EID1_MOUSE
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 03-AUG-2022, entry version 126.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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 NR0B2,
RP 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}, 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., 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 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., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
CC -!- FUNCTION: Interacts with RB1 and EP300 and acts as a repressor of MYOD1
CC transactivation. Inhibits EP300 and CBP histone acetyltransferase
CC activity. May be involved in coupling cell cycle exit to the
CC transcriptional activation of genes required for cellular
CC differentiation. May act as a candidate coinhibitory factor for NR0B2
CC that can be directly linked to transcription inhibitory mechanisms.
CC {ECO:0000269|PubMed:11964378}.
CC -!- SUBUNIT: Interacts via its LXCXE motif with the entire pocket region of
CC RB1. Interacts with EP300, NR0B2 and TRIM27.
CC {ECO:0000250|UniProtKB:Q9Y6B2, ECO:0000269|PubMed:11964378}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11964378}. Cytoplasm
CC {ECO:0000269|PubMed:11964378}. Note=May shuttle between nucleus and
CC 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 Name=2 {ECO:0000269|PubMed:11964378};
CC IsoId=Q9DCR4-2; Sequence=VSP_052455;
CC -!- TISSUE SPECIFICITY: Expressed in all adult tissues examined and during
CC embryogenesis. {ECO:0000269|PubMed:11964378}.
CC -!- MISCELLANEOUS: Inhibition of MYOD1 may be partly due to the ability of
CC EID1 to bind and inhibit EP300 histone acetyltransferase activity.
CC {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; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS50696.1; -. [Q9DCR4-2]
DR RefSeq; NP_079889.2; NM_025613.3. [Q9DCR4-2]
DR PDB; 4NUF; X-ray; 2.80 A; P=91-106.
DR PDBsum; 4NUF; -.
DR AlphaFoldDB; Q9DCR4; -.
DR SMR; Q9DCR4; -.
DR BioGRID; 208425; 4.
DR IntAct; Q9DCR4; 1.
DR STRING; 10090.ENSMUSP00000129413; -.
DR iPTMnet; Q9DCR4; -.
DR PhosphoSitePlus; Q9DCR4; -.
DR PaxDb; Q9DCR4; -.
DR PRIDE; Q9DCR4; -.
DR ProteomicsDB; 277842; -. [Q9DCR4-1]
DR ProteomicsDB; 277843; -. [Q9DCR4-2]
DR Antibodypedia; 53733; 146 antibodies from 25 providers.
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 VEuPathDB; HostDB:ENSMUSG00000091337; -.
DR eggNOG; ENOG502RQIS; Eukaryota.
DR GeneTree; ENSGT00940000154796; -.
DR HOGENOM; CLU_1421050_0_0_1; -.
DR InParanoid; Q9DCR4; -.
DR OMA; WSGAMHR; -.
DR OrthoDB; 1497086at2759; -.
DR PhylomeDB; Q9DCR4; -.
DR TreeFam; TF337633; -.
DR BioGRID-ORCS; 58521; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Eid1; mouse.
DR PRO; PR:Q9DCR4; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9DCR4; protein.
DR Bgee; ENSMUSG00000091337; Expressed in barrel cortex and 252 other tissues.
DR Genevisible; Q9DCR4; MM.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
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 by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0045595; P:regulation of cell differentiation; IEA:InterPro.
DR IDEAL; IID50234; -.
DR InterPro; IPR033258; EID.
DR InterPro; IPR033255; EID-1.
DR PANTHER; PTHR15556; PTHR15556; 1.
DR PANTHER; PTHR15556:SF5; PTHR15556:SF5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cytoplasm; Differentiation;
KW Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..169
FT /note="EP300-interacting inhibitor of differentiation 1"
FT /id="PRO_0000289157"
FT REGION 31..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..120
FT /note="Interaction with NR0B2"
FT /evidence="ECO:0000269|PubMed:11964378"
FT MOTIF 150..154
FT /note="LXCXE motif"
FT VAR_SEQ 160..169
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11964378,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_052455"
FT CONFLICT 13
FT /note="E -> K (in Ref. 2; BAB30797)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="G -> W (in Ref. 2; BAB22187)"
FT /evidence="ECO:0000305"
FT CONFLICT 37
FT /note="P -> Q (in Ref. 2; BAC37261)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="L -> S (in Ref. 2; BAB30797)"
FT /evidence="ECO:0000305"
FT HELIX 94..101
FT /evidence="ECO:0007829|PDB:4NUF"
FT HELIX 102..105
FT /evidence="ECO:0007829|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
