EMSY_HUMAN
ID EMSY_HUMAN Reviewed; 1322 AA.
AC Q7Z589; B7ZKT8; B7ZKU0; B7ZKU2; Q17RM7; Q4G109; Q8NBU6; Q8TE50; Q9H8I9;
AC Q9NRH0;
DT 24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=BRCA2-interacting transcriptional repressor EMSY {ECO:0000312|HGNC:HGNC:18071};
GN Name=EMSY {ECO:0000312|HGNC:HGNC:18071}; Synonyms=C11orf30; ORFNames=GL002;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP INVOLVEMENT IN CANCER, INTERACTION WITH BRCA2; CBX1 AND ZMYND11, AND
RP MUTAGENESIS OF 100-VAL--LEU-102 AND LEU-106.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 4; 5; 6 AND 7), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1082-1322 (ISOFORM 1).
RC TISSUE=Brain, Testis, and Urinary bladder;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 861-1322 (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 861-1322 (ISOFORM 2).
RC TISSUE=Brain;
RA Guo J.H., Zan Q., Yu L.;
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1115-1322 (ISOFORM 1).
RC TISSUE=Liver;
RA Li Y., Wu T., Xu S., Ren S., Chen Z., Han Z.;
RT "A novel gene expressed in human liver non-tumor tissues.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1136, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209 AND SER-1136, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP FUNCTION, IDENTIFICATION IN A NUCLEAR RECEPTOR HORMONE COMPLEX, AND
RP INTERACTION WITH ZNF335; CCAR2; ASH2L; RBBP5.
RX PubMed=19131338; DOI=10.1074/jbc.m805872200;
RA Garapaty S., Xu C.F., Trojer P., Mahajan M.A., Neubert T.A., Samuels H.H.;
RT "Identification and characterization of a novel nuclear protein complex
RT involved in nuclear hormone receptor-mediated gene regulation.";
RL J. Biol. Chem. 284:7542-7552(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-207, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP GLYCOSYLATION AT SER-228; SER-236; THR-271; THR-501; THR-506; SER-557 AND
RP THR-1120.
RX PubMed=20068230; DOI=10.1126/scisignal.2000526;
RA Wang Z., Udeshi N.D., Slawson C., Compton P.D., Sakabe K., Cheung W.D.,
RA Shabanowitz J., Hunt D.F., Hart G.W.;
RT "Extensive crosstalk between O-GlcNAcylation and phosphorylation regulates
RT cytokinesis.";
RL Sci. Signal. 3:RA2-RA2(2010).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209 AND SER-1136, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-207; SER-209; SER-238 AND
RP SER-1136, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-108, AND INTERACTION WITH
RP ZMYND11.
RX PubMed=15947784; DOI=10.1038/sj.embor.7400415;
RA Ekblad C.M.S., Chavali G.B., Basu B.P., Freund S.M.V., Veprintsev D.,
RA Hughes-Davies L., Kouzarides T., Doherty A.J., Itzhaki L.S.;
RT "Binding of EMSY to HP1beta: implications for recruitment of HP1beta and
RT BS69.";
RL EMBO Rep. 6:675-680(2005).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 1-100, AND SUBUNIT.
RX PubMed=15978617; DOI=10.1016/j.jmb.2005.05.047;
RA Chavali G.B., Ekblad C.M., Basu B.P., Brissett N.C., Veprintsev D.,
RA Hughes-Davies L., Kouzarides T., Itzhaki L.S., Doherty A.J.;
RT "Crystal structure of the ENT domain of human EMSY.";
RL J. Mol. Biol. 350:964-973(2005).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 9-139 IN COMPLEX WITH CBX1.
RX PubMed=16615912; DOI=10.1016/j.str.2006.01.007;
RA Huang Y., Myers M.P., Xu R.-M.;
RT "Crystal structure of the HP1-EMSY complex reveals an unusual mode of HP1
RT binding.";
RL Structure 14:703-712(2006).
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 (PubMed:14651845). Its interaction with
CC BRCA2 suggests that it may play a central role in the DNA repair
CC function of BRCA2 (PubMed:14651845). Mediates ligand-dependent
CC transcriptional activation by nuclear hormone receptors
CC (PubMed:19131338). {ECO:0000269|PubMed:14651845,
CC ECO:0000269|PubMed:19131338}.
CC -!- SUBUNIT: Homodimer (PubMed:15978617). Interacts with the
CC transactivation domain of BRCA2 (PubMed:14651845). Interacts with CBX1
CC (via chromoshadow domain) (PubMed:14651845, PubMed:16615912). Interacts
CC with ZMYND11 (PubMed:14651845, PubMed:15947784). Does not interact with
CC CBX3 or CBX5 (PubMed:14651845). Component of a nuclear receptor-
CC mediated transcription complex composed of at least ZNF335, CCAR2 and
CC EMSY; the complex stimulates the transcription of nuclear receptor
CC target genes such as SOX9 and HOXA1 (PubMed:19131338). Within the
CC complex interacts with CCAR2 and ZNF335 (PubMed:19131338). Components
CC of this complex may associate with components of a histone methylation
CC complex to form a complex at least composed of ZNF335, HCFC1, CCAR2,
CC EMSY, MKI67, RBBP5, ASH2L and WDR5 (PubMed:19131338). Within this
CC complex, interacts with ASH2L and RBBP5 (PubMed:19131338).
CC {ECO:0000269|PubMed:14651845, ECO:0000269|PubMed:15947784,
CC ECO:0000269|PubMed:15978617, ECO:0000269|PubMed:16615912,
CC ECO:0000269|PubMed:19131338}.
CC -!- INTERACTION:
CC Q7Z589; P83916: CBX1; NbExp=3; IntAct=EBI-6598631, EBI-78129;
CC Q7Z589; P35638-2: DDIT3; NbExp=3; IntAct=EBI-6598631, EBI-10173632;
CC Q7Z589; O15015: ZNF646; NbExp=3; IntAct=EBI-6598631, EBI-745608;
CC Q7Z589-5; Q96BJ3: AIDA; NbExp=3; IntAct=EBI-11989522, EBI-4401674;
CC Q7Z589-5; Q5SYC1: CLVS2; NbExp=3; IntAct=EBI-11989522, EBI-12357161;
CC Q7Z589-5; P35638: DDIT3; NbExp=3; IntAct=EBI-11989522, EBI-742651;
CC Q7Z589-5; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-11989522, EBI-11988027;
CC Q7Z589-5; O43681: GET3; NbExp=3; IntAct=EBI-11989522, EBI-2515857;
CC Q7Z589-5; Q8N485: LIX1; NbExp=3; IntAct=EBI-11989522, EBI-10694501;
CC Q7Z589-5; P25786: PSMA1; NbExp=3; IntAct=EBI-11989522, EBI-359352;
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=7;
CC Name=1;
CC IsoId=Q7Z589-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z589-2; Sequence=VSP_010431;
CC Name=3;
CC IsoId=Q7Z589-3; Sequence=VSP_020774, VSP_020775;
CC Name=4;
CC IsoId=Q7Z589-4; Sequence=VSP_054139, VSP_054140, VSP_054143;
CC Name=5;
CC IsoId=Q7Z589-5; Sequence=VSP_054140;
CC Name=6;
CC IsoId=Q7Z589-6; Sequence=VSP_054139, VSP_054141, VSP_054142;
CC Name=7;
CC IsoId=Q7Z589-7; Sequence=VSP_054139, VSP_054140;
CC -!- PTM: O-glycosylated during cytokinesis at sites identical or close to
CC phosphorylation sites, this interferes with the phosphorylation status.
CC {ECO:0000269|PubMed:20068230}.
CC -!- MISCELLANEOUS: Defects in EMSY may be a cause of sporadic breast cancer
CC and higher-grade ovarian cancers. Overexpressed through amplification
CC almost exclusively in sporadic breast cancer (13%) and higher-grade
CC ovarian cancer (17%). Amplification is associated with worse survival,
CC particularly in node-negative breast cancer, suggesting that it may be
CC of prognostic value.
CC -!- MISCELLANEOUS: Was named EMSY by PubMed:14651845 because the protein
CC sequence contains the word 'SISTER', after the first author's sister,
CC who is a breast cancer nurse.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF86947.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH29375.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAL65260.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB14627.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/C11ORF30ID173.html";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ430203; CAD22881.1; -; mRNA.
DR EMBL; AP002360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP003165; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471076; EAW74998.1; -; Genomic_DNA.
DR EMBL; BC029375; AAH29375.1; ALT_INIT; mRNA.
DR EMBL; BC033404; AAH33404.1; -; mRNA.
DR EMBL; BC117265; AAI17266.1; -; mRNA.
DR EMBL; BC143370; AAI43371.1; -; mRNA.
DR EMBL; BC143374; AAI43375.1; -; mRNA.
DR EMBL; BC143376; AAI43377.1; -; mRNA.
DR EMBL; AK023651; BAB14627.1; ALT_INIT; mRNA.
DR EMBL; AY070433; AAL65260.1; ALT_INIT; mRNA.
DR EMBL; AF226047; AAF86947.1; ALT_INIT; mRNA.
DR CCDS; CCDS73349.1; -. [Q7Z589-7]
DR CCDS; CCDS73350.1; -. [Q7Z589-4]
DR CCDS; CCDS73351.1; -. [Q7Z589-5]
DR CCDS; CCDS8244.1; -. [Q7Z589-1]
DR RefSeq; NP_001287871.1; NM_001300942.1. [Q7Z589-7]
DR RefSeq; NP_001287872.1; NM_001300943.1. [Q7Z589-5]
DR RefSeq; NP_001287873.1; NM_001300944.1. [Q7Z589-4]
DR RefSeq; NP_064578.2; NM_020193.4. [Q7Z589-1]
DR PDB; 1UTU; X-ray; 2.00 A; A/B=1-108.
DR PDB; 1UZ3; X-ray; 1.10 A; A/B=1-100.
DR PDB; 2FMM; X-ray; 1.80 A; E=9-139.
DR PDBsum; 1UTU; -.
DR PDBsum; 1UZ3; -.
DR PDBsum; 2FMM; -.
DR AlphaFoldDB; Q7Z589; -.
DR SMR; Q7Z589; -.
DR BioGRID; 121270; 118.
DR CORUM; Q7Z589; -.
DR DIP; DIP-29099N; -.
DR IntAct; Q7Z589; 66.
DR MINT; Q7Z589; -.
DR STRING; 9606.ENSP00000433205; -.
DR GlyConnect; 1657; 2 N-Linked glycans (1 site), 1 O-Linked glycan (9 sites).
DR GlyGen; Q7Z589; 55 sites, 2 N-linked glycans (1 site), 2 O-linked glycans (54 sites).
DR iPTMnet; Q7Z589; -.
DR PhosphoSitePlus; Q7Z589; -.
DR BioMuta; EMSY; -.
DR DMDM; 47605660; -.
DR EPD; Q7Z589; -.
DR jPOST; Q7Z589; -.
DR MassIVE; Q7Z589; -.
DR MaxQB; Q7Z589; -.
DR PaxDb; Q7Z589; -.
DR PeptideAtlas; Q7Z589; -.
DR PRIDE; Q7Z589; -.
DR ProteomicsDB; 61157; -.
DR ProteomicsDB; 7194; -.
DR ProteomicsDB; 7195; -.
DR ProteomicsDB; 7196; -.
DR Antibodypedia; 31192; 183 antibodies from 27 providers.
DR DNASU; 56946; -.
DR Ensembl; ENST00000334736.7; ENSP00000334130.3; ENSG00000158636.16. [Q7Z589-1]
DR Ensembl; ENST00000524767.5; ENSP00000433205.1; ENSG00000158636.16. [Q7Z589-7]
DR Ensembl; ENST00000525038.5; ENSP00000436968.1; ENSG00000158636.16. [Q7Z589-4]
DR Ensembl; ENST00000525919.5; ENSP00000432010.1; ENSG00000158636.16. [Q7Z589-5]
DR Ensembl; ENST00000529032.5; ENSP00000432327.1; ENSG00000158636.16. [Q7Z589-1]
DR Ensembl; ENST00000533248.5; ENSP00000433634.1; ENSG00000158636.16. [Q7Z589-6]
DR Ensembl; ENST00000533988.5; ENSP00000434665.1; ENSG00000158636.16. [Q7Z589-3]
DR GeneID; 56946; -.
DR KEGG; hsa:56946; -.
DR UCSC; uc001oxj.4; human. [Q7Z589-1]
DR CTD; 56946; -.
DR DisGeNET; 56946; -.
DR GeneCards; EMSY; -.
DR HGNC; HGNC:18071; EMSY.
DR HPA; ENSG00000158636; Low tissue specificity.
DR MIM; 608574; gene.
DR neXtProt; NX_Q7Z589; -.
DR OpenTargets; ENSG00000158636; -.
DR PharmGKB; PA134904392; -.
DR VEuPathDB; HostDB:ENSG00000158636; -.
DR eggNOG; KOG4675; Eukaryota.
DR GeneTree; ENSGT00390000009554; -.
DR HOGENOM; CLU_197021_0_0_1; -.
DR InParanoid; Q7Z589; -.
DR OMA; EYITTEC; -.
DR OrthoDB; 150416at2759; -.
DR PhylomeDB; Q7Z589; -.
DR TreeFam; TF332401; -.
DR PathwayCommons; Q7Z589; -.
DR SignaLink; Q7Z589; -.
DR SIGNOR; Q7Z589; -.
DR BioGRID-ORCS; 56946; 46 hits in 1051 CRISPR screens.
DR ChiTaRS; EMSY; human.
DR EvolutionaryTrace; Q7Z589; -.
DR GeneWiki; C11orf30; -.
DR GenomeRNAi; 56946; -.
DR Pharos; Q7Z589; Tbio.
DR PRO; PR:Q7Z589; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q7Z589; protein.
DR Bgee; ENSG00000158636; Expressed in ventricular zone and 174 other tissues.
DR ExpressionAtlas; Q7Z589; baseline and differential.
DR Genevisible; Q7Z589; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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 IDEAL; IID00281; -.
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 3D-structure; Alternative splicing; Chromatin regulator; DNA damage;
KW DNA repair; Glycoprotein; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..1322
FT /note="BRCA2-interacting transcriptional repressor EMSY"
FT /id="PRO_0000086968"
FT DOMAIN 16..100
FT /note="ENT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00476"
FT REGION 1..478
FT /note="Interaction with BRCA2"
FT /evidence="ECO:0000269|PubMed:14651845"
FT REGION 104..108
FT /note="Interaction with ZMYND11"
FT REGION 148..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 698..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1205..1231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1290..1322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1205..1223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1307..1322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 207
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BMB0"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 818
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BMB0"
FT MOD_RES 821
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BMB0"
FT MOD_RES 1136
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT CARBOHYD 228
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000269|PubMed:20068230"
FT CARBOHYD 236
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000269|PubMed:20068230"
FT CARBOHYD 271
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000269|PubMed:20068230"
FT CARBOHYD 501
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000269|PubMed:20068230"
FT CARBOHYD 506
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000269|PubMed:20068230"
FT CARBOHYD 557
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000269|PubMed:20068230"
FT CARBOHYD 1120
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000269|PubMed:20068230"
FT VAR_SEQ 82
FT /note="N -> K (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020774"
FT VAR_SEQ 82
FT /note="N -> KMNLSLYLGERPSYS (in isoform 4, isoform 6 and
FT isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054139"
FT VAR_SEQ 83..1322
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020775"
FT VAR_SEQ 140
FT /note="E -> EV (in isoform 4, isoform 5 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054140"
FT VAR_SEQ 733..747
FT /note="SQPVVHVIASRRQDW -> AVVISGEISSPPLFS (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054141"
FT VAR_SEQ 748..852
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054142"
FT VAR_SEQ 839..852
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_054143"
FT VAR_SEQ 1091..1257
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_010431"
FT MUTAGEN 100..102
FT /note="VPL->APA: Abolishes interaction with CBX1."
FT /evidence="ECO:0000269|PubMed:14651845"
FT MUTAGEN 106
FT /note="L->A: Abolishes interaction with ZMYND11."
FT /evidence="ECO:0000269|PubMed:14651845"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:1UZ3"
FT HELIX 13..38
FT /evidence="ECO:0007829|PDB:1UZ3"
FT HELIX 43..55
FT /evidence="ECO:0007829|PDB:1UZ3"
FT HELIX 60..71
FT /evidence="ECO:0007829|PDB:1UZ3"
FT HELIX 74..84
FT /evidence="ECO:0007829|PDB:1UZ3"
FT HELIX 90..97
FT /evidence="ECO:0007829|PDB:1UZ3"
FT STRAND 98..103
FT /evidence="ECO:0007829|PDB:2FMM"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:2FMM"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:2FMM"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:2FMM"
SQ SEQUENCE 1322 AA; 141468 MW; 7F8C95E8BA0FC9F0 CRC64;
MPVVWPTLLD LSRDECKRIL RKLELEAYAG VISALRAQGD LTKEKKDLLG ELSKVLSIST
ERHRAEVRRA VNDERLTTIA HNMSGPNSSS EWSIEGRRLV PLMPRLVPQT AFTVTANAVA
NAAIQHNASL PVPAETGSKE VVCYSYTSTT STPTSTPVPS GSIATVKSPR PASPASNVVV
LPSGSTVYVK SVSCSDEDEK PRKRRRTNSS SSSPVVLKEV PKAVVPVSKT ITVPVSGSPK
MSNIMQSIAN SLPPHMSPVK ITFTKPSTQT TNTTTQKVII VTTSPSSTFV PNILSKSHNY
AAVTKLVPTS VIASTTQKPP VVITASQSSL VSNSSSGSSS STPSPIPNTV AVTAVVSSTP
SVVMSTVAQG VSTSAIKMAS TRLPSPKSLV SAPTQILAQF PKQHQQSPKQ QLYQVQQQTQ
QQVAQPSPVS HQQQPQQSPL PPGIKPTIQI KQESGVKIIT QQVQPSKILP KPVTATLPTS
SNSPIMVVSS NGAIMTTKLV TTPTGTQATY TRPTVSPSIG RMAATPGAAT YVKTTSGSII
TVVPKSLATL GGKIISSNIV SGTTTKITTI PMTSKPNVIV VQKTTGKGTT IQGLPGKNVV
TTLLNAGGEK TIQTVPTGAK PAILTATRPI TKMIVTQPKG IGSTVQPAAK IIPTKIVYGQ
QGKTQVLIKP KPVTFQATVV SEQTRQLVTE TLQQASRVAE AGNSSIQEGK EEPQNYTDSS
SSSTESSQSS QDSQPVVHVI ASRRQDWSEH EIAMETSPTI IYQDVSSESQ SATSTIKALL
ELQQTTVKEK LESKPRQPTI DLSQMAVPIQ MTQEKRHSPE SPSIAVVESE LVAEYITTER
TDEGTEVAFP LLVSHRSQPQ QPSQPQRTLL QHVAQSQTAT QTSVVVKSIP ASSPGAITHI
MQQALSSHTA FTKHSEELGT EEGEVEEMDT LDPQTGLFYR SALTQSQSAK QQKLSQPPLE
QTQLQVKTLQ CFQTKQKQTI HLQADQLQHK LPQMPQLSIR HQKLTPLQQE QAQPKPDVQH
TQHPMVAKDR QLPTLMAQPP QTVVQVLAVK TTQQLPKLQQ APNQPKIYVQ PQTPQSQMSL
PASSEKQTAS QVEQPIITQG SSVTKITFEG RQPPTVTKIT GGSSVPKLTS PVTSISPIQA
SEKTAVSDIL KMSLMEAQID TNVEHMIVDP PKKALATSML TGEAGSLPST HMVVAGMANS
TPQQQKCRES CSSPSTVGSS LTTRKIDPPA VPATGQFMRI QNVGQKKAEE SPAEIIIQAI
PQYAIPCHSS SNVVVEPSGL LELNNFTSQQ LDDEETAMEQ DIDSSTEDGT EPSPSQSSAE
RS
