FOXM1_RAT
ID FOXM1_RAT Reviewed; 759 AA.
AC P97691;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Forkhead box protein M1;
DE AltName: Full=INS-1 winged helix;
DE AltName: Full=Winged-helix factor from INS-1 cells;
GN Name=Foxm1; Synonyms=Win;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC TISSUE=Insulinoma;
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).
CC -!- FUNCTION: Transcription factor regulating the expression of cell cycle
CC genes essential for DNA replication and mitosis. Plays a role in the
CC control of cell proliferation. Also plays a role in DNA break repair,
CC participating in the DNA damage checkpoint response. Promotes
CC transcription of PHB2. {ECO:0000250|UniProtKB:Q08050}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=P97691-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P97691-2; Sequence=VSP_001550;
CC Name=3;
CC IsoId=P97691-3; Sequence=VSP_001549;
CC Name=4;
CC IsoId=P97691-4; Sequence=Not described;
CC -!- TISSUE SPECIFICITY: Highly expressed in thymus and testis, but weakly
CC in intestine and lung. Appears to be expressed only in adult organs
CC containing proliferating/cycling cells or in response to growth
CC factors.
CC -!- DEVELOPMENTAL STAGE: Expressed from E12 day to neonate in developing
CC pancreas. Also expressed at E14 day in liver, thymus, testis and fat
CC (pregnant mother).
CC -!- INDUCTION: Activated in S phase.
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 (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: [Isoform 4]: Has been shown to exist only in human so
CC far. {ECO:0000305}.
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DR EMBL; U83112; AAC63594.1; -; mRNA.
DR AlphaFoldDB; P97691; -.
DR SMR; P97691; -.
DR STRING; 10116.ENSRNOP00000008003; -.
DR PaxDb; P97691; -.
DR UCSC; RGD:61807; rat. [P97691-1]
DR RGD; 61807; Foxm1.
DR eggNOG; KOG2294; Eukaryota.
DR InParanoid; P97691; -.
DR Reactome; R-RNO-156711; Polo-like kinase mediated events.
DR Reactome; R-RNO-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR PRO; PR:P97691; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:RGD.
DR GO; GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; ISO:RGD.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0001889; P:liver development; ISO:RGD.
DR GO; GO:0032873; P:negative regulation of stress-activated MAPK cascade; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:RGD.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; ISO:RGD.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:RGD.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0046578; P:regulation of Ras protein signal transduction; ISO:RGD.
DR GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0051591; P:response to cAMP; IEP:RGD.
DR GO; GO:0034698; P:response to gonadotropin; IEP:RGD.
DR GO; GO:0001570; P:vasculogenesis; ISO:RGD.
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 2: Evidence at transcript level;
KW Activator; Alternative splicing; Cell cycle; DNA damage; DNA repair;
KW DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..759
FT /note="Forkhead box protein M1"
FT /id="PRO_0000091865"
FT DNA_BIND 234..326
FT /note="Fork-head"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 681..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..552
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 330
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08050"
FT MOD_RES 375
FT /note="Phosphoserine; by CHEK2"
FT /evidence="ECO:0000250|UniProtKB:Q08050"
FT MOD_RES 521
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q08050"
FT MOD_RES 608
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q08050"
FT MOD_RES 624
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q08050"
FT MOD_RES 726
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:Q08050"
FT MOD_RES 735
FT /note="Phosphoserine; by PLK1"
FT /evidence="ECO:0000250|UniProtKB:Q08050"
FT CROSSLNK 200
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q08050"
FT CROSSLNK 324
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q08050"
FT CROSSLNK 355
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q08050"
FT CROSSLNK 421
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q08050"
FT CROSSLNK 439
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q08050"
FT VAR_SEQ 281
FT /note="K -> KCWHQAYHKLGPQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9242644"
FT /id="VSP_001549"
FT VAR_SEQ 325..339
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9242644"
FT /id="VSP_001550"
SQ SEQUENCE 759 AA; 83672 MW; 77231ED495840709 CRC64;
MRTSPRRPLI LKRRRLPLPI QNAPSETSEE EAKRSPGQQE PTQAQASQDV AESSSCKFPA
GIKIINHPTV PNTQVVAIPN NADIQSIITA LTAKGKESGS SGPNKFILIS SGGASSHPPD
PQSQAQTSTD SKRTELITET LGPKPGAKGV PVPKPPGALP RQRQESCGGE AAGCTLDNSL
TNIQWLGKMS SDGLGRCSIK QELEEKENCH LEQNRVKVEA PSRASVSWQD SVSERPPYSY
MAMIQFAINS TERKRMTLKD IYTWIEDHFP YFKHIAKPGW KNSIRHNLSL HDMFVRETSA
NGKVSFWTIH PSANRYLTLD QVFKPLEPGS PQSPEHLESQ QKRPNPELRR NVTIKTELPL
GARRKMKPLL PRVSSYLVPI QFPVNQSLVL QPSVKVPLPL AASLMSSELA RHSKRVRIAP
KVLLSNEGIA PLPATEPMKE EKPLLGEGLL PLLPIQSIKE EVIQPGEDIP HLERPIKVES
PPLEEWPSPC ASVKEELSNS WEDSSCSPTP KPKKSYCGLK SPTRCVSEML VTKRREKREV
SRSRRKQHLQ PPCLDEPELF FSEDSSTFRP AMEILAESSE PAPQLSCPQE EGGPFKTPIK
ETLPVSSTPS KSVLSRDPES WRLTPPAKVG GLDFSPVRTP QGAFGPLPDS LGLMELNTTP
LKSVPLFDSP RELLNSEAFD LASDPFSSSP PPHLEAKPGS PELQVPSLSA NRSLTEGLVL
DTMNDSLSKI LLDISFPGLE EDPLGPDNIN WSQFIPELR
