ID FOXM1_HUMAN Reviewed; 763 AA. AC Q08050; O43258; O43259; O43260; Q4ZGG7; Q9BRL2; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 3. DT 27-MAR-2024, entry version 228. DE RecName: Full=Forkhead box protein M1; DE AltName: Full=Forkhead-related protein FKHL16; DE AltName: Full=Hepatocyte nuclear factor 3 forkhead homolog 11; DE Short=HFH-11; DE Short=HNF-3/fork-head homolog 11; DE AltName: Full=M-phase phosphoprotein 2; DE AltName: Full=MPM-2 reactive phosphoprotein 2; DE AltName: Full=Transcription factor Trident; DE AltName: Full=Winged-helix factor from INS-1 cells; GN Name=FOXM1; Synonyms=FKHL16, HFH11, MPP2, WIN; 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] (ISOFORMS 2 AND 4). RC TISSUE=Colon carcinoma; RX PubMed=9032290; DOI=10.1128/mcb.17.3.1626; RA Ye H., Kelly T.F., Samadani U., Lim L., Rubio S., Overdier D.G., RA Roebuck K.A., Costa R.H.; RT "Hepatocyte nuclear factor 3/fork head homolog 11 is expressed in RT proliferating epithelial and mesenchymal cells of embryonic and adult RT tissues."; RL Mol. Cell. Biol. 17:1626-1641(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Pancreatic carcinoma, and Testis; RX PubMed=9242644; DOI=10.1074/jbc.272.32.19827; RA Yao K.-M., Sha M., Lu Z., Wong G.G.; RT "Molecular analysis of a novel winged helix protein, WIN. Expression RT pattern, DNA binding property, and alternative splicing within the DNA RT binding domain."; RL J. Biol. Chem. 272:19827-19836(1997). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLU-402; LEU-450; PRO-643; RP ARG-669 AND LEU-673. RG NIEHS SNPs program; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT RP PRO-643. RC TISSUE=Lung, Ovary, and Skin; 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 543-763. RC TISSUE=Lymphoblast; RX PubMed=8290587; DOI=10.1073/pnas.91.2.714; RA Westendorf J.M., Rao P.N., Gerace L.; RT "Cloning of cDNAs for M-phase phosphoproteins recognized by the MPM2 RT monoclonal antibody and determination of the phosphorylated epitope."; RL Proc. Natl. Acad. Sci. U.S.A. 91:714-718(1994). RN [6] RP FUNCTION IN DNA REPAIR, AND PHOSPHORYLATION AT SER-376 BY CHEK2. 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 [7] RP FUNCTION, PHOSPHORYLATION AT THR-611; SER-693; SER-730 AND SER-739, AND RP MUTAGENESIS OF THR-611; SER-693; SER-730 AND SER-739. RX PubMed=19160488; DOI=10.1038/ncb1767; RA Fu Z., Malureanu L., Huang J., Wang W., Li H., van Deursen J.M., RA Tindall D.J., Chen J.; RT "Plk1-dependent phosphorylation of FoxM1 regulates a transcriptional RT programme required for mitotic progression."; RL Nat. Cell Biol. 10:1076-1082(2008). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331; THR-620 AND THR-627, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-730 AND SER-739, AND 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-522, 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 [11] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-356 AND LYS-440, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [12] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-201; LYS-356 AND LYS-422, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033; RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., RA Vertegaal A.C.; RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."; RL Cell Rep. 10:1778-1791(2015). RN [13] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-201 AND LYS-356, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.o114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., RA Vertegaal A.C.; RT "System-wide analysis of SUMOylation dynamics in response to replication RT stress reveals novel small ubiquitin-like modified target proteins and RT acceptor lysines relevant for genome stability."; RL Mol. Cell. Proteomics 14:1419-1434(2015). RN [14] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-163; LYS-201; LYS-325; LYS-356; RP LYS-422 AND LYS-440, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [15] RP FUNCTION, AND INTERACTION WITH PINT87AA. RX PubMed=33754036; DOI=10.7150/thno.55672; RA Xiang X., Fu Y., Zhao K., Miao R., Zhang X., Ma X., Liu C., Zhang N., RA Qu K.; RT "Cellular senescence in hepatocellular carcinoma induced by a long non- RT coding RNA-encoded peptide PINT87aa by blocking FOXM1-mediated PHB2."; RL Theranostics 11:4929-4944(2021). RN [16] RP PHOSPHORYLATION. RX PubMed=30139873; DOI=10.1126/science.aap9346; RA Saldivar J.C., Hamperl S., Bocek M.J., Chung M., Bass T.E., RA Cisneros-Soberanis F., Samejima K., Xie L., Paulson J.R., Earnshaw W.C., RA Cortez D., Meyer T., Cimprich K.A.; RT "An intrinsic S/G2 checkpoint enforced by ATR."; RL Science 361:806-810(2018). RN [17] RP X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 222-360 IN COMPLEX WITH PROMOTER RP DNA, AND FUNCTION. RX PubMed=20360045; DOI=10.1093/nar/gkq194; RA Littler D.R., Alvarez-Fernandez M., Stein A., Hibbert R.G., Heidebrecht T., RA Aloy P., Medema R.H., Perrakis A.; RT "Structure of the FoxM1 DNA-recognition domain bound to a promoter RT sequence."; RL Nucleic Acids Res. 38:4527-4538(2010). CC -!- FUNCTION: Transcription factor regulating the expression of cell cycle CC genes essential for DNA replication and mitosis (PubMed:19160488, CC PubMed:20360045). Plays a role in the control of cell proliferation CC (PubMed:19160488). Also plays a role in DNA break repair, participating CC in the DNA damage checkpoint response (PubMed:17101782). Promotes CC transcription of PHB2 (PubMed:33754036). {ECO:0000269|PubMed:17101782, CC ECO:0000269|PubMed:19160488, ECO:0000269|PubMed:20360045, CC ECO:0000269|PubMed:33754036}. CC -!- SUBUNIT: Interacts with PINT87aa which is encoded by the circular form CC of the long non-coding RNA LINC-PINT; the interaction inhibits FOXM1- CC mediated transcription of PHB2. {ECO:0000269|PubMed:33754036}. CC -!- INTERACTION: CC Q08050; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-866480, EBI-11524452; CC Q08050; Q8N9N5-7: BANP; NbExp=3; IntAct=EBI-866480, EBI-16429296; CC Q08050; P24864: CCNE1; NbExp=2; IntAct=EBI-866480, EBI-519526; CC Q08050; P35222: CTNNB1; NbExp=16; IntAct=EBI-866480, EBI-491549; CC Q08050; P14868: DARS1; NbExp=2; IntAct=EBI-866480, EBI-358730; CC Q08050; O43524: FOXO3; NbExp=2; IntAct=EBI-866480, EBI-1644164; CC Q08050; A0A455ZAR2: LINC-PINT; NbExp=4; IntAct=EBI-866480, EBI-27121529; CC Q08050; Q13416: ORC2; NbExp=2; IntAct=EBI-866480, EBI-374957; CC Q08050; O00541: PES1; NbExp=2; IntAct=EBI-866480, EBI-1053271; CC Q08050; O75152: ZC3H11A; NbExp=2; IntAct=EBI-866480, EBI-748480; CC Q08050-1; Q00534: CDK6; NbExp=2; IntAct=EBI-866499, EBI-295663; CC Q08050-1; P03129: E7; Xeno; NbExp=3; IntAct=EBI-866499, EBI-866453; CC Q08050-2; B4DE54: BANP; NbExp=3; IntAct=EBI-5237510, EBI-16429313; CC Q08050-2; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-5237510, EBI-11524452; CC Q08050-2; Q8N9N5-7: BANP; NbExp=3; IntAct=EBI-5237510, EBI-16429296; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Isoform 1 and isoform 2 appear to be the only activators of CC gene transcription. Isoform 3, found in rat, does not seem to exist CC in human.; CC Name=1; Synonyms=FoxM1C, FOXM1-c; CC IsoId=Q08050-1; Sequence=Displayed; CC Name=2; Synonyms=FoxM1B, FOXM1-b; CC IsoId=Q08050-2; Sequence=VSP_001547; CC Name=4; Synonyms=FoxM1A, FOXM1-a; CC IsoId=Q08050-3; Sequence=VSP_001548; CC -!- TISSUE SPECIFICITY: Expressed in thymus, testis, small intestine, colon CC followed by ovary. Appears to be expressed only in adult organs CC containing proliferating/cycling cells or in response to growth CC factors. Also expressed in epithelial cell lines derived from tumors. CC Not expressed in resting cells. Isoform 2 is highly expressed in CC testis. CC -!- DEVELOPMENTAL STAGE: Embryonic expression pattern: liver, lung, CC intestine, kidney, urinary tract; adult expression pattern: intestine, CC colon, testis and thymus. CC -!- INDUCTION: Induced during liver regeneration and oxidative stress. CC -!- DOMAIN: Within the protein there is a domain which acts as a CC transcriptional activator. Insertion of a splicing sequence within it CC inactivates this transcriptional activity, as it is the case for CC isoform 4. CC -!- PTM: Phosphorylated in M (mitotic) phase (PubMed:17101782, CC PubMed:19160488, PubMed:30139873). Phosphorylation by the checkpoint CC kinase CHEK2 in response to DNA damage increases the FOXM1 protein CC stability probably stimulating the transcription of genes involved in CC DNA repair (PubMed:17101782). Phosphorylated by CDK1 in late S and G2 CC phases, creating docking sites for the POLO box domains of PLK1 CC (PubMed:19160488, PubMed:30139873). Subsequently, PLK1 binds and CC phosphorylates FOXM1, leading to activation of transcriptional activity CC and subsequent enhanced expression of key mitotic regulators CC (PubMed:19160488). {ECO:0000269|PubMed:17101782, CC ECO:0000269|PubMed:19160488, ECO:0000269|PubMed:30139873}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/40631/FOXM1"; CC -!- WEB RESOURCE: Name=NIEHS-SNPs; CC URL="http://egp.gs.washington.edu/data/foxm1/"; 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; U74612; AAC51128.1; -; mRNA. DR EMBL; U74613; AAC51129.1; -; mRNA. DR EMBL; U83113; AAC63595.1; -; mRNA. DR EMBL; DQ022289; AAY26401.1; -; Genomic_DNA. DR EMBL; BC006192; AAH06192.1; -; mRNA. DR EMBL; BC006529; AAH06529.1; -; mRNA. DR EMBL; BC012863; AAH12863.1; -; mRNA. DR EMBL; L16783; AAC37541.1; -; mRNA. DR CCDS; CCDS8515.1; -. [Q08050-1] DR CCDS; CCDS8516.1; -. [Q08050-3] DR CCDS; CCDS8517.1; -. [Q08050-2] DR PIR; B36881; B36881. DR RefSeq; NP_001230017.1; NM_001243088.1. DR RefSeq; NP_001230018.1; NM_001243089.1. DR RefSeq; NP_068772.2; NM_021953.3. [Q08050-1] DR RefSeq; NP_973731.1; NM_202002.2. [Q08050-3] DR RefSeq; NP_973732.1; NM_202003.2. [Q08050-2] DR PDB; 3G73; X-ray; 2.21 A; A/B=222-360. DR PDB; 7FJ2; X-ray; 3.10 A; A/B/E/F=222-337. DR PDBsum; 3G73; -. DR PDBsum; 7FJ2; -. DR AlphaFoldDB; Q08050; -. DR SMR; Q08050; -. DR BioGRID; 108594; 114. DR ComplexPortal; CPX-7462; Myb-MuvB-FOXM1 transcriptional activation complex. DR CORUM; Q08050; -. DR DIP; DIP-36754N; -. DR IntAct; Q08050; 64. DR MINT; Q08050; -. DR STRING; 9606.ENSP00000342307; -. DR BindingDB; Q08050; -. DR ChEMBL; CHEMBL4739852; -. DR GlyGen; Q08050; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q08050; -. DR PhosphoSitePlus; Q08050; -. DR SwissPalm; Q08050; -. DR BioMuta; FOXM1; -. DR DMDM; 12644391; -. DR CPTAC; CPTAC-1242; -. DR EPD; Q08050; -. DR jPOST; Q08050; -. DR MassIVE; Q08050; -. DR MaxQB; Q08050; -. DR PaxDb; 9606-ENSP00000342307; -. DR PeptideAtlas; Q08050; -. DR ProteomicsDB; 58567; -. [Q08050-1] DR ProteomicsDB; 58568; -. [Q08050-2] DR ProteomicsDB; 58569; -. [Q08050-3] DR Antibodypedia; 4507; 537 antibodies from 38 providers. DR DNASU; 2305; -. DR Ensembl; ENST00000342628.6; ENSP00000342307.2; ENSG00000111206.13. [Q08050-3] DR Ensembl; ENST00000359843.8; ENSP00000352901.4; ENSG00000111206.13. [Q08050-1] DR Ensembl; ENST00000361953.7; ENSP00000354492.3; ENSG00000111206.13. [Q08050-2] DR GeneID; 2305; -. DR KEGG; hsa:2305; -. DR MANE-Select; ENST00000359843.8; ENSP00000352901.4; NM_021953.4; NP_068772.2. DR UCSC; uc001qle.4; human. [Q08050-1] DR AGR; HGNC:3818; -. DR CTD; 2305; -. DR DisGeNET; 2305; -. DR GeneCards; FOXM1; -. DR HGNC; HGNC:3818; FOXM1. DR HPA; ENSG00000111206; Tissue enhanced (bone marrow, lymphoid tissue, testis). DR MIM; 602341; gene. DR neXtProt; NX_Q08050; -. DR OpenTargets; ENSG00000111206; -. DR PharmGKB; PA28236; -. DR VEuPathDB; HostDB:ENSG00000111206; -. DR eggNOG; KOG2294; Eukaryota. DR GeneTree; ENSGT00940000158804; -. DR HOGENOM; CLU_027498_0_0_1; -. DR InParanoid; Q08050; -. DR OMA; APKQEHR; -. DR OrthoDB; 5385885at2759; -. DR PhylomeDB; Q08050; -. DR TreeFam; TF333250; -. DR PathwayCommons; Q08050; -. DR Reactome; R-HSA-156711; Polo-like kinase mediated events. DR Reactome; R-HSA-69273; Cyclin A/B1/B2 associated events during G2/M transition. DR SignaLink; Q08050; -. DR SIGNOR; Q08050; -. DR BioGRID-ORCS; 2305; 205 hits in 1185 CRISPR screens. DR ChiTaRS; FOXM1; human. DR EvolutionaryTrace; Q08050; -. DR GeneWiki; FOXM1; -. DR GenomeRNAi; 2305; -. DR Pharos; Q08050; Tchem. DR PRO; PR:Q08050; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q08050; Protein. DR Bgee; ENSG00000111206; Expressed in ventricular zone and 107 other cell types or tissues. DR ExpressionAtlas; Q08050; baseline and differential. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB. 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:0019901; F:protein kinase binding; IPI:UniProtKB. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB. 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; IDA:UniProtKB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IMP:BHF-UCL. DR GO; GO:0032873; P:negative regulation of stress-activated MAPK cascade; IMP:BHF-UCL. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:BHF-UCL. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:BHF-UCL. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:2000781; P:positive regulation of double-strand break repair; IMP:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0051726; P:regulation of cell cycle; IMP:BHF-UCL. DR GO; GO:0001558; P:regulation of cell growth; TAS:UniProtKB. DR GO; GO:0042127; P:regulation of cell population proliferation; IBA:GO_Central. DR GO; GO:0046578; P:regulation of Ras protein signal transduction; IMP:BHF-UCL. DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IMP:BHF-UCL. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR CDD; cd20029; FH_FOXM; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR InterPro; IPR047516; FH_FOXM1. 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; FORKHEAD BOX PROTEIN M1; 1. DR PANTHER; PTHR46878:SF1; FORKHEAD BOX PROTEIN M1; 1. DR Pfam; PF00250; Forkhead; 1. DR PRINTS; PR00053; FORKHEAD. DR SMART; SM00339; FH; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. DR PROSITE; PS00657; FORK_HEAD_1; 1. DR PROSITE; PS00658; FORK_HEAD_2; 1. DR PROSITE; PS50039; FORK_HEAD_3; 1. DR Genevisible; Q08050; HS. PE 1: Evidence at protein level; KW 3D-structure; Activator; Alternative splicing; Cell cycle; DNA damage; KW DNA repair; DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; KW Reference proteome; Transcription; Transcription regulation; KW Ubl conjugation. FT CHAIN 1..763 FT /note="Forkhead box protein M1" FT /id="PRO_0000091863" FT DNA_BIND 235..327 FT /note="Fork-head" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089" FT REGION 1..53 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 198..232 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 329..351 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 482..711 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 199..220 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 503..523 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 604..620 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 659..673 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 331 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 376 FT /note="Phosphoserine; by CHEK2" FT /evidence="ECO:0000269|PubMed:17101782" FT MOD_RES 522 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 611 FT /note="Phosphothreonine; by CDK1" FT /evidence="ECO:0000269|PubMed:19160488" FT MOD_RES 620 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 627 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 662 FT /note="Phosphothreonine" FT /evidence="ECO:0000305" FT MOD_RES 693 FT /note="Phosphoserine; by CDK1" FT /evidence="ECO:0000269|PubMed:19160488" FT MOD_RES 730 FT /note="Phosphoserine; by PLK1" FT /evidence="ECO:0000269|PubMed:19160488, FT ECO:0007744|PubMed:20068231" FT MOD_RES 739 FT /note="Phosphoserine; by PLK1" FT /evidence="ECO:0000269|PubMed:19160488, FT ECO:0007744|PubMed:20068231" FT CROSSLNK 163 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 201 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT CROSSLNK 325 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 356 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 422 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 440 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT VAR_SEQ 326..340 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:9032290" FT /id="VSP_001547" FT VAR_SEQ 423 FT /note="V -> VFGEQVVFGYMSKFFSGDLRDFGTPITSLFNFIFLCLSV (in FT isoform 4)" FT /evidence="ECO:0000303|PubMed:9032290" FT /id="VSP_001548" FT VARIANT 402 FT /note="A -> E (in dbSNP:rs28990715)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_025239" FT VARIANT 450 FT /note="F -> L (in dbSNP:rs28919868)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_025240" FT VARIANT 643 FT /note="S -> P (in dbSNP:rs3742076)" FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3" FT /id="VAR_020024" FT VARIANT 669 FT /note="P -> R (in dbSNP:rs28919869)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_025241" FT VARIANT 673 FT /note="P -> L (in dbSNP:rs28919870)" FT /evidence="ECO:0000269|Ref.3" FT /id="VAR_025242" FT MUTAGEN 611 FT /note="T->A: Prevents phosphorylation by CDK1 and FT subsequent binding of POLO box domains of PLK1; when FT associated with A-693." FT /evidence="ECO:0000269|PubMed:19160488" FT MUTAGEN 693 FT /note="S->A: Prevents phosphorylation by CDK1 and FT subsequent binding of POLO box domains of PLK1; when FT associated with A-611." FT /evidence="ECO:0000269|PubMed:19160488" FT MUTAGEN 730 FT /note="S->A: Prevents phosphorylation by PLK1 and impairs FT transcription activity; when associated with A-739." FT /evidence="ECO:0000269|PubMed:19160488" FT MUTAGEN 739 FT /note="S->A: Prevents phosphorylation by PLK1 and impairs FT transcription activity; when associated with A-730." FT /evidence="ECO:0000269|PubMed:19160488" FT CONFLICT 3 FT /note="T -> A (in Ref. 2; AAC63595)" FT /evidence="ECO:0000305" FT HELIX 241..250 FT /evidence="ECO:0007829|PDB:3G73" FT STRAND 255..257 FT /evidence="ECO:0007829|PDB:3G73" FT HELIX 259..269 FT /evidence="ECO:0007829|PDB:3G73" FT HELIX 272..275 FT /evidence="ECO:0007829|PDB:3G73" FT HELIX 281..291 FT /evidence="ECO:0007829|PDB:3G73" FT STRAND 295..299 FT /evidence="ECO:0007829|PDB:3G73" FT STRAND 306..310 FT /evidence="ECO:0007829|PDB:3G73" FT TURN 312..314 FT /evidence="ECO:0007829|PDB:3G73" SQ SEQUENCE 763 AA; 84283 MW; 963CAC8FE7498E9B CRC64; MKTSPRRPLI LKRRRLPLPV QNAPSETSEE EPKRSPAQQE SNQAEASKEV AESNSCKFPA GIKIINHPTM PNTQVVAIPN NANIHSIITA LTAKGKESGS SGPNKFILIS CGGAPTQPPG LRPQTQTSYD AKRTEVTLET LGPKPAARDV NLPRPPGALC EQKRETCADG EAAGCTINNS LSNIQWLRKM SSDGLGSRSI KQEMEEKENC HLEQRQVKVE EPSRPSASWQ NSVSERPPYS YMAMIQFAIN STERKRMTLK DIYTWIEDHF PYFKHIAKPG WKNSIRHNLS LHDMFVRETS ANGKVSFWTI HPSANRYLTL DQVFKPLDPG SPQLPEHLES QQKRPNPELR RNMTIKTELP LGARRKMKPL LPRVSSYLVP IQFPVNQSLV LQPSVKVPLP LAASLMSSEL ARHSKRVRIA PKVLLAEEGI APLSSAGPGK EEKLLFGEGF SPLLPVQTIK EEEIQPGEEM PHLARPIKVE SPPLEEWPSP APSFKEESSH SWEDSSQSPT PRPKKSYSGL RSPTRCVSEM LVIQHRERRE RSRSRRKQHL LPPCVDEPEL LFSEGPSTSR WAAELPFPAD SSDPASQLSY SQEVGGPFKT PIKETLPISS TPSKSVLPRT PESWRLTPPA KVGGLDFSPV QTSQGASDPL PDPLGLMDLS TTPLQSAPPL ESPQRLLSSE PLDLISVPFG NSSPSDIDVP KPGSPEPQVS GLAANRSLTE GLVLDTMNDS LSKILLDISF PGLDEDPLGP DNINWSQFIP ELQ //