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Database: UniProt
Entry: P41156
LinkDB: P41156
Original site: P41156 
ID   ETS1_RAT                Reviewed;         441 AA.
AC   P41156; Q3T1H1;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   07-OCT-2020, entry version 174.
DE   RecName: Full=Protein C-ets-1;
DE   AltName: Full=p54;
GN   Name=Ets1; Synonyms=Ets-1;
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].
RX   PubMed=8139017;
RA   Bellacosa A., Datta K., Bear S.E., Patriotis C., Lazo P.A., Copeland N.G.,
RA   Jenkins N.A., Tsichlis P.N.;
RT   "Effects of provirus integration in the Tpl-1/Ets-1 locus in Moloney murine
RT   leukemia virus-induced rat T-cell lymphomas: levels of expression,
RT   polyadenylation, transcriptional initiation, and differential splicing of
RT   the Ets-1 mRNA.";
RL   J. Virol. 68:2320-2330(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251 AND SER-282, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Transcription factor. Directly controls the expression of
CC       cytokine and chemokine genes in a wide variety of different cellular
CC       contexts. May control the differentiation, survival and proliferation
CC       of lymphoid cells. May also regulate angiogenesis through regulation of
CC       expression of genes controlling endothelial cell migration and invasion
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Binds DNA as a homodimer; homodimerization is required for
CC       transcription activation. Interacts with MAF and MAFB. Interacts with
CC       PAX5; the interaction alters DNA-binding properties. Interacts with
CC       DAXX. Interacts with UBE2I. Interacts with SP100; the interaction is
CC       direct and modulates ETS1 transcriptional activity (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P14921}. Nucleus
CC       {ECO:0000250|UniProtKB:P14921}. Note=Delocalizes from nucleus to
CC       cytoplasm when coexpressed with isoform Ets-1 p27.
CC       {ECO:0000250|UniProtKB:P14921}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=At least 2 isoforms are produced.;
CC       Name=1;
CC         IsoId=P41156-1; Sequence=Displayed;
CC   -!- PTM: Sumoylated on Lys-15 and Lys-227, preferentially with SUMO2; which
CC       inhibits transcriptional activity. {ECO:0000250}.
CC   -!- PTM: Ubiquitinated; which induces proteasomal degradation.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
DR   EMBL; L20681; AAA21093.1; -; mRNA.
DR   EMBL; BC101927; AAI01928.1; -; mRNA.
DR   PIR; A53988; A53988.
DR   RefSeq; NP_036687.1; NM_012555.2. [P41156-1]
DR   BMRB; P41156; -.
DR   SMR; P41156; -.
DR   MINT; P41156; -.
DR   STRING; 10116.ENSRNOP00000011925; -.
DR   iPTMnet; P41156; -.
DR   PhosphoSitePlus; P41156; -.
DR   PaxDb; P41156; -.
DR   PRIDE; P41156; -.
DR   Ensembl; ENSRNOT00000011925; ENSRNOP00000011925; ENSRNOG00000008941. [P41156-1]
DR   GeneID; 24356; -.
DR   KEGG; rno:24356; -.
DR   UCSC; RGD:2583; rat. [P41156-1]
DR   CTD; 2113; -.
DR   RGD; 2583; Ets1.
DR   eggNOG; KOG3806; Eukaryota.
DR   GeneTree; ENSGT00940000159519; -.
DR   HOGENOM; CLU_031197_0_0_1; -.
DR   InParanoid; P41156; -.
DR   KO; K02678; -.
DR   OMA; SFESCER; -.
DR   OrthoDB; 526256at2759; -.
DR   PhylomeDB; P41156; -.
DR   TreeFam; TF316214; -.
DR   Reactome; R-RNO-2559585; Oncogene Induced Senescence.
DR   PRO; PR:P41156; -.
DR   Proteomes; UP000002494; Chromosome 8.
DR   Bgee; ENSRNOG00000008941; Expressed in thymus and 20 other tissues.
DR   Genevisible; P41156; RN.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042025; C:host cell nucleus; IEA:InterPro.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0005634; C:nucleus; IDA:RGD.
DR   GO; GO:0005667; C:transcription regulator complex; ISO:RGD.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; 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; ISO:RGD.
DR   GO; GO:0035035; F:histone acetyltransferase binding; IPI: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; ISO:RGD.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:RGD.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR   GO; GO:0060055; P:angiogenesis involved in wound healing; IEP:RGD.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0048870; P:cell motility; ISO:RGD.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; IEP:RGD.
DR   GO; GO:0044849; P:estrous cycle; IEP:RGD.
DR   GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR   GO; GO:0021854; P:hypothalamus development; IEP:RGD.
DR   GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR   GO; GO:0045786; P:negative regulation of cell cycle; ISO:RGD.
DR   GO; GO:0050728; P:negative regulation of inflammatory response; ISO:RGD.
DR   GO; GO:0021983; P:pituitary gland development; IEP:RGD.
DR   GO; GO:0030578; P:PML body organization; ISO:RGD.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IMP:RGD.
DR   GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; ISO:RGD.
DR   GO; GO:0030335; P:positive regulation of cell migration; IMP:RGD.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:RGD.
DR   GO; GO:0051272; P:positive regulation of cellular component movement; ISO:RGD.
DR   GO; GO:0010595; P:positive regulation of endothelial cell migration; ISS:UniProtKB.
DR   GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISS:UniProtKB.
DR   GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
DR   GO; GO:0050729; P:positive regulation of inflammatory response; ISO:RGD.
DR   GO; GO:1904996; P:positive regulation of leukocyte adhesion to vascular endothelial cell; ISO:RGD.
DR   GO; GO:1902895; P:positive regulation of pri-miRNA transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0045765; P:regulation of angiogenesis; ISS:UniProtKB.
DR   GO; GO:0042981; P:regulation of apoptotic process; ISO:RGD.
DR   GO; GO:0010715; P:regulation of extracellular matrix disassembly; IMP:RGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0046677; P:response to antibiotic; ISO:RGD.
DR   GO; GO:0032355; P:response to estradiol; IEP:RGD.
DR   GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR   GO; GO:0070555; P:response to interleukin-1; IEP:RGD.
DR   GO; GO:0034616; P:response to laminar fluid shear stress; IEP:RGD.
DR   GO; GO:0009612; P:response to mechanical stimulus; IEP:RGD.
DR   GO; GO:0009611; P:response to wounding; IEP:RGD.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; ISO:RGD.
DR   CDD; cd08542; SAM_PNT-ETS-1; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 1.10.150.50; -; 1.
DR   InterPro; IPR000418; Ets_dom.
DR   InterPro; IPR003118; Pointed_dom.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR041886; SAM_PNT-ETS-1.
DR   InterPro; IPR016311; Transform_prot_C-ets.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF00178; Ets; 1.
DR   Pfam; PF02198; SAM_PNT; 1.
DR   PIRSF; PIRSF001698; Transforming_factor_C-ets; 1.
DR   PRINTS; PR00454; ETSDOMAIN.
DR   SMART; SM00413; ETS; 1.
DR   SMART; SM00251; SAM_PNT; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF47769; SSF47769; 1.
DR   PROSITE; PS00345; ETS_DOMAIN_1; 1.
DR   PROSITE; PS00346; ETS_DOMAIN_2; 1.
DR   PROSITE; PS50061; ETS_DOMAIN_3; 1.
DR   PROSITE; PS51433; PNT; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Cytoplasm; DNA-binding; Immunity;
KW   Isopeptide bond; Nucleus; Phosphoprotein; Proto-oncogene;
KW   Reference proteome; Transcription; Transcription regulation;
KW   Ubl conjugation.
FT   CHAIN           1..441
FT                   /note="Protein C-ets-1"
FT                   /id="PRO_0000204071"
FT   DOMAIN          51..136
FT                   /note="PNT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00762"
FT   DNA_BIND        335..415
FT                   /note="ETS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT   REGION          130..243
FT                   /note="Activation domain; required for transcription
FT                   activation"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         8
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P14921"
FT   MOD_RES         15
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P14921"
FT   MOD_RES         38
FT                   /note="Phosphothreonine; by MAPK"
FT                   /evidence="ECO:0000250|UniProtKB:P27577"
FT   MOD_RES         223
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P14921"
FT   MOD_RES         251
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:22673903"
FT   MOD_RES         254
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P27577"
FT   MOD_RES         265
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P14921"
FT   MOD_RES         267
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P14921"
FT   MOD_RES         270
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P14921"
FT   MOD_RES         282
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:22673903"
FT   MOD_RES         285
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P14921"
FT   MOD_RES         305
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P14921"
FT   CROSSLNK        8
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P14921"
FT   CROSSLNK        15
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO); alternate"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        15
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P14921"
FT   CROSSLNK        138
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P14921"
FT   CROSSLNK        227
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   441 AA;  50423 MW;  981E029CABFBBE6B CRC64;
     MKAAVDLKPT LTIIKTEKVD LELFPSPDME CADVPLLTPS SKEMMSQALK ATFSGFTKEQ
     QRLGIPKDPR QWTETHVRDW VMWAVNEFSL KGVDFQKFCM NGAALCALGK ECFLELAPDF
     VGDILWEHLE ILQKEDVKPY QVNGVNPTYP ESRYTSDYFI SYGIEHAQCV PPSEFSEPSF
     ITESYQTLHP ISSEELLSLK YENDYPSVIL RDPLQTDTLQ TDYFAIKQEV LTPDNMCMGR
     ASRGKLGGQD SFESIESYDS CDRLTQSWSS QSSFNSLQRV PSYDSFDSED YPAALPNHKP
     KGTFKDYVRD RADLNKDKPV IPAAALAGYT GSGPIQLWQF LLELLTDKSC QSFISWTGDG
     WEFKLSDPDE VARRWGKRKN KPKMNYEKLS RGLRYYYDKN IIHKTAGKRY VYRFVCDLQS
     LLGYTPEELH AMLDVKPDAD E
//
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