ETS2_BOVIN
ID ETS2_BOVIN Reviewed; 470 AA.
AC A1A4L6;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Protein C-ets-2;
GN Name=ETS2;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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-225 may create a phosphodegron
CC that targets ETS2 for proteasomal degradation.
CC -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
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DR EMBL; BC126692; AAI26693.1; -; mRNA.
DR RefSeq; NP_001073683.1; NM_001080214.1.
DR AlphaFoldDB; A1A4L6; -.
DR SMR; A1A4L6; -.
DR STRING; 9913.ENSBTAP00000012144; -.
DR PaxDb; A1A4L6; -.
DR Ensembl; ENSBTAT00000012144; ENSBTAP00000012144; ENSBTAG00000009214.
DR Ensembl; ENSBTAT00000074510; ENSBTAP00000072496; ENSBTAG00000009214.
DR GeneID; 281148; -.
DR KEGG; bta:281148; -.
DR CTD; 2114; -.
DR VEuPathDB; HostDB:ENSBTAG00000009214; -.
DR VGNC; VGNC:28627; ETS2.
DR eggNOG; KOG3806; Eukaryota.
DR GeneTree; ENSGT00940000160202; -.
DR InParanoid; A1A4L6; -.
DR OMA; RSWNSQS; -.
DR OrthoDB; 526256at2759; -.
DR Proteomes; UP000009136; Chromosome 1.
DR Bgee; ENSBTAG00000009214; Expressed in infraspinatus muscle and 104 other tissues.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
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 2: Evidence at transcript level;
KW DNA-binding; Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..470
FT /note="Protein C-ets-2"
FT /id="PRO_0000287131"
FT DOMAIN 85..170
FT /note="PNT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00762"
FT DNA_BIND 364..444
FT /note="ETS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT REGION 270..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15036"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15036"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15037"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15037"
SQ SEQUENCE 470 AA; 52654 MW; A0F1364B8DACC6AA CRC64;
MNDFGIKNMD QVAPVASSYR GTLKRQAAFD TFDGSLLAVF PSLNEEQTLQ EVPTGLDSIS
HDSANCELPL LTPCSKAVMS QALKATFSGF KKEQRRLGIP KNPWLWTEQQ VCQWLLWATN
EFSLVDVNLQ RFGMTGQVLC NLGKERFLEL APDFVGDILW EHLEQMIKEN QEKNEDQYEE
NSHLNSVPHW INSNSLGFGV EQAPYGMQTQ SYPKGGLLDG LCPASSAPST LGPEQDFQMF
PKARLNTVSV NYCSVGQDFP AGSLNLLSSA SGKPRDHDSA ETGGDSFESS ESLLQSWNSQ
SSLLDVQRVP SFESFEDDCS QSLGLSKPTM SFKDYIQDRS DPVEQGKPVI PAAVLAGFTG
SGPIQLWQFL LELLSDKSCQ SFISWTGDGW EFKLADPDEV ARRWGKRKNK PKMNYEKLSR
GLRYYYDKNI IHKTSGKRYV YRFVCDLQNL LGFTPEELHA ILGVQPDTED