FOXM1_MOUSE
ID FOXM1_MOUSE Reviewed; 760 AA.
AC O08696;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Forkhead box protein M1;
DE AltName: Full=Forkhead homolog 16;
DE AltName: Full=Winged-helix transcription factor Trident;
GN Name=Foxm1; Synonyms=Fkh16;
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=Thymus;
RX PubMed=9108152; DOI=10.1093/nar/25.9.1715;
RA Korver W., Roose J., Clevers H.;
RT "The winged-helix transcription factor Trident is expressed in cycling
RT cells.";
RL Nucleic Acids Res. 25:1715-1719(1997).
RN [2]
RP FUNCTION IN DNA REPAIR.
RX PubMed=17101782; DOI=10.1128/mcb.01068-06;
RA Tan Y., Raychaudhuri P., Costa R.H.;
RT "Chk2 mediates stabilization of the FoxM1 transcription factor to stimulate
RT expression of DNA repair genes.";
RL Mol. Cell. Biol. 27:1007-1016(2007).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
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 regulating the expression of cell cycle
CC genes essential for DNA replication and mitosis (By similarity). Plays
CC a role in the control of cell proliferation (By similarity). Also plays
CC a role in DNA break repair, participating in the DNA damage checkpoint
CC response (PubMed:17101782). Promotes transcription of PHB2 (By
CC similarity). {ECO:0000250|UniProtKB:Q08050,
CC ECO:0000269|PubMed:17101782}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089}.
CC -!- TISSUE SPECIFICITY: Expressed in fetal heart, brain, liver, lung,
CC kidney and limb, but only in adult thymus. Appears to be expressed only
CC in adult organs containing proliferating/cycling cells or in response
CC to growth factors.
CC -!- DEVELOPMENTAL STAGE: Expressed at 14 dpc in the embryo.
CC -!- PTM: Phosphorylated in M (mitotic) phase. Phosphorylation by the
CC checkpoint kinase CHEK2 in response to DNA damage increases the FOXM1
CC protein stability probably stimulating the transcription of genes
CC involved in DNA repair. Phosphorylated by CDK1 in late S and G2 phases,
CC creating docking sites for the POLO box domains of PLK1. Subsequently,
CC PLK1 binds and phosphorylates FOXM1, leading to activation of
CC transcriptional activity and subsequent enhanced expression of key
CC mitotic regulators (By similarity). {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA72115.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; Y11245; CAA72115.1; ALT_SEQ; mRNA.
DR AlphaFoldDB; O08696; -.
DR SMR; O08696; -.
DR IntAct; O08696; 2.
DR MINT; O08696; -.
DR STRING; 10090.ENSMUSP00000073041; -.
DR iPTMnet; O08696; -.
DR PhosphoSitePlus; O08696; -.
DR MaxQB; O08696; -.
DR PaxDb; O08696; -.
DR PRIDE; O08696; -.
DR ProteomicsDB; 271797; -.
DR MGI; MGI:1347487; Foxm1.
DR eggNOG; KOG2294; Eukaryota.
DR InParanoid; O08696; -.
DR PhylomeDB; O08696; -.
DR Reactome; R-MMU-156711; Polo-like kinase mediated events.
DR Reactome; R-MMU-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR ChiTaRS; Foxm1; mouse.
DR PRO; PR:O08696; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; O08696; protein.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:MGI.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; IMP:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0001889; P:liver development; IMP:MGI.
DR GO; GO:0032873; P:negative regulation of stress-activated MAPK cascade; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; IMP:UniProtKB.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IMP:MGI.
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; IMP:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0046578; P:regulation of Ras protein signal transduction; ISO:MGI.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0072089; P:stem cell proliferation; IMP:MGI.
DR GO; GO:0001570; P:vasculogenesis; IMP:MGI.
DR CDD; cd00059; FH; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR001766; Fork_head_dom.
DR InterPro; IPR042839; FOXM1.
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 PANTHER; PTHR46878; PTHR46878; 1.
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; Cell cycle; DNA damage; DNA repair; DNA-binding;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..760
FT /note="Forkhead box protein M1"
FT /id="PRO_0000091864"
FT DNA_BIND 233..325
FT /note="Fork-head"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 500..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..552
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..698
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08050"
FT MOD_RES 374
FT /note="Phosphoserine; by CHEK2"
FT /evidence="ECO:0000250|UniProtKB:Q08050"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08050"
FT MOD_RES 608
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q08050"
FT MOD_RES 624
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q08050"
FT MOD_RES 727
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:Q08050"
FT MOD_RES 736
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:Q08050"
FT CROSSLNK 199
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q08050"
FT CROSSLNK 323
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q08050"
FT CROSSLNK 354
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q08050"
FT CROSSLNK 420
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q08050"
FT CROSSLNK 438
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q08050"
SQ SEQUENCE 760 AA; 83694 MW; AA614CB940EE7492 CRC64;
MRTSPRRPLI LKRRRLPLPV QNAPSETSEE EAKRSPAQPE PAPAQASQEV AESSSCKFPA
GIKIINHPTT PNTQVVAIPS NADIQSIITA LTAKGKESGT SGPNRFILIS SGGPSSHPSQ
PQAHSSRDSK RAEVITETLG PKPAAKGVPV PKPPGAPPRQ RQESYAGGEA AGCTLDNSLT
NIQWLGKMSS DGLGPCSVKQ ELEEKENCHL EQNRVKVEEP SGVSTSWQDS VSERPPYSYM
AMIQFAINST ERKRMTLKDI YTWIEDHFPY FKHIAKPGWK NSIRHNLSLH DMFVRETSAN
GKVSFWTIHP SANRHLTLDQ VFKPLEPGSP QSPEHLESQQ KRPNPELHRN VTIKTEIPLG
ARRKMKPLLP RVSSYLEPIQ FPVNQSLVLQ PSVKVPFRLA ASLMSSELAR HSKRVRIAPK
VLLSSEGIAP LPATEPPKEE KPLLGGEGLL PLLPIQSIKE EEMQPEEDIA HLERPIKVES
PPLEEWPSPC ASLKEELSNS WEDSSCSPTP KPKKSYCGLK SPTRCVSEML VTKRREKREV
SRSRRKQHLQ PPCLDEPDLF FPEDSSTFRP AVELLAESSE PAPHLSCPQE EGGPFKTPIK
ETLPVSSTPS KSVLSRDPES WRLTPPAKVG GLDFSPVRTP QGAFGLLPDS LGLMELNTTP
LKSGPLFDSP RELLNSEPFD LASDPFGSPP PPHVEGPKPG SPELQIPSLS ANRSLTEGLV
LDTMNDSLSK ILLDISFPGL EEDPLGPDNI NWSQFIPELR
