ENY2_MOUSE
ID ENY2_MOUSE Reviewed; 101 AA.
AC Q9JIX0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Transcription and mRNA export factor ENY2 {ECO:0000255|HAMAP-Rule:MF_03046};
DE AltName: Full=Enhancer of yellow 2 transcription factor homolog {ECO:0000255|HAMAP-Rule:MF_03046};
GN Name=Eny2;
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].
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Wolffian duct;
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].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Pancreas, 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).
CC -!- FUNCTION: Involved in mRNA export coupled transcription activation by
CC association with both the TREX-2 and the SAGA complexes. The
CC transcription regulatory histone acetylation (HAT) complex SAGA is a
CC multiprotein complex that activates transcription by remodeling
CC chromatin and mediating histone acetylation and deubiquitination.
CC Within the SAGA complex, participates in a subcomplex that specifically
CC deubiquitinates both histones H2A and H2B. The SAGA complex is
CC recruited to specific gene promoters by activators such as MYC, where
CC it is required for transcription. Required for nuclear receptor-
CC mediated transactivation. As a component of the TREX-2 complex,
CC involved in the export of mRNAs to the cytoplasm through the nuclear
CC pores (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9NPA8}.
CC -!- SUBUNIT: Component of the nuclear pore complex (NPC)-associated TREX-2
CC complex (transcription and export complex 2), composed of at least
CC ENY2, the isoform GANP of the MCM3AP gene, PCID2, SEM1, and either
CC centrin CETN2 or CETN3. TREX-2 contains 2 ENY2 chains. The TREX-2
CC complex also associates with ALYREF/ALY and with the nucleoporin NUP153
CC (By similarity). Component of some SAGA transcription coactivator-HAT
CC complexes, at least composed of ATXN7, ATXN7L3, ENY2, GCN5L2, SUPT3H,
CC TAF10, TRRAP and USP22. Within the SAGA complex, ENY2, ATXN7, ATXN7L3,
CC and USP22 form an additional subcomplex of SAGA called the DUB module
CC (deubiquitination module). Interacts with the RNA polymerase II subunit
CC POLR2A (By similarity). Interacts with ATXN7L3B (By similarity).
CC {ECO:0000250|UniProtKB:Q9NPA8, ECO:0000255|HAMAP-Rule:MF_03046}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000255|HAMAP-
CC Rule:MF_03046}.
CC -!- SIMILARITY: Belongs to the ENY2 family. {ECO:0000255|HAMAP-
CC Rule:MF_03046}.
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DR EMBL; AF173297; AAF89830.1; -; mRNA.
DR EMBL; AK032957; BAC28097.1; -; mRNA.
DR EMBL; BC048361; AAH48361.1; -; mRNA.
DR CCDS; CCDS27456.1; -.
DR RefSeq; NP_778174.1; NM_175009.3.
DR AlphaFoldDB; Q9JIX0; -.
DR SMR; Q9JIX0; -.
DR BioGRID; 230155; 10.
DR ComplexPortal; CPX-6803; SAGA complex, KAT2B variant.
DR ComplexPortal; CPX-916; TFTC histone acetylation complex.
DR ComplexPortal; CPX-920; SAGA complex, KAT2A variant.
DR IntAct; Q9JIX0; 1.
DR MINT; Q9JIX0; -.
DR STRING; 10090.ENSMUSP00000052905; -.
DR iPTMnet; Q9JIX0; -.
DR PhosphoSitePlus; Q9JIX0; -.
DR EPD; Q9JIX0; -.
DR jPOST; Q9JIX0; -.
DR MaxQB; Q9JIX0; -.
DR PaxDb; Q9JIX0; -.
DR PeptideAtlas; Q9JIX0; -.
DR PRIDE; Q9JIX0; -.
DR ProteomicsDB; 275923; -.
DR Antibodypedia; 7042; 120 antibodies from 19 providers.
DR DNASU; 223527; -.
DR Ensembl; ENSMUST00000060652; ENSMUSP00000052905; ENSMUSG00000022338.
DR GeneID; 223527; -.
DR KEGG; mmu:223527; -.
DR UCSC; uc007vpu.1; mouse.
DR CTD; 56943; -.
DR MGI; MGI:1919286; Eny2.
DR VEuPathDB; HostDB:ENSMUSG00000022338; -.
DR eggNOG; KOG4479; Eukaryota.
DR GeneTree; ENSGT00390000011748; -.
DR HOGENOM; CLU_134052_1_1_1; -.
DR InParanoid; Q9JIX0; -.
DR OrthoDB; 1538551at2759; -.
DR PhylomeDB; Q9JIX0; -.
DR TreeFam; TF326556; -.
DR BioGRID-ORCS; 223527; 25 hits in 74 CRISPR screens.
DR ChiTaRS; Eny2; mouse.
DR PRO; PR:Q9JIX0; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9JIX0; protein.
DR Bgee; ENSMUSG00000022338; Expressed in yolk sac and 257 other tissues.
DR ExpressionAtlas; Q9JIX0; baseline and differential.
DR Genevisible; Q9JIX0; MM.
DR GO; GO:0071819; C:DUBm complex; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0044615; C:nuclear pore nuclear basket; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000124; C:SAGA complex; ISS:UniProtKB.
DR GO; GO:0070390; C:transcription export complex 2; ISS:UniProtKB.
DR GO; GO:0033276; C:transcription factor TFTC complex; IC:ComplexPortal.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016578; P:histone deubiquitination; ISO:MGI.
DR GO; GO:0043966; P:histone H3 acetylation; ISO:MGI.
DR GO; GO:0035521; P:monoubiquitinated histone deubiquitination; ISO:MGI.
DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; ISO:MGI.
DR GO; GO:0061179; P:negative regulation of insulin secretion involved in cellular response to glucose stimulus; ISO:MGI.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006282; P:regulation of DNA repair; IC:ComplexPortal.
DR GO; GO:0043484; P:regulation of RNA splicing; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
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; Isopeptide bond; mRNA transport; Nucleus;
KW Protein transport; Reference proteome; Transcription;
KW Transcription regulation; Translocation; Transport; Ubl conjugation.
FT CHAIN 1..101
FT /note="Transcription and mRNA export factor ENY2"
FT /id="PRO_0000314131"
FT CROSSLNK 74
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9NPA8"
SQ SEQUENCE 101 AA; 11529 MW; A0617024C59AABFB CRC64;
MVVSKMNKDA QMRAAINQKL IETGERERLK ELLRAKLIEC GWKDQLKAHC KEVIKEKGLE
HVTVDDLVAE ITPKGRALVP DSVKKELLQR IRTFLAQHAS L
