ID   E2F2_MOUSE              Reviewed;         443 AA.
AC   P56931; A2AW43; Q8BID0;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 2.
DT   27-MAR-2024, entry version 175.
DE   RecName: Full=Transcription factor E2F2;
DE            Short=E2F-2;
GN   Name=E2f2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Eye;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PRELIMINARY NUCLEOTIDE SEQUENCE OF 49-254, AND DEVELOPMENTAL STAGE.
RC   TISSUE=Embryo;
RX   PubMed=9149906;
RA   Dagnino L., Fry C.J., Bartley S.M., Farnham P., Gallie B.L., Phillips R.A.;
RT   "Expression patterns of the E2F family of transcription factors during
RT   murine epithelial development.";
RL   Cell Growth Differ. 8:553-563(1997).
RN   [5]
RP   DEVELOPMENTAL STAGE.
RX   PubMed=9376316; DOI=10.1016/s0925-4773(97)00083-x;
RA   Dagnino L., Fry C.J., Bartley S.M., Farnham P., Gallie B.L., Phillips R.A.;
RT   "Expression patterns of the E2F family of transcription factors during
RT   mouse nervous system development.";
RL   Mech. Dev. 66:13-25(1997).
RN   [6]
RP   INTERACTION WITH EAPP.
RX   PubMed=15716352; DOI=10.1091/mbc.e04-11-0975;
RA   Novy M., Pohn R., Andorfer P., Novy-Weiland T., Galos B., Schwarzmayr L.,
RA   Rotheneder H.;
RT   "EAPP, a novel E2F binding protein that modulates E2F-dependent
RT   transcription.";
RL   Mol. Biol. Cell 16:2181-2190(2005).
CC   -!- FUNCTION: Transcription activator that binds DNA cooperatively with DP
CC       proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in
CC       the promoter region of a number of genes whose products are involved in
CC       cell cycle regulation or in DNA replication. The DRTF1/E2F complex
CC       functions in the control of cell-cycle progression from g1 to s phase.
CC       E2F2 binds specifically to RB1 in a cell-cycle dependent manner.
CC   -!- SUBUNIT: Component of the DRTF1/E2F transcription factor complex. Forms
CC       heterodimers with DP family members. The E2F2 complex binds
CC       specifically hypophosphorylated retinoblastoma protein RB1. During the
CC       cell cycle, RB1 becomes phosphorylated in mid-to-late G1 phase,
CC       detaches from the DRTF1/E2F complex, rendering E2F transcriptionally
CC       active. Viral oncoproteins, notably E1A, T-antigen and HPV E7, are
CC       capable of sequestering RB protein, thus releasing the active complex.
CC       Binds EAPP.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the developing epidermis and
CC       intestinal epithelium. First detected in the epidermis at stage 13.5-
CC       14.5 dpc with higher levels in the head and thorax regions. At 15.5
CC       dpc, expression is found in both the epithelium and, to a lesser extent
CC       in the underlying mesenchyme. At day 16.5 dpc, high expression in the
CC       basal cells. Later expression is found in the developing hair
CC       follicles, around the dermal papillae. In the developing intestinal
CC       epithelium, expression first observed around 14.5 dpc. Levels continue
CC       to increase at least until 19.5 dpc, with highest levels in the
CC       intervillus epithelium and in the bottom half of the villi. In the
CC       nervous system, first expressed at 9.5 dpc, in the forebrain. At 10.5
CC       dpc, expressed broadly in the brain, and at lower levels in the upper
CC       regions of the spinal cord. By 11.5 dpc, E2F2 expression is found
CC       throughout the central nervous system and levels peak at 12.5-15.5 dpc.
CC       In the developing spinal cord, E2F2 expression found only in the dorsal
CC       region. In the developing retina, highest expression found in the 14.5-
CC       18.5 dpc embryonic retinoblastic cell layer. In other developing
CC       tissues, E2F2 is found highest in thymus and liver, with lower
CC       expression in lung, heart, kidney and skeletal muscle. Also found in
CC       choroid plexus and chondrocytes. {ECO:0000269|PubMed:9149906,
CC       ECO:0000269|PubMed:9376316}.
CC   -!- PTM: Phosphorylated by CDK2 and cyclin A-CDK2 in the S-phase.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}.
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DR   EMBL; AK087452; BAC39881.1; -; mRNA.
DR   EMBL; AL935264; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC062101; AAH62101.1; -; mRNA.
DR   CCDS; CCDS18801.1; -.
DR   RefSeq; NP_001292328.1; NM_001305399.1.
DR   RefSeq; NP_808401.1; NM_177733.7.
DR   AlphaFoldDB; P56931; -.
DR   SMR; P56931; -.
DR   BioGRID; 232447; 3.
DR   ComplexPortal; CPX-176; E2F2-DP1 transcription factor complex.
DR   ComplexPortal; CPX-177; RB1-E2F2-DP1 transcription repressor complex.
DR   CORUM; P56931; -.
DR   DIP; DIP-48416N; -.
DR   IntAct; P56931; 3.
DR   STRING; 10090.ENSMUSP00000050047; -.
DR   iPTMnet; P56931; -.
DR   PhosphoSitePlus; P56931; -.
DR   EPD; P56931; -.
DR   jPOST; P56931; -.
DR   PaxDb; 10090-ENSMUSP00000050047; -.
DR   ProteomicsDB; 277699; -.
DR   Antibodypedia; 4274; 392 antibodies from 36 providers.
DR   DNASU; 242705; -.
DR   Ensembl; ENSMUST00000061721.6; ENSMUSP00000050047.6; ENSMUSG00000018983.10.
DR   GeneID; 242705; -.
DR   KEGG; mmu:242705; -.
DR   UCSC; uc008vht.3; mouse.
DR   AGR; MGI:1096341; -.
DR   CTD; 1870; -.
DR   MGI; MGI:1096341; E2f2.
DR   VEuPathDB; HostDB:ENSMUSG00000018983; -.
DR   eggNOG; KOG2577; Eukaryota.
DR   GeneTree; ENSGT00940000160992; -.
DR   HOGENOM; CLU_032091_0_0_1; -.
DR   InParanoid; P56931; -.
DR   OMA; WVGRGIF; -.
DR   OrthoDB; 1761at2759; -.
DR   PhylomeDB; P56931; -.
DR   TreeFam; TF105566; -.
DR   Reactome; R-MMU-69231; Cyclin D associated events in G1.
DR   BioGRID-ORCS; 242705; 7 hits in 62 CRISPR screens.
DR   ChiTaRS; E2f2; mouse.
DR   PRO; PR:P56931; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; P56931; Protein.
DR   Bgee; ENSMUSG00000018983; Expressed in blood and 168 other cell types or tissues.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0035189; C:Rb-E2F complex; ISS:ComplexPortal.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR   GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; IDA:MGI.
DR   GO; GO:1990086; P:lens fiber cell apoptotic process; IDA:MGI.
DR   GO; GO:1903671; P:negative regulation of sprouting angiogenesis; ISO:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0051726; P:regulation of cell cycle; IDA:MGI.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd14660; E2F_DD; 1.
DR   Gene3D; 6.10.250.540; -; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR015633; E2F.
DR   InterPro; IPR037241; E2F-DP_heterodim.
DR   InterPro; IPR032198; E2F_CC-MB.
DR   InterPro; IPR003316; E2F_WHTH_DNA-bd_dom.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR12081; TRANSCRIPTION FACTOR E2F; 1.
DR   PANTHER; PTHR12081:SF50; TRANSCRIPTION FACTOR E2F2; 1.
DR   Pfam; PF16421; E2F_CC-MB; 1.
DR   Pfam; PF02319; E2F_TDP; 1.
DR   SMART; SM01372; E2F_TDP; 1.
DR   SUPFAM; SSF144074; E2F-DP heterodimerization region; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   Genevisible; P56931; MM.
PE   1: Evidence at protein level;
KW   Activator; Cell cycle; DNA-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..443
FT                   /note="Transcription factor E2F2"
FT                   /id="PRO_0000219465"
FT   DNA_BIND        109..198
FT                   /evidence="ECO:0000255"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          67..107
FT                   /note="Cyclin A/CDK2 binding"
FT                   /evidence="ECO:0000255"
FT   REGION          157..178
FT                   /note="Leucine-zipper"
FT   REGION          199..291
FT                   /note="Dimerization"
FT                   /evidence="ECO:0000255"
FT   REGION          306..341
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          361..443
FT                   /note="Transactivation"
FT                   /evidence="ECO:0000255"
FT   REGION          416..433
FT                   /note="Retinoblastoma protein binding"
FT                   /evidence="ECO:0000255"
FT   MOTIF           162..198
FT                   /note="DEF box"
SQ   SEQUENCE   443 AA;  48499 MW;  DFC8158E5A8254F0 CRC64;
     MLRAPRTLAP ATAQPTKSLP ALNPTELWPS GLSSPQLCPA TTATTYYTSL YTQTVPSSVA
     LGTCLDATPH GPEGQIVRCA PAGRLPAKRK LDLEGIGRPT VPEFRTPKGK CIRVDGLPSP
     KTPKSPGEKT RYDTSLGLLT KKFIYLLSES EDGVLDLNWA AEVLDVQKRR IYDITNVLEG
     IQLIRKKSKN NIQWVGRELF EDPTRPSRQQ QLGQELKELM NAEQTLDQLI QSCSLSFKHL
     TEDNANKKLA YVTYQDIRAV GNFKEQTVIA VKAPPQTRLE VPDRAEENLQ IYLKSTQGPI
     EVYLCPEEGQ EPDSPAKEAL PSTSALSPIP DCAQPGCSTD SGIAETIEPS VLIPQPIPPP
     PPPPLPPAPS LVPLEATDNM LELSHPLLQQ TEDQFLSPIL AANSPLISFS PPLDQDEYLW
     GMDEGEGISD LFDSYDLGDL LIN
//