ELF2_MOUSE
ID ELF2_MOUSE Reviewed; 593 AA.
AC Q9JHC9; Q6NST2; Q8BTX8; Q9JHC7; Q9JHC8; Q9JHD0;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=ETS-related transcription factor Elf-2;
DE AltName: Full=E74-like factor 2;
DE AltName: Full=New ETS-related factor;
GN Name=Elf2 {ECO:0000312|MGI:MGI:1916507}; Synonyms=Nerf;
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] {ECO:0000305, ECO:0000312|EMBL:AAF67191.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, AND
RP INTERACTION WITH LMO2.
RC TISSUE=T-cell {ECO:0000269|PubMed:9001422};
RX PubMed=9001422; DOI=10.1038/sj.leu.2400516;
RA Wilkinson D.A., Neale G.A.M., Mao S., Naeve C.W., Goorha R.M.;
RT "Elf-2, a rhombotin-2 binding ets transcription factor: discovery and
RT potential role in T cell leukemia.";
RL Leukemia 11:86-96(1997).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAF67192.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
RA Wilkinson D.A., Neale G.A.M., Mao S., Fernandes E.R., Davenport J.W.,
RA Naeve C.W., Goorha R.M.;
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=NOD; TISSUE=Thymus;
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 [4] {ECO:0000305, ECO:0000312|EMBL:AAH69901.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-175 (ISOFORM 1).
RC STRAIN=NMRI {ECO:0000312|EMBL:AAH69901.1};
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH69901.1};
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107; THR-182; SER-185;
RP SER-191; SER-372 AND THR-376, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Spleen, and Testis;
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).
RN [6]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-496, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Probably transcriptionally activates the LYN and BLK
CC promoters and acts synergistically with RUNX1 to transactivate the BLK
CC promoter. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with LIM domains of LMO2. Interacts via its N-
CC terminal region with RUNX1. {ECO:0000250|UniProtKB:Q15723,
CC ECO:0000269|PubMed:9001422}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=4;
CC IsoId=Q9JHC9-1; Sequence=Displayed;
CC Name=1 {ECO:0000269|PubMed:9001422}; Synonyms=elf-2a
CC {ECO:0000303|PubMed:9001422};
CC IsoId=Q9JHC9-2; Sequence=VSP_014160;
CC Name=2 {ECO:0000269|PubMed:9001422}; Synonyms=elf-2b
CC {ECO:0000303|PubMed:9001422};
CC IsoId=Q9JHC9-3; Sequence=VSP_014159, VSP_014160;
CC Name=3;
CC IsoId=Q9JHC9-4; Sequence=VSP_014159;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined. Highest levels
CC in thymocytes and bone marrow. {ECO:0000269|PubMed:9001422}.
CC -!- SIMILARITY: Belongs to the ETS family. {ECO:0000255}.
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DR EMBL; AF256216; AAF67191.1; -; mRNA.
DR EMBL; AF256217; AAF67192.1; -; mRNA.
DR EMBL; AF256218; AAF67193.1; -; mRNA.
DR EMBL; AF256219; AAF67194.1; -; mRNA.
DR EMBL; AK088422; BAC40346.1; -; mRNA.
DR EMBL; BC069901; AAH69901.1; -; mRNA.
DR CCDS; CCDS17337.1; -. [Q9JHC9-1]
DR CCDS; CCDS71240.1; -. [Q9JHC9-3]
DR CCDS; CCDS71241.1; -. [Q9JHC9-4]
DR CCDS; CCDS71242.1; -. [Q9JHC9-2]
DR RefSeq; NP_001277988.1; NM_001291059.1. [Q9JHC9-2]
DR RefSeq; NP_001277991.1; NM_001291062.1. [Q9JHC9-3]
DR RefSeq; NP_001277992.1; NM_001291063.1. [Q9JHC9-4]
DR RefSeq; NP_075991.1; NM_023502.2. [Q9JHC9-1]
DR AlphaFoldDB; Q9JHC9; -.
DR SMR; Q9JHC9; -.
DR BioGRID; 213319; 5.
DR IntAct; Q9JHC9; 2.
DR STRING; 10090.ENSMUSP00000088678; -.
DR iPTMnet; Q9JHC9; -.
DR PhosphoSitePlus; Q9JHC9; -.
DR EPD; Q9JHC9; -.
DR jPOST; Q9JHC9; -.
DR MaxQB; Q9JHC9; -.
DR PaxDb; Q9JHC9; -.
DR PeptideAtlas; Q9JHC9; -.
DR PRIDE; Q9JHC9; -.
DR ProteomicsDB; 277776; -. [Q9JHC9-1]
DR ProteomicsDB; 277777; -. [Q9JHC9-2]
DR ProteomicsDB; 277778; -. [Q9JHC9-3]
DR ProteomicsDB; 277779; -. [Q9JHC9-4]
DR Antibodypedia; 896; 157 antibodies from 26 providers.
DR DNASU; 69257; -.
DR Ensembl; ENSMUST00000062009; ENSMUSP00000061076; ENSMUSG00000037174. [Q9JHC9-2]
DR Ensembl; ENSMUST00000108051; ENSMUSP00000103686; ENSMUSG00000037174. [Q9JHC9-3]
DR Ensembl; ENSMUST00000108053; ENSMUSP00000103688; ENSMUSG00000037174. [Q9JHC9-4]
DR Ensembl; ENSMUST00000163748; ENSMUSP00000126871; ENSMUSG00000037174. [Q9JHC9-1]
DR Ensembl; ENSMUST00000194641; ENSMUSP00000141197; ENSMUSG00000037174. [Q9JHC9-1]
DR GeneID; 69257; -.
DR KEGG; mmu:69257; -.
DR UCSC; uc008pdo.2; mouse. [Q9JHC9-3]
DR UCSC; uc008pdp.2; mouse. [Q9JHC9-4]
DR UCSC; uc008pdq.2; mouse. [Q9JHC9-1]
DR CTD; 1998; -.
DR MGI; MGI:1916507; Elf2.
DR VEuPathDB; HostDB:ENSMUSG00000037174; -.
DR eggNOG; KOG3804; Eukaryota.
DR GeneTree; ENSGT00940000154953; -.
DR HOGENOM; CLU_027279_2_0_1; -.
DR InParanoid; Q9JHC9; -.
DR OMA; MKNHEEN; -.
DR OrthoDB; 837296at2759; -.
DR PhylomeDB; Q9JHC9; -.
DR TreeFam; TF318679; -.
DR Reactome; R-MMU-8939245; RUNX1 regulates transcription of genes involved in BCR signaling.
DR BioGRID-ORCS; 69257; 4 hits in 76 CRISPR screens.
DR ChiTaRS; Elf2; mouse.
DR PRO; PR:Q9JHC9; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9JHC9; protein.
DR Bgee; ENSMUSG00000037174; Expressed in spermatocyte and 281 other tissues.
DR ExpressionAtlas; Q9JHC9; baseline and differential.
DR Genevisible; Q9JHC9; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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; ISO:MGI.
DR GO; GO:0043565; F: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:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR000418; Ets_dom.
DR InterPro; IPR046328; ETS_fam.
DR InterPro; IPR022084; TF_Elf_N.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR11849; PTHR11849; 1.
DR Pfam; PF12310; Elf-1_N; 1.
DR Pfam; PF00178; Ets; 1.
DR PRINTS; PR00454; ETSDOMAIN.
DR SMART; SM00413; ETS; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS00345; ETS_DOMAIN_1; 1.
DR PROSITE; PS00346; ETS_DOMAIN_2; 1.
DR PROSITE; PS50061; ETS_DOMAIN_3; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; DNA-binding; Isopeptide bond; Methylation;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..593
FT /note="ETS-related transcription factor Elf-2"
FT /id="PRO_0000204088"
FT DNA_BIND 208..290
FT /note="ETS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00237"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 182
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15723"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 376
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15723"
FT MOD_RES 496
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 523
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q15723"
FT CROSSLNK 538
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15723"
FT VAR_SEQ 1..79
FT /note="MASAVVDSGGSALELPSDGGENQEGGDTGPDCPAVIVEPVPSARLEQGYAAQ
FT VLVYDDETYMMQDVAEEQEVETENSET -> MATSLHEGPTNQLDLLIRA (in
FT isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072,
FT ECO:0000303|PubMed:9001422, ECO:0000303|Ref.2"
FT /id="VSP_014159"
FT VAR_SEQ 118..129
FT /note="Missing (in isoform 1 and isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:9001422"
FT /id="VSP_014160"
FT CONFLICT 159
FT /note="S -> W (in Ref. 3; BAC40346)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="M -> K (in Ref. 4; AAH69901)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 593 AA; 63203 MW; A6E67486141AB903 CRC64;
MASAVVDSGG SALELPSDGG ENQEGGDTGP DCPAVIVEPV PSARLEQGYA AQVLVYDDET
YMMQDVAEEQ EVETENSETV EASVHSSNAH CTDKTIEAAE ALLHMESPTC LRDSRSPVEV
FVPPCISTPE FIHAAMRPDV ITETVVEVST EESEPMDASP IPTSPDSHEP MKKKKVGRKP
KTQQSPVSNG SPELGIKKKA REGKGNTTYL WEFLLDLLQD KNTCPRYIKW TQREKGIFKL
VDSKAVSKLW GKHKNKPDMN YETMGRALRY YYQRGILAKV EGQRLVYQFK DMPKNIVVID
DDKSETCPED LAAAADDKSL ERVSLSAESL LKAATAVRGG KNSSPLNCSR AEKGVARVVN
ITSPTHDGSS RSPTTTAPVS AAAAPRTVRV AMQVPVVMTS LGQKISAVAV QSVNAGTGSP
LITSTSPASA SSPKVVIQTV PTVMPASTEN GDRITMQPAK IITIPATQLA QCQLQAKSNL
TGSGSINIVG TPLAVRALTP VSIAHGTPVM RLSVPAQQAS GQTPPRVISA LLKGPEGKSE
AKKQEHDVKT LQLVEEKGAD GNKTVTHVVV VSAPSAIALP VTMKTEGLVT CEK
