ERG_MOUSE
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 03-AUG-2022, entry version 174.
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.ENSMUSP00000109477; -.
DR iPTMnet; P81270; -.
DR PhosphoSitePlus; P81270; -.
DR MaxQB; P81270; -.
DR PaxDb; P81270; -.
DR PRIDE; P81270; -.
DR ProteomicsDB; 275775; -. [P81270-1]
DR ProteomicsDB; 275776; -. [P81270-3]
DR ProteomicsDB; 275777; -. [P81270-2]
DR ProteomicsDB; 275778; -. [P81270-4]
DR Antibodypedia; 4338; 638 antibodies from 41 providers.
DR DNASU; 13876; -.
DR Ensembl; ENSMUST00000113848; ENSMUSP00000109479; ENSMUSG00000040732. [P81270-2]
DR Ensembl; ENSMUST00000122199; ENSMUSP00000114072; ENSMUSG00000040732. [P81270-4]
DR Ensembl; ENSMUST00000233269; ENSMUSP00000156926; ENSMUSG00000040732. [P81270-3]
DR Ensembl; ENSMUST00000233881; ENSMUSP00000156669; ENSMUSG00000040732. [P81270-1]
DR GeneID; 13876; -.
DR KEGG; mmu:13876; -.
DR UCSC; uc008acb.2; mouse. [P81270-1]
DR UCSC; uc008acc.2; mouse. [P81270-2]
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; 1113327at2759; -.
DR PhylomeDB; P81270; -.
DR TreeFam; TF350537; -.
DR BioGRID-ORCS; 13876; 2 hits in 73 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 225 other tissues.
DR ExpressionAtlas; P81270; baseline and differential.
DR Genevisible; P81270; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0030154; P:cell differentiation; IBA:GO_Central.
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; 1.10.10.10; -; 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; 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 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
