ENY2_DROME
ID ENY2_DROME Reviewed; 101 AA.
AC Q9VYX1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Enhancer of yellow 2 transcription factor {ECO:0000255|HAMAP-Rule:MF_03046};
GN Name=e(y)2 {ECO:0000255|HAMAP-Rule:MF_03046}; Synonyms=ENY2;
GN ORFNames=CG15191;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND INTERACTION WITH E(Y)1.
RX PubMed=11438676; DOI=10.1128/mcb.21.15.5223-5231.2001;
RA Georgieva S., Nabirochkina E., Dilworth F.J., Eickhoff H., Becker P.,
RA Tora L., Georgiev P., Soldatov A.;
RT "The novel transcription factor e(y)2 interacts with TAF(II)40 and
RT potentiates transcription activation on chromatin templates.";
RL Mol. Cell. Biol. 21:5223-5231(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5]
RP FUNCTION, IDENTIFICATION IN THE SAGA COMPLEX, IDENTIFICATION IN THE AMEX
RP COMPLEX, SUBCELLULAR LOCATION, AND INTERACTION WITH XMAS.
RX PubMed=18034162; DOI=10.1038/sj.emboj.7601901;
RA Kurshakova M.M., Krasnov A.N., Kopytova D.V., Shidlovskii Y.V.,
RA Nikolenko J.V., Nabirochkina E.N., Spehner D., Schultz P., Tora L.,
RA Georgieva S.G.;
RT "SAGA and a novel Drosophila export complex anchor efficient transcription
RT and mRNA export to NPC.";
RL EMBO J. 26:4956-4965(2007).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SU(HW).
RX PubMed=17643381; DOI=10.1016/j.molcel.2007.05.035;
RA Kurshakova M., Maksimenko O., Golovnin A., Pulina M., Georgieva S.,
RA Georgiev P., Krasnov A.;
RT "Evolutionarily conserved E(y)2/Sus1 protein is essential for the barrier
RT activity of Su(Hw)-dependent insulators in Drosophila.";
RL Mol. Cell 27:332-338(2007).
RN [7]
RP FUNCTION.
RX PubMed=18206972; DOI=10.1016/j.molcel.2007.12.011;
RA Zhao Y., Lang G., Ito S., Bonnet J., Metzger E., Sawatsubashi S.,
RA Suzuki E., Le Guezennec X., Stunnenberg H.G., Krasnov A., Georgieva S.G.,
RA Schuele R., Takeyama K., Kato S., Tora L., Devys D.;
RT "A TFTC/STAGA module mediates histone H2A and H2B deubiquitination,
RT coactivates nuclear receptors, and counteracts heterochromatin silencing.";
RL Mol. Cell 29:92-101(2008).
RN [8]
RP FUNCTION, AND IDENTIFICATION IN THE SAGA COMPLEX.
RX PubMed=19947544;
RA Kurshakova M.M., Kopytova D.V., Nabirochkina E.N., Nikolenko Y.V.,
RA Shidlovskii Y.V., Georgieva S.G., Krasnov A.N.;
RT "Conservative E(y)2/Sus1 protein is the member of SAGA complex and new
RT nuclear pore-associated complex in Drosophila.";
RL Genetika 45:1332-1340(2009).
RN [9]
RP FUNCTION, IDENTIFICATION IN THE THO COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=20714859; DOI=10.1134/s1607672910040174;
RA Gurskiy D.Y., Nabirochkina E.N., Kopytova D.V., Nikolenko Y.V., Ilyin Y.V.,
RA Georgieva S.G., Shidlovskii Y.V.;
RT "ENY2 protein forms a part of the THO complex of Drosophila melanogaster.";
RL Dokl. Biochem. Biophys. 433:212-215(2010).
RN [10]
RP FUNCTION, IDENTIFICATION IN THE THO COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=20048002; DOI=10.1101/gad.550010;
RA Kopytova D.V., Orlova A.V., Krasnov A.N., Gurskiy D.Y., Nikolenko J.V.,
RA Nabirochkina E.N., Shidlovskii Y.V., Georgieva S.G.;
RT "Multifunctional factor ENY2 is associated with the THO complex and
RT promotes its recruitment onto nascent mRNA.";
RL Genes Dev. 24:86-96(2010).
RN [11]
RP INTERACTION WITH ORC3, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RX DOI=10.21767/2471-8084.100023;
RA Popova V., Georgieva S., Kopytova D.;
RT "Orc3, A Subunit of Drosophila Pre-Replication Complex Directly Binds mRNA
RT and Interacts with ENY2 Subunit of the TREX-2 mRNA Export Complex.";
RL Biochem. Mol. Biol. J. 2:1-7(2016).
RN [12]
RP FUNCTION, IDENTIFICATION IN THE AMEX COMPLEX, INTERACTION WITH ORC3 AND
RP ORC6, AND DEVELOPMENTAL STAGE.
RX PubMed=27016737; DOI=10.1093/nar/gkw192;
RA Kopytova D., Popova V., Kurshakova M., Shidlovskii Y., Nabirochkina E.,
RA Brechalov A., Georgiev G., Georgieva S.;
RT "ORC interacts with THSC/TREX-2 and its subunits promote Nxf1 association
RT with mRNP and mRNA export in Drosophila.";
RL Nucleic Acids Res. 44:4920-4933(2016).
RN [13]
RP INTERACTION WITH CG9890.
RX PubMed=30713769;
RA Fursova N.A., Nikolenko J.V., Soshnikova N.V., Mazina M.Y., Vorobyova N.E.,
RA Krasnov A.N.;
RT "Zinc Finger Protein CG9890 - New Component of ENY2-Containing Complexes of
RT Drosophila.";
RL Acta Naturae 10:110-114(2018).
CC -!- FUNCTION: Involved in mRNA export coupled transcription activation by
CC association with both the TREX-2/AMEX and the SAGA complexes
CC (PubMed:18034162, PubMed:19947544, PubMed:27016737). The SAGA complex
CC is a multiprotein complex that activates transcription by remodeling
CC chromatin and mediating histone acetylation and deubiquitination
CC (PubMed:11438676, PubMed:18206972). Within the SAGA complex,
CC participates in a subcomplex that specifically deubiquitinates histone
CC H2B (PubMed:18206972). The SAGA complex is recruited to specific gene
CC promoters by activators, where it is required for transcription
CC (PubMed:18034162, PubMed:19947544). Required for nuclear receptor-
CC mediated transactivation (PubMed:20714859, PubMed:20048002). Involved
CC in transcription elongation by recruiting the THO complex onto nascent
CC mRNA (PubMed:20048002). The TREX-2/AMEX complex functions in docking
CC export-competent ribonucleoprotein particles (mRNPs) to the nuclear
CC entrance of the nuclear pore complex (nuclear basket)
CC (PubMed:27016737). TREX-2/AMEX participates in mRNA export and accurate
CC chromatin positioning in the nucleus by tethering genes to the nuclear
CC periphery (PubMed:17643381, PubMed:27016737). Recruited to the su(Hw)
CC insulators via its interaction with su(Hw) and participates in the
CC barrier activity of such insulators (PubMed:17643381). In contrast, it
CC does not participate in the enhancer-blocking activity of the su(Hw)
CC insulators (PubMed:17643381). {ECO:0000269|PubMed:11438676,
CC ECO:0000269|PubMed:17643381, ECO:0000269|PubMed:18034162,
CC ECO:0000269|PubMed:18206972, ECO:0000269|PubMed:19947544,
CC ECO:0000269|PubMed:20048002, ECO:0000269|PubMed:20714859,
CC ECO:0000269|PubMed:27016737}.
CC -!- SUBUNIT: Component of the nuclear pore complex (NPC)-associated TREX-
CC 2/AMEX complex (anchoring and mRNA export complex), composed of e(y)2,
CC xmas and PCID2 (PubMed:18034162, PubMed:27016737). Within the TREX-2/
CC AMEX complex, interactions with xmas is required for localization to
CC the nuclear periphery (PubMed:18034162). Component of the SAGA
CC transcription coactivator-HAT complexes, at least composed of Ada2b,
CC e(y)2, Pcaf/Gcn5, Taf10 and Nipped-A/Trrap (PubMed:18034162,
CC PubMed:19947544). Within the SAGA complex, e(y)2, Sgf11, and
CC not/nonstop form an additional subcomplex of SAGA called the DUB module
CC (deubiquitination module) (By similarity). Component of the THO
CC complex, composed of at least e(y)2, HPR1, THO2, THOC5, THOC6 and THOC7
CC (PubMed:20714859, PubMed:20048002). Interacts with e(y)1
CC (PubMed:11438676). Interacts with su(Hw) (via zinc fingers)
CC (PubMed:17643381). Interacts with the nuclear pore complex (NPC)
CC (PubMed:18034162, PubMed:20048002). Interaction between the TREX-2/AMEX
CC complex and the ORC complex is required for ORC localization to mRNPs,
CC and consequently mRNA export (PubMed:27016737, Ref.11). Within the
CC TREX-2/AMEX-ORC complex, interacts with Orc6 and (via N-terminus or C-
CC terminus) with Orc3 (PubMed:27016737, Ref.11). Interacts with the zinc
CC finger protein CG9890 (PubMed:30713769). {ECO:0000255|HAMAP-
CC Rule:MF_03046, ECO:0000269|PubMed:11438676,
CC ECO:0000269|PubMed:17643381, ECO:0000269|PubMed:18034162,
CC ECO:0000269|PubMed:19947544, ECO:0000269|PubMed:20048002,
CC ECO:0000269|PubMed:20714859, ECO:0000269|PubMed:27016737,
CC ECO:0000269|PubMed:30713769, ECO:0000269|Ref.11}.
CC -!- INTERACTION:
CC Q9VYX1; Q9VZJ9: Mul1; NbExp=4; IntAct=EBI-2549759, EBI-156824;
CC Q9VYX1; Q9VRY7: Rsph3; NbExp=4; IntAct=EBI-2549759, EBI-15108291;
CC Q9VYX1; Q9U3V9: xmas-2; NbExp=5; IntAct=EBI-2549759, EBI-2550689;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000255|HAMAP-
CC Rule:MF_03046, ECO:0000269|PubMed:17643381,
CC ECO:0000269|PubMed:20048002}. Cytoplasm {ECO:0000255|HAMAP-
CC Rule:MF_03046, ECO:0000269|PubMed:27016737}. Nucleus membrane
CC {ECO:0000269|PubMed:18034162, ECO:0000269|PubMed:20048002,
CC ECO:0000269|PubMed:27016737}; Peripheral membrane protein
CC {ECO:0000269|PubMed:18034162, ECO:0000269|PubMed:20048002,
CC ECO:0000269|PubMed:27016737}. Nucleus {ECO:0000269|Ref.11}.
CC Note=Localizes to nuclear periphery, in contact with the nuclear pore
CC complex (NPC). {ECO:0000269|PubMed:18034162,
CC ECO:0000269|PubMed:20048002}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11438676}.
CC -!- DEVELOPMENTAL STAGE: Detected in embryos (at protein level)
CC (PubMed:27016737, Ref.11). Expressed at all stages of development
CC (PubMed:11438676). {ECO:0000269|PubMed:11438676,
CC ECO:0000269|PubMed:27016737, ECO:0000269|Ref.11}.
CC -!- SIMILARITY: Belongs to the ENY2 family. {ECO:0000255|HAMAP-
CC Rule:MF_03046}.
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DR EMBL; AF173294; AAF89805.1; -; Genomic_DNA.
DR EMBL; AF173295; AAF89806.1; -; mRNA.
DR EMBL; AE014298; AAF48062.1; -; Genomic_DNA.
DR EMBL; BT022196; AAY51590.1; -; mRNA.
DR RefSeq; NP_524846.1; NM_080107.3.
DR AlphaFoldDB; Q9VYX1; -.
DR SMR; Q9VYX1; -.
DR BioGRID; 69925; 50.
DR IntAct; Q9VYX1; 16.
DR MINT; Q9VYX1; -.
DR STRING; 7227.FBpp0073385; -.
DR PaxDb; Q9VYX1; -.
DR DNASU; 45848; -.
DR EnsemblMetazoa; FBtr0073540; FBpp0073385; FBgn0000618.
DR GeneID; 45848; -.
DR KEGG; dme:Dmel_CG15191; -.
DR CTD; 45848; -.
DR FlyBase; FBgn0000618; e(y)2.
DR VEuPathDB; VectorBase:FBgn0000618; -.
DR eggNOG; KOG4479; Eukaryota.
DR GeneTree; ENSGT00390000011748; -.
DR HOGENOM; CLU_134052_1_2_1; -.
DR InParanoid; Q9VYX1; -.
DR OMA; RLMCRNI; -.
DR OrthoDB; 1538551at2759; -.
DR PhylomeDB; Q9VYX1; -.
DR BioGRID-ORCS; 45848; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 45848; -.
DR PRO; PR:Q9VYX1; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0000618; Expressed in saliva-secreting gland and 25 other tissues.
DR ExpressionAtlas; Q9VYX1; baseline and differential.
DR Genevisible; Q9VYX1; DM.
DR GO; GO:0000785; C:chromatin; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0071819; C:DUBm complex; IDA:FlyBase.
DR GO; GO:0034399; C:nuclear periphery; IDA:FlyBase.
DR GO; GO:0005643; C:nuclear pore; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000124; C:SAGA complex; IDA:UniProtKB.
DR GO; GO:0070390; C:transcription export complex 2; IDA:FlyBase.
DR GO; GO:0070742; F:C2H2 zinc finger domain binding; IPI:FlyBase.
DR GO; GO:0003682; F:chromatin binding; IDA:FlyBase.
DR GO; GO:0043035; F:chromatin insulator sequence binding; IDA:UniProtKB.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IEA:UniProtKB-UniRule.
DR GO; GO:0001094; F:TFIID-class transcription factor complex binding; IPI:FlyBase.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0033696; P:heterochromatin boundary formation; IMP:FlyBase.
DR GO; GO:0016578; P:histone deubiquitination; IDA:FlyBase.
DR GO; GO:0006406; P:mRNA export from nucleus; IDA:FlyBase.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.246.140; -; 1.
DR HAMAP; MF_03046; ENY2_Sus1; 1.
DR InterPro; IPR018783; TF_ENY2.
DR InterPro; IPR038212; TF_EnY2_sf.
DR PANTHER; PTHR12514; PTHR12514; 1.
DR Pfam; PF10163; EnY2; 1.
PE 1: Evidence at protein level;
KW Activator; Chromatin regulator; Cytoplasm; Membrane; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..101
FT /note="Enhancer of yellow 2 transcription factor"
FT /id="PRO_0000314134"
SQ SEQUENCE 101 AA; 11474 MW; FC55DCBA1D2BAFCB CRC64;
MSTSGAVDQY TVLTGDRSKI KDLLCSRLTE CGWRDEVRLM CRNILMEKGT NNSFTVEQLI
AEVTPKARTL VPDAVKKELL MKIRTILTEI EEEPDEPEDE S
