FOXM1_HUMAN
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 03-AUG-2022, entry version 219.
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 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; A0A455ZAR2: circPINTexon2; NbExp=4; IntAct=EBI-866480, EBI-27121529;
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; 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. 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. {ECO:0000269|PubMed:17101782,
CC ECO:0000269|PubMed:19160488}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/FOXM1ID40631ch12p13.html";
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/foxm1/";
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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; 102.
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 iPTMnet; Q08050; -.
DR PhosphoSitePlus; 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; Q08050; -.
DR PeptideAtlas; Q08050; -.
DR PRIDE; Q08050; -.
DR ProteomicsDB; 58567; -. [Q08050-1]
DR ProteomicsDB; 58568; -. [Q08050-2]
DR ProteomicsDB; 58569; -. [Q08050-3]
DR Antibodypedia; 4507; 497 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 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; SWQDSMS; -.
DR OrthoDB; 1270467at2759; -.
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; 185 hits in 1104 CRISPR screens.
DR ChiTaRS; FOXM1; human.
DR EvolutionaryTrace; Q08050; -.
DR GeneWiki; FOXM1; -.
DR GenomeRNAi; 2305; -.
DR Pharos; Q08050; Tbio.
DR PRO; PR:Q08050; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q08050; protein.
DR Bgee; ENSG00000111206; Expressed in ventricular zone and 105 other tissues.
DR ExpressionAtlas; Q08050; baseline and differential.
DR Genevisible; Q08050; HS.
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: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:0045892; P:negative regulation of transcription, DNA-templated; IMP:BHF-UCL.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:BHF-UCL.
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:0045893; P:positive regulation of transcription, DNA-templated; 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; 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 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
