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E2F7_RAT
ID   E2F7_RAT                Reviewed;         902 AA.
AC   D4A4D7;
DT   09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Transcription factor E2F7;
DE            Short=E2F-7;
GN   Name=E2f7;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
CC   -!- FUNCTION: Atypical E2F transcription factor that participates in
CC       various processes such as angiogenesis, polyploidization of specialized
CC       cells and DNA damage response. Mainly acts as a transcription repressor
CC       that binds DNA independently of DP proteins and specifically recognizes
CC       the E2 recognition site 5'-TTTC[CG]CGC-3'. Directly represses
CC       transcription of classical E2F transcription factors such as E2F1. Acts
CC       as a regulator of S-phase by recognizing and binding the E2-related
CC       site 5'-TTCCCGCC-3' and mediating repression of G1/S-regulated genes.
CC       Plays a key role in polyploidization of cells in placenta and liver by
CC       regulating the endocycle, probably by repressing genes promoting
CC       cytokinesis and antagonizing action of classical E2F proteins (E2F1,
CC       E2F2 and/or E2F3). Required for placental development by promoting
CC       polyploidization of trophoblast giant cells. Also involved in DNA
CC       damage response: up-regulated by p53/TP53 following genotoxic stress
CC       and acts as a downstream effector of p53/TP53-dependent repression by
CC       mediating repression of indirect p53/TP53 target genes involved in DNA
CC       replication. Acts as a promoter of sprouting angiogenesis, possibly by
CC       acting as a transcription activator: associates with HIF1A, recognizes
CC       and binds the VEGFA promoter, which is different from canonical E2
CC       recognition site, and activates expression of the VEGFA gene. Acts as a
CC       negative regulator of keratinocyte differentiation (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer and heterodimer: mainly forms homodimers and, to a
CC       lesser extent, heterodimers with E2F8. Dimerization is important for
CC       DNA-binding. Interacts with HIF1A (By similarity). Interacts with MN1
CC       (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q96AV8}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- DOMAIN: In contrast to classical members of the E2F transcription
CC       factor, atypical members contain 2 DNA-binding domains and regulate
CC       transcription in a DP-independent manner. Both DNA-binding domains are
CC       required for DNA-binding and are proposed to form an intramolecular
CC       structure that is similar to the winged helix structure of the E2F-DP
CC       heterodimer (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the E2F/DP family. {ECO:0000305}.
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DR   RefSeq; XP_006241382.1; XM_006241320.2.
DR   RefSeq; XP_006241383.1; XM_006241321.2.
DR   AlphaFoldDB; D4A4D7; -.
DR   SMR; D4A4D7; -.
DR   STRING; 10116.ENSRNOP00000030798; -.
DR   PaxDb; D4A4D7; -.
DR   PRIDE; D4A4D7; -.
DR   Ensembl; ENSRNOT00000104778; ENSRNOP00000081093; ENSRNOG00000026252.
DR   GeneID; 314818; -.
DR   UCSC; RGD:1310258; rat.
DR   CTD; 144455; -.
DR   RGD; 1310258; E2f7.
DR   eggNOG; KOG2578; Eukaryota.
DR   GeneTree; ENSGT00940000157713; -.
DR   InParanoid; D4A4D7; -.
DR   OrthoDB; 145070at2759; -.
DR   PhylomeDB; D4A4D7; -.
DR   TreeFam; TF105567; -.
DR   Reactome; R-RNO-6804116; TP53 Regulates Transcription of Genes Involved in G1 Cell Cycle Arrest.
DR   PRO; PR:D4A4D7; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IBA:GO_Central.
DR   GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0001217; F:DNA-binding transcription repressor activity; ISS:UniProtKB.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:RGD.
DR   GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:RGD.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR   GO; GO:0060718; P:chorionic trophoblast cell differentiation; ISS:UniProtKB.
DR   GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB.
DR   GO; GO:0070365; P:hepatocyte differentiation; ISS:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0032466; P:negative regulation of cytokinesis; ISS:UniProtKB.
DR   GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0071930; P:negative regulation of transcription involved in G1/S transition of mitotic cell cycle; ISS:UniProtKB.
DR   GO; GO:0001890; P:placenta development; ISS:UniProtKB.
DR   GO; GO:0032877; P:positive regulation of DNA endoreduplication; ISS:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
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; ISO:RGD.
DR   GO; GO:0002040; P:sprouting angiogenesis; ISS:UniProtKB.
DR   GO; GO:0060707; P:trophoblast giant cell differentiation; ISS:UniProtKB.
DR   Gene3D; 1.10.10.10; -; 2.
DR   InterPro; IPR015633; E2F.
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; 1.
DR   Pfam; PF02319; E2F_TDP; 2.
DR   SMART; SM01372; E2F_TDP; 2.
DR   SUPFAM; SSF46785; SSF46785; 2.
PE   3: Inferred from homology;
KW   Activator; Cell cycle; DNA damage; DNA-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repressor; Transcription; Transcription regulation.
FT   CHAIN           1..902
FT                   /note="Transcription factor E2F7"
FT                   /id="PRO_0000420705"
FT   DNA_BIND        143..212
FT                   /evidence="ECO:0000255"
FT   DNA_BIND        283..368
FT                   /evidence="ECO:0000255"
FT   REGION          253..283
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          418..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          589..627
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          665..690
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          844..902
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        253..270
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        418..437
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        590..611
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        882..902
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         96
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96AV8"
FT   MOD_RES         411
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96AV8"
FT   MOD_RES         832
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96AV8"
SQ   SEQUENCE   902 AA;  99029 MW;  F48A0A0D3A961013 CRC64;
     MEVNCLTLKD LISPRQTRLD FAVEDAETAQ KENIFVDRSR MTPKTPMKNE PIDLSKQRIF
     TPERSPITPV KLVDRQPQVE PWTPTANLKM LISAASPDIR DREKKKELFR PIENKGDAFV
     NSLQLDVVGD SAVDDYEKRR PSRKQKSLGL LCQKFLARYP SYPLSTEKTT ISLDEVAVSL
     GVERRRIYDI VNVLESLHLV SRVAKNQYGW HGRHSLPKTL RTLQRLGEEQ KYEEQMACLQ
     QKELDLMEYR FGERRKDGSP DPRDQHLLDF SESDYPSSSA NSRKDKSLRI MSQKFVMLFL
     VSKTKIVTLD VAAKILIEES QDTPDHSKFK TKVRRLYDIA NVLTSLALIK KVHVTEERGR
     KPAFKWIGPV DFSSIDEELL DVSASVLPEL KKETYGQIRV CAKERLARYG SFNTVQTSEK
     IQRKVNSEPS SPQGGKQGPA YSLEIGSLAA IYRQKVEDSS QGEAFVNKRA APPASVLDPT
     LPVDSEYCVK PLAQPVFSVA QTDLQAFSAQ NGLNGQVGVP VPSAASDAET LKSALLASQP
     LVYVPSTSLF MLYGSVQEAL SPESRSEEDG SGSDVPADLS LAPTAQKRLC EERNPLEDDE
     PAVKRQSREF EDSPLSLVMP KKPSNSTDLA FPVTTGNGRA TPLEDACVKG QLPAAEDASG
     RAVPNGFIAS ECGNPSRNPD TEKSSNDNEI TKDPSLLQYL YVQSPAGLNG FNMLLPGGQT
     PHAVAPSSAA MPSFGVPCMF LPSPGLGPFP VLYSPAIPGP ISSAPGTLPN TGPMNFGLST
     LASASHLLIS PAAMVNPKSS TLPSADPQLR CQPPLNPNPV MPGSHGVIHP ESPGYMRHPV
     SMVKAEQSPA PATPKSIQRR HRETFFKTPG SLGDPAFRRE RNQSRNTSSA QRRLEISSSG
     PD
 
 
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