0032355; P:response to estradiol; IDA:UniProtKB.
DR GO; GO:0060528; P:secretory columnal luminar epithelial cell differentiation involved in prostate glandular acinus development; IEA:Ensembl.
DR GO; GO:0007224; P:smoothened signaling pathway; IEA:Ensembl.
DR CDD; cd00059; FH; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR013638; Fork-head_N.
DR InterPro; IPR001766; Fork_head_dom.
DR InterPro; IPR018533; Forkhead_box_C.
DR InterPro; IPR018122; TF_fork_head_CS_1.
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; PF08430; Forkhead_N; 1.
DR Pfam; PF09354; HNF_C; 1.
DR PRINTS; PR00053; FORKHEAD.
DR SMART; SM00339; FH; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS00657; FORK_HEAD_1; 1.
DR PROSITE; PS00658; FORK_HEAD_2; 1.
DR PROSITE; PS50039; FORK_HEAD_3; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Chromatin regulator;
KW Developmental protein; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..472
FT /note="Hepatocyte nuclear factor 3-alpha"
FT /id="PRO_0000091792"
FT DNA_BIND 169..260
FT /note="Fork-head"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT REGION 269..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..33
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055094"
FT VARIANT 72
FT /note="G -> A"
FT /evidence="ECO:0000269|PubMed:10899756,
FT ECO:0000269|PubMed:8652662"
FT /id="VAR_015183"
FT VARIANT 83
FT /note="A -> T (in dbSNP:rs7144658)"
FT /evidence="ECO:0000269|PubMed:10899756"
FT /id="VAR_013457"
FT VARIANT 87
FT /note="G -> E (in dbSNP:rs35220193)"
FT /id="VAR_055835"
FT VARIANT 124
FT /note="M -> MM"
FT /evidence="ECO:0000269|PubMed:10899756,
FT ECO:0000269|PubMed:8652662"
FT /id="VAR_015184"
FT VARIANT 185
FT /note="Q -> R"
FT /evidence="ECO:0000269|PubMed:10899756,
FT ECO:0000269|PubMed:8652662"
FT /id="VAR_015185"
FT VARIANT 448
FT /note="S -> N (in dbSNP:rs33984772)"
FT /evidence="ECO:0000269|PubMed:10899756"
FT /id="VAR_013458"
SQ SEQUENCE 472 AA; 49148 MW; B2489523459EEB4C CRC64;
MLGTVKMEGH ETSDWNSYYA DTQEAYSSVP VSNMNSGLGS MNSMNTYMTM NTMTTSGNMT
PASFNMSYAN PGLGAGLSPG AVAGMPGGSA GAMNSMTAAG VTAMGTALSP SGMGAMGAQQ
AASMNGLGPY AAAMNPCMSP MAYAPSNLGR SRAGGGGDAK TFKRSYPHAK PPYSYISLIT
MAIQQAPSKM LTLSEIYQWI MDLFPYYRQN QQRWQNSIRH SLSFNDCFVK VARSPDKPGK
GSYWTLHPDS GNMFENGCYL RRQKRFKCEK QPGAGGGGGS GSGGSGAKGG PESRKDPSGA
SNPSADSPLH RGVHGKTGQL EGAPAPGPAA SPQTLDHSGA TATGGASELK TPASSTAPPI
SSGPGALASV PASHPAHGLA PHESQLHLKG DPHYSFNHPF SINNLMSSSE QQHKLDFKAY
EQALQYSPYG STLPASLPLG SASVTTRSPI EPSALEPAYY QGVYSRPVLN TS
