EMSY_MOUSE
ID EMSY_MOUSE Reviewed; 1264 AA.
AC Q8BMB0; Q5FWK5; Q80XU1; Q8VDW9;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=BRCA2-interacting transcriptional repressor EMSY {ECO:0000250|UniProtKB:Q7Z589};
GN Name=Emsy {ECO:0000250|UniProtKB:Q7Z589};
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, Czech II, and FVB/N;
RC TISSUE=Brain, Kidney, and Mammary gland;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-750 (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Mesonephros;
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 SUBCELLULAR LOCATION, AND INTERACTION WITH BRCA2.
RX PubMed=14651845; DOI=10.1016/s0092-8674(03)00930-9;
RA Hughes-Davies L., Huntsman D., Ruas M., Fuks F., Bye J., Chin S.-F.,
RA Milner J., Brown L.A., Hsu F., Gilks B., Nielsen T., Schulzer M., Chia S.,
RA Ragaz J., Cahn A., Linger L., Ozdag H., Cattaneo E., Jordanova E.S.,
RA Schuuring E., Yu D.S., Venkitaraman A., Ponder B., Doherty A., Aparicio S.,
RA Bentley D., Theillet C., Ponting C.P., Caldas C., Kouzarides T.;
RT "EMSY links the BRCA2 pathway to sporadic breast and ovarian cancer.";
RL Cell 115:523-535(2003).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT SER-192.
RC TISSUE=Brain;
RX PubMed=16452088; DOI=10.1074/mcp.t500040-mcp200;
RA Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G., Thalhammer A.,
RA Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F., Maltby D.A.,
RA Schoepfer R., Burlingame A.L.;
RT "O-linked N-acetylglucosamine proteomics of postsynaptic density
RT preparations using lectin weak affinity chromatography and mass
RT spectrometry.";
RL Mol. Cell. Proteomics 5:923-934(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-173; SER-177; SER-782 AND
RP SER-785, AND IDENTIFICATION BY MASS SPECTROMETRY [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).
CC -!- FUNCTION: Regulator which is able to repress transcription, possibly
CC via its interaction with a multiprotein chromatin remodeling complex
CC that modifies the chromatin (By similarity). Its interaction with BRCA2
CC suggests that it may play a central role in the DNA repair function of
CC BRCA2 (By similarity). Mediates ligand-dependent transcriptional
CC activation by nuclear hormone receptors (By similarity).
CC {ECO:0000250|UniProtKB:Q7Z589}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with the transactivation
CC domain of BRCA2 (PubMed:14651845). Interacts with CBX1 (via
CC chromoshadow domain) (By similarity). Interacts with ZMYND11 (By
CC similarity). Does not interact with CBX3 or CBX5 (By similarity).
CC Component of a nuclear receptor-mediated transcription complex composed
CC of at least ZNF335, CCAR2 and EMSY; the complex stimulates the
CC transcription of nuclear receptor target genes such as SOX9 and HOXA1
CC (By similarity). Within the complex interacts with CCAR2 and ZNF335 (By
CC similarity). Components of this complex may associate with components
CC of a histone methylation complex to form a complex at least composed of
CC ZNF335, HCFC1, CCAR2, EMSY, MKI67, RBBP5, ASH2L and WDR5 (By
CC similarity). Within this complex, interacts with ASH2L and RBBP5 (By
CC similarity). {ECO:0000250|UniProtKB:Q7Z589,
CC ECO:0000269|PubMed:14651845}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14651845}.
CC Note=Localizes to DNA damage markers in irradiated cells, suggesting
CC that it participates in DNA repair process.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BMB0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BMB0-2; Sequence=VSP_010433, VSP_010434;
CC Name=3;
CC IsoId=Q8BMB0-3; Sequence=VSP_010432;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH20109.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BC039956; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BC020109; AAH20109.1; ALT_INIT; mRNA.
DR EMBL; BC039956; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC089304; AAH89304.1; -; mRNA.
DR EMBL; AK032985; BAC28113.2; -; mRNA.
DR CCDS; CCDS40028.1; -. [Q8BMB0-1]
DR RefSeq; NP_758484.2; NM_172280.2. [Q8BMB0-1]
DR RefSeq; XP_006507693.1; XM_006507630.3. [Q8BMB0-2]
DR AlphaFoldDB; Q8BMB0; -.
DR SMR; Q8BMB0; -.
DR BioGRID; 231423; 6.
DR IntAct; Q8BMB0; 3.
DR STRING; 10090.ENSMUSP00000038216; -.
DR GlyGen; Q8BMB0; 7 sites.
DR iPTMnet; Q8BMB0; -.
DR PhosphoSitePlus; Q8BMB0; -.
DR EPD; Q8BMB0; -.
DR jPOST; Q8BMB0; -.
DR MaxQB; Q8BMB0; -.
DR PaxDb; Q8BMB0; -.
DR PeptideAtlas; Q8BMB0; -.
DR PRIDE; Q8BMB0; -.
DR ProteomicsDB; 277863; -. [Q8BMB0-1]
DR ProteomicsDB; 277864; -. [Q8BMB0-2]
DR ProteomicsDB; 277865; -. [Q8BMB0-3]
DR Antibodypedia; 31192; 183 antibodies from 27 providers.
DR DNASU; 233545; -.
DR Ensembl; ENSMUST00000038359; ENSMUSP00000038216; ENSMUSG00000035401. [Q8BMB0-2]
DR Ensembl; ENSMUST00000205276; ENSMUSP00000145858; ENSMUSG00000035401. [Q8BMB0-1]
DR GeneID; 233545; -.
DR KEGG; mmu:233545; -.
DR UCSC; uc009iko.1; mouse. [Q8BMB0-1]
DR UCSC; uc009ikp.1; mouse. [Q8BMB0-2]
DR UCSC; uc009ikr.1; mouse. [Q8BMB0-3]
DR CTD; 56946; -.
DR MGI; MGI:1924203; Emsy.
DR VEuPathDB; HostDB:ENSMUSG00000035401; -.
DR eggNOG; KOG4675; Eukaryota.
DR GeneTree; ENSGT00390000009554; -.
DR HOGENOM; CLU_007404_0_0_1; -.
DR InParanoid; Q8BMB0; -.
DR OMA; EYITTEC; -.
DR OrthoDB; 150416at2759; -.
DR PhylomeDB; Q8BMB0; -.
DR TreeFam; TF332401; -.
DR BioGRID-ORCS; 233545; 9 hits in 106 CRISPR screens.
DR ChiTaRS; Emsy; mouse.
DR PRO; PR:Q8BMB0; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BMB0; protein.
DR Bgee; ENSMUSG00000035401; Expressed in embryonic post-anal tail and 251 other tissues.
DR ExpressionAtlas; Q8BMB0; baseline and differential.
DR Genevisible; Q8BMB0; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 1.10.1240.40; -; 1.
DR InterPro; IPR033482; EMSY.
DR InterPro; IPR005491; ENT_dom.
DR InterPro; IPR036142; ENT_dom-like_sf.
DR PANTHER; PTHR16500; PTHR16500; 1.
DR Pfam; PF03735; ENT; 1.
DR SMART; SM01191; ENT; 1.
DR SUPFAM; SSF158639; SSF158639; 1.
DR PROSITE; PS51138; ENT; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromatin regulator; DNA damage; DNA repair;
KW Glycoprotein; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..1264
FT /note="BRCA2-interacting transcriptional repressor EMSY"
FT /id="PRO_0000086969"
FT DOMAIN 16..114
FT /note="ENT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00476"
FT REGION 1..442
FT /note="Interaction with BRCA2"
FT /evidence="ECO:0000250"
FT REGION 118..122
FT /note="Interaction with ZMYND11"
FT /evidence="ECO:0000250"
FT REGION 145..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 660..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1232..1264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1249..1264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 171
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z589"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 177
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z589"
FT MOD_RES 782
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 785
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1085
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z589"
FT CARBOHYD 192
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000269|PubMed:16452088"
FT CARBOHYD 200
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 235
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 465
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 470
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 521
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 1069
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 82..96
FT /note="KMNLSLYLGERPSYS -> N (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_010432"
FT VAR_SEQ 802
FT /note="T -> TERTDEGTEVAFPLL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010433"
FT VAR_SEQ 1040..1199
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010434"
FT CONFLICT 975
FT /note="V -> A (in Ref. 1; BC039956)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1264 AA; 135291 MW; F4BA591D43912B2A CRC64;
MPVVWPTLLD LSRDECKRIL RKLELEAYAG VISALRAQGD LTKEKKDLLG ELSKVLSIST
ERHRAEVRRA VNDERLTTIA HKMNLSLYLG ERPSYSMSGP NSSSEWSIEG RRLVPLMPRL
VPQTAFTVTA NAVANAAVQH NASLPVPAET ASKDGVSCSD EDEKPRKRRR TNSSSSSPVV
LKEVPKAVVP VSKTITVPVS GSPKMSNIMQ SIANSLPPHM SPVKITFTKP STQTTNTTTQ
KVIIVTTSPS STFVPNILSK SHNYAAVTKL VPTSVIASTT QKPPVVITAS QASLVTSSSN
GNSSSTSSPI SSTVAVTTVV SSTPSVVMST VAQGVSTSAI KVASTRLPSP KSLVSGPTQI
LAQFPKQHQQ SPKQQLQQVQ QQTQQPVAQP SSVSQQQQPQ QSALPPGIKP TIQIKQESGV
KIITQQVQPS KILPKPVTAT LPTSSNSPIM VVSSNGAIMT TKLVTTPTGT QATYTRPTVS
PSLGRVATTP GAATYVKTTS GSIITVVPKS LATLGGKIIS SNIVSGTTTK ITTIPMTSKP
NVIVVQKTTG KGTTIQGLPG KNVVTTLLNA GGEKTLQTVP AGAKPAIITA TRPITKMIVT
QPKGIGSAVQ PAAKIIPTKI VYGQQGKTQV LIKPKPVTFQ ATVVSEQTRQ LVTETLQQAS
RVADASNSSA QEGKEEPQGY TDSSSSSTES SQSSQDSQPV VHVIASRRQD WSEHEIAMET
SPTIIYQDVS SESQSATSTI KALLELQQTT VKEKLESKPR QPTIDLSQMA VPIQMTQEKR
HSPESPSIAV VESELVAEYI TTVSHRSQPQ QPSQPQRTLL QHVAQSQTAT QTSVVVKSIP
ASSPGAITHI MQQALSSHTA FTKHSEELGT EEGEVEEMDT LDPQTGLFYR SALTQSQSTK
QQKLSQPQLE QTQLQVKTLQ CFQTKQKQTI HLQADQLQHK LTQMPQLSIR HQKLNPLQQE
QAQPKPDAQH TQHTVVAKDR QLPTLMAQPP QTVVQVLAVK TTQQLPKLQQ APNQPKIYVQ
PQTPQSQMAL PSSEKQPASQ VEQPIITQGS SVTKITFEGR QPPTVTKITG GSSVPKLTSP
VTSISPIQAS EKTAVSDILQ MSLMEAQIDT NVEHMVVDPP KKALATNVLT GEAGALPSTH
VVVAGMTKCR ESCSSPSAVG PPLTTRKIEA AGVPTTGQFM RIQNVGQKKA EESPTEIIIQ
AIPQYAIPCH SSSNVVVEPS GLLELNNFTS QQLDDDETAM EQDIDSSTED GTEPSPSQSA
VERS
