EID2_MOUSE
ID EID2_MOUSE Reviewed; 236 AA.
AC Q6X7S9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=EP300-interacting inhibitor of differentiation 2;
DE Short=EID-2;
DE AltName: Full=CREBBP/EP300 inhibitor 2;
DE AltName: Full=EID-1-like inhibitor of differentiation 2;
GN Name=Eid2 {ECO:0000312|EMBL:AAH94513.1, ECO:0000312|MGI:MGI:2681174};
GN Synonyms=Cri2 {ECO:0000312|MGI:MGI:2681174};
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:AAP12560.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=14585496; DOI=10.1016/j.gene.2003.06.001;
RA Ji A., Dao D., Chen J., MacLellan W.R.;
RT "EID-2, a novel member of the EID family of p300-binding proteins inhibits
RT transactivation by MyoD.";
RL Gene 318:35-43(2003).
RN [2] {ECO:0000312|EMBL:AAH94513.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH94513.1};
RC TISSUE=Mammary tumor {ECO:0000312|EMBL:AAH94513.1};
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 [3]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-63, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Interacts with EP300 and acts as a repressor of MYOD-
CC dependent transcription and muscle differentiation. Inhibits EP300
CC histone acetyltransferase activity. Acts as a repressor of TGFB/SMAD
CC transcriptional responses. May act as a repressor of the TGFB/SMAD3-
CC dependent signaling by selectively blocking formation of TGFB-induced
CC SMAD3-SMAD4 complex (By similarity). {ECO:0000250|UniProtKB:Q8N6I1}.
CC -!- SUBUNIT: Heterodimer with EID2B. Interacts with the C-terminus of
CC EP300. Interacts with HDAC1 and HDAC2. Interacts with SMAD2, SMAD4 and
CC with the MH2 domain of SMAD3 (By similarity).
CC {ECO:0000250|UniProtKB:Q8N6I1}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8N6I1}.
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, kidney and pancreas. Not
CC detected in placenta. {ECO:0000269|PubMed:14585496}.
CC -!- DEVELOPMENTAL STAGE: First detected at 10.5 dpc with highest expression
CC at 11.5 dpc. Expression decreases during later stages of development at
CC 12.5 dpc and 14.5 dpc (at protein level).
CC {ECO:0000269|PubMed:14585496}.
CC -!- DOMAIN: The N-terminal portion of EID2 is required for nuclear
CC localization. {ECO:0000250|UniProtKB:Q8N6I1}.
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DR EMBL; AY251273; AAP12560.1; -; mRNA.
DR EMBL; BC094513; AAH94513.1; -; mRNA.
DR CCDS; CCDS21038.1; -.
DR RefSeq; NP_940817.1; NM_198425.2.
DR AlphaFoldDB; Q6X7S9; -.
DR BioGRID; 239752; 2.
DR STRING; 10090.ENSMUSP00000062345; -.
DR iPTMnet; Q6X7S9; -.
DR PhosphoSitePlus; Q6X7S9; -.
DR jPOST; Q6X7S9; -.
DR MaxQB; Q6X7S9; -.
DR PaxDb; Q6X7S9; -.
DR PRIDE; Q6X7S9; -.
DR ProteomicsDB; 277815; -.
DR Antibodypedia; 48019; 78 antibodies from 17 providers.
DR DNASU; 386655; -.
DR Ensembl; ENSMUST00000059596; ENSMUSP00000062345; ENSMUSG00000046058.
DR GeneID; 386655; -.
DR KEGG; mmu:386655; -.
DR UCSC; uc009fyc.1; mouse.
DR CTD; 163126; -.
DR MGI; MGI:2681174; Eid2.
DR VEuPathDB; HostDB:ENSMUSG00000046058; -.
DR eggNOG; ENOG502RU2W; Eukaryota.
DR GeneTree; ENSGT00940000154796; -.
DR HOGENOM; CLU_102589_0_0_1; -.
DR InParanoid; Q6X7S9; -.
DR OMA; FDAEYMR; -.
DR OrthoDB; 1475530at2759; -.
DR PhylomeDB; Q6X7S9; -.
DR TreeFam; TF337633; -.
DR BioGRID-ORCS; 386655; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q6X7S9; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q6X7S9; protein.
DR Bgee; ENSMUSG00000046058; Expressed in superior cervical ganglion and 218 other tissues.
DR Genevisible; Q6X7S9; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0046332; F:SMAD binding; ISS:HGNC-UCL.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
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:HGNC-UCL.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISS:HGNC-UCL.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISS:HGNC-UCL.
DR GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; ISS:HGNC-UCL.
DR GO; GO:0007183; P:SMAD protein complex assembly; ISS:HGNC-UCL.
DR GO; GO:0007181; P:transforming growth factor beta receptor complex assembly; ISS:HGNC-UCL.
DR InterPro; IPR033258; EID.
DR InterPro; IPR033256; EID-2.
DR PANTHER; PTHR15556; PTHR15556; 1.
DR PANTHER; PTHR15556:SF3; PTHR15556:SF3; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Developmental protein; Differentiation; Methylation;
KW Myogenesis; Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..236
FT /note="EP300-interacting inhibitor of differentiation 2"
FT /id="PRO_0000315902"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 170..190
FT /evidence="ECO:0000255"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 63
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 79
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q8N6I1"
SQ SEQUENCE 236 AA; 25304 MW; DF943D14D37451DF CRC64;
MSQLPAVSSA PQTGAASRDR RLPQAEVGGG RRALPGPARP GETRGRPMAA AREGPAAPAA
AARGGRVAAA REGRAAAARG GPGAAPRGGA AAREGPAAAA ASREARMAEV ARLLGDPLEE
EAPEGRPRSR AGGLAAMPYM RFRHPLSVLG INYQQFLRHY LENYPIAPGR IQELEERRRR
FVEACRAREA AFDIEYLRNP QRVDFDILTF TIALTASEVI NPLIEELGCD KFIHRE
