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ETS-related transcription factor Elf-2 (E74-like factor 2) (New ETS-related factor)

 ELF2_HUMAN              Reviewed;         593 AA.
Q15723; E9PCX3; Q15724; Q15725; Q6P1K5;
21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
21-JUN-2005, sequence version 2.
05-DEC-2018, entry version 166.
RecName: Full=ETS-related transcription factor Elf-2;
AltName: Full=E74-like factor 2;
AltName: Full=New ETS-related factor;
Name=ELF2 {ECO:0000312|EMBL:AAF67195.1};
Synonyms=NERF {ECO:0000303|PubMed:8756667};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305, ECO:0000312|EMBL:AAB37759.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 5), FUNCTION, AND
TISSUE SPECIFICITY.
TISSUE=Fetal brain {ECO:0000269|PubMed:8756667},
Fetal liver {ECO:0000269|PubMed:8756667}, and
Spleen {ECO:0000312|EMBL:AAB37759.1};
PubMed=8756667; DOI=10.1128/MCB.16.9.5091;
Oettgen P., Akbarali Y., Boltax J., Best J., Kunsch C.,
Libermann T.A.;
"Characterization of NERF, a novel transcription factor related to the
Ets factor ELF-1.";
Mol. Cell. Biol. 16:5091-5106(1996).
[2] {ECO:0000305, ECO:0000312|EMBL:AAF67195.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
TISSUE=Chronic myeloid leukemia cell;
Wilkinson D.A., Neale G.A.M., Mao S., Fernandes E.R., Davenport J.W.,
Naeve C.W., Goorha R.M.;
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4] {ECO:0000305, ECO:0000312|EMBL:AAH34951.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
TISSUE=Testis {ECO:0000312|EMBL:AAH34951.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5] {ECO:0000305}
INTERACTION WITH RUNX1.
PubMed=10207087; DOI=10.1128/MCB.19.5.3635;
Mao S., Frank R.C., Zhang J., Miyazaki Y., Nimer S.D.;
"Functional and physical interactions between AML1 proteins and an ETS
protein, MEF: implications for the pathogenesis of t(8;21)-positive
leukemias.";
Mol. Cell. Biol. 19:3635-3644(1999).
[6] {ECO:0000305}
FUNCTION, AND INTERACTION WITH RUNX1.
PubMed=14970218; DOI=10.1074/jbc.M309074200;
Cho J.-Y., Akbarali Y., Zerbini L.F., Gu X., Boltax J., Wang Y.,
Oettgen P., Zhang D.-E., Libermann T.A.;
"Isoforms of the Ets transcription factor NERF/ELF-2 physically
interact with AML1 and mediate opposing effects on AML1-mediated
transcription of the B cell-specific blk gene.";
J. Biol. Chem. 279:19512-19522(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-185 AND SER-430, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107; SER-185; SER-191;
SER-363 AND THR-521, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[13]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-494, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[14]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-536, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
-!- FUNCTION: Isoform 1 transcriptionally activates the LYN and BLK
promoters and acts synergistically with RUNX1 to transactivate the
BLK promoter.
-!- FUNCTION: Isoform 2 may function in repression of RUNX1-mediated
transactivation.
-!- SUBUNIT: Interacts with the LIM domains of LMO2 (By similarity).
Interacts via its N-terminal region with RUNX1.
{ECO:0000250|UniProtKB:Q9JHC9, ECO:0000269|PubMed:10207087,
ECO:0000269|PubMed:14970218}.
-!- INTERACTION:
Q01196:RUNX1; NbExp=2; IntAct=EBI-956941, EBI-925904;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=5 {ECO:0000269|PubMed:8756667}; Synonyms=NERF-2b
{ECO:0000303|PubMed:8756667};
IsoId=Q15723-5; Sequence=Displayed;
Name=1 {ECO:0000269|PubMed:8756667}; Synonyms=NERF-2
{ECO:0000303|PubMed:8756667}, NERF-2a
{ECO:0000303|PubMed:8756667};
IsoId=Q15723-1; Sequence=VSP_014155;
Name=2 {ECO:0000269|PubMed:8756667}; Synonyms=NERF-1a
{ECO:0000303|PubMed:8756667};
IsoId=Q15723-2; Sequence=VSP_014154, VSP_014155;
Name=3 {ECO:0000269|PubMed:8756667}; Synonyms=NERF-1b
{ECO:0000303|PubMed:8756667};
IsoId=Q15723-3; Sequence=VSP_014154;
Name=4 {ECO:0000305};
IsoId=Q15723-4; Sequence=VSP_014154, VSP_014156;
Note=No experimental confirmation available. {ECO:0000305};
-!- TISSUE SPECIFICITY: Expressed in all fetal and adult tissues
examined. Among fetal tissues, highest levels of expression
detected in heart, lung, liver and kidney, and lower levels in
brain. Among adult tissues, highest levels of expression detected
in heart, placenta, lung, skeletal muscle, spleen, thymus, testis
and ovary. Moderate expression in prostate, small intestine,
kidney, liver and pancreas, and weak expression in colon, brain
and peripheral blood lymphocytes. {ECO:0000269|PubMed:8756667}.
-!- SIMILARITY: Belongs to the ETS family. {ECO:0000255}.
-!- SEQUENCE CAUTION:
Sequence=AAH65025.1; Type=Frameshift; Positions=541; Evidence={ECO:0000305};
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EMBL; U43188; AAB37759.1; -; mRNA.
EMBL; U43189; AAB37760.1; -; mRNA.
EMBL; U43189; AAB37761.1; -; mRNA.
EMBL; AF256222; AAF67195.1; -; mRNA.
EMBL; AF256223; AAF67196.1; -; mRNA.
EMBL; AC024032; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC093602; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC034951; AAH34951.1; -; mRNA.
EMBL; BC065025; AAH65025.1; ALT_FRAME; mRNA.
CCDS; CCDS3744.1; -. [Q15723-1]
CCDS; CCDS3745.1; -. [Q15723-3]
CCDS; CCDS64062.1; -. [Q15723-2]
CCDS; CCDS64063.1; -. [Q15723-4]
CCDS; CCDS82954.1; -. [Q15723-5]
PIR; G02318; G02318.
RefSeq; NP_001263386.1; NM_001276457.1. [Q15723-4]
RefSeq; NP_001263387.1; NM_001276458.1. [Q15723-2]
RefSeq; NP_001263388.1; NM_001276459.1.
RefSeq; NP_001317965.1; NM_001331036.1. [Q15723-5]
RefSeq; NP_006865.1; NM_006874.3. [Q15723-3]
RefSeq; NP_973728.1; NM_201999.2. [Q15723-1]
RefSeq; XP_005262861.1; XM_005262804.2. [Q15723-1]
UniGene; Hs.634040; -.
ProteinModelPortal; Q15723; -.
BioGrid; 108313; 18.
IntAct; Q15723; 10.
MINT; Q15723; -.
STRING; 9606.ENSP00000265495; -.
iPTMnet; Q15723; -.
PhosphoSitePlus; Q15723; -.
DMDM; 68052029; -.
EPD; Q15723; -.
PaxDb; Q15723; -.
PeptideAtlas; Q15723; -.
PRIDE; Q15723; -.
ProteomicsDB; 60718; -.
ProteomicsDB; 60719; -. [Q15723-1]
ProteomicsDB; 60720; -. [Q15723-2]
ProteomicsDB; 60721; -. [Q15723-3]
ProteomicsDB; 60722; -. [Q15723-4]
DNASU; 1998; -.
Ensembl; ENST00000358635; ENSP00000351458; ENSG00000109381. [Q15723-3]
Ensembl; ENST00000379549; ENSP00000368867; ENSG00000109381. [Q15723-4]
Ensembl; ENST00000379550; ENSP00000368868; ENSG00000109381. [Q15723-5]
Ensembl; ENST00000394235; ENSP00000377782; ENSG00000109381. [Q15723-1]
Ensembl; ENST00000510408; ENSP00000426997; ENSG00000109381. [Q15723-2]
GeneID; 1998; -.
KEGG; hsa:1998; -.
UCSC; uc003ihm.3; human. [Q15723-5]
CTD; 1998; -.
DisGeNET; 1998; -.
EuPathDB; HostDB:ENSG00000109381.19; -.
GeneCards; ELF2; -.
H-InvDB; HIX0164010; -.
HGNC; HGNC:3317; ELF2.
HPA; HPA006057; -.
HPA; HPA071166; -.
neXtProt; NX_Q15723; -.
OpenTargets; ENSG00000109381; -.
PharmGKB; PA27745; -.
eggNOG; KOG3804; Eukaryota.
eggNOG; ENOG4111K4J; LUCA.
GeneTree; ENSGT00940000154953; -.
HOGENOM; HOG000049253; -.
HOVERGEN; HBG007183; -.
InParanoid; Q15723; -.
KO; K09428; -.
OMA; GSNVHCT; -.
OrthoDB; EOG091G04CD; -.
PhylomeDB; Q15723; -.
TreeFam; TF318679; -.
Reactome; R-HSA-8939245; RUNX1 regulates transcription of genes involved in BCR signaling.
SignaLink; Q15723; -.
SIGNOR; Q15723; -.
ChiTaRS; ELF2; human.
GeneWiki; ELF2; -.
GenomeRNAi; 1998; -.
PRO; PR:Q15723; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000109381; Expressed in 219 organ(s), highest expression level in stomach.
CleanEx; HS_ELF2; -.
ExpressionAtlas; Q15723; baseline and differential.
Genevisible; Q15723; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:NTNU_SB.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0050855; P:regulation of B cell receptor signaling pathway; TAS:Reactome.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:UniProtKB.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR000418; Ets_dom.
InterPro; IPR022084; TF_Elf_N.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
Pfam; PF12310; Elf-1_N; 1.
Pfam; PF00178; Ets; 1.
PRINTS; PR00454; ETSDOMAIN.
SMART; SM00413; ETS; 1.
SUPFAM; SSF46785; SSF46785; 1.
PROSITE; PS00345; ETS_DOMAIN_1; 1.
PROSITE; PS00346; ETS_DOMAIN_2; 1.
PROSITE; PS50061; ETS_DOMAIN_3; 1.
1: Evidence at protein level;
Activator; Alternative splicing; Complete proteome; DNA-binding;
Isopeptide bond; Methylation; Nucleus; Phosphoprotein;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 593 ETS-related transcription factor Elf-2.
/FTId=PRO_0000204087.
DNA_BIND 208 290 ETS. {ECO:0000255|PROSITE-
ProRule:PRU00237}.
MOD_RES 107 107 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 182 182 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9JHC9}.
MOD_RES 185 185 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 191 191 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 363 363 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 372 372 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 376 376 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9JHC9}.
MOD_RES 430 430 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 494 494 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 521 521 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 536 536 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447}.
VAR_SEQ 1 79 MTSAVVDSGGTILELSSNGVENQEESEKVSEYPAVIVEPVP
SARLEQGYAAQVLVYDDETYMMQDVAEEQEVETENVET ->
MATSLHEGPTNQLDLLIRA (in isoform 2,
isoform 3 and isoform 4).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8756667,
ECO:0000303|Ref.2}.
/FTId=VSP_014154.
VAR_SEQ 117 129 PVEVFVPPCVSTP -> P (in isoform 1 and
isoform 2). {ECO:0000303|PubMed:8756667,
ECO:0000303|Ref.2}.
/FTId=VSP_014155.
VAR_SEQ 175 203 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_014156.
SEQUENCE 593 AA; 63967 MW; B67013B453559910 CRC64;
MTSAVVDSGG TILELSSNGV ENQEESEKVS EYPAVIVEPV PSARLEQGYA AQVLVYDDET
YMMQDVAEEQ EVETENVETV EASVHSSNAH CTDKTIEAAE ALLHMESPTC LRDSRSPVEV
FVPPCVSTPE FIHAAMRPDV ITETVVEVST EESEPMDTSP IPTSPDSHEP MKKKKVGRKP
KTQQSPISNG SPELGIKKKP REGKGNTTYL WEFLLDLLQD KNTCPRYIKW TQREKGIFKL
VDSKAVSKLW GKHKNKPDMN YETMGRALRY YYQRGILAKV EGQRLVYQFK DMPKNIVVID
DDKSETCNED LAGTTDEKSL ERVSLSAESL LKAASSVRSG KNSSPINCSR AEKGVARVVN
ITSPGHDASS RSPTTTASVS ATAAPRTVRV AMQVPVVMTS LGQKISTVAV QSVNAGAPLI
TSTSPTTATS PKVVIQTIPT VMPASTENGD KITMQPAKII TIPATQLAQC QLQTKSNLTG
SGSINIVGTP LAVRALTPVS IAHGTPVMRL SMPTQQASGQ TPPRVISAVI KGPEVKSEAV
AKKQEHDVKT LQLVEEKPAD GNKTVTHVVV VSAPSAIALP VTMKTEGLVT CEK


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18-003-42070 ETS-related transcription factor Elf-2 - E74-like factor 2; New ETS-related factor Polyclonal 0.05 mg Aff Pur
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EIAAB11483 Dmrt8.1,Dmrtc1,Dmrtc1a,Doublesex- and mab-3-related transcription factor 8.1,Doublesex- and mab-3-related transcription factor C1,Mouse,Mus musculus
EIAAB27019 Chicken,Gallus gallus,NFE2L1,NF-E2-related factor 1,NFE2-related factor 1,NRF1,Nuclear factor erythroid 2-related factor 1,Nuclear factor, erythroid derived 2, like 1,RCJMB04_7g14
EIAAB11491 Bos taurus,Bovine,DMRT5,DMRTA2,Doublesex- and mab-3-related transcription factor 5,Doublesex- and mab-3-related transcription factor A2
EIAAB11490 Dmrt5,Dmrta2,Doublesex- and mab-3-related transcription factor 5,Doublesex- and mab-3-related transcription factor A2,Mouse,Mus musculus
EIAAB11481 Dmrt6,Dmrtb1,Doublesex- and mab-3-related transcription factor 6,Doublesex- and mab-3-related transcription factor B1,Mouse,Mus musculus
EIAAB11488 Dmrt7,Dmrtc2,Doublesex- and mab-3-related transcription factor 7,Doublesex- and mab-3-related transcription factor C2,Mouse,Mus musculus
EIAAB11480 Dmrt4,Dmrta1,Doublesex- and mab-3-related transcription factor 4,Doublesex- and mab-3-related transcription factor A1,Mouse,Mus musculus
EIAAB12785 E74-like factor 4,ELF4,ELFR,ETS-related transcription factor Elf-4,Homo sapiens,Human,MEF,Myeloid Elf-1-like factor
18-003-43244 Nuclear factor erythroid 2-related factor 2 - NF-E2-related factor 2; NFE2-related factor 2; Nuclear factor. erythroid derived 2. like 2; HEBP1 Polyclonal 0.1 mg Protein A


 

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