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ETS translocation variant 3 (ETS domain transcriptional repressor PE1) (PE-1) (Mitogenic Ets transcriptional suppressor)

 ETV3_MOUSE              Reviewed;         513 AA.
Q8R4Z4; G5E907; Q9QZW1;
12-APR-2005, integrated into UniProtKB/Swiss-Prot.
03-OCT-2012, sequence version 2.
25-OCT-2017, entry version 121.
RecName: Full=ETS translocation variant 3;
AltName: Full=ETS domain transcriptional repressor PE1;
Short=PE-1;
AltName: Full=Mitogenic Ets transcriptional suppressor;
Name=Etv3; Synonyms=Mets, Pe1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
PubMed=12007404; DOI=10.1016/S0092-8674(02)00714-6;
Klappacher G.W., Lunyak V.V., Sykes D.B., Sawka-Verhelle D., Sage J.,
Brard G., Ngo S.D., Gangadharan D., Jacks T., Kamps M.P., Rose D.W.,
Rosenfeld M.G., Glass C.K.;
"An induced Ets repressor complex regulates growth arrest during
terminal macrophage differentiation.";
Cell 109:169-180(2002).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/SvJ;
PubMed=14754893; DOI=10.1074/jbc.M311991200;
Sawka-Verhelle D., Escoubet-Lozach L., Fong A.L., Hester K.D.,
Herzig S., Lebrun P., Glass C.K.;
"PE-1/METS, an antiproliferative Ets repressor factor, is induced by
CREB-1/CREM-1 during macrophage differentiation.";
J. Biol. Chem. 279:17772-17784(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
TISSUE=Brain;
PubMed=10913304; DOI=10.1021/bi000343+;
Bidder M., Loewy A.P., Latifi T., Newberry E.P., Ferguson G.,
Willis D.M., Towler D.A.;
"Ets domain transcription factor PE1 suppresses human interstitial
collagenase promoter activity by antagonizing protein-DNA interactions
at a critical AP1 element.";
Biochemistry 39:8917-8928(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=NMRI; TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Transcriptional repressor that contribute to growth
arrest during terminal macrophage differentiation by repressing
target genes involved in Ras-dependent proliferation. Represses
MMP1 promoter activity. {ECO:0000269|PubMed:10913304,
ECO:0000269|PubMed:12007404}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00237}.
-!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
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EMBL; AF218539; AAK56845.1; -; mRNA.
EMBL; AY274927; AAQ18663.1; -; Genomic_DNA.
EMBL; AF156530; AAF09185.1; -; mRNA.
EMBL; AC139241; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466547; EDL15354.1; -; Genomic_DNA.
EMBL; BC078636; AAH78636.1; -; mRNA.
CCDS; CCDS17453.1; -.
RefSeq; NP_001076787.1; NM_001083318.2.
RefSeq; NP_001273773.1; NM_001286844.1.
RefSeq; NP_036181.3; NM_012051.4.
UniGene; Mm.219460; -.
ProteinModelPortal; Q8R4Z4; -.
SMR; Q8R4Z4; -.
BioGrid; 205105; 2.
IntAct; Q8R4Z4; 1.
STRING; 10090.ENSMUSP00000112915; -.
iPTMnet; Q8R4Z4; -.
PhosphoSitePlus; Q8R4Z4; -.
EPD; Q8R4Z4; -.
MaxQB; Q8R4Z4; -.
PaxDb; Q8R4Z4; -.
PRIDE; Q8R4Z4; -.
Ensembl; ENSMUST00000119109; ENSMUSP00000112915; ENSMUSG00000003382.
Ensembl; ENSMUST00000170036; ENSMUSP00000127419; ENSMUSG00000003382.
GeneID; 27049; -.
KEGG; mmu:27049; -.
UCSC; uc008psh.2; mouse.
CTD; 2117; -.
MGI; MGI:1350926; Etv3.
eggNOG; KOG3806; Eukaryota.
eggNOG; ENOG410Z0ZF; LUCA.
GeneTree; ENSGT00760000118907; -.
HOGENOM; HOG000070246; -.
HOVERGEN; HBG005183; -.
InParanoid; Q8R4Z4; -.
KO; K09433; -.
OMA; VPPLQCQ; -.
OrthoDB; EOG091G05C7; -.
TreeFam; TF351065; -.
PRO; PR:Q8R4Z4; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000003382; -.
CleanEx; MM_ETV3; -.
ExpressionAtlas; Q8R4Z4; baseline and differential.
Genevisible; Q8R4Z4; MM.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0090571; C:RNA polymerase II transcription repressor complex; IDA:BHF-UCL.
GO; GO:0017053; C:transcriptional repressor complex; IDA:MGI.
GO; GO:0017151; F:DEAD/H-box RNA helicase binding; IPI:BHF-UCL.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0001227; F:transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding; IDA:BHF-UCL.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0097011; P:cellular response to granulocyte macrophage colony-stimulating factor stimulus; IDA:BHF-UCL.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR000418; Ets_dom.
InterPro; IPR032929; ETV3.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
PANTHER; PTHR11849:SF264; PTHR11849:SF264; 1.
Pfam; PF00178; Ets; 1.
PRINTS; PR00454; ETSDOMAIN.
SMART; SM00413; ETS; 1.
SUPFAM; SSF46785; SSF46785; 1.
PROSITE; PS00345; ETS_DOMAIN_1; 1.
PROSITE; PS00346; ETS_DOMAIN_2; 1.
PROSITE; PS50061; ETS_DOMAIN_3; 1.
1: Evidence at protein level;
Acetylation; Complete proteome; DNA-binding; Isopeptide bond; Nucleus;
Phosphoprotein; Reference proteome; Repressor; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 513 ETS translocation variant 3.
/FTId=PRO_0000204115.
DNA_BIND 35 116 ETS. {ECO:0000255|PROSITE-
ProRule:PRU00237}.
MOD_RES 139 139 Phosphoserine.
{ECO:0000250|UniProtKB:P41162}.
MOD_RES 159 159 Phosphoserine.
{ECO:0000250|UniProtKB:P41162}.
MOD_RES 315 315 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 388 388 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P41162}.
CROSSLNK 381 381 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P41162}.
CROSSLNK 388 388 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P41162}.
CONFLICT 182 182 G -> R (in Ref. 3; AAF09185).
{ECO:0000305}.
CONFLICT 244 244 H -> R (in Ref. 3; AAF09185).
{ECO:0000305}.
CONFLICT 410 410 M -> I (in Ref. 1; AAK56845, 2; AAQ18663,
3; AAF09185 and 6; AAH78636).
{ECO:0000305}.
CONFLICT 454 454 V -> A (in Ref. 1; AAK56845, 2; AAQ18663,
3; AAF09185 and 6; AAH78636).
{ECO:0000305}.
SEQUENCE 513 AA; 57026 MW; 67BCFA849A3BF7E3 CRC64;
MKAGCSIVEK PEGGGGYQFP DWAYKAESSP GSRQIQLWHF ILELLQKEEF RHVIAWQQGE
YGEFVIKDPD EVARLWGRRK CKPQMNYDKL SRALRYYYNK RILHKTKGKR FTYKFNFNKL
VMPNYPFINI RSSGVVPQSA PPVPTASSRF HFPPLDSHSP TGDVQPGRFS ASSLSASGPE
SGVTTDRKVE PSDLEDGSAS DWHRGMDFMP SRNALGGGAV GHQKRKPDIL LPLFTRPAMY
PDPHSPFAIS PVPGRGGVLN VPISPALSLT PTMFSYSPSP GLSPFTSSSC FSFNPEEMKH
YLHSQACSVF NYHLSPRTFP RYPGLMVPPL QCQMHPEEPS QFSIKLQPPP AGRKNRERVE
SREEAVRGSV PASAPVPSRI KVEPATEKDP DSLRQSTQGK EEQTQEVDSM RSRTIEEGKG
TGFAHPSPTW PSVSISTPSD EPLEGTEDSE DRSVREPGVP EKKEDALMPP KLRLKRRWND
DPEARELNKT GKFLWNGAGP QGLATTATAA ADA


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