ID   ERG_MOUSE               Reviewed;         486 AA.
AC   P81270; A6H6E7; Q8C5L4; Q920K7; Q920K8; Q920K9;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2003, sequence version 2.
DT   24-JAN-2024, entry version 182.
DE   RecName: Full=Transcriptional regulator ERG;
GN   Name=Erg; Synonyms=Erg-3;
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] (ISOFORMS 1; 2 AND 3).
RA   Ozawa R., Noguchi H., Taylor T.D., Takeda T., Hattori M., Sakaki Y.;
RL   Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 5).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Medulla oblongata;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Brain;
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   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 181-452.
RX   PubMed=8413305; DOI=10.1128/mcb.13.11.7163-7169.1993;
RA   Rivera R.R., Stuiver M.H., Steenbergen R., Murre C.;
RT   "Ets proteins: new factors that regulate immunoglobulin heavy-chain gene
RT   expression.";
RL   Mol. Cell. Biol. 13:7163-7169(1993).
RN   [5]
RP   INTERACTION WITH SETDB1.
RX   PubMed=11791185; DOI=10.1038/sj.onc.1204998;
RA   Yang L., Xia L., Wu D.Y., Wang H., Chansky H.A., Schubach W.H.,
RA   Hickstein D.D., Zhang Y.;
RT   "Molecular cloning of ESET, a novel histone H3-specific methyltransferase
RT   that interacts with ERG transcription factor.";
RL   Oncogene 21:148-152(2002).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55; SER-88 AND SER-103, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose 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: Transcriptional regulator. May participate in transcriptional
CC       regulation through the recruitment of SETDB1 histone methyltransferase
CC       and subsequent modification of local chromatin structure.
CC   -!- SUBUNIT: Identified in a IGF2BP1-dependent mRNP granule complex
CC       containing untranslated mRNAs. Interacts with SETDB1.
CC       {ECO:0000269|PubMed:11791185}.
CC   -!- INTERACTION:
CC       P81270; O88974: Setdb1; NbExp=3; IntAct=EBI-79647, EBI-79658;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}. Note=Localized
CC       in cytoplasmic mRNP granules containing untranslated mRNAs.
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=3;
CC         IsoId=P81270-1; Sequence=Displayed;
CC       Name=1;
CC         IsoId=P81270-3; Sequence=VSP_007641;
CC       Name=2;
CC         IsoId=P81270-2; Sequence=VSP_007642;
CC       Name=5;
CC         IsoId=P81270-4; Sequence=VSP_026585;
CC   -!- SIMILARITY: Belongs to the ETS family. {ECO:0000305}.
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DR   EMBL; AB073078; BAB69948.1; -; mRNA.
DR   EMBL; AB073079; BAB69949.1; -; mRNA.
DR   EMBL; AB073080; BAB69950.1; -; mRNA.
DR   EMBL; AK050922; BAC34461.1; -; mRNA.
DR   EMBL; AK078113; BAC37131.1; -; mRNA.
DR   EMBL; BC145850; AAI45851.1; -; mRNA.
DR   EMBL; S66169; AAB28525.1; -; mRNA.
DR   CCDS; CCDS37411.1; -. [P81270-1]
DR   CCDS; CCDS79493.1; -. [P81270-4]
DR   CCDS; CCDS79495.1; -. [P81270-3]
DR   CCDS; CCDS79496.1; -. [P81270-2]
DR   PIR; A54617; A54617.
DR   RefSeq; NP_001289081.1; NM_001302152.1. [P81270-3]
DR   RefSeq; NP_001289082.1; NM_001302153.1. [P81270-4]
DR   RefSeq; NP_001289083.1; NM_001302154.1.
DR   RefSeq; NP_001289108.1; NM_001302179.1. [P81270-2]
DR   RefSeq; NP_001289112.1; NM_001302183.1.
DR   RefSeq; NP_598420.1; NM_133659.3. [P81270-1]
DR   RefSeq; XP_006522957.1; XM_006522894.3. [P81270-1]
DR   RefSeq; XP_006522958.1; XM_006522895.2. [P81270-1]
DR   RefSeq; XP_006522959.1; XM_006522896.3. [P81270-1]
DR   RefSeq; XP_006522962.1; XM_006522899.3. [P81270-2]
DR   RefSeq; XP_006522963.1; XM_006522900.2. [P81270-3]
DR   AlphaFoldDB; P81270; -.
DR   BMRB; P81270; -.
DR   SMR; P81270; -.
DR   BioGRID; 199504; 5.
DR   IntAct; P81270; 2.
DR   STRING; 10090.ENSMUSP00000156669; -.
DR   iPTMnet; P81270; -.
DR   PhosphoSitePlus; P81270; -.
DR   MaxQB; P81270; -.
DR   PaxDb; 10090-ENSMUSP00000109477; -.
DR   ProteomicsDB; 275775; -. [P81270-1]
DR   ProteomicsDB; 275776; -. [P81270-3]
DR   ProteomicsDB; 275777; -. [P81270-2]
DR   ProteomicsDB; 275778; -. [P81270-4]
DR   Antibodypedia; 4338; 734 antibodies from 41 providers.
DR   DNASU; 13876; -.
DR   Ensembl; ENSMUST00000113848.11; ENSMUSP00000109479.5; ENSMUSG00000040732.21. [P81270-2]
DR   Ensembl; ENSMUST00000122199.10; ENSMUSP00000114072.4; ENSMUSG00000040732.21. [P81270-4]
DR   Ensembl; ENSMUST00000233269.2; ENSMUSP00000156926.2; ENSMUSG00000040732.21. [P81270-3]
DR   Ensembl; ENSMUST00000233881.2; ENSMUSP00000156669.2; ENSMUSG00000040732.21. [P81270-1]
DR   GeneID; 13876; -.
DR   KEGG; mmu:13876; -.
DR   UCSC; uc008acb.2; mouse. [P81270-1]
DR   UCSC; uc008acc.2; mouse. [P81270-2]
DR   AGR; MGI:95415; -.
DR   CTD; 2078; -.
DR   MGI; MGI:95415; Erg.
DR   VEuPathDB; HostDB:ENSMUSG00000040732; -.
DR   eggNOG; KOG3806; Eukaryota.
DR   GeneTree; ENSGT00940000160662; -.
DR   InParanoid; P81270; -.
DR   OMA; RVPQQEW; -.
DR   OrthoDB; 2882052at2759; -.
DR   PhylomeDB; P81270; -.
DR   TreeFam; TF350537; -.
DR   BioGRID-ORCS; 13876; 2 hits in 78 CRISPR screens.
DR   ChiTaRS; Erg; mouse.
DR   PRO; PR:P81270; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; P81270; Protein.
DR   Bgee; ENSMUSG00000040732; Expressed in brain blood vessel and 226 other cell types or tissues.
DR   ExpressionAtlas; P81270; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISO:MGI.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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; ETS; 1.
DR   PANTHER; PTHR11849:SF216; TRANSCRIPTIONAL REGULATOR ERG; 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; SSF47769; SAM/Pointed domain; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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.
DR   Genevisible; P81270; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; DNA-binding; Isopeptide bond; Nucleus;
KW   Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN           1..486
FT                   /note="Transcriptional regulator ERG"
FT                   /id="PRO_0000204104"
FT   DOMAIN          120..206
FT                   /note="PNT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00762"
FT   DNA_BIND        318..398
FT                   /note="ETS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT   REGION          41..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          79..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          249..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        269..290
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         55
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         88
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         103
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   CROSSLNK        289
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:P11308"
FT   VAR_SEQ         1..11
FT                   /note="MIQTVPDPAAH -> MAST (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_026585"
FT   VAR_SEQ         232..255
FT                   /note="Missing (in isoform 1)"
FT                   /evidence="ECO:0000303|PubMed:16141072, ECO:0000303|Ref.1"
FT                   /id="VSP_007641"
FT   VAR_SEQ         256..278
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072, ECO:0000303|Ref.1"
FT                   /id="VSP_007642"
FT   CONFLICT        175
FT                   /note="L -> Q (in Ref. 2; BAC37131)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   486 AA;  54614 MW;  BF1ADF00A4772F75 CRC64;
     MIQTVPDPAA HIKEALSVVS EDQSLFECAY GTPHLAKTEM TASSSSDYGQ TSKMSPRVPQ
     QDWLSQAPAR VTIKMECNPS QVNGSRNSPD ECSVNKGGKM VGSPDTVGMS YGSYMEEKHV
     PPPNMTTNER RVIVPADPTL WSTDHVRQWL EWAVKEYGLL DVDVLLFQNI DGKELCKMTK
     DDFQRLTPSY NADILLSHLH YLRETPLPHL TSDDVDKALQ NSPRLMHARN TGGAAFIFPN
     TSVYPEATQR ITTRPDLPYE PPRRSAWTGH SHLTPQSKAA QPSPSAVPKT EDQRPQLDPY
     QILGPTSSRL ANPGSGQIQL WQFLLELLSD SSNSNCITWE GTNGEFKMTD PDEVARRWGE
     RKSKPNMNYD KLSRALRYYY DKNIMTKVHG KRYAYKFDFH GIAQALQPHP PESSLYKYPS
     DLPYMGSYHA HPQKMNFVSP HPPALPVTSS SFFASPNPYW NSPTGGIYPN TRLPASHMPS
     HLGTYY
//