LOCUS       NP_758484               1264 aa            linear   ROD 30-APR-2024
DEFINITION  BRCA2-interacting transcriptional repressor EMSY isoform 4 [Mus
            musculus].
ACCESSION   NP_758484 XP_902428 XP_902460 XP_902497 XP_902505 XP_902516
            XP_902525 XP_902547 XP_902556 XP_902568 XP_924282 XP_924333
            XP_924348 XP_924369 XP_924388 XP_924400 XP_979562 XP_979717
            XP_993619
VERSION     NP_758484.2
DBSOURCE    REFSEQ: accession NM_172280.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1264)
  AUTHORS   Adams,D.J., Barlas,B., McIntyre,R.E., Salguero,I., van der
            Weyden,L., Barros,A., Vicente,J.R., Karimpour,N., Haider,A.,
            Ranzani,M., Turner,G., Thompson,N.A., Harle,V., Olvera-Leon,R.,
            Robles-Espinoza,C.D., Speak,A.O., Geisler,N., Weninger,W.J.,
            Geyer,S.H., Hewinson,J., Karp,N.A., Fu,B., Yang,F., Kozik,Z.,
            Choudhary,J., Yu,L., van Ruiten,M.S., Rowland,B.D., Lelliott,C.J.,
            Del Castillo Velasco-Herrera,M., Verstraten,R., Bruckner,L.,
            Henssen,A.G., Rooimans,M.A., de Lange,J., Mohun,T.J., Arends,M.J.,
            Kentistou,K.A., Coelho,P.A., Zhao,Y., Zecchini,H., Perry,J.R.B.,
            Jackson,S.P. and Balmus,G.
  CONSRTM   Sanger Mouse Genetics Project
  TITLE     Genetic determinants of micronucleus formation in vivo
  JOURNAL   Nature 627 (8002), 130-136 (2024)
   PUBMED   38355793
REFERENCE   2  (residues 1 to 1264)
  AUTHORS   Marzio,A., Kurz,E., Sahni,J.M., Di Feo,G., Puccini,J., Jiang,S.,
            Hirsch,C.A., Arbini,A.A., Wu,W.L., Pass,H.I., Bar-Sagi,D.,
            Papagiannakopoulos,T. and Pagano,M.
  TITLE     EMSY inhibits homologous recombination repair and the interferon
            response, promoting lung cancer immune evasion
  JOURNAL   Cell 185 (1), 169-183 (2022)
   PUBMED   34963055
  REMARK    GeneRIF: EMSY inhibits homologous recombination repair and the
            interferon response, promoting lung cancer immune evasion.
REFERENCE   3  (residues 1 to 1264)
  AUTHORS   Ezell,S.A., Polytarchou,C., Hatziapostolou,M., Guo,A., Sanidas,I.,
            Bihani,T., Comb,M.J., Sourvinos,G. and Tsichlis,P.N.
  TITLE     The protein kinase Akt1 regulates the interferon response through
            phosphorylation of the transcriptional repressor EMSY
  JOURNAL   Proc Natl Acad Sci U S A 109 (10), E613-E621 (2012)
   PUBMED   22315412
  REMARK    GeneRIF: Akt1 regulates the interferon response through
            phosphorylation of the transcriptional repressor EMSY
REFERENCE   4  (residues 1 to 1264)
  AUTHORS   Vosseller,K., Trinidad,J.C., Chalkley,R.J., Specht,C.G.,
            Thalhammer,A., Lynn,A.J., Snedecor,J.O., Guan,S.,
            Medzihradszky,K.F., Maltby,D.A., Schoepfer,R. and Burlingame,A.L.
  TITLE     O-linked N-acetylglucosamine proteomics of postsynaptic density
            preparations using lectin weak affinity chromatography and mass
            spectrometry
  JOURNAL   Mol Cell Proteomics 5 (5), 923-934 (2006)
   PUBMED   16452088
REFERENCE   5  (residues 1 to 1264)
  AUTHORS   Ekblad,C.M., Chavali,G.B., Basu,B.P., Freund,S.M., Veprintsev,D.,
            Hughes-Davies,L., Kouzarides,T., Doherty,A.J. and Itzhaki,L.S.
  TITLE     Binding of EMSY to HP1beta: implications for recruitment of HP1beta
            and BS69
  JOURNAL   EMBO Rep 6 (7), 675-680 (2005)
   PUBMED   15947784
REFERENCE   6  (residues 1 to 1264)
  AUTHORS   Hughes-Davies,L., Huntsman,D., Ruas,M., Fuks,F., Bye,J., Chin,S.F.,
            Milner,J., Brown,L.A., Hsu,F., Gilks,B., Nielsen,T., Schulzer,M.,
            Chia,S., Ragaz,J., Cahn,A., Linger,L., Ozdag,H., Cattaneo,E.,
            Jordanova,E.S., Schuuring,E., Yu,D.S., Venkitaraman,A., Ponder,B.,
            Doherty,A., Aparicio,S., Bentley,D., Theillet,C., Ponting,C.P.,
            Caldas,C. and Kouzarides,T.
  TITLE     EMSY links the BRCA2 pathway to sporadic breast and ovarian cancer
  JOURNAL   Cell 115 (5), 523-535 (2003)
   PUBMED   14651845
REFERENCE   7  (residues 1 to 1264)
  AUTHORS   Stryke,D., Kawamoto,M., Huang,C.C., Johns,S.J., King,L.A.,
            Harper,C.A., Meng,E.C., Lee,R.E., Yee,A., L'Italien,L.,
            Chuang,P.T., Young,S.G., Skarnes,W.C., Babbitt,P.C. and Ferrin,T.E.
  TITLE     BayGenomics: a resource of insertional mutations in mouse embryonic
            stem cells
  JOURNAL   Nucleic Acids Res 31 (1), 278-281 (2003)
   PUBMED   12520002
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BC089304.1.
            
            On or before Jan 29, 2007 this sequence version replaced
            XP_902556.1, XP_902525.1, XP_902568.2, XP_902547.1, XP_902497.1,
            XP_902460.1, XP_902516.1, XP_902505.1, XP_902428.1, XP_924388.1,
            XP_924333.1, XP_924400.2, XP_924369.1, XP_979717.1, XP_924348.1,
            XP_979562.1, XP_924282.1, XP_993619.1, NP_758484.1.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC089304.1, SRR9219380.7494.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN01164138 [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1264
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="7"
                     /map="7 53.86 cM"
     Protein         1..1264
                     /product="BRCA2-interacting transcriptional repressor EMSY
                     isoform 4"
                     /note="protein EMSY; BRCA2-interacting transcriptional
                     repressor EMSY"
                     /calculated_mol_wt=135160
     Region          1..442
                     /region_name="Interaction with BRCA2.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BMB0.2)"
     Region          17..81
                     /region_name="ENT"
                     /note="ENT domain; pfam03735"
                     /db_xref="CDD:461032"
     Region          118..122
                     /region_name="Interaction with ZMYND11.
                     /evidence=ECO:0000250"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BMB0.2)"
     Region          145..179
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BMB0.2)"
     Site            171
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z589; propagated from
                     UniProtKB/Swiss-Prot (Q8BMB0.2)"
     Site            173
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8BMB0.2)"
     Site            177
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8BMB0.2)"
     Site            192
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine.
                     /evidence=ECO:0000269|PubMed:16452088; propagated from
                     UniProtKB/Swiss-Prot (Q8BMB0.2)"
     Site            200
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q8BMB0.2)"
     Site            202
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z589; propagated from
                     UniProtKB/Swiss-Prot (Q8BMB0.2)"
     Site            235
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q8BMB0.2)"
     Region          364..407
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BMB0.2)"
     Region          <433..534
                     /region_name="COG3889"
                     /note="Extracellular solute-binding protein, contains
                     Ig-fold domain [General function prediction only]"
                     /db_xref="CDD:443097"
     Site            465
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q8BMB0.2)"
     Site            470
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q8BMB0.2)"
     Site            521
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) serine. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q8BMB0.2)"
     Region          660..700
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BMB0.2)"
     Site            782
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8BMB0.2)"
     Site            785
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:21183079; propagated from
                     UniProtKB/Swiss-Prot (Q8BMB0.2)"
     Region          <900..1043
                     /region_name="PABP-1234"
                     /note="polyadenylate binding protein, human types 1, 2, 3,
                     4 family; TIGR01628"
                     /db_xref="CDD:130689"
     Site            1069
                     /site_type="glycosylation"
                     /note="O-linked (GlcNAc) threonine. /evidence=ECO:0000250;
                     propagated from UniProtKB/Swiss-Prot (Q8BMB0.2)"
     Site            1085
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q7Z589; propagated from
                     UniProtKB/Swiss-Prot (Q8BMB0.2)"
     Region          1232..1264
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q8BMB0.2)"
     CDS             1..1264
                     /gene="Emsy"
                     /gene_synonym="2210018M11Rik; 2310016L09Rik"
                     /coded_by="NM_172280.2:136..3930"
                     /note="isoform 4 is encoded by transcript variant 4"
                     /db_xref="CCDS:CCDS40028.1"
                     /db_xref="GeneID:233545"
                     /db_xref="MGI:MGI:1924203"
ORIGIN      
        1 mpvvwptlld lsrdeckril rkleleayag visalraqgd ltkekkdllg elskvlsist
       61 erhraevrra vnderlttia hkmnlslylg erpsysmsgp nsssewsieg rrlvplmprl
      121 vpqtaftvta navanaavqh naslpvpaet askdgvscsd edekprkrrr tnssssspvv
      181 lkevpkavvp vsktitvpvs gspkmsnimq sianslpphm spvkitftkp stqttntttq
      241 kviivttsps stfvpnilsk shnyaavtkl vptsviastt qkppvvitas qaslvtsssn
      301 gnssstsspi sstvavttvv sstpsvvmst vaqgvstsai kvastrlpsp kslvsgptqi
      361 laqfpkqhqq spkqqlqqvq qqtqqpvaqp ssvsqqqqpq qsalppgikp tiqikqesgv
      421 kiitqqvqps kilpkpvtat lptssnspim vvssngaimt tklvttptgt qatytrptvs
      481 pslgrvattp gaatyvktts gsiitvvpks latlggkiis snivsgtttk ittipmtskp
      541 nvivvqkttg kgttiqglpg knvvttllna ggektlqtvp agakpaiita trpitkmivt
      601 qpkgigsavq paakiiptki vygqqgktqv likpkpvtfq atvvseqtrq lvtetlqqas
      661 rvadasnssa qegkeepqgy tdssssstes sqssqdsqpv vhviasrrqd wseheiamet
      721 sptiiyqdvs sesqsatsti kallelqqtt vkekleskpr qptidlsqma vpiqmtqekr
      781 hspespsiav veselvaeyi ttvshrsqpq qpsqpqrtll qhvaqsqtat qtsvvvksip
      841 asspgaithi mqqalsshta ftkhseelgt eegeveemdt ldpqtglfyr saltqsqstk
      901 qqklsqpqle qtqlqvktlq cfqtkqkqti hlqadqlqhk ltqmpqlsir hqklnplqqe
      961 qaqpkpdaqh tqhtvvakdr qlptlmaqpp qtvvqvlavk ttqqlpklqq apnqpkiyvq
     1021 pqtpqsqmal pssekqpasq veqpiitqgs svtkitfegr qpptvtkitg gssvpkltsp
     1081 vtsispiqas ektavsdilq mslmeaqidt nvehmvvdpp kkalatnvlt geagalpsth
     1141 vvvagmtkcr escsspsavg pplttrkiea agvpttgqfm riqnvgqkka eespteiiiq
     1201 aipqyaipch sssnvvveps gllelnnfts qqldddetam eqdidssted gtepspsqsa
     1261 vers
//
