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E2F5_MOUSE
ID   E2F5_MOUSE              Reviewed;         335 AA.
AC   Q61502; Q99LK0;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   03-AUG-2022, entry version 167.
DE   RecName: Full=Transcription factor E2F5;
DE            Short=E2F-5;
GN   Name=E2f5;
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 [MRNA].
RX   PubMed=7542760;
RA   Buck V., Allen K.E., Soerensen T., Bybee A., Hijmans E.M., Voorhoeve P.M.,
RA   Bernards R., la Thangue N.B.;
RT   "Molecular and functional characterisation of E2F-5, a new member of the
RT   E2F family.";
RL   Oncogene 11:31-38(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=NOD; TISSUE=Spleen;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
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   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   [5]
RP   DEVELOPMENTAL STAGE.
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).
CC   -!- FUNCTION: Transcriptional activator that binds to E2F sites, these
CC       sites are present in the promoter of many genes whose products are
CC       involved in cell proliferation. May mediate growth factor-initiated
CC       signal transduction. It is likely involved in the early responses of
CC       resting cells to growth factor stimulation. Specifically required for
CC       multiciliate cell differentiation: together with MCIDAS and E2F5, binds
CC       and activate genes required for centriole biogenesis.
CC       {ECO:0000250|UniProtKB:Q6DE14}.
CC   -!- SUBUNIT: Component of the DRTF1/E2F transcription factor complex. Binds
CC       cooperatively with DP-1 to E2F sites. Interaction with retinoblastoma
CC       protein RB1 or proteins RBL1 and RBL2 inhibits the E2F transactivation
CC       domain. Component of the DREAM complex (also named LINC complex) at
CC       least composed of E2F4, E2F5, LIN9, LIN37, LIN52, LIN54, MYBL1, MYBL2,
CC       RBL1, RBL2, RBBP4, TFDP1 and TFDP2. The complex exists in quiescent
CC       cells where it represses cell cycle-dependent genes. It dissociates in
CC       S phase when LIN9, LIN37, LIN52 and LIN54 form a subcomplex that binds
CC       to MYBL2 (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q61502; Q64163-4: Tfdp2; NbExp=2; IntAct=EBI-7225685, EBI-8077763;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- DEVELOPMENTAL STAGE: In the developing epidermis, first detected in
CC       13.5-14.5 dpc embryos. With the appearance of stratified epithelium,
CC       levels of E2F5 expression increase and by 16.5 dpc, high expression
CC       found in the suprabasal cell layers. High expression also found in
CC       other regions with stratified squamous epithelia including the
CC       developing palate, lip and tongue. In the developing nervous system,
CC       first detected in the forebrain at 9.5 dpc. At 10.5 dpc, strongly
CC       expressed in the rostral region of the spinal cord. By 11.5 dpc, E2F5
CC       is expressed throughout the developing central nervous system. In 12.5-
CC       15.5 dpc embryos, expression found in the undifferentiated ventricular
CC       regions of the brain. In the retina, expressed, in 14.5-18.5 dpc
CC       embryos, in the retinoblastic cell layer. In other developing tissues,
CC       highly expressed in the choroid plexus. Also found in the kidney,
CC       liver, lung, heart and weakly, in developing skeletal muscle and
CC       chondrocytes. {ECO:0000269|PubMed:9149906, ECO:0000269|PubMed:9376316}.
CC   -!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}.
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DR   EMBL; X86925; CAA60508.1; -; mRNA.
DR   EMBL; AK156760; BAE33842.1; -; mRNA.
DR   EMBL; BC003220; AAH03220.1; -; mRNA.
DR   CCDS; CCDS38391.1; -.
DR   PIR; I48338; I48338.
DR   RefSeq; NP_031918.2; NM_007892.2.
DR   AlphaFoldDB; Q61502; -.
DR   SMR; Q61502; -.
DR   BioGRID; 199352; 4.
DR   CORUM; Q61502; -.
DR   IntAct; Q61502; 3.
DR   MINT; Q61502; -.
DR   STRING; 10090.ENSMUSP00000127877; -.
DR   iPTMnet; Q61502; -.
DR   PhosphoSitePlus; Q61502; -.
DR   MaxQB; Q61502; -.
DR   PaxDb; Q61502; -.
DR   PeptideAtlas; Q61502; -.
DR   PRIDE; Q61502; -.
DR   ProteomicsDB; 277433; -.
DR   Antibodypedia; 6582; 212 antibodies from 29 providers.
DR   DNASU; 13559; -.
DR   Ensembl; ENSMUST00000029069; ENSMUSP00000029069; ENSMUSG00000027552.
DR   GeneID; 13559; -.
DR   KEGG; mmu:13559; -.
DR   UCSC; uc008oqk.1; mouse.
DR   CTD; 1875; -.
DR   MGI; MGI:105091; E2f5.
DR   VEuPathDB; HostDB:ENSMUSG00000027552; -.
DR   eggNOG; KOG2577; Eukaryota.
DR   GeneTree; ENSGT00940000157353; -.
DR   HOGENOM; CLU_032091_2_0_1; -.
DR   InParanoid; Q61502; -.
DR   OrthoDB; 1087250at2759; -.
DR   Reactome; R-MMU-1538133; G0 and Early G1.
DR   Reactome; R-MMU-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR   Reactome; R-MMU-69231; Cyclin D associated events in G1.
DR   BioGRID-ORCS; 13559; 2 hits in 73 CRISPR screens.
DR   ChiTaRS; E2f5; mouse.
DR   PRO; PR:Q61502; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q61502; protein.
DR   Bgee; ENSMUSG00000027552; Expressed in animal zygote and 254 other tissues.
DR   ExpressionAtlas; Q61502; baseline and differential.
DR   Genevisible; Q61502; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR   GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0005635; C:nuclear envelope; TAS:MGI.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IBA:GO_Central.
DR   GO; GO:0016528; C:sarcoplasm; ISO:MGI.
DR   GO; GO:0001216; F:DNA-binding transcription activator activity; 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:0009887; P:animal organ morphogenesis; IMP:MGI.
DR   GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:MGI.
DR   GO; GO:0051726; P:regulation of cell cycle; TAS:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR   CDD; cd14660; E2F_DD; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR015633; E2F.
DR   InterPro; IPR037241; E2F-DP_heterodim.
DR   InterPro; IPR028316; E2F5.
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; PTHR12081; 2.
DR   PANTHER; PTHR12081:SF35; PTHR12081:SF35; 2.
DR   Pfam; PF16421; E2F_CC-MB; 1.
DR   Pfam; PF02319; E2F_TDP; 1.
DR   SMART; SM01372; E2F_TDP; 1.
DR   SUPFAM; SSF144074; SSF144074; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
PE   1: Evidence at protein level;
KW   Activator; Cilium biogenesis/degradation; DNA-binding; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..335
FT                   /note="Transcription factor E2F5"
FT                   /id="PRO_0000219470"
FT   DNA_BIND        37..108
FT                   /evidence="ECO:0000255"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          66..88
FT                   /note="Leucine-zipper"
FT   REGION          109..205
FT                   /note="Dimerization"
FT                   /evidence="ECO:0000255"
FT   REGION          226..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          277..335
FT                   /note="Transactivation"
FT                   /evidence="ECO:0000255"
FT   REGION          312..329
FT                   /note="RBL2 association"
FT                   /evidence="ECO:0000255"
FT   MOTIF           71..108
FT                   /note="DEF box"
FT   COMPBIAS        240..284
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        32..35
FT                   /note="AALA -> RRSR (in Ref. 1; CAA60508)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   335 AA;  36555 MW;  7922ACE79C73944B CRC64;
     MAAAEPTSSA QPTPQAQAQP PPHGAPSSQP SAALAGGSSR HEKSLGLLTT KFVSLLQEAQ
     DGVLDLKAAA DTLAVRQKRR IYDITNVLEG IDLIEKKSKN SIQWKGVGAG CNTKEVIDRL
     RCLKAEIEDL ELKERELDQQ KLWLQQSIKN VMEDSINNRF SYVTHEDICN CFHGDTLLAI
     QAPSGTQLEV PIPEMGQNGQ KKYQINLKSH SGPIHVLLIN KESSSSKPVV FPVPPPDDLT
     QPSSQSSTSV TPQKSTMAAQ NLPEQHVSER SQTFQQTPAA EVSSGSISGD IIDELMSSDV
     FPLLRLSPTP ADDYNFNLDD NEGVCDLFDV QILNY
 
 
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