ETV6_MOUSE
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 03-AUG-2022, entry version 168.
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}.
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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 AlphaFoldDB; P97360; -.
DR BMRB; P97360; -.
DR SMR; P97360; -.
DR BioGRID; 199540; 7.
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 ProteomicsDB; 275803; -.
DR Antibodypedia; 634; 397 antibodies from 35 providers.
DR DNASU; 14011; -.
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 VEuPathDB; HostDB:ENSMUSG00000030199; -.
DR eggNOG; KOG3804; Eukaryota.
DR GeneTree; ENSGT00940000159508; -.
DR InParanoid; P97360; -.
DR OMA; NPRHSMD; -.
DR OrthoDB; 827924at2759; -.
DR PhylomeDB; P97360; -.
DR TreeFam; TF318679; -.
DR BioGRID-ORCS; 14011; 5 hits in 77 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 236 other tissues.
DR ExpressionAtlas; P97360; baseline and differential.
DR Genevisible; P97360; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
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; IPR046328; ETS_fam.
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 PANTHER; PTHR11849; PTHR11849; 1.
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 REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 157..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:0007744|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:0007744|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:0007744|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:0007829|PDB:4MHG"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:4MHG"
FT TURN 351..353
FT /evidence="ECO:0007829|PDB:4MHG"
FT STRAND 354..358
FT /evidence="ECO:0007829|PDB:4MHG"
FT TURN 359..362
FT /evidence="ECO:0007829|PDB:4MHG"
FT STRAND 363..367
FT /evidence="ECO:0007829|PDB:4MHG"
FT HELIX 369..379
FT /evidence="ECO:0007829|PDB:4MHG"
FT HELIX 387..399
FT /evidence="ECO:0007829|PDB:4MHG"
FT STRAND 402..405
FT /evidence="ECO:0007829|PDB:4MHG"
FT STRAND 412..417
FT /evidence="ECO:0007829|PDB:4MHG"
FT HELIX 419..422
FT /evidence="ECO:0007829|PDB:4MHG"
FT TURN 423..429
FT /evidence="ECO:0007829|PDB:2LF7"
FT HELIX 430..433
FT /evidence="ECO:0007829|PDB:2LF7"
FT STRAND 451..453
FT /evidence="ECO:0007829|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
