ID   EID1_MOUSE              Reviewed;         169 AA.
AC   Q9DCR4; Q3T9D1; Q8BP25; Q9CQ17; Q9CYM0;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 2.
DT   22-JUL-2015, entry version 89.
DE   RecName: Full=EP300-interacting inhibitor of differentiation 1;
DE   AltName: Full=CREBBP/EP300 inhibitory protein 1;
DE   AltName: Full=E1A-like inhibitor of differentiation 1;
DE            Short=EID-1;
GN   Name=Eid1 {ECO:0000312|MGI:MGI:1889651};
GN   Synonyms=Cri1 {ECO:0000312|MGI:MGI:1889651};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAM34760.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH
RP   NR0B2, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   STRAIN=Swiss Webster / NIH {ECO:0000312|EMBL:AAM34760.1};
RC   TISSUE=Embryo {ECO:0000312|EMBL:AAM34760.1};
RX   PubMed=11964378; DOI=10.1093/embo-reports/kvf087;
RA   Bavner A., Johansson L., Toresson G., Gustafsson J.-A., Treuter E.;
RT   "A transcriptional inhibitor targeted by the atypical orphan nuclear
RT   receptor SHP.";
RL   EMBO Rep. 3:478-484(2002).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:BAB22187.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB22187.1}, and
RC   NOD {ECO:0000312|EMBL:BAE41254.1};
RC   TISSUE=Cerebellum {ECO:0000312|EMBL:BAB23911.1},
RC   Embryo {ECO:0000312|EMBL:BAB30797.1},
RC   Embryonic lung {ECO:0000312|EMBL:BAC37412.1},
RC   Kidney {ECO:0000312|EMBL:BAB22187.1},
RC   Spleen {ECO:0000312|EMBL:BAE43093.1},
RC   Sympathetic ganglion {ECO:0000312|EMBL:BAE28618.1},
RC   Thymus {ECO:0000312|EMBL:BAC37007.1}, and
RC   Wolffian duct {ECO:0000312|EMBL:BAC37257.1};
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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- FUNCTION: Interacts with RB1 and EP300 and acts as a repressor of
CC       MYOD1 transactivation. Inhibits EP300 and CBP histone
CC       acetyltransferase activity. May be involved in coupling cell cycle
CC       exit to the transcriptional activation of genes required for
CC       cellular differentiation. May act as a candidate coinhibitory
CC       factor for NR0B2 that can be directly linked to transcription
CC       inhibitory mechanisms. {ECO:0000269|PubMed:11964378}.
CC   -!- SUBUNIT: Interacts via its LXCXE motif with the entire pocket
CC       region of RB1. Interacts with EP300, NR0B2 and TRIM27.
CC       {ECO:0000250|UniProtKB:Q9Y6B2, ECO:0000269|PubMed:11964378}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11964378}.
CC       Cytoplasm {ECO:0000269|PubMed:11964378}. Note=May shuttle between
CC       nucleus and cytoplasm. {ECO:0000269|PubMed:11964378}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1 {ECO:0000269|PubMed:16141072};
CC         IsoId=Q9DCR4-1; Sequence=Displayed;
CC         Note=No experimental confirmation available. {ECO:0000305};
CC       Name=2 {ECO:0000269|PubMed:11964378};
CC         IsoId=Q9DCR4-2; Sequence=VSP_052455;
CC   -!- TISSUE SPECIFICITY: Expressed in all adult tissues examined and
CC       during embryogenesis. {ECO:0000269|PubMed:11964378}.
CC   -!- MISCELLANEOUS: Inhibition of MYOD1 may be partly due to the
CC       ability of EID1 to bind and inhibit EP300 histone
CC       acetyltransferase activity. {ECO:0000250|UniProtKB:Q9Y6B2}.
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DR   EMBL; AF509968; AAM34760.1; -; mRNA.
DR   EMBL; AK002559; BAB22187.1; -; mRNA.
DR   EMBL; AK005258; BAB23911.1; -; mRNA.
DR   EMBL; AK011293; BAB27521.1; -; mRNA.
DR   EMBL; AK014440; BAB29352.1; -; mRNA.
DR   EMBL; AK017543; BAB30797.1; -; mRNA.
DR   EMBL; AK077783; BAC37007.1; -; mRNA.
DR   EMBL; AK078402; BAC37257.1; -; mRNA.
DR   EMBL; AK078409; BAC37261.1; -; mRNA.
DR   EMBL; AK078826; BAC37412.1; -; mRNA.
DR   EMBL; AK148555; BAE28618.1; -; mRNA.
DR   EMBL; AK169604; BAE41254.1; -; mRNA.
DR   EMBL; AK172612; BAE43093.1; -; mRNA.
DR   EMBL; AL929166; CAM20858.1; -; Genomic_DNA.
DR   CCDS; CCDS50696.1; -. [Q9DCR4-2]
DR   RefSeq; NP_079889.2; NM_025613.3. [Q9DCR4-2]
DR   UniGene; Mm.425101; -.
DR   UniGene; Mm.490315; -.
DR   PDB; 4NUF; X-ray; 2.80 A; P=91-106.
DR   PDBsum; 4NUF; -.
DR   BioGrid; 208425; 3.
DR   STRING; 10090.ENSMUSP00000129413; -.
DR   PhosphoSite; Q9DCR4; -.
DR   PRIDE; Q9DCR4; -.
DR   DNASU; 58521; -.
DR   Ensembl; ENSMUST00000164756; ENSMUSP00000129413; ENSMUSG00000091337. [Q9DCR4-2]
DR   GeneID; 58521; -.
DR   KEGG; mmu:58521; -.
DR   UCSC; uc008mcx.1; mouse. [Q9DCR4-1]
DR   CTD; 23741; -.
DR   MGI; MGI:1889651; Eid1.
DR   eggNOG; NOG320805; -.
DR   GeneTree; ENSGT00500000045230; -.
DR   HOGENOM; HOG000054219; -.
DR   HOVERGEN; HBG107840; -.
DR   InParanoid; Q9DCR4; -.
DR   OMA; MAEPQGE; -.
DR   OrthoDB; EOG7SXW53; -.
DR   PhylomeDB; Q9DCR4; -.
DR   TreeFam; TF337633; -.
DR   NextBio; 314334; -.
DR   PRO; PR:Q9DCR4; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   Bgee; Q9DCR4; -.
DR   CleanEx; MM_EID1; -.
DR   Genevisible; Q9DCR4; MM.
DR   GO; GO:0016235; C:aggresome; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0035035; F:histone acetyltransferase binding; ISS:UniProtKB.
DR   GO; GO:0035034; F:histone acetyltransferase regulator activity; ISS:UniProtKB.
DR   GO; GO:0003714; F:transcription corepressor activity; IMP:UniProtKB.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; ISS:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISO:MGI.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0035065; P:regulation of histone acetylation; ISO:MGI.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell cycle; Complete proteome;
KW   Cytoplasm; Differentiation; Nucleus; Reference proteome; Repressor;
KW   Transcription; Transcription regulation.
FT   CHAIN         1    169       EP300-interacting inhibitor of
FT                                differentiation 1.
FT                                /FTId=PRO_0000289157.
FT   REGION       54    120       Interaction with NR0B2.
FT                                {ECO:0000269|PubMed:11964378}.
FT   MOTIF       150    154       LXCXE motif.
FT   VAR_SEQ     160    169       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:11964378,
FT                                ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_052455.
FT   CONFLICT     13     13       E -> K (in Ref. 2; BAB30797).
FT                                {ECO:0000305}.
FT   CONFLICT     36     36       G -> W (in Ref. 2; BAB22187).
FT                                {ECO:0000305}.
FT   CONFLICT     37     37       P -> Q (in Ref. 2; BAC37261).
FT                                {ECO:0000305}.
FT   CONFLICT    160    160       L -> S (in Ref. 2; BAB30797).
FT                                {ECO:0000305}.
FT   HELIX        94    101       {ECO:0000244|PDB:4NUF}.
FT   HELIX       102    105       {ECO:0000244|PDB:4NUF}.
SQ   SEQUENCE   169 AA;  18921 MW;  DA9C99F5509073E8 CRC64;
     MAEMAELCEL YEESNELQMD VLPGEGYMEV GRGARGPAPE EGPMEEEAGP AAARAQRGLF
     PEAGADLEGD EFDDWEDDYE FPEEERWSGA MHRVSAALEE ANKVFLRTAR AGDALDGGFQ
     ARCEKSPFDQ LAFIEELFSL MVVNRLTEEL GCDEIIDREL MLTREEETT
//