FOXM1_XENLA
ID FOXM1_XENLA Reviewed; 759 AA.
AC Q5W1J6;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Forkhead box protein M1;
DE AltName: Full=XlFoxM1;
GN Name=foxm1 {ECO:0000312|EMBL:CAH68560.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAH68560.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Embryo {ECO:0000269|PubMed:15744668};
RX PubMed=15744668; DOI=10.1387/ijdb.051977bp;
RA Pohl B.S., Roessner A., Knoechel W.;
RT "The Fox gene family in Xenopus laevis: FoxI2, FoxM1 and FoxP1 in early
RT development.";
RL Int. J. Dev. Biol. 49:53-58(2005).
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:0000305}.
CC -!- TISSUE SPECIFICITY: Localized to the animal hemisphere of early
CC cleavage stage embryos. During neurulation, expressed in the neural
CC folds. Later, expressed in the spinal cord and in the eye field. During
CC tailbud stages, expression is still restricted to the neuroectoderm,
CC predominantly to the hindbrain, the eye and the spinal cord. With
CC ongoing development, expression is also found at lower levels in the
CC branchial arches. At stage 35, expressed in the rhombencephalon and in
CC the eye retina. {ECO:0000269|PubMed:15744668}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Maternal levels decrease rapidly until the blastula stage. Absent from
CC gastrula stage embryos and then zygotic expression starts during
CC neurulation and persists until the end of organogenesis.
CC {ECO:0000269|PubMed:15744668}.
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DR EMBL; AJ853462; CAH68560.1; -; mRNA.
DR RefSeq; NP_001089001.1; NM_001095532.1.
DR AlphaFoldDB; Q5W1J6; -.
DR SMR; Q5W1J6; -.
DR GeneID; 496385; -.
DR KEGG; xla:496385; -.
DR CTD; 496385; -.
DR Xenbase; XB-GENE-854084; foxm1.S.
DR OrthoDB; 1270467at2759; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 496385; Expressed in blastula and 17 other tissues.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IEA:InterPro.
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; 2.
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; Cell cycle; DNA damage; DNA repair; DNA-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..759
FT /note="Forkhead box protein M1"
FT /id="PRO_0000247731"
FT DNA_BIND 260..358
FT /note="Fork-head"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 596..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..450
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 759 AA; 84333 MW; 9EE352BA1C585305 CRC64;
MRTSPRRPLI LKRRKLSLPH QDATPCPGAS EQGKAAMMKT ANLPEQTLAH ELEDMAPKSK
ADQETPGQNE GGDTLGQSLA PTMRLPSNPP QSCPEDIPGF PSGVRIMGHP TMADAQLVII
PSQSNVQSII QALTARGKEQ GGPNKYIIIS SESAIQTQAW HQGPQIKEEE CVNSQSEATC
ISKQKPTGNS RKAKHRQEEQ LNASLSNIQW LGNMSSESLG QYSIKEEQED KENQIPECAK
MEEEPQSFPD PQWPLSVTER PPYSYMALIQ FAINSTPRKR MTLKDIYTWI EDHFPYFKHV
AKPGWKNSIR HNLSLHDMFV RESEANNKVS YWTIHPQANR CLTLDQVFKT ASPMSPADNE
PQKKMIPDIR KSFQSAACAS NKERKMKPLL PRVNSYLIPV HFPVAQPVLL PALEPYAFGA
ESSDGQQSSK RVKIAPKATA DDGESPKHLG LCSVKEEPDI SNLKCEDLFQ CKRVSSSRRK
QQLLPPHSEE PELVLPESIA SDSGLDTDFS FIQDASANPN QNLTSHPTQN CPSNVTQEGL
LHLTHDGPSY LTQVSSSHFT QDDPCQFTKD DTFYFTQDNP IQLTQDEDYT FKTPIKEHFS
KPTTSSTPSK PTDTGLLQPW ESETSLPRDP VLDFSPVRIP QGSTFTPFKD NLGTLSFGDT
PFKDFGIFGS PQNLLNALSP ASSPLLRLES PCVSRQQKRC SKELQVGASA NRSLLEGLVL
DTVDDSLSKI LLDISFSGME EGNGLEVDGV WSQFLPEFK
