EID2_HUMAN
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 03-AUG-2022, entry version 133.
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, 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
RC Skin {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}.
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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; 7.
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; Q8N6I1; -.
DR PeptideAtlas; Q8N6I1; -.
DR PRIDE; Q8N6I1; -.
DR ProteomicsDB; 72178; -. [Q8N6I1-1]
DR ProteomicsDB; 72179; -. [Q8N6I1-2]
DR Antibodypedia; 48019; 78 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 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; 1475530at2759; -.
DR PhylomeDB; Q8N6I1; -.
DR TreeFam; TF337633; -.
DR PathwayCommons; Q8N6I1; -.
DR SignaLink; Q8N6I1; -.
DR SIGNOR; Q8N6I1; -.
DR BioGRID-ORCS; 163126; 22 hits in 1088 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 177 other tissues.
DR Genevisible; Q8N6I1; HS.
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:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:InterPro.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; 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:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IDA:HGNC-UCL.
DR GO; GO:0007183; P:SMAD protein complex assembly; IDA:HGNC-UCL.
DR GO; GO:0007181; P:transforming growth factor beta receptor complex assembly; IDA: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 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
