ID EID2_HUMAN Reviewed; 236 AA. AC Q8N6I1; A7YQ71; Q6X7T0; Q6ZR61; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2005, sequence version 3. DT 24-JAN-2024, entry version 140. 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:AAH30137.3}; GN Synonyms=CRI2 {ECO:0000312|EMBL:EAW56909.1, GN ECO:0000312|HGNC:HGNC:28292}; 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] {ECO:0000305, ECO:0000312|EMBL:AAP12559.1} RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH EP300, RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DOMAIN. 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:0000305, ECO:0000312|EMBL:BAC87454.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT THR-6. RC TISSUE=Kidney {ECO:0000312|EMBL:BAC87454.1}; 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 [3] {ECO:0000312|EMBL:EAW56909.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.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] {ECO:0000305, ECO:0000312|EMBL:AAH30137.3} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung {ECO:0000312|EMBL:AAH30137.3}, and Skin RC {ECO:0000312|EMBL:AAH99899.1}; 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 [5] {ECO:0000305} RP FUNCTION, AND INTERACTION WITH HDAC1 AND HDAC2. RX PubMed=12586827; DOI=10.1074/jbc.m212212200; RA Miyake S., Yanagisawa Y., Yuasa Y.; RT "A novel EID-1 family member, EID-2, associates with histone deacetylases RT and inhibits muscle differentiation."; RL J. Biol. Chem. 278:17060-17065(2003). RN [6] {ECO:0000305} RP FUNCTION, AND INTERACTION WITH SMAD2; SMAD3 AND SMAD4. RX PubMed=14612439; DOI=10.1074/jbc.m310591200; RA Lee H.-J., Lee J.K., Miyake S., Kim S.-J.; RT "A novel E1A-like inhibitor of differentiation (EID) family member, EID-2, RT suppresses transforming growth factor (TGF)-beta signaling by blocking TGF- RT beta-induced formation of Smad3-Smad4 complexes."; RL J. Biol. Chem. 279:2666-2672(2004). RN [7] {ECO:0000305} RP SUBUNIT. RX PubMed=15970276; DOI=10.1016/j.bbrc.2005.06.013; RA Sasajima Y., Tanaka H., Miyake S., Yuasa Y.; RT "A novel EID family member, EID-3, inhibits differentiation and forms a RT homodimer or heterodimer with EID-2."; RL Biochem. Biophys. Res. Commun. 333:969-975(2005). RN [8] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-75, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; 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. {ECO:0000269|PubMed:12586827, CC ECO:0000269|PubMed:14585496, ECO:0000269|PubMed:14612439}. 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. {ECO:0000269|PubMed:12586827, CC ECO:0000269|PubMed:14585496, ECO:0000269|PubMed:14612439, CC ECO:0000269|PubMed:15970276}. CC -!- INTERACTION: CC Q8N6I1; Q96D98: EID2B; NbExp=2; IntAct=EBI-5525894, EBI-724968; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14585496}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1 {ECO:0000269|PubMed:14585496, ECO:0000269|PubMed:15489334}; CC IsoId=Q8N6I1-1; Sequence=Displayed; CC Name=2 {ECO:0000269|PubMed:14702039}; CC IsoId=Q8N6I1-2; Sequence=VSP_052648; CC -!- TISSUE SPECIFICITY: Most abundantly expressed in placenta. Highly CC expressed in liver, brain, heart, skeletal muscle, and kidney. CC {ECO:0000269|PubMed:14585496}. CC -!- DOMAIN: The N-terminal portion of EID2 is required for nuclear CC localization. {ECO:0000269|PubMed:14585496}. 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; AY251272; AAP12559.1; -; mRNA. DR EMBL; AK128468; BAC87454.1; -; mRNA. DR EMBL; CH471126; EAW56909.1; -; Genomic_DNA. DR EMBL; BC030137; AAH30137.3; -; mRNA. DR EMBL; BC099899; AAH99899.1; -; mRNA. DR CCDS; CCDS12540.2; -. [Q8N6I1-1] DR RefSeq; NP_694964.3; NM_153232.3. [Q8N6I1-1] DR AlphaFoldDB; Q8N6I1; -. DR BioGRID; 127852; 20. DR IntAct; Q8N6I1; 9. DR STRING; 9606.ENSP00000375073; -. DR iPTMnet; Q8N6I1; -. DR MetOSite; Q8N6I1; -. DR PhosphoSitePlus; Q8N6I1; -. DR BioMuta; EID2; -. DR DMDM; 74762532; -. DR EPD; Q8N6I1; -. DR MassIVE; Q8N6I1; -. DR MaxQB; Q8N6I1; -. DR PaxDb; 9606-ENSP00000375073; -. DR PeptideAtlas; Q8N6I1; -. DR ProteomicsDB; 72178; -. [Q8N6I1-1] DR ProteomicsDB; 72179; -. [Q8N6I1-2] DR Pumba; Q8N6I1; -. DR Antibodypedia; 48019; 91 antibodies from 17 providers. DR DNASU; 163126; -. DR Ensembl; ENST00000390658.4; ENSP00000375073.2; ENSG00000176396.11. [Q8N6I1-1] DR GeneID; 163126; -. DR KEGG; hsa:163126; -. DR MANE-Select; ENST00000390658.4; ENSP00000375073.2; NM_153232.4; NP_694964.3. DR UCSC; uc002oma.5; human. [Q8N6I1-1] DR AGR; HGNC:28292; -. DR CTD; 163126; -. DR GeneCards; EID2; -. DR HGNC; HGNC:28292; EID2. DR HPA; ENSG00000176396; Low tissue specificity. DR MIM; 609773; gene. DR neXtProt; NX_Q8N6I1; -. DR OpenTargets; ENSG00000176396; -. DR PharmGKB; PA162384544; -. DR VEuPathDB; HostDB:ENSG00000176396; -. DR eggNOG; ENOG502RU2W; Eukaryota. DR GeneTree; ENSGT00940000154796; -. DR HOGENOM; CLU_102589_0_0_1; -. DR InParanoid; Q8N6I1; -. DR OMA; FDAEYMR; -. DR OrthoDB; 5267112at2759; -. DR PhylomeDB; Q8N6I1; -. DR TreeFam; TF337633; -. DR PathwayCommons; Q8N6I1; -. DR SignaLink; Q8N6I1; -. DR SIGNOR; Q8N6I1; -. DR BioGRID-ORCS; 163126; 22 hits in 1167 CRISPR screens. DR ChiTaRS; EID2; human. DR GenomeRNAi; 163126; -. DR Pharos; Q8N6I1; Tbio. DR PRO; PR:Q8N6I1; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q8N6I1; Protein. DR Bgee; ENSG00000176396; Expressed in left ventricle myocardium and 179 other cell types or tissues. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; TAS:HGNC-UCL. DR GO; GO:0046332; F:SMAD binding; IDA: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:0045892; P:negative regulation of DNA-templated transcription; IBA:GO_Central. DR GO; GO:0060392; P:negative regulation of SMAD protein signal transduction; IDA:HGNC-UCL. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:HGNC-UCL. DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IDA:HGNC-UCL. DR GO; GO:0042127; P:regulation of cell population proliferation; IDA:HGNC-UCL. DR GO; GO:0007181; P:transforming growth factor beta receptor complex assembly; IDA:HGNC-UCL. DR InterPro; IPR033258; EID. DR PANTHER; PTHR15556:SF3; EP300-INTERACTING INHIBITOR OF DIFFERENTIATION 2; 1. DR PANTHER; PTHR15556; EP300-INTERACTING INHIBITOR OF DIFFERENTIATION 2-RELATED; 1. DR Genevisible; Q8N6I1; HS. PE 1: Evidence at protein level; KW Alternative splicing; Coiled coil; Developmental protein; Differentiation; KW Methylation; Myogenesis; Nucleus; Reference proteome; Repressor; KW Transcription; Transcription regulation. FT CHAIN 1..236 FT /note="EP300-interacting inhibitor of differentiation 2" FT /id="PRO_0000315901" FT REGION 1..71 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 112..131 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 COMPBIAS 24..38 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 112..126 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 59 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q6X7S9" FT MOD_RES 75 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT VAR_SEQ 43..91 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_052648" FT VARIANT 6 FT /note="A -> T (in dbSNP:rs7252027)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_038351" FT VARIANT 60 FT /note="E -> A (in dbSNP:rs3746086)" FT /id="VAR_050964" SQ SEQUENCE 236 AA; 25190 MW; A69BD5AA098EDC95 CRC64; MSKLPADSSV PQTGAANGDR DVPQAEVGRG RREPAPAQPE EAGEGAMAAA RGGPVPAARE GRMAAARAAP AAAARGAPVA AAALARAAAA GRESPAAAAA REARMAEVAR LLGEPVDEEG PEGRPRSRHG NGGLAALPYL RLRHPLSVLG INYQQFLRHY LENYPIAPGR IQELEERRRR FVEACRAREA AFDAEYQRNP HRVDLDILTF TIALTASEVI NPLIEELGCD KFINRE //