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Database: UniProt
Entry: ETS2_MOUSE
LinkDB: ETS2_MOUSE
Original site: 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   11-DEC-2019, entry version 161.
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}.
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   SMR; P15037; -.
DR   BioGrid; 204766; 6.
DR   CORUM; P15037; -.
DR   DIP; DIP-41847N; -.
DR   IntAct; P15037; 1.
DR   STRING; 10090.ENSMUSP00000023612; -.
DR   iPTMnet; P15037; -.
DR   PhosphoSitePlus; P15037; -.
DR   PaxDb; P15037; -.
DR   PRIDE; P15037; -.
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   eggNOG; KOG3806; Eukaryota.
DR   eggNOG; ENOG410Z0ZF; LUCA.
DR   GeneTree; ENSGT00940000160202; -.
DR   HOGENOM; HOG000285953; -.
DR   InParanoid; P15037; -.
DR   KO; K21932; -.
DR   OMA; RSWNSQS; -.
DR   OrthoDB; 526256at2759; -.
DR   PhylomeDB; P15037; -.
DR   TreeFam; TF316214; -.
DR   Reactome; R-MMU-2559585; Oncogene Induced Senescence.
DR   ChiTaRS; Ets2; mouse.
DR   PRO; PR:P15037; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; P15037; protein.
DR   Bgee; ENSMUSG00000022895; Expressed in 338 organ(s), highest expression level in pituitary gland.
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:0003700; F:DNA-binding transcription factor activity; 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: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 regulatory region sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA: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:0045893; P:positive regulation of transcription, DNA-templated; 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; IPR000418; Ets_dom.
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   Pfam; PF00178; Ets; 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   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:0000244|PubMed:21183079"
FT   MOD_RES         300
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|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
//
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