FOXF2_HUMAN
ID FOXF2_HUMAN Reviewed; 444 AA.
AC Q12947; Q5TGJ1; Q9UQ85;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Forkhead box protein F2;
DE AltName: Full=Forkhead-related activator 2;
DE Short=FREAC-2;
DE AltName: Full=Forkhead-related protein FKHL6;
DE AltName: Full=Forkhead-related transcription factor 2;
GN Name=FOXF2; Synonyms=FKHL6, FREAC2;
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 [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RX PubMed=9799607; DOI=10.1006/geno.1998.5451;
RA Blixt A., Mahlapuu M., Bjursell C., Darnfors C., Johannesson T.,
RA Enerbaeck S., Carlsson P.;
RT "The two-exon gene of the human forkhead transcription factor FREAC-2
RT (FKHL6) is located at 6p25.3.";
RL Genomics 53:387-390(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 37-444, AND TISSUE SPECIFICITY.
RC TISSUE=Lung;
RX PubMed=8626802; DOI=10.1074/jbc.271.8.4482;
RA Hellqvist M., Mahlapuu M., Samuelsson L., Enerbaeck S., Carlsson P.;
RT "Differential activation of lung-specific genes by two forkhead proteins,
RT FREAC-1 and FREAC-2.";
RL J. Biol. Chem. 271:4482-4490(1996).
RN [5]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7957066; DOI=10.1002/j.1460-2075.1994.tb06827.x;
RA Pierrou S., Hellqvist M., Samuelsson L., Enerbaeck S., Carlsson P.;
RT "Cloning and characterization of seven human forkhead proteins: binding
RT site specificity and DNA bending.";
RL EMBO J. 13:5002-5012(1994).
RN [6]
RP DOMAIN, AND INTERACTION WITH TBP AND TFIIB.
RX PubMed=9722567; DOI=10.1074/jbc.273.36.23335;
RA Hellqvist M., Mahlapuu M., Blixt A., Enerbaeck S., Carlsson P.;
RT "The human forkhead protein FREAC-2 contains two functionally redundant
RT activation domains and interacts with TBP and TFIIB.";
RL J. Biol. Chem. 273:23335-23343(1998).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=29374064; DOI=10.1158/0008-5472.can-17-2403;
RA Higashimori A., Dong Y., Zhang Y., Kang W., Nakatsu G., Ng S.S.M.,
RA Arakawa T., Sung J.J.Y., Chan F.K.L., Yu J.;
RT "Forkhead Box F2 Suppresses Gastric Cancer through a Novel FOXF2-IRF2BPL-
RT beta-Catenin Signaling Axis.";
RL Cancer Res. 78:1643-1656(2018).
CC -!- FUNCTION: Probable transcription activator for a number of lung-
CC specific genes (PubMed:8626802). Mediates up-regulation of the E3
CC ligase IRF2BPL and drives ubiquitination and degradation of CTNNB1
CC (PubMed:29374064). {ECO:0000269|PubMed:29374064,
CC ECO:0000269|PubMed:8626802}.
CC -!- SUBUNIT: Interacts with the transcription factors TBP and TFIIB.
CC {ECO:0000269|PubMed:9722567}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29374064,
CC ECO:0000269|PubMed:9799607}.
CC -!- TISSUE SPECIFICITY: Lung and placenta (PubMed:8626802). Predominantly
CC expressed in gastrointestinal tract including stomach
CC (PubMed:29374064). {ECO:0000269|PubMed:29374064,
CC ECO:0000269|PubMed:8626802}.
CC -!- DOMAIN: Two activation domains, AD1 and AD2, C-terminal of (and
CC distinct from) the forkhead domains are necessary for transcriptional
CC activation. {ECO:0000269|PubMed:9722567}.
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; AF084939; AAD19875.1; -; Genomic_DNA.
DR EMBL; AF084938; AAD19875.1; JOINED; Genomic_DNA.
DR EMBL; AL034346; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471087; EAW55072.1; -; Genomic_DNA.
DR EMBL; U13220; AAC32226.1; -; mRNA.
DR CCDS; CCDS4472.1; -.
DR PIR; S51625; S51625.
DR PIR; T09474; T09474.
DR RefSeq; NP_001443.1; NM_001452.1.
DR AlphaFoldDB; Q12947; -.
DR SMR; Q12947; -.
DR BioGRID; 108584; 54.
DR IntAct; Q12947; 14.
DR MINT; Q12947; -.
DR STRING; 9606.ENSP00000259806; -.
DR iPTMnet; Q12947; -.
DR PhosphoSitePlus; Q12947; -.
DR BioMuta; FOXF2; -.
DR DMDM; 8247925; -.
DR jPOST; Q12947; -.
DR MassIVE; Q12947; -.
DR MaxQB; Q12947; -.
DR PaxDb; Q12947; -.
DR PeptideAtlas; Q12947; -.
DR PRIDE; Q12947; -.
DR ProteomicsDB; 59042; -.
DR Antibodypedia; 9203; 241 antibodies from 23 providers.
DR DNASU; 2295; -.
DR Ensembl; ENST00000645481.2; ENSP00000496415.1; ENSG00000137273.6.
DR GeneID; 2295; -.
DR KEGG; hsa:2295; -.
DR MANE-Select; ENST00000645481.2; ENSP00000496415.1; NM_001452.2; NP_001443.1.
DR UCSC; uc003mtm.3; human.
DR CTD; 2295; -.
DR DisGeNET; 2295; -.
DR GeneCards; FOXF2; -.
DR HGNC; HGNC:3810; FOXF2.
DR HPA; ENSG00000137273; Tissue enhanced (intestine).
DR MIM; 603250; gene.
DR neXtProt; NX_Q12947; -.
DR OpenTargets; ENSG00000137273; -.
DR PharmGKB; PA28227; -.
DR VEuPathDB; HostDB:ENSG00000137273; -.
DR eggNOG; KOG2294; Eukaryota.
DR GeneTree; ENSGT00940000162527; -.
DR HOGENOM; CLU_039845_1_0_1; -.
DR InParanoid; Q12947; -.
DR OMA; CPVTANG; -.
DR OrthoDB; 1120805at2759; -.
DR PhylomeDB; Q12947; -.
DR TreeFam; TF351598; -.
DR PathwayCommons; Q12947; -.
DR SignaLink; Q12947; -.
DR SIGNOR; Q12947; -.
DR BioGRID-ORCS; 2295; 15 hits in 1097 CRISPR screens.
DR GenomeRNAi; 2295; -.
DR Pharos; Q12947; Tbio.
DR PRO; PR:Q12947; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q12947; protein.
DR Bgee; ENSG00000137273; Expressed in periodontal ligament and 128 other tissues.
DR Genevisible; Q12947; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0140296; F:general transcription initiation factor binding; IPI:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0001093; F:TFIIB-class transcription factor binding; IPI:UniProtKB.
DR GO; GO:0009887; P:animal organ morphogenesis; IBA:GO_Central.
DR GO; GO:0048596; P:embryonic camera-type eye morphogenesis; IEA:Ensembl.
DR GO; GO:0048566; P:embryonic digestive tract development; IEA:Ensembl.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; NAS:UniProtKB.
DR GO; GO:0042249; P:establishment of planar polarity of embryonic epithelium; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
DR GO; GO:0048806; P:genitalia development; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0032434; P:regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
DR GO; GO:1902914; P:regulation of protein polyubiquitination; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0060021; P:roof of mouth development; IMP:UniProtKB.
DR CDD; cd00059; FH; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR001766; Fork_head_dom.
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 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; DNA-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..444
FT /note="Forkhead box protein F2"
FT /id="PRO_0000091834"
FT DNA_BIND 99..190
FT /note="Fork-head"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT REGION 32..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 338..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 444 AA; 45993 MW; 32BDC5F373CFB147 CRC64;
MTTEGGPPPA PLRRACSPVP GALQAALMSP PPAAAAAAAA APETTSSSSS SSSASCASSS
SSSNSASAPS AACKSAGGGG AGAGSGGAKK ASSGLRRPEK PPYSYIALIV MAIQSSPSKR
LTLSEIYQFL QARFPFFRGA YQGWKNSVRH NLSLNECFIK LPKGLGRPGK GHYWTIDPAS
EFMFEEGSFR RRPRGFRRKC QALKPMYHRV VSGLGFGASL LPQGFDFQAP PSAPLGCHSQ
GGYGGLDMMP AGYDAGAGAP SHAHPHHHHH HHVPHMSPNP GSTYMASCPV PAGPGGVGAA
GGGGGGDYGP DSSSSPVPSS PAMASAIECH SPYTSPAAHW SSPGASPYLK QPPALTPSSN
PAASAGLHSS MSSYSLEQSY LHQNAREDLS VGLPRYQHHS TPVCDRKDFV LNFNGISSFH
PSASGSYYHH HHQSVCQDIK PCVM
