Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O08696 (FOXM1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Forkhead box protein M1
Alternative name(s):
Forkhead homolog 16
Winged-helix transcription factor Trident
Gene names
Name:Foxm1
Synonyms:Fkh16
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length760 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.2

Subcellular location

Nucleus By similarity.

Tissue specificity

Expressed in fetal heart, brain, liver, lung, kidney and limb, but only in adult thymus. Appears to be expressed only in adult organs containing proliferating/cycling cells or in response to growth factors.

Developmental stage

Expressed at E14 day in the embryo.

Post-translational modification

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 By similarity.

Sequence similarities

Contains 1 fork-head DNA-binding domain.

Sequence caution

The sequence CAA72115.1 differs from that shown. Reason: Erroneous termination at position 758. Translated as Glu.

Ontologies

Keywords
   Biological processCell cycle
DNA damage
DNA repair
Transcription
Transcription regulation
   Cellular componentNucleus
   LigandDNA-binding
   Molecular functionActivator
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator

Inferred from mutant phenotype Ref.2. Source: UniProtKB

DNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

G2/M transition of mitotic cell cycle

Inferred from sequence or structural similarity. Source: UniProtKB

liver development

Inferred from mutant phenotype PubMed 15531365. Source: MGI

negative regulation of stress-activated MAPK cascade

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of transcription from RNA polymerase II promoter

Inferred from Biological aspect of Ancestor. Source: RefGenome

pattern specification process

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of cell proliferation

Inferred from mutant phenotype PubMed 15817462. Source: MGI

positive regulation of double-strand break repair

Inferred from mutant phenotype Ref.2. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype Ref.2. Source: UniProtKB

regulation of Ras protein signal transduction

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of cell cycle arrest

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of cell proliferation

Inferred from mutant phenotype PubMed 15531365. Source: MGI

regulation of sequence-specific DNA binding transcription factor activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

tissue development

Inferred from Biological aspect of Ancestor. Source: RefGenome

transcription from RNA polymerase II promoter

Inferred from Biological aspect of Ancestor. Source: GOC

vasculogenesis

Inferred from mutant phenotype PubMed 15817462. Source: MGI

   Cellular_componentnucleus

Inferred from direct assay PubMed 17261592. Source: MGI

transcription factor complex

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Molecular_functionDNA binding

Inferred from sequence or structural similarity PubMed 9242644. Source: UniProtKB

DNA binding, bending

Inferred from Biological aspect of Ancestor. Source: RefGenome

RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

double-stranded DNA binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein binding

Inferred from physical interaction PubMed 10523841. Source: UniProtKB

sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding transcription factor activity

Inferred from sequence or structural similarity PubMed 10523841. Source: UniProtKB

transcription factor binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

transcription regulatory region DNA binding

Inferred from direct assay PubMed 17261592. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 760760Forkhead box protein M1
PRO_0000091864

Regions

DNA binding233 – 32593Fork-head
Compositional bias479 – 51234Glu/Pro/Ser/Thr-rich

Amino acid modifications

Modified residue3291Phosphoserine By similarity
Modified residue3741Phosphoserine; by CHEK2 By similarity
Modified residue6081Phosphothreonine; by CDK1 By similarity
Modified residue6241Phosphothreonine By similarity
Modified residue7271Phosphoserine; by PLK1 By similarity
Modified residue7361Phosphoserine; by PLK1 By similarity

Sequences

Sequence LengthMass (Da)Tools
O08696 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: AA614CB940EE7492

FASTA76083,694
        10         20         30         40         50         60 
MRTSPRRPLI LKRRRLPLPV QNAPSETSEE EAKRSPAQPE PAPAQASQEV AESSSCKFPA 

        70         80         90        100        110        120 
GIKIINHPTT PNTQVVAIPS NADIQSIITA LTAKGKESGT SGPNRFILIS SGGPSSHPSQ 

       130        140        150        160        170        180 
PQAHSSRDSK RAEVITETLG PKPAAKGVPV PKPPGAPPRQ RQESYAGGEA AGCTLDNSLT 

       190        200        210        220        230        240 
NIQWLGKMSS DGLGPCSVKQ ELEEKENCHL EQNRVKVEEP SGVSTSWQDS VSERPPYSYM 

       250        260        270        280        290        300 
AMIQFAINST ERKRMTLKDI YTWIEDHFPY FKHIAKPGWK NSIRHNLSLH DMFVRETSAN 

       310        320        330        340        350        360 
GKVSFWTIHP SANRHLTLDQ VFKPLEPGSP QSPEHLESQQ KRPNPELHRN VTIKTEIPLG 

       370        380        390        400        410        420 
ARRKMKPLLP RVSSYLEPIQ FPVNQSLVLQ PSVKVPFRLA ASLMSSELAR HSKRVRIAPK 

       430        440        450        460        470        480 
VLLSSEGIAP LPATEPPKEE KPLLGGEGLL PLLPIQSIKE EEMQPEEDIA HLERPIKVES 

       490        500        510        520        530        540 
PPLEEWPSPC ASLKEELSNS WEDSSCSPTP KPKKSYCGLK SPTRCVSEML VTKRREKREV 

       550        560        570        580        590        600 
SRSRRKQHLQ PPCLDEPDLF FPEDSSTFRP AVELLAESSE PAPHLSCPQE EGGPFKTPIK 

       610        620        630        640        650        660 
ETLPVSSTPS KSVLSRDPES WRLTPPAKVG GLDFSPVRTP QGAFGLLPDS LGLMELNTTP 

       670        680        690        700        710        720 
LKSGPLFDSP RELLNSEPFD LASDPFGSPP PPHVEGPKPG SPELQIPSLS ANRSLTEGLV 

       730        740        750        760 
LDTMNDSLSK ILLDISFPGL EEDPLGPDNI NWSQFIPELR 

« Hide

References

[1]"The winged-helix transcription factor Trident is expressed in cycling cells."
Korver W., Roose J., Clevers H.
Nucleic Acids Res. 25:1715-1719(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Thymus.
[2]"Chk2 mediates stabilization of the FoxM1 transcription factor to stimulate expression of DNA repair genes."
Tan Y., Raychaudhuri P., Costa R.H.
Mol. Cell. Biol. 27:1007-1016(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DNA REPAIR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y11245 mRNA. Translation: CAA72115.1. Sequence problems.
UniGeneMm.42148.

3D structure databases

ProteinModelPortalO08696.
SMRO08696. Positions 230-319.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO08696. 2 interactions.

PTM databases

PhosphoSiteO08696.

Proteomic databases

PRIDEO08696.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

MGIMGI:1347487. Foxm1.

Phylogenomic databases

eggNOGCOG5025.
HOGENOMHOG000112633.
HOVERGENHBG051652.
InParanoidO08696.
PhylomeDBO08696.

Gene expression databases

CleanExMM_FOXM1.
GenevestigatorO08696.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
InterProIPR001766. TF_fork_head.
IPR018122. TF_fork_head_CS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF00250. Fork_head. 1 hit.
[Graphical view]
PRINTSPR00053. FORKHEAD.
SMARTSM00339. FH. 1 hit.
[Graphical view]
PROSITEPS00657. FORK_HEAD_1. 1 hit.
PS00658. FORK_HEAD_2. 1 hit.
PS50039. FORK_HEAD_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFOXM1. mouse.
PROO08696.
SOURCESearch...

Entry information

Entry nameFOXM1_MOUSE
AccessionPrimary (citable) accession number: O08696
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: July 9, 2014
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot