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Database: UniProt
Entry: P97360
LinkDB: P97360
Original site: P97360 
ID   ETV6_MOUSE              Reviewed;         485 AA.
AC   P97360;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   07-OCT-2020, entry version 160.
DE   RecName: Full=Transcription factor ETV6;
DE   AltName: Full=ETS translocation variant 6;
DE   AltName: Full=ETS-related protein Tel1;
DE            Short=Tel;
GN   Name=Etv6; Synonyms=Tel, Tel1;
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].
RC   STRAIN=C57BL/6J;
RA   Bernard O.;
RL   Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-165; SER-240 AND SER-319, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Kidney, Lung, Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Transcriptional repressor; binds to the DNA sequence 5'-
CC       CCGGAAGT-3'. Plays a role in hematopoiesis and malignant
CC       transformation. {ECO:0000250|UniProtKB:P41212}.
CC   -!- SUBUNIT: Can form homodimers or heterodimers with TEL2 or FLI1.
CC       Interacts with L3MBTL1 and HDAC9 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00237}.
CC   -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
DR   EMBL; Y07915; CAA69220.1; -; mRNA.
DR   CCDS; CCDS39677.1; -.
DR   RefSeq; NP_031987.3; NM_007961.4.
DR   PDB; 2LF7; NMR; -; A=335-436.
DR   PDB; 2LF8; NMR; -; A=335-458.
DR   PDB; 2MD5; NMR; -; A=329-426.
DR   PDB; 4MHG; X-ray; 2.20 A; A=329-426.
DR   PDBsum; 2LF7; -.
DR   PDBsum; 2LF8; -.
DR   PDBsum; 2MD5; -.
DR   PDBsum; 4MHG; -.
DR   BMRB; P97360; -.
DR   SMR; P97360; -.
DR   BioGRID; 199540; 5.
DR   STRING; 10090.ENSMUSP00000079818; -.
DR   iPTMnet; P97360; -.
DR   PhosphoSitePlus; P97360; -.
DR   EPD; P97360; -.
DR   jPOST; P97360; -.
DR   MaxQB; P97360; -.
DR   PaxDb; P97360; -.
DR   PeptideAtlas; P97360; -.
DR   PRIDE; P97360; -.
DR   Antibodypedia; 634; 377 antibodies.
DR   Ensembl; ENSMUST00000081028; ENSMUSP00000079818; ENSMUSG00000030199.
DR   GeneID; 14011; -.
DR   KEGG; mmu:14011; -.
DR   UCSC; uc009eke.2; mouse.
DR   CTD; 2120; -.
DR   MGI; MGI:109336; Etv6.
DR   eggNOG; KOG3804; Eukaryota.
DR   GeneTree; ENSGT00940000159508; -.
DR   InParanoid; P97360; -.
DR   KO; K03211; -.
DR   OMA; CIKQERI; -.
DR   OrthoDB; 827924at2759; -.
DR   PhylomeDB; P97360; -.
DR   TreeFam; TF318679; -.
DR   BioGRID-ORCS; 14011; 2 hits in 19 CRISPR screens.
DR   ChiTaRS; Etv6; mouse.
DR   PRO; PR:P97360; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; P97360; protein.
DR   Bgee; ENSMUSG00000030199; Expressed in embryonic post-anal tail and 284 other tissues.
DR   ExpressionAtlas; P97360; baseline and differential.
DR   Genevisible; P97360; MM.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0042025; C:host cell nucleus; IEA:InterPro.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IDA:MGI.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
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:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:0030154; P:cell differentiation; IDA:MGI.
DR   GO; GO:0071425; P:hematopoietic stem cell proliferation; ISS:UniProtKB.
DR   GO; GO:0097152; P:mesenchymal cell apoptotic process; IMP:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0022008; P:neurogenesis; IMP:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
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   GO; GO:0007296; P:vitellogenesis; IMP:MGI.
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; 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   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; PS00346; ETS_DOMAIN_2; 1.
DR   PROSITE; PS50061; ETS_DOMAIN_3; 1.
DR   PROSITE; PS51433; PNT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; DNA-binding; Isopeptide bond; Nucleus;
KW   Phosphoprotein; Reference proteome; Repressor; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN           1..485
FT                   /note="Transcription factor ETV6"
FT                   /id="PRO_0000204122"
FT   DOMAIN          41..125
FT                   /note="PNT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00762"
FT   DNA_BIND        335..416
FT                   /note="ETS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT   MOD_RES         11
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P41212"
FT   MOD_RES         18
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:P41212"
FT   MOD_RES         22
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P41212"
FT   MOD_RES         165
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000244|PubMed:21183079"
FT   MOD_RES         215
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P41212"
FT   MOD_RES         240
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:21183079"
FT   MOD_RES         251
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P41212"
FT   MOD_RES         298
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P41212"
FT   MOD_RES         319
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:21183079"
FT   CROSSLNK        11
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P41212"
FT   CROSSLNK        284
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P41212"
FT   CROSSLNK        298
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P41212"
FT   CROSSLNK        399
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P41212"
FT   CROSSLNK        417
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P41212"
FT   HELIX           337..345
FT                   /evidence="ECO:0000244|PDB:4MHG"
FT   HELIX           348..350
FT                   /evidence="ECO:0000244|PDB:4MHG"
FT   TURN            351..353
FT                   /evidence="ECO:0000244|PDB:4MHG"
FT   STRAND          354..358
FT                   /evidence="ECO:0000244|PDB:4MHG"
FT   TURN            359..362
FT                   /evidence="ECO:0000244|PDB:4MHG"
FT   STRAND          363..367
FT                   /evidence="ECO:0000244|PDB:4MHG"
FT   HELIX           369..379
FT                   /evidence="ECO:0000244|PDB:4MHG"
FT   HELIX           387..399
FT                   /evidence="ECO:0000244|PDB:4MHG"
FT   STRAND          402..405
FT                   /evidence="ECO:0000244|PDB:4MHG"
FT   STRAND          412..417
FT                   /evidence="ECO:0000244|PDB:4MHG"
FT   HELIX           419..422
FT                   /evidence="ECO:0000244|PDB:4MHG"
FT   TURN            423..429
FT                   /evidence="ECO:0000244|PDB:2LF7"
FT   HELIX           430..433
FT                   /evidence="ECO:0000244|PDB:2LF7"
FT   STRAND          451..453
FT                   /evidence="ECO:0000244|PDB:2LF8"
SQ   SEQUENCE   485 AA;  56406 MW;  ECFCDFEC88EA0424 CRC64;
     MSETPAQSSI KQERISYTPP ESPVASHRSS TPLHVHTVPR ALRMEEDSIH LPTHLRLQPI
     YWSRDDVAQW LKWAENEFSL RPIESNKFEM NGKALLLLTK EDFRYRSPHS GDVLYELLQH
     ILKQRKSRML FSPFFPPGDS IHTKPEVLLH QNHDEDNCVQ RTPRTPAESV HHNPPTIELL
     HRPRSPITTN HRPSPDPEQQ RPQRSPLDNM SRRLSPVEKA QGPRLQQENN HQETYPLSVS
     PVENNHCLPS SPWQESTRVI QLMPSPIMHP LILNPRHSHS VDFKQSRHSE DGMNREGKPI
     NLSHREDLAY LNHIMVSMSP PEEHAMPIGR IADCRLLWDY VYQLLSDSRY ENFIRWEDKE
     SKIFRIVDPN GLARLWGNHK NRTNMTYEKM SRALRHYYKL NIIRKEPGQR LLFRFMKTPD
     EIMSGRTDRL EHLESQVLDE QTYQEDEPTI ASPVGWPRGN LPTGTAGGVM EAGELGVAVK
     EETRE
//
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