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FOXO6_HUMAN
ID   FOXO6_HUMAN             Reviewed;         492 AA.
AC   A8MYZ6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Forkhead box protein O6;
GN   Name=FOXO6;
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 [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
CC   -!- FUNCTION: Transcriptional activator. {ECO:0000250}.
CC   -!- INTERACTION:
CC       A8MYZ6; P41235: HNF4A; NbExp=2; IntAct=EBI-8531039, EBI-1049011;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC       {ECO:0000255|PROSITE-ProRule:PRU00089}. Note=When phosphorylated,
CC       translocated from nucleus to cytoplasm. High nuclear localization after
CC       stimulation with growth factors (By similarity). {ECO:0000250}.
CC   -!- PTM: Phosphorylation of Ser-184 is be important in regulating the
CC       transacriptional activity. {ECO:0000250}.
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DR   EMBL; AC093151; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A8MYZ6; -.
DR   SMR; A8MYZ6; -.
DR   IntAct; A8MYZ6; 14.
DR   MINT; A8MYZ6; -.
DR   STRING; 9606.ENSP00000361672; -.
DR   iPTMnet; A8MYZ6; -.
DR   PhosphoSitePlus; A8MYZ6; -.
DR   BioMuta; FOXO6; -.
DR   jPOST; A8MYZ6; -.
DR   MassIVE; A8MYZ6; -.
DR   MaxQB; A8MYZ6; -.
DR   PaxDb; A8MYZ6; -.
DR   PeptideAtlas; A8MYZ6; -.
DR   PRIDE; A8MYZ6; -.
DR   ProteomicsDB; 2440; -.
DR   Antibodypedia; 46860; 63 antibodies from 19 providers.
DR   Ensembl; ENST00000641094.2; ENSP00000493184.1; ENSG00000204060.8.
DR   UCSC; uc057fie.1; human.
DR   GeneCards; FOXO6; -.
DR   HGNC; HGNC:24814; FOXO6.
DR   HPA; ENSG00000204060; Not detected.
DR   MIM; 611457; gene.
DR   neXtProt; NX_A8MYZ6; -.
DR   OpenTargets; ENSG00000204060; -.
DR   PharmGKB; PA162388893; -.
DR   VEuPathDB; HostDB:ENSG00000204060; -.
DR   eggNOG; KOG2294; Eukaryota.
DR   GeneTree; ENSGT00940000161401; -.
DR   HOGENOM; CLU_023456_2_0_1; -.
DR   InParanoid; A8MYZ6; -.
DR   OMA; QPAMSLM; -.
DR   PhylomeDB; A8MYZ6; -.
DR   PathwayCommons; A8MYZ6; -.
DR   Reactome; R-HSA-198693; AKT phosphorylates targets in the nucleus.
DR   Reactome; R-HSA-5674400; Constitutive Signaling by AKT1 E17K in Cancer.
DR   Reactome; R-HSA-9614399; Regulation of localization of FOXO transcription factors.
DR   Reactome; R-HSA-9615017; FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes.
DR   SignaLink; A8MYZ6; -.
DR   SIGNOR; A8MYZ6; -.
DR   ChiTaRS; FOXO6; human.
DR   Pharos; A8MYZ6; Tbio.
DR   PRO; PR:A8MYZ6; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; A8MYZ6; protein.
DR   Bgee; ENSG00000204060; Expressed in cortical plate and 89 other tissues.
DR   Genevisible; A8MYZ6; HS.
DR   GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR   GO; GO:0005737; C:cytoplasm; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0005634; C:nucleus; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0007613; P:memory; IEA:Ensembl.
DR   GO; GO:0060999; P:positive regulation of dendritic spine development; ISS:ParkinsonsUK-UCL.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:ParkinsonsUK-UCL.
DR   CDD; cd00059; FH; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR001766; Fork_head_dom.
DR   InterPro; IPR032067; FOXO-TAD.
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; PF16676; FOXO-TAD; 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.
PE   1: Evidence at protein level;
KW   Activator; Cytoplasm; DNA-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..492
FT                   /note="Forkhead box protein O6"
FT                   /id="PRO_0000317413"
FT   DNA_BIND        88..182
FT                   /note="Fork-head"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT   REGION          1..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          163..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          315..338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          466..492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        470..492
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         184
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q70KY4"
SQ   SEQUENCE   492 AA;  50595 MW;  85061867EDA1D656 CRC64;
     MAAKLRAHQV DVDPDFAPQS RPRSCTWPLP QPDLAGDEDG ALGAGVAEGA EDCGPERRAT
     APAMAPAPPL GAEVGPLRKA KSSRRNAWGN LSYADLITKA IESAPDKRLT LSQIYDWMVR
     YVPYFKDKGD SNSSAGWKNS IRHNLSLHTR FIRVQNEGTG KSSWWMLNPE GGKTGKTPRR
     RAVSMDNGAK FLRIKGKASK KKQLQAPERS PDDSSPSAPA PGPVPAAAKW AASPASHASD
     DYEAWADFRG GGRPLLGEAA ELEDDEALEA LAPSSPLMYP SPASALSPAL GSRCPGELPR
     LAELGGPLGL HGGGGAGLPE GLLDGAQDAY GPRPAPRPGP VLGAPGELAL AGAAAAYPGK
     GAAPYAPPAP SRSALAHPIS LMTLPGEAGA AGLAPPGHAA AFGGPPGGLL LDALPGPYAA
     AAAGPLGAAP DRFPADLDLD MFSGSLECDV ESIILNDFMD SDEMDFNFDS ALPPPPPGLA
     GAPPPNQSWV PG
 
 
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