FOXA2_MOUSE
ID FOXA2_MOUSE Reviewed; 459 AA.
AC P35583; A2AR89; Q60602;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Hepatocyte nuclear factor 3-beta;
DE Short=HNF-3-beta;
DE Short=HNF-3B;
DE AltName: Full=Forkhead box protein A2;
GN Name=Foxa2; Synonyms=Hnf3b, Tcf-3b, Tcf3b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8034310; DOI=10.1006/geno.1994.1191;
RA Kaestner K., Hiemisch H., Luckow B., Schuetz G.;
RT "The HNF-3 gene family of transcription factors in mice: gene structure,
RT cDNA sequence, and mRNA distribution.";
RL Genomics 20:377-385(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8375339; DOI=10.1242/dev.118.1.47;
RA Sasaki H., Hogan B.L.;
RT "Differential expression of multiple fork head related genes during
RT gastrulation and axial pattern formation in the mouse embryo.";
RL Development 118:47-59(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 201-459.
RX PubMed=8306889; DOI=10.1242/dev.119.4.1301;
RA Ang S.-L., Wierda A., Wong D., Stevens K.A., Cascio S., Rossant J.,
RA Zaret K.S.;
RT "The formation and maintenance of the definitive endoderm lineage in the
RT mouse: involvement of HNF3/forkhead proteins.";
RL Development 119:1301-1315(1993).
RN [5]
RP DISRUPTION PHENOTYPE, AND FUNCTION IN NOTOCHORD FORMATION.
RX PubMed=8069909; DOI=10.1016/0092-8674(94)90522-3;
RA Ang S.L., Rossant J.;
RT "HNF-3 beta is essential for node and notochord formation in mouse
RT development.";
RL Cell 78:561-574(1994).
RN [6]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=11445544; DOI=10.1101/gad.901601;
RA Sund N.J., Vatamaniuk M.Z., Casey M., Ang S.L., Magnuson M.A.,
RA Stoffers D.A., Matschinsky F.M., Kaestner K.H.;
RT "Tissue-specific deletion of Foxa2 in pancreatic beta cells results in
RT hyperinsulinemic hypoglycemia.";
RL Genes Dev. 15:1706-1715(2001).
RN [7]
RP FUNCTION IN REGULATION OF GLUCOSE HOMEOSTASIS.
RX PubMed=11875061; DOI=10.1074/jbc.m111037200;
RA Wang H., Gauthier B.R., Hagenfeldt-Johansson K.A., Iezzi M., Wollheim C.B.;
RT "Foxa2 (HNF3beta) controls multiple genes implicated in metabolism-
RT secretion coupling of glucose-induced insulin release.";
RL J. Biol. Chem. 277:17564-17570(2002).
RN [8]
RP INTERACTION WITH AKT1.
RX PubMed=14500912; DOI=10.1073/pnas.1931483100;
RA Wolfrum C., Besser D., Luca E., Stoffel M.;
RT "Insulin regulates the activity of forkhead transcription factor Hnf-
RT 3beta/Foxa-2 by Akt-mediated phosphorylation and nuclear/cytosolic
RT localization.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11624-11629(2003).
RN [9]
RP PHOSPHORYLATION AT THR-156, SUBCELLULAR LOCATION, AND FUNCTION IN
RP REGULATION OF LIPID METABOLISM AND KETOGENESIS.
RX PubMed=15616563; DOI=10.1038/nature03047;
RA Wolfrum C., Asilmaz E., Luca E., Friedman J.M., Stoffel M.;
RT "Foxa2 regulates lipid metabolism and ketogenesis in the liver during
RT fasting and in diabetes.";
RL Nature 432:1027-1032(2004).
RN [10]
RP FUNCTION IN LUNG DEVELOPMENT.
RX PubMed=15668254; DOI=10.1074/jbc.m414122200;
RA Wan H., Dingle S., Xu Y., Besnard V., Kaestner K.H., Ang S.L., Wert S.,
RA Stahlman M.T., Whitsett J.A.;
RT "Compensatory roles of Foxa1 and Foxa2 during lung morphogenesis.";
RL J. Biol. Chem. 280:13809-13816(2005).
RN [11]
RP FUNCTION IN LIVER DEVELOPMENT.
RX PubMed=15959514; DOI=10.1038/nature03649;
RA Lee C.S., Friedman J.R., Fulmer J.T., Kaestner K.H.;
RT "The initiation of liver development is dependent on Foxa transcription
RT factors.";
RL Nature 435:944-947(2005).
RN [12]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16740652; DOI=10.1210/me.2006-0008;
RA Yu X., Suzuki K., Wang Y., Gupta A., Jin R., Orgebin-Crist M.C.,
RA Matusik R.;
RT "The role of forkhead box A2 to restrict androgen-regulated gene expression
RT of lipocalin 5 in the mouse epididymis.";
RL Mol. Endocrinol. 20:2418-2431(2006).
RN [13]
RP FUNCTION IN NEURON DEVELOPMENT.
RX PubMed=17596284; DOI=10.1242/dev.000141;
RA Ferri A.L., Lin W., Mavromatakis Y.E., Wang J.C., Sasaki H., Whitsett J.A.,
RA Ang S.L.;
RT "Foxa1 and Foxa2 regulate multiple phases of midbrain dopaminergic neuron
RT development in a dosage-dependent manner.";
RL Development 134:2761-2769(2007).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [15]
RP FUNCTION.
RX PubMed=18336786; DOI=10.1016/j.bbrc.2008.02.158;
RA van der Sluis M., Vincent A., Bouma J., Korteland-Van Male A.,
RA van Goudoever J.B., Renes I.B., Van Seuningen I.;
RT "Forkhead box transcription factors Foxa1 and Foxa2 are important
RT regulators of Muc2 mucin expression in intestinal epithelial cells.";
RL Biochem. Biophys. Res. Commun. 369:1108-1113(2008).
RN [16]
RP FUNCTION IN PANCREAS DEVELOPMENT.
RX PubMed=19141476; DOI=10.1101/gad.1752608;
RA Gao N., LeLay J., Vatamaniuk M.Z., Rieck S., Friedman J.R., Kaestner K.H.;
RT "Dynamic regulation of Pdx1 enhancers by Foxa1 and Foxa2 is essential for
RT pancreas development.";
RL Genes Dev. 22:3435-3448(2008).
RN [17]
RP FUNCTION IN BILE DUCT DEVELOPMENT.
RX PubMed=19436110; DOI=10.1172/jci38201;
RA Li Z., White P., Tuteja G., Rubins N., Sackett S., Kaestner K.H.;
RT "Foxa1 and Foxa2 regulate bile duct development in mice.";
RL J. Clin. Invest. 119:1537-1545(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-302, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Lung, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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). In embryonic
CC development is required for notochord formation. Involved in the
CC development of multiple endoderm-derived organ systems such as the
CC liver, pancreas and lungs; Foxa1 and Foxa2 seem to have at least in
CC part redundant roles. FOXA1 and FOXA2 are essential for hepatic
CC specification. FOXA1 and FOXA2 are required for morphogenesis and cell
CC differentiation during formation of the lung. FOXA1 and FOXA2 are
CC involved in bile duct formation; they positively regulate the binding
CC glucocorticoid receptor/NR3C1 to the IL6 promoter. FOXA1 and FOXA2
CC regulate multiple phases of midbrain dopaminergic neuron development;
CC they regulate expression of NEUROG2 at the beginning of mDA
CC neurogenesis and of NR4A2 and EN1 in immature mDA neurons. Modulates
CC the transcriptional activity of nuclear hormone receptors; inhibits AR-
CC mediated transcription from the LCN5 promoter. Binds to fibrinogen beta
CC promoter and is involved in IL6-induced fibrinogen beta transcriptional
CC activation. 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; regulates the expression of
CC genes important for glucose sensing in pancreatic beta-cells and
CC glucose homeostasis. In pancreatic beta cells activates transcription
CC of potassium channel subunits KCNJ11 and ABCC8. Involved in regulation
CC of fat metabolism; activates transcriptional programs of lipid
CC metabolism and ketogenesis at low insulin state. Involved in
CC transcriptional regulation of MUC2 in the intestine. {ECO:0000250,
CC ECO:0000269|PubMed:11445544, ECO:0000269|PubMed:11875061,
CC ECO:0000269|PubMed:15616563, ECO:0000269|PubMed:15668254,
CC ECO:0000269|PubMed:15959514, ECO:0000269|PubMed:16740652,
CC ECO:0000269|PubMed:17596284, ECO:0000269|PubMed:18336786,
CC ECO:0000269|PubMed:19141476, ECO:0000269|PubMed:19436110,
CC ECO:0000269|PubMed:8069909}.
CC -!- SUBUNIT: Binds DNA as a monomer. Binds TLE1. Interacts with FOXA1 and
CC FOXA3. Interacts with PRKDC (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P35583; Q61221: Hif1a; NbExp=5; IntAct=EBI-2893341, EBI-298954;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089,
CC ECO:0000269|PubMed:15616563}. Cytoplasm {ECO:0000269|PubMed:15616563}.
CC Note=Shuttles between the nucleus and cytoplasm in a CRM1-dependent
CC manner; in response to insulin signaling via AKT1 is exported from the
CC nucleus.
CC -!- TISSUE SPECIFICITY: Restricted mainly to endoderm-derived tissues
CC (lung, liver, stomach, and small intestine). Expressed in epididymis
CC with region-specific expression pattern: no expression is observed in
CC initial segment, low expression in proximal caput, gradiently higher
CC levels of expression in middle and distal caput and highest level in
CC corpus and cauda (at protein level). {ECO:0000269|PubMed:16740652}.
CC -!- DEVELOPMENTAL STAGE: Most abundant in midgestation embryos (day 9.5).
CC -!- PTM: Phosphorylation on Thr-156 abolishes binding to target promoters
CC and subsequent transcription activation upon insulin stimulation.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Embryonic lethal; absence of organized node and
CC notochord formation, which leads to secondary defects in dorsal-ventral
CC patterning of the neural tube. Mice deficient for Fox1a and deficient
CC for Foxa2 in the endoderm from 8.5 dpc onwards do not show hepatic bud
CC formation. Mice deficient for Fox1a and deficient for Foxa2 in the
CC midbrain from 10.5 dpc onwards show almost complete loss of mDA
CC neurons. Mice deficient for Fox1a and deficient for Foxa2 in the
CC embryonic liver show hyperplasia of the biliary tree due to at least in
CC part activation of IL-6 expression, a proliferative signal for
CC cholangiocytes. Mice deficient for Fox2a in pancreatic beta cell show
CC hypoglycemia and disorganized islets arrangements.
CC {ECO:0000269|PubMed:11445544, ECO:0000269|PubMed:8069909}.
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; X74937; CAA52891.1; -; mRNA.
DR EMBL; L10409; AAA03161.1; -; mRNA.
DR EMBL; AL845297; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U04197; AAA03606.1; -; mRNA.
DR CCDS; CCDS16836.1; -.
DR PIR; B54258; B54258.
DR RefSeq; NP_001277994.1; NM_001291065.1.
DR RefSeq; NP_034576.2; NM_010446.3.
DR AlphaFoldDB; P35583; -.
DR SMR; P35583; -.
DR IntAct; P35583; 7.
DR STRING; 10090.ENSMUSP00000045918; -.
DR iPTMnet; P35583; -.
DR PhosphoSitePlus; P35583; -.
DR MaxQB; P35583; -.
DR PaxDb; P35583; -.
DR PRIDE; P35583; -.
DR ProteomicsDB; 271591; -.
DR Antibodypedia; 3772; 871 antibodies from 47 providers.
DR DNASU; 15376; -.
DR Ensembl; ENSMUST00000047315; ENSMUSP00000045918; ENSMUSG00000037025.
DR GeneID; 15376; -.
DR KEGG; mmu:15376; -.
DR UCSC; uc008mtb.2; mouse.
DR CTD; 3170; -.
DR MGI; MGI:1347476; Foxa2.
DR VEuPathDB; HostDB:ENSMUSG00000037025; -.
DR eggNOG; KOG3563; Eukaryota.
DR GeneTree; ENSGT00940000155999; -.
DR HOGENOM; CLU_027910_4_1_1; -.
DR InParanoid; P35583; -.
DR OrthoDB; 1181467at2759; -.
DR TreeFam; TF316127; -.
DR BioGRID-ORCS; 15376; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Foxa2; mouse.
DR PRO; PR:P35583; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P35583; protein.
DR Bgee; ENSMUSG00000037025; Expressed in digestive tract diverticulum and 147 other tissues.
DR ExpressionAtlas; P35583; baseline and differential.
DR Genevisible; P35583; MM.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; ISO:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; IGI:MGI.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
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; IDA:MGI.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; TAS:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0046332; F:SMAD binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI.
DR GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
DR GO; GO:0048646; P:anatomical structure formation involved in morphogenesis; IGI:MGI.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IGI:MGI.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IGI:MGI.
DR GO; GO:0048468; P:cell development; IMP:MGI.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0021533; P:cell differentiation in hindbrain; IMP:MGI.
DR GO; GO:0001708; P:cell fate specification; IDA:MGI.
DR GO; GO:0071276; P:cellular response to cadmium ion; IDA:MGI.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0061448; P:connective tissue development; IGI:MGI.
DR GO; GO:0071542; P:dopaminergic neuron differentiation; IMP:MGI.
DR GO; GO:0021904; P:dorsal/ventral neural tube patterning; IDA:MGI.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IGI:MGI.
DR GO; GO:0001705; P:ectoderm formation; IGI:MGI.
DR GO; GO:0031018; P:endocrine pancreas development; IMP:MGI.
DR GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IGI:MGI.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0030324; P:lung development; IGI:MGI.
DR GO; GO:0060487; P:lung epithelial cell differentiation; IGI:MGI.
DR GO; GO:0048382; P:mesendoderm development; IMP:MGI.
DR GO; GO:2000971; P:negative regulation of detection of glucose; IDA:BHF-UCL.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISO:MGI.
DR GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; ISO:MGI.
DR GO; GO:0033132; P:negative regulation of glucokinase activity; IDA:BHF-UCL.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IGI:MGI.
DR GO; GO:0061987; P:negative regulation of transcription from RNA polymerase II promoter by glucose; IDA:BHF-UCL.
DR GO; GO:0030182; P:neuron differentiation; IMP:MGI.
DR GO; GO:0048665; P:neuron fate specification; IMP:MGI.
DR GO; GO:0007219; P:Notch signaling pathway; IDA:MGI.
DR GO; GO:0007389; P:pattern specification process; IGI:MGI.
DR GO; GO:1904340; P:positive regulation of dopaminergic neuron differentiation; IMP:MGI.
DR GO; GO:0040019; P:positive regulation of embryonic development; IMP:UniProtKB.
DR GO; GO:2000543; P:positive regulation of gastrulation; IMP:UniProtKB.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IGI:MGI.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IGI:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; IMP:UniProtKB.
DR GO; GO:0000432; P:positive regulation of transcription from RNA polymerase II promoter by glucose; IDA:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0090009; P:primitive streak formation; IMP:UniProtKB.
DR GO; GO:0030193; P:regulation of blood coagulation; ISO:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IGI:MGI.
DR GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; IDA:BHF-UCL.
DR GO; GO:0019216; P:regulation of lipid metabolic process; IDA:MGI.
DR GO; GO:0019218; P:regulation of steroid metabolic process; IDA:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0070741; P:response to interleukin-6; TAS:UniProtKB.
DR GO; GO:0023019; P:signal transduction involved in regulation of gene expression; IDA:MGI.
DR GO; GO:0007224; P:smoothened signaling pathway; IGI:MGI.
DR GO; GO:0032525; P:somite rostral/caudal axis specification; IMP:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:MGI.
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; Chromatin regulator; Cytoplasm; Developmental protein;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..459
FT /note="Hepatocyte nuclear factor 3-beta"
FT /id="PRO_0000091796"
FT DNA_BIND 159..252
FT /note="Fork-head"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT REGION 14..93
FT /note="Transactivation domain 1"
FT /evidence="ECO:0000250"
FT REGION 268..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..459
FT /note="Transactivation domain 2"
FT /evidence="ECO:0000250"
FT MOTIF 106..113
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 275..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 156
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:15616563"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32182"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32182"
FT MOD_RES 302
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y261"
FT MOD_RES 307
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32182"
FT MOD_RES 308
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32182"
FT MOD_RES 310
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y261"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32182"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P32182"
FT CONFLICT 10
FT /note="H -> L (in Ref. 1; CAA52891)"
FT /evidence="ECO:0000305"
FT CONFLICT 434
FT /note="G -> S (in Ref. 4; AAA03606)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 459 AA; 48498 MW; 2F20F15AB372F557 CRC64;
MLGAVKMEGH EPSDWSSYYA EPEGYSSVSN MNAGLGMNGM NTYMSMSAAA MGGGSGNMSA
GSMNMSSYVG AGMSPSLAGM SPGAGAMAGM SGSAGAAGVA GMGPHLSPSL SPLGGQAAGA
MGGLAPYANM NSMSPMYGQA GLSRARDPKT YRRSYTHAKP PYSYISLITM AIQQSPNKML
TLSEIYQWIM DLFPFYRQNQ QRWQNSIRHS LSFNDCFLKV PRSPDKPGKG SFWTLHPDSG
NMFENGCYLR RQKRFKCEKQ LALKEAAGAA SSGGKKTAPG SQASQAQLGE AAGSASETPA
GTESPHSSAS PCQEHKRGGL SELKGAPASA LSPPEPAPSP GQQQQAAAHL LGPPHHPGLP
PEAHLKPEHH YAFNHPFSIN NLMSSEQQHH HSHHHHQPHK MDLKAYEQVM HYPGGYGSPM
PGSLAMGPVT NKAGLDASPL AADTSYYQGV YSRPIMNSS
