Q08050 (FOXM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Forkhead box protein M1

Alternative name(s):
Forkhead-related protein FKHL16
Hepatocyte nuclear factor 3 forkhead homolog 11
Short name=HFH-11
Short name=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

Gene names

Name:	FOXM1
Synonyms:	FKHL16, HFH11, MPP2, WIN

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	763 AA.
Sequence status	Complete.
Protein existence	Evidence 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.6 Ref.7 Ref.10
Subcellular location	Nucleus.
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.
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. Ref.6 Ref.7
Sequence similarities	Contains 1 fork-head DNA-binding domain.

Ontologies

Keywords
Biological process	Cell cycle DNA damage DNA repair Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	DNA-binding
Molecular function	Activator
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Inferred from mutant phenotype Ref.6. Source: UniProtKB DNA repair Inferred from electronic annotation. Source: UniProtKB-KW G2/M transition of mitotic cell cycle Inferred from direct assay Ref.7. Source: UniProtKB cell cycle Traceable author statement PubMed 10523841. Source: UniProtKB embryo development Inferred from Biological aspect of Ancestor. Source: RefGenome liver development Inferred from Biological aspect of Ancestor. Source: RefGenome negative regulation of cell aging Inferred from mutant phenotype PubMed 19696738. Source: UniProtKB negative regulation of stress-activated MAPK cascade Inferred from mutant phenotype PubMed 19696738. Source: BHF-UCL negative regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype PubMed 20531406. Source: BHF-UCL pattern specification process Inferred from Biological aspect of Ancestor. Source: RefGenome positive regulation of cell proliferation Inferred from mutant phenotype PubMed 19696738. Source: BHF-UCL positive regulation of double-strand break repair Inferred from mutant phenotype Ref.6. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.7. Source: UniProtKB regulation of Ras protein signal transduction Inferred from mutant phenotype PubMed 19696738. Source: BHF-UCL regulation of cell cycle arrest Inferred from mutant phenotype PubMed 19696738. Source: BHF-UCL regulation of cell growth Traceable author statement PubMed 10523841. Source: UniProtKB regulation of cell proliferation Non-traceable author statement PubMed 9441747. Source: UniProtKB regulation of reactive oxygen species metabolic process Inferred from mutant phenotype PubMed 19696738. Source: BHF-UCL 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 direct assay Ref.1. Source: UniProtKB vasculogenesis Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA transcription factor complex Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	DNA binding Inferred from direct assay Ref.1. 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 domain specific binding Inferred from Biological aspect of Ancestor. Source: RefGenome sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro sequence-specific DNA binding transcription factor activity Inferred from direct assay PubMed 10523841Ref.1. Source: UniProtKB transcription factor binding Inferred from Biological aspect of Ancestor. Source: RefGenome transcription regulatory region DNA binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDK6	Q00534	2	EBI-866499,EBI-295663
CTNNB1	P35222	16	EBI-866480,EBI-491549
E7	P03129	3	EBI-866499,EBI-866453	From a different organism.
FOXO3	O43524	2	EBI-866480,EBI-1644164

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: 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.

Isoform 1 (identifier: Q08050-1)

Also known as: FoxM1C; FOXM1-c;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q08050-2)

Also known as: FoxM1B; FOXM1-b;

The sequence of this isoform differs from the canonical sequence as follows:
     326-340: Missing.

Isoform 4 (identifier: Q08050-3)

Also known as: FoxM1A; FOXM1-a;

The sequence of this isoform differs from the canonical sequence as follows:
     423-423: V → VFGEQVVFGYMSKFFSGDLRDFGTPITSLFNFIFLCLSV

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 763

763

Forkhead box protein M1

PRO_0000091863

Regions

DNA binding

235 – 327

93

Fork-head

Compositional bias

480 – 513

34

Glu/Pro/Ser/Thr-rich

Amino acid modifications

Modified residue

331

1

Phosphoserine Ref.8

Modified residue

376

1

Phosphoserine; by CHEK2 Ref.6

Modified residue

611

1

Phosphothreonine; by CDK1 Ref.7

Modified residue

620

1

Phosphothreonine Ref.8

Modified residue

627

1

Phosphothreonine Ref.8

Modified residue

662

1

Phosphothreonine Probable

Modified residue

693

1

Phosphoserine; by CDK1 Ref.7

Modified residue

730

1

Phosphoserine; by PLK1 Ref.7 Ref.9

Modified residue

739

1

Phosphoserine; by PLK1 Ref.7 Ref.9

Natural variations

Alternative sequence

326 – 340

15

Missing in isoform 2.

VSP_001547

Alternative sequence

423

1

V → VFGEQVVFGYMSKFFSGDLR DFGTPITSLFNFIFLCLSV in isoform 4.

VSP_001548

Natural variant

402

1

A → E. Ref.3
Corresponds to variant rs28990715 [ dbSNP | Ensembl ].

VAR_025239

Natural variant

450

1

F → L. Ref.3
Corresponds to variant rs28919868 [ dbSNP | Ensembl ].

VAR_025240

Natural variant

643

1

S → P. Ref.3 Ref.4
Corresponds to variant rs3742076 [ dbSNP | Ensembl ].

VAR_020024

Natural variant

669

1

P → R. Ref.3
Corresponds to variant rs28919869 [ dbSNP | Ensembl ].

VAR_025241

Natural variant

673

1

P → L. Ref.3
Corresponds to variant rs28919870 [ dbSNP | Ensembl ].

VAR_025242

Experimental info

Mutagenesis

611

1

T → A: Prevents phosphorylation by CDK1 and subsequent binding of POLO box domains of PLK1; when associated with A-693. Ref.7

Mutagenesis

693

1

S → A: Prevents phosphorylation by CDK1 and subsequent binding of POLO box domains of PLK1; when associated with A-611. Ref.7

Mutagenesis

730

1

S → A: Prevents phosphorylation by PLK1 and impairs transcription activity; when associated with A-739. Ref.7

Mutagenesis

739

1

S → A: Prevents phosphorylation by PLK1 and impairs transcription activity; when associated with A-730. Ref.7

Sequence conflict

3

1

T → A in AAC63595. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

763

Helix Strand Turn

Details...

Helix

241 – 250

10

Beta strand

255 – 257

3

Helix

259 – 269

11

Helix

272 – 275

4

Helix

281 – 291

11

Beta strand

295 – 299

5

Beta strand

306 – 310

5

Turn

312 – 314

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (FoxM1C) (FOXM1-c) [UniParc]. Last modified December 1, 2000. Version 3. Checksum: 963CAC8FE7498E9B	FASTA	763	84,283
	10 20 30 40 50 60 MKTSPRRPLI LKRRRLPLPV QNAPSETSEE EPKRSPAQQE SNQAEASKEV AESNSCKFPA 70 80 90 100 110 120 GIKIINHPTM PNTQVVAIPN NANIHSIITA LTAKGKESGS SGPNKFILIS CGGAPTQPPG 130 140 150 160 170 180 LRPQTQTSYD AKRTEVTLET LGPKPAARDV NLPRPPGALC EQKRETCADG EAAGCTINNS 190 200 210 220 230 240 LSNIQWLRKM SSDGLGSRSI KQEMEEKENC HLEQRQVKVE EPSRPSASWQ NSVSERPPYS 250 260 270 280 290 300 YMAMIQFAIN STERKRMTLK DIYTWIEDHF PYFKHIAKPG WKNSIRHNLS LHDMFVRETS 310 320 330 340 350 360 ANGKVSFWTI HPSANRYLTL DQVFKPLDPG SPQLPEHLES QQKRPNPELR RNMTIKTELP 370 380 390 400 410 420 LGARRKMKPL LPRVSSYLVP IQFPVNQSLV LQPSVKVPLP LAASLMSSEL ARHSKRVRIA 430 440 450 460 470 480 PKVLLAEEGI APLSSAGPGK EEKLLFGEGF SPLLPVQTIK EEEIQPGEEM PHLARPIKVE 490 500 510 520 530 540 SPPLEEWPSP APSFKEESSH SWEDSSQSPT PRPKKSYSGL RSPTRCVSEM LVIQHRERRE 550 560 570 580 590 600 RSRSRRKQHL LPPCVDEPEL LFSEGPSTSR WAAELPFPAD SSDPASQLSY SQEVGGPFKT 610 620 630 640 650 660 PIKETLPISS TPSKSVLPRT PESWRLTPPA KVGGLDFSPV QTSQGASDPL PDPLGLMDLS 670 680 690 700 710 720 TTPLQSAPPL ESPQRLLSSE PLDLISVPFG NSSPSDIDVP KPGSPEPQVS GLAANRSLTE 730 740 750 760 GLVLDTMNDS LSKILLDISF PGLDEDPLGP DNINWSQFIP ELQ
	Isoform 2 (FoxM1B) (FOXM1-b) [UniParc]. Checksum: 3224A22B1434A531	FASTA	748	82,685
	10 20 30 40 50 60 MKTSPRRPLI LKRRRLPLPV QNAPSETSEE EPKRSPAQQE SNQAEASKEV AESNSCKFPA 70 80 90 100 110 120 GIKIINHPTM PNTQVVAIPN NANIHSIITA LTAKGKESGS SGPNKFILIS CGGAPTQPPG 130 140 150 160 170 180 LRPQTQTSYD AKRTEVTLET LGPKPAARDV NLPRPPGALC EQKRETCADG EAAGCTINNS 190 200 210 220 230 240 LSNIQWLRKM SSDGLGSRSI KQEMEEKENC HLEQRQVKVE EPSRPSASWQ NSVSERPPYS 250 260 270 280 290 300 YMAMIQFAIN STERKRMTLK DIYTWIEDHF PYFKHIAKPG WKNSIRHNLS LHDMFVRETS 310 320 330 340 350 360 ANGKVSFWTI HPSANRYLTL DQVFKQQKRP NPELRRNMTI KTELPLGARR KMKPLLPRVS 370 380 390 400 410 420 SYLVPIQFPV NQSLVLQPSV KVPLPLAASL MSSELARHSK RVRIAPKVLL AEEGIAPLSS 430 440 450 460 470 480 AGPGKEEKLL FGEGFSPLLP VQTIKEEEIQ PGEEMPHLAR PIKVESPPLE EWPSPAPSFK 490 500 510 520 530 540 EESSHSWEDS SQSPTPRPKK SYSGLRSPTR CVSEMLVIQH RERRERSRSR RKQHLLPPCV 550 560 570 580 590 600 DEPELLFSEG PSTSRWAAEL PFPADSSDPA SQLSYSQEVG GPFKTPIKET LPISSTPSKS 610 620 630 640 650 660 VLPRTPESWR LTPPAKVGGL DFSPVQTSQG ASDPLPDPLG LMDLSTTPLQ SAPPLESPQR 670 680 690 700 710 720 LLSSEPLDLI SVPFGNSSPS DIDVPKPGSP EPQVSGLAAN RSLTEGLVLD TMNDSLSKIL 730 740 LDISFPGLDE DPLGPDNINW SQFIPELQ
	Isoform 4 (FoxM1A) (FOXM1-a) [UniParc]. Checksum: 82416A3FA271C5D5	FASTA	801	88,596
	10 20 30 40 50 60 MKTSPRRPLI LKRRRLPLPV QNAPSETSEE EPKRSPAQQE SNQAEASKEV AESNSCKFPA 70 80 90 100 110 120 GIKIINHPTM PNTQVVAIPN NANIHSIITA LTAKGKESGS SGPNKFILIS CGGAPTQPPG 130 140 150 160 170 180 LRPQTQTSYD AKRTEVTLET LGPKPAARDV NLPRPPGALC EQKRETCADG EAAGCTINNS 190 200 210 220 230 240 LSNIQWLRKM SSDGLGSRSI KQEMEEKENC HLEQRQVKVE EPSRPSASWQ NSVSERPPYS 250 260 270 280 290 300 YMAMIQFAIN STERKRMTLK DIYTWIEDHF PYFKHIAKPG WKNSIRHNLS LHDMFVRETS 310 320 330 340 350 360 ANGKVSFWTI HPSANRYLTL DQVFKPLDPG SPQLPEHLES QQKRPNPELR RNMTIKTELP 370 380 390 400 410 420 LGARRKMKPL LPRVSSYLVP IQFPVNQSLV LQPSVKVPLP LAASLMSSEL ARHSKRVRIA 430 440 450 460 470 480 PKVFGEQVVF GYMSKFFSGD LRDFGTPITS LFNFIFLCLS VLLAEEGIAP LSSAGPGKEE 490 500 510 520 530 540 KLLFGEGFSP LLPVQTIKEE EIQPGEEMPH LARPIKVESP PLEEWPSPAP SFKEESSHSW 550 560 570 580 590 600 EDSSQSPTPR PKKSYSGLRS PTRCVSEMLV IQHRERRERS RSRRKQHLLP PCVDEPELLF 610 620 630 640 650 660 SEGPSTSRWA AELPFPADSS DPASQLSYSQ EVGGPFKTPI KETLPISSTP SKSVLPRTPE 670 680 690 700 710 720 SWRLTPPAKV GGLDFSPVQT SQGASDPLPD PLGLMDLSTT PLQSAPPLES PQRLLSSEPL 730 740 750 760 770 780 DLISVPFGNS SPSDIDVPKP GSPEPQVSGL AANRSLTEGL VLDTMNDSLS KILLDISFPG 790 800 LDEDPLGPDN INWSQFIPEL Q

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Hepatocyte nuclear factor 3/fork head homolog 11 is expressed in proliferating epithelial and mesenchymal cells of embryonic and adult tissues." Ye H., Kelly T.F., Samadani U., Lim L., Rubio S., Overdier D.G., Roebuck K.A., Costa R.H. Mol. Cell. Biol. 17:1626-1641(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 4). Tissue: Colon carcinoma.
[2]	"Molecular analysis of a novel winged helix protein, WIN. Expression pattern, DNA binding property, and alternative splicing within the DNA binding domain." Yao K.-M., Sha M., Lu Z., Wong G.G. J. Biol. Chem. 272:19827-19836(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Pancreatic carcinoma and Testis.
[3]	NIEHS SNPs program Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLU-402; LEU-450; PRO-643; ARG-669 AND LEU-673.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT PRO-643. Tissue: Lung, Ovary and Skin.
[5]	"Cloning of cDNAs for M-phase phosphoproteins recognized by the MPM2 monoclonal antibody and determination of the phosphorylated epitope." Westendorf J.M., Rao P.N., Gerace L. Proc. Natl. Acad. Sci. U.S.A. 91:714-718(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 543-763. Tissue: Lymphoblast.
[6]	"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, PHOSPHORYLATION AT SER-376 BY CHEK2.
[7]	"Plk1-dependent phosphorylation of FoxM1 regulates a transcriptional programme required for mitotic progression." Fu Z., Malureanu L., Huang J., Wang W., Li H., van Deursen J.M., Tindall D.J., Chen J. Nat. Cell Biol. 10:1076-1082(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION AT THR-611; SER-693; SER-730 AND SER-739, MUTAGENESIS OF THR-611; SER-693; SER-730 AND SER-739.
[8]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331; THR-620 AND THR-627, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." 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. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-730 AND SER-739, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Structure of the FoxM1 DNA-recognition domain bound to a promoter sequence." Littler D.R., Alvarez-Fernandez M., Stein A., Hibbert R.G., Heidebrecht T., Aloy P., Medema R.H., Perrakis A. Nucleic Acids Res. 38:4527-4538(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 222-360 IN COMPLEX WITH PROMOTER DNA, FUNCTION.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U74612 mRNA. Translation: AAC51128.1.
U74613 mRNA. Translation: AAC51129.1.
U83113 mRNA. Translation: AAC63595.1.
DQ022289 Genomic DNA. Translation: AAY26401.1.
BC006192 mRNA. Translation: AAH06192.1.
BC006529 mRNA. Translation: AAH06529.1.
BC012863 mRNA. Translation: AAH12863.1.
L16783 mRNA. Translation: AAC37541.1.

IPI

IPI00032162.
IPI00216686.
IPI00401044.

PIR

B36881.

RefSeq

NP_001230017.1. NM_001243088.1.
NP_001230018.1. NM_001243089.1.
NP_068772.2. NM_021953.3.
NP_973731.1. NM_202002.2.
NP_973732.1. NM_202003.2.

UniGene

Hs.239.
Hs.735243.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3G73	X-ray	2.21	A/B	222-360	[»]

ProteinModelPortal

Q08050.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q08050. 11 interactions.

MINT

MINT-107757.

STRING

9606.ENSP00000342307.

PTM databases

PhosphoSite

Q08050.

Polymorphism databases

DMDM

12644391.

Proteomic databases

PaxDb

Q08050.

PRIDE

Q08050.

Protocols and materials databases

DNASU

2305.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000342628; ENSP00000342307; ENSG00000111206.
ENST00000359843; ENSP00000352901; ENSG00000111206.
ENST00000361953; ENSP00000354492; ENSG00000111206.

GeneID

2305.

KEGG

hsa:2305.

UCSC

uc001qle.3. human.
uc001qlf.3. human.
uc001qlg.3. human.

Organism-specific databases

CTD

2305.

GeneCards

GC12M002966.

HGNC

HGNC:3818. FOXM1.

HPA

CAB017832.
HPA029974.
HPA029975.
HPA029976.

MIM

602341. gene.

neXtProt

NX_Q08050.

PharmGKB

PA28236.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5025.

HOGENOM

HOG000112633.

HOVERGEN

HBG051652.

KO

K09406.

OMA

GARRKMK.

Enzyme and pathway databases

Pathway_Interaction_DB

foxm1pathway. FOXM1 transcription factor network.

Gene expression databases

ArrayExpress

Q08050.

Bgee

Q08050.

CleanEx

HS_FOXM1.
HS_MPP2.

Genevestigator

Q08050.

GermOnline

ENSG00000111206. Homo sapiens.

Family and domain databases

Gene3D

1.10.10.10. 1 hit.

InterPro

IPR001766. TF_fork_head.
IPR018122. TF_fork_head_CS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]

Pfam

PF00250. Fork_head. 1 hit.
[Graphical view]

PRINTS

PR00053. FORKHEAD.

SMART

SM00339. FH. 1 hit.
[Graphical view]

PROSITE

PS00657. FORK_HEAD_1. 1 hit.
PS00658. FORK_HEAD_2. 1 hit.
PS50039. FORK_HEAD_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q08050.

GenomeRNAi

2305.

NextBio

9359.

SOURCE

Search...

Entry information

Entry name

FOXM1_HUMAN

Accession

Primary (citable) accession number: Q08050
Secondary accession number(s): O43258 , O43259, O43260, Q4ZGG7, Q9BRL2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	December 1, 2000
Last modified:	May 1, 2013
This is version 141 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.