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Forkhead box protein M1 (Forkhead-related protein FKHL16) (Hepatocyte nuclear factor 3 forkhead homolog 11) (HFH-11) (HNF-3/fork-head homolog 11) (M-phase phosphoprotein 2) (MPM-2 reactive phosphoprotein 2) (Transcription factor Trident) (Winged-helix factor from INS-1 cells)

 FOXM1_HUMAN             Reviewed;         763 AA.
Q08050; O43258; O43259; O43260; Q4ZGG7; Q9BRL2;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-DEC-2000, sequence version 3.
25-OCT-2017, entry version 187.
RecName: Full=Forkhead box protein M1;
AltName: Full=Forkhead-related protein FKHL16;
AltName: Full=Hepatocyte nuclear factor 3 forkhead homolog 11;
Short=HFH-11;
Short=HNF-3/fork-head homolog 11;
AltName: Full=M-phase phosphoprotein 2;
AltName: Full=MPM-2 reactive phosphoprotein 2;
AltName: Full=Transcription factor Trident;
AltName: Full=Winged-helix factor from INS-1 cells;
Name=FOXM1; Synonyms=FKHL16, HFH11, MPP2, WIN;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 4).
TISSUE=Colon carcinoma;
PubMed=9032290; DOI=10.1128/MCB.17.3.1626;
Ye H., Kelly T.F., Samadani U., Lim L., Rubio S., Overdier D.G.,
Roebuck K.A., Costa R.H.;
"Hepatocyte nuclear factor 3/fork head homolog 11 is expressed in
proliferating epithelial and mesenchymal cells of embryonic and adult
tissues.";
Mol. Cell. Biol. 17:1626-1641(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Pancreatic carcinoma, and Testis;
PubMed=9242644; DOI=10.1074/jbc.272.32.19827;
Yao K.-M., Sha M., Lu Z., Wong G.G.;
"Molecular analysis of a novel winged helix protein, WIN. Expression
pattern, DNA binding property, and alternative splicing within the DNA
binding domain.";
J. Biol. Chem. 272:19827-19836(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLU-402; LEU-450;
PRO-643; ARG-669 AND LEU-673.
NIEHS SNPs program;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
PRO-643.
TISSUE=Lung, Ovary, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 543-763.
TISSUE=Lymphoblast;
PubMed=8290587; DOI=10.1073/pnas.91.2.714;
Westendorf J.M., Rao P.N., Gerace L.;
"Cloning of cDNAs for M-phase phosphoproteins recognized by the MPM2
monoclonal antibody and determination of the phosphorylated epitope.";
Proc. Natl. Acad. Sci. U.S.A. 91:714-718(1994).
[6]
FUNCTION IN DNA REPAIR, AND PHOSPHORYLATION AT SER-376 BY CHEK2.
PubMed=17101782; DOI=10.1128/MCB.01068-06;
Tan Y., Raychaudhuri P., Costa R.H.;
"Chk2 mediates stabilization of the FoxM1 transcription factor to
stimulate expression of DNA repair genes.";
Mol. Cell. Biol. 27:1007-1016(2007).
[7]
FUNCTION, PHOSPHORYLATION AT THR-611; SER-693; SER-730 AND SER-739,
AND MUTAGENESIS OF THR-611; SER-693; SER-730 AND SER-739.
PubMed=19160488; DOI=10.1038/ncb1767;
Fu Z., Malureanu L., Huang J., Wang W., Li H., van Deursen J.M.,
Tindall D.J., Chen J.;
"Plk1-dependent phosphorylation of FoxM1 regulates a transcriptional
programme required for mitotic progression.";
Nat. Cell Biol. 10:1076-1082(2008).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331; THR-620 AND
THR-627, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-730 AND SER-739, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-522, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[11]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-356 AND LYS-440, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[12]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-201; LYS-356 AND LYS-422,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[13]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-201 AND LYS-356, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[14]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-163; LYS-201; LYS-325;
LYS-356; LYS-422 AND LYS-440, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[15]
X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 222-360 IN COMPLEX WITH
PROMOTER DNA, AND FUNCTION.
PubMed=20360045; DOI=10.1093/nar/gkq194;
Littler D.R., Alvarez-Fernandez M., Stein A., Hibbert R.G.,
Heidebrecht T., Aloy P., Medema R.H., Perrakis A.;
"Structure of the FoxM1 DNA-recognition domain bound to a promoter
sequence.";
Nucleic Acids Res. 38:4527-4538(2010).
-!- FUNCTION: Transcriptional factor regulating the expression of cell
cycle genes essential for DNA replication and mitosis. Plays a
role in the control of cell proliferation. Plays also a role in
DNA breaks repair participating in the DNA damage checkpoint
response. {ECO:0000269|PubMed:17101782,
ECO:0000269|PubMed:19160488, ECO:0000269|PubMed:20360045}.
-!- INTERACTION:
P24864:CCNE1; NbExp=2; IntAct=EBI-866480, EBI-519526;
Q00534:CDK6; NbExp=2; IntAct=EBI-866499, EBI-295663;
P35222:CTNNB1; NbExp=16; IntAct=EBI-866480, EBI-491549;
P14868:DARS; NbExp=2; IntAct=EBI-866480, EBI-358730;
P03129:E7 (xeno); NbExp=3; IntAct=EBI-866499, EBI-866453;
O43524:FOXO3; NbExp=2; IntAct=EBI-866480, EBI-1644164;
Q13416:ORC2; NbExp=2; IntAct=EBI-866480, EBI-374957;
O00541:PES1; NbExp=2; IntAct=EBI-866480, EBI-1053271;
O75152:ZC3H11A; NbExp=2; IntAct=EBI-866480, EBI-748480;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Comment=Isoform 1 and isoform 2 appear to be the only activators
of gene transcription. Isoform 3, found in rat, does not seem to
exist in human.;
Name=1; Synonyms=FoxM1C, FOXM1-c;
IsoId=Q08050-1; Sequence=Displayed;
Name=2; Synonyms=FoxM1B, FOXM1-b;
IsoId=Q08050-2; Sequence=VSP_001547;
Name=4; Synonyms=FoxM1A, FOXM1-a;
IsoId=Q08050-3; Sequence=VSP_001548;
-!- TISSUE SPECIFICITY: Expressed in thymus, testis, small intestine,
colon followed by ovary. Appears to be expressed only in adult
organs containing proliferating/cycling cells or in response to
growth factors. Also expressed in epithelial cell lines derived
from tumors. Not expressed in resting cells. Isoform 2 is highly
expressed in testis.
-!- DEVELOPMENTAL STAGE: Embryonic expression pattern: liver, lung,
intestine, kidney, urinary tract; adult expression pattern:
intestine, colon, testis and thymus.
-!- INDUCTION: Induced during liver regeneration and oxidative stress.
-!- DOMAIN: Within the protein there is a domain which acts as a
transcriptional activator. Insertion of a splicing sequence within
it inactivates this transcriptional activity, as it is the case
for isoform 4.
-!- PTM: Phosphorylated in M (mitotic) phase. Phosphorylation by the
checkpoint kinase CHEK2 in response to DNA damage increases the
FOXM1 protein stability probably stimulating the transcription of
genes involved in DNA repair. Phosphorylated by CDK1 in late S and
G2 phases, creating docking sites for the POLO box domains of
PLK1. Subsequently, PLK1 binds and phosphorylates FOXM1, leading
to activation of transcriptional activity and subsequent enhanced
expression of key mitotic regulators.
{ECO:0000269|PubMed:17101782, ECO:0000269|PubMed:19160488}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/FOXM1ID40631ch12p13.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/foxm1/";
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EMBL; U74612; AAC51128.1; -; mRNA.
EMBL; U74613; AAC51129.1; -; mRNA.
EMBL; U83113; AAC63595.1; -; mRNA.
EMBL; DQ022289; AAY26401.1; -; Genomic_DNA.
EMBL; BC006192; AAH06192.1; -; mRNA.
EMBL; BC006529; AAH06529.1; -; mRNA.
EMBL; BC012863; AAH12863.1; -; mRNA.
EMBL; L16783; AAC37541.1; -; mRNA.
CCDS; CCDS8515.1; -. [Q08050-1]
CCDS; CCDS8516.1; -. [Q08050-3]
CCDS; CCDS8517.1; -. [Q08050-2]
PIR; B36881; B36881.
RefSeq; NP_001230017.1; NM_001243088.1.
RefSeq; NP_001230018.1; NM_001243089.1.
RefSeq; NP_068772.2; NM_021953.3. [Q08050-1]
RefSeq; NP_973731.1; NM_202002.2. [Q08050-3]
RefSeq; NP_973732.1; NM_202003.2. [Q08050-2]
UniGene; Hs.239; -.
UniGene; Hs.735243; -.
PDB; 3G73; X-ray; 2.21 A; A/B=222-360.
PDBsum; 3G73; -.
ProteinModelPortal; Q08050; -.
SMR; Q08050; -.
BioGrid; 108594; 79.
CORUM; Q08050; -.
DIP; DIP-36754N; -.
IntAct; Q08050; 60.
MINT; MINT-107757; -.
STRING; 9606.ENSP00000342307; -.
iPTMnet; Q08050; -.
PhosphoSitePlus; Q08050; -.
BioMuta; FOXM1; -.
DMDM; 12644391; -.
PaxDb; Q08050; -.
PeptideAtlas; Q08050; -.
PRIDE; Q08050; -.
DNASU; 2305; -.
Ensembl; ENST00000342628; ENSP00000342307; ENSG00000111206. [Q08050-3]
Ensembl; ENST00000359843; ENSP00000352901; ENSG00000111206. [Q08050-1]
Ensembl; ENST00000361953; ENSP00000354492; ENSG00000111206. [Q08050-2]
GeneID; 2305; -.
KEGG; hsa:2305; -.
UCSC; uc001qle.4; human. [Q08050-1]
CTD; 2305; -.
DisGeNET; 2305; -.
EuPathDB; HostDB:ENSG00000111206.12; -.
GeneCards; FOXM1; -.
HGNC; HGNC:3818; FOXM1.
HPA; CAB017832; -.
HPA; HPA029974; -.
MIM; 602341; gene.
neXtProt; NX_Q08050; -.
OpenTargets; ENSG00000111206; -.
PharmGKB; PA28236; -.
eggNOG; KOG2294; Eukaryota.
eggNOG; COG5025; LUCA.
GeneTree; ENSGT00790000123003; -.
HOGENOM; HOG000112633; -.
HOVERGEN; HBG051652; -.
InParanoid; Q08050; -.
KO; K09406; -.
OMA; FKTPIKE; -.
OrthoDB; EOG091G03GL; -.
PhylomeDB; Q08050; -.
TreeFam; TF333250; -.
Reactome; R-HSA-156711; Polo-like kinase mediated events.
Reactome; R-HSA-69273; Cyclin A/B1/B2 associated events during G2/M transition.
SIGNOR; Q08050; -.
EvolutionaryTrace; Q08050; -.
GeneWiki; FOXM1; -.
GenomeRNAi; 2305; -.
PRO; PR:Q08050; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000111206; -.
CleanEx; HS_FOXM1; -.
CleanEx; HS_MPP2; -.
ExpressionAtlas; Q08050; baseline and differential.
Genevisible; Q08050; HS.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0001227; F:transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding; IC:NTNU_SB.
GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
GO; GO:0007049; P:cell cycle; TAS:UniProtKB.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; IMP:UniProtKB.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IDA:UniProtKB.
GO; GO:0090344; P:negative regulation of cell aging; IMP:UniProtKB.
GO; GO:0032873; P:negative regulation of stress-activated MAPK cascade; IMP:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:BHF-UCL.
GO; GO:2000781; P:positive regulation of double-strand break repair; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0051726; P:regulation of cell cycle; TAS:Reactome.
GO; GO:0071156; P:regulation of cell cycle arrest; IMP:BHF-UCL.
GO; GO:0001558; P:regulation of cell growth; TAS:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; NAS:UniProtKB.
GO; GO:0046578; P:regulation of Ras protein signal transduction; IMP:BHF-UCL.
GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IMP:BHF-UCL.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00059; FH; 1.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR001766; Fork_head_dom.
InterPro; IPR018122; TF_fork_head_CS_1.
InterPro; IPR030456; TF_fork_head_CS_2.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
Pfam; PF00250; Forkhead; 1.
PRINTS; PR00053; FORKHEAD.
SMART; SM00339; FH; 1.
SUPFAM; SSF46785; SSF46785; 1.
PROSITE; PS00657; FORK_HEAD_1; 1.
PROSITE; PS00658; FORK_HEAD_2; 1.
PROSITE; PS50039; FORK_HEAD_3; 1.
1: Evidence at protein level;
3D-structure; Activator; Alternative splicing; Cell cycle;
Complete proteome; DNA damage; DNA repair; DNA-binding;
Isopeptide bond; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 763 Forkhead box protein M1.
/FTId=PRO_0000091863.
DNA_BIND 235 327 Fork-head. {ECO:0000255|PROSITE-
ProRule:PRU00089}.
COMPBIAS 480 513 Glu/Pro/Ser/Thr-rich.
MOD_RES 331 331 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 376 376 Phosphoserine; by CHEK2.
{ECO:0000269|PubMed:17101782}.
MOD_RES 522 522 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 611 611 Phosphothreonine; by CDK1.
{ECO:0000269|PubMed:19160488}.
MOD_RES 620 620 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 627 627 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 662 662 Phosphothreonine. {ECO:0000305}.
MOD_RES 693 693 Phosphoserine; by CDK1.
{ECO:0000269|PubMed:19160488}.
MOD_RES 730 730 Phosphoserine; by PLK1.
{ECO:0000244|PubMed:20068231,
ECO:0000269|PubMed:19160488}.
MOD_RES 739 739 Phosphoserine; by PLK1.
{ECO:0000244|PubMed:20068231,
ECO:0000269|PubMed:19160488}.
CROSSLNK 163 163 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 201 201 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 325 325 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 356 356 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 422 422 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CROSSLNK 440 440 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 326 340 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9032290}.
/FTId=VSP_001547.
VAR_SEQ 423 423 V -> VFGEQVVFGYMSKFFSGDLRDFGTPITSLFNFIFLC
LSV (in isoform 4).
{ECO:0000303|PubMed:9032290}.
/FTId=VSP_001548.
VARIANT 402 402 A -> E (in dbSNP:rs28990715).
{ECO:0000269|Ref.3}.
/FTId=VAR_025239.
VARIANT 450 450 F -> L (in dbSNP:rs28919868).
{ECO:0000269|Ref.3}.
/FTId=VAR_025240.
VARIANT 643 643 S -> P (in dbSNP:rs3742076).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.3}.
/FTId=VAR_020024.
VARIANT 669 669 P -> R (in dbSNP:rs28919869).
{ECO:0000269|Ref.3}.
/FTId=VAR_025241.
VARIANT 673 673 P -> L (in dbSNP:rs28919870).
{ECO:0000269|Ref.3}.
/FTId=VAR_025242.
MUTAGEN 611 611 T->A: Prevents phosphorylation by CDK1
and subsequent binding of POLO box
domains of PLK1; when associated with A-
693. {ECO:0000269|PubMed:19160488}.
MUTAGEN 693 693 S->A: Prevents phosphorylation by CDK1
and subsequent binding of POLO box
domains of PLK1; when associated with A-
611. {ECO:0000269|PubMed:19160488}.
MUTAGEN 730 730 S->A: Prevents phosphorylation by PLK1
and impairs transcription activity; when
associated with A-739.
{ECO:0000269|PubMed:19160488}.
MUTAGEN 739 739 S->A: Prevents phosphorylation by PLK1
and impairs transcription activity; when
associated with A-730.
{ECO:0000269|PubMed:19160488}.
CONFLICT 3 3 T -> A (in Ref. 2; AAC63595).
{ECO:0000305}.
HELIX 241 250 {ECO:0000244|PDB:3G73}.
STRAND 255 257 {ECO:0000244|PDB:3G73}.
HELIX 259 269 {ECO:0000244|PDB:3G73}.
HELIX 272 275 {ECO:0000244|PDB:3G73}.
HELIX 281 291 {ECO:0000244|PDB:3G73}.
STRAND 295 299 {ECO:0000244|PDB:3G73}.
STRAND 306 310 {ECO:0000244|PDB:3G73}.
TURN 312 314 {ECO:0000244|PDB:3G73}.
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


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