ETS1_RAT
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 03-AUG-2022, entry version 180.
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; DOI=10.1128/jvi.68.4.2320-2330.1994;
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}.
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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 AlphaFoldDB; P41156; -.
DR BMRB; P41156; -.
DR SMR; P41156; -.
DR MINT; P41156; -.
DR STRING; 10116.ENSRNOP00000011925; -.
DR iPTMnet; P41156; -.
DR PhosphoSitePlus; P41156; -.
DR PaxDb; 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 OMA; ADMECAD; -.
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 18 other tissues.
DR Genevisible; P41156; RN.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0140297; F:DNA-binding transcription factor binding; 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:0030374; F:nuclear receptor coactivator activity; ISO:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor 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:0000976; F:transcription cis-regulatory region binding; ISO:RGD.
DR GO; GO:0001222; F:transcription corepressor 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: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: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 miRNA transcription; 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: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: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:1902074; P:response to salt; IEP:RGD.
DR GO; GO:0009611; P:response to wounding; IEP: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; IPR045688; Ets1_N_flank.
DR InterPro; IPR000418; Ets_dom.
DR InterPro; IPR046328; ETS_fam.
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 PANTHER; PTHR11849; PTHR11849; 1.
DR Pfam; PF00178; Ets; 1.
DR Pfam; PF19525; Ets1_N_flank; 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:0007744|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:0007744|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
