ETS2_MOUSE
ID ETS2_MOUSE Reviewed; 468 AA.
AC P15037;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Protein C-ets-2;
GN Name=Ets2;
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].
RX PubMed=2847145; DOI=10.1073/pnas.85.21.7862;
RA Watson D.K., McWilliams M.J., Lapis P., Lautenberger J.A.,
RA Schweinfest C.W., Papas T.S.;
RT "Mammalian ets-1 and ets-2 genes encode highly conserved proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:7862-7866(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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-297 AND SER-300, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Lung, and Spleen;
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: Transcription factor activating transcription. Binds
CC specifically the GGA DNA motif in gene promoters and stimulates
CC transcription of those genes (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: Phosphorylation by CDK10 at Ser-220 and Ser-225 creates a
CC phosphodegron that targets ETS2 for proteasomal degradation.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
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DR EMBL; J04103; AAA37581.1; -; mRNA.
DR EMBL; BC005504; AAH05504.1; -; mRNA.
DR CCDS; CCDS37412.1; -.
DR PIR; C32066; TVMSE2.
DR RefSeq; NP_035939.3; NM_011809.3.
DR AlphaFoldDB; P15037; -.
DR SMR; P15037; -.
DR BioGRID; 204766; 7.
DR CORUM; P15037; -.
DR DIP; DIP-41847N; -.
DR IntAct; P15037; 2.
DR STRING; 10090.ENSMUSP00000023612; -.
DR iPTMnet; P15037; -.
DR PhosphoSitePlus; P15037; -.
DR PaxDb; P15037; -.
DR PRIDE; P15037; -.
DR ProteomicsDB; 271504; -.
DR Antibodypedia; 8721; 416 antibodies from 32 providers.
DR DNASU; 23872; -.
DR Ensembl; ENSMUST00000023612; ENSMUSP00000023612; ENSMUSG00000022895.
DR GeneID; 23872; -.
DR KEGG; mmu:23872; -.
DR UCSC; uc008ace.2; mouse.
DR CTD; 2114; -.
DR MGI; MGI:95456; Ets2.
DR VEuPathDB; HostDB:ENSMUSG00000022895; -.
DR eggNOG; KOG3806; Eukaryota.
DR GeneTree; ENSGT00940000160202; -.
DR HOGENOM; CLU_031197_1_1_1; -.
DR InParanoid; P15037; -.
DR OMA; RSWNSQS; -.
DR OrthoDB; 526256at2759; -.
DR PhylomeDB; P15037; -.
DR TreeFam; TF316214; -.
DR Reactome; R-MMU-2559585; Oncogene Induced Senescence.
DR BioGRID-ORCS; 23872; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Ets2; mouse.
DR PRO; PR:P15037; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; P15037; protein.
DR Bgee; ENSMUSG00000022895; Expressed in placenta labyrinth and 301 other tissues.
DR ExpressionAtlas; P15037; baseline and differential.
DR Genevisible; P15037; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; ISO: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:0035259; F:nuclear glucocorticoid receptor binding; 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; ISO:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0001712; P:ectodermal cell fate commitment; IGI:MGI.
DR GO; GO:0007498; P:mesoderm development; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0090009; P:primitive streak formation; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
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; IPR016311; Transform_prot_C-ets.
DR InterPro; IPR027276; Transform_prot_C-ets-2.
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; PIRSF501032; C-ets-2; 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 DNA-binding; Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..468
FT /note="Protein C-ets-2"
FT /id="PRO_0000204078"
FT DOMAIN 85..170
FT /note="PNT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00762"
FT DNA_BIND 362..442
FT /note="ETS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT REGION 262..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15036"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15036"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15036"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 468 AA; 52827 MW; 5260F3085B7EB831 CRC64;
MNDFGIKNMD QVAPVANSFR GTLKRQPAFD TFDGSLFAVL PSLSEDQTLQ EVPTGLDSVS
HDSASCELPL LTPCSKAVMS QALKATFSGF QKEQRRLGIP KNPWLWSEQQ VCQWLLWATN
EFSLVNVNLH QFGMNGQMLC NLGKERFLEL APDFVGDILW EHLEQMIKEN QEKTEDQYEE
NSHLNAVPHW INSNTLGFSM EQAPYGMQAP NYPKDNLLDS MCPPSATPAA LGSELQMLPK
SRLNTVNVNY CSISQDFPSS NVNLLNNNSG KPKDHDSPEN GGDSFESSDS LLRSWNSQSS
LLDVQRVPSF ESFEEDCSQS LCLSKLTMSF KDYIQERSDP VEQGKPVIPA AVLAGFTGSG
PIQLWQFLLE LLSDKSCQSF ISWTGDGWEF KLADPDEVAR RWGKRKNKPK MNYEKLSRGL
RYYYDKNIIH KTSGKRYVYR FVCDLQNLLG FTPEELHAIL GVQPDTED
