EID1_HUMAN
ID EID1_HUMAN Reviewed; 187 AA.
AC Q9Y6B2; B2RD11; Q8N7I4; Q9BZT9;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=EP300-interacting inhibitor of differentiation 1;
DE AltName: Full=21 kDa pRb-associated protein;
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|EMBL:AAI14947.1};
GN Synonyms=C15orf3, CRI1 {ECO:0000312|HGNC:HGNC:1191}, RBP21;
GN ORFNames=PNAS-22, PTD014;
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:AAK29640.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH EP300
RP AND RB1, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF
RP CYS-180.
RX PubMed=11073990; DOI=10.1128/mcb.20.23.8903-8915.2000;
RA MacLellan W.R., Xiao G., Abdellatif M., Schneider M.D.;
RT "A novel Rb- and p300-binding protein inhibits transactivation by MyoD.";
RL Mol. Cell. Biol. 20:8903-8915(2000).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAG35179.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH RB1, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF LEU-178; CYS-180 AND
RP GLU-182.
RX PubMed=11223246; DOI=10.1016/s0378-1119(00)00585-0;
RA Wen H., Ao S.;
RT "Identification and characterization of a novel human cDNA encoding a 21
RT kDa pRb-associated protein.";
RL Gene 263:85-92(2001).
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAD40377.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Pituitary tumor {ECO:0000312|EMBL:AAD40377.1};
RA Huang Q., Peng Y., Dai M., Song H., Mao Y., Zhang Q., Mao M., Fu G.,
RA Luo M., Chen J., Hu R.;
RT "Human PTD014 mRNA, complete cds.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAD40377.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Neonatal brain {ECO:0000312|EMBL:CAB52022.1}, and
RC Retina {ECO:0000312|EMBL:CAB93108.1};
RG The European IMAGE consortium;
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305, ECO:0000312|EMBL:BAC05296.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain {ECO:0000312|EMBL:BAC05296.1};
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 [6] {ECO:0000305, ECO:0000312|EMBL:AAD40377.1}
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 [7] {ECO:0000305, ECO:0000312|EMBL:AAI14945.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 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 [8] {ECO:0000305, ECO:0000312|EMBL:AAD40377.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 97-187.
RC TISSUE=Promyelocytic leukemia {ECO:0000312|EMBL:AAK07524.1};
RA Yu W.-Q., Sun B.-Z., Chai Y.-B., Zhu F., Liu X.-S., Li Z., Lu F., Yan W.,
RA Yang H., Zhao Z.-L.;
RT "Human acute promyelocytic leukemia cell line NB4's apoptosis related
RT genes.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [9] {ECO:0000305}
RP FUNCTION, INTERACTION WITH EP300 AND RB1, UBIQUITINATION, AND INDUCTION.
RX PubMed=11073989; DOI=10.1128/mcb.20.23.8889-8902.2000;
RA Miyake S., Sellers W.R., Safran M., Li X., Zhao W., Grossman S.R., Gan J.,
RA DeCaprio J.A., Adams P.D., Kaelin W.G. Jr.;
RT "Cells degrade a novel inhibitor of differentiation with E1A-like
RT properties upon exiting the cell cycle.";
RL Mol. Cell. Biol. 20:8889-8902(2000).
RN [10] {ECO:0000305}
RP INTERACTION WITH TRIM27.
RX PubMed=15837424; DOI=10.1016/j.molcel.2005.03.009;
RA Krutzfeldt M., Ellis M., Weekes D.B., Bull J.J., Eilers M., Vivanco M.D.,
RA Sellers W.R., Mittnacht S.;
RT "Selective ablation of retinoblastoma protein function by the RET finger
RT protein.";
RL Mol. Cell 18:213-224(2005).
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:11073989, ECO:0000269|PubMed:11073990}.
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:Q9DCR4, ECO:0000269|PubMed:11073989,
CC ECO:0000269|PubMed:11073990, ECO:0000269|PubMed:11223246,
CC ECO:0000269|PubMed:15837424}.
CC -!- INTERACTION:
CC Q9Y6B2; Q99608: NDN; NbExp=3; IntAct=EBI-1049975, EBI-718177;
CC Q9Y6B2; P25233: Ndn; Xeno; NbExp=5; IntAct=EBI-1049975, EBI-1801080;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11223246}. Cytoplasm
CC {ECO:0000269|PubMed:11223246}. Note=May shuttle between nucleus and
CC cytoplasm. {ECO:0000250|UniProtKB:Q9DCR4, ECO:0000269|PubMed:11223246}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:11073990, ECO:0000269|PubMed:11223246,
CC ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3};
CC IsoId=Q9Y6B2-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:14702039};
CC IsoId=Q9Y6B2-2; Sequence=VSP_052454;
CC -!- TISSUE SPECIFICITY: Widely expressed. Most abundantly expressed in
CC heart, skeletal muscle, pancreas, brain and testis. Expressed at much
CC lower levels in placenta and peripheral blood leukocyte. Barely
CC detectable in lung. Also weakly expressed in lung carcinoma A-549 and
CC various leukemia cell lines. {ECO:0000269|PubMed:11073990,
CC ECO:0000269|PubMed:11223246}.
CC -!- DEVELOPMENTAL STAGE: Expression decreased with development in
CC ventricular tissue while remaining highly expressed in adult atrial
CC tissue. In primary cultures of human skeletal myocytes, expression
CC decreased during myogenic differentiation (at protein level).
CC {ECO:0000269|PubMed:11073990}.
CC -!- INDUCTION: Down-regulated in differentiating U-937 leukemia cells.
CC {ECO:0000269|PubMed:11073989}.
CC -!- PTM: Ubiquitinated in U2OS osteosarcoma cells and is rapidly degraded
CC by proteasome as cells exit the cell cycle exit.
CC {ECO:0000269|PubMed:11073989}.
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:0000269|PubMed:11073990}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK07524.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF349444; AAK29640.1; -; mRNA.
DR EMBL; AF109873; AAG35179.1; -; mRNA.
DR EMBL; AF092135; AAD40377.1; -; mRNA.
DR EMBL; AL109701; CAB52022.1; -; mRNA.
DR EMBL; AL357456; CAB93108.1; -; mRNA.
DR EMBL; AK098383; BAC05296.1; -; mRNA.
DR EMBL; AK315365; BAG37758.1; -; mRNA.
DR EMBL; CH471082; EAW77357.1; -; Genomic_DNA.
DR EMBL; BC114944; AAI14945.1; -; mRNA.
DR EMBL; BC114946; AAI14947.1; -; mRNA.
DR EMBL; AF274947; AAK07524.1; ALT_INIT; mRNA.
DR CCDS; CCDS53941.1; -. [Q9Y6B2-1]
DR RefSeq; NP_055150.1; NM_014335.2. [Q9Y6B2-1]
DR AlphaFoldDB; Q9Y6B2; -.
DR BioGRID; 117243; 48.
DR ELM; Q9Y6B2; -.
DR IntAct; Q9Y6B2; 22.
DR MINT; Q9Y6B2; -.
DR STRING; 9606.ENSP00000431162; -.
DR iPTMnet; Q9Y6B2; -.
DR PhosphoSitePlus; Q9Y6B2; -.
DR BioMuta; EID1; -.
DR DMDM; 74721525; -.
DR MassIVE; Q9Y6B2; -.
DR MaxQB; Q9Y6B2; -.
DR PaxDb; Q9Y6B2; -.
DR PeptideAtlas; Q9Y6B2; -.
DR PRIDE; Q9Y6B2; -.
DR ProteomicsDB; 86644; -. [Q9Y6B2-1]
DR ProteomicsDB; 86645; -. [Q9Y6B2-2]
DR Antibodypedia; 53733; 146 antibodies from 25 providers.
DR DNASU; 23741; -.
DR Ensembl; ENST00000530028.3; ENSP00000431162.2; ENSG00000255302.5. [Q9Y6B2-1]
DR GeneID; 23741; -.
DR KEGG; hsa:23741; -.
DR MANE-Select; ENST00000530028.3; ENSP00000431162.2; NM_014335.3; NP_055150.1.
DR UCSC; uc001zxc.2; human. [Q9Y6B2-1]
DR CTD; 23741; -.
DR DisGeNET; 23741; -.
DR GeneCards; EID1; -.
DR HGNC; HGNC:1191; EID1.
DR HPA; ENSG00000255302; Low tissue specificity.
DR MIM; 605894; gene.
DR neXtProt; NX_Q9Y6B2; -.
DR OpenTargets; ENSG00000255302; -.
DR PharmGKB; PA26876; -.
DR VEuPathDB; HostDB:ENSG00000255302; -.
DR eggNOG; ENOG502RQIS; Eukaryota.
DR GeneTree; ENSGT00940000154796; -.
DR InParanoid; Q9Y6B2; -.
DR OMA; WSGAMHR; -.
DR OrthoDB; 1497086at2759; -.
DR PhylomeDB; Q9Y6B2; -.
DR TreeFam; TF337633; -.
DR PathwayCommons; Q9Y6B2; -.
DR SignaLink; Q9Y6B2; -.
DR SIGNOR; Q9Y6B2; -.
DR BioGRID-ORCS; 23741; 10 hits in 1082 CRISPR screens.
DR ChiTaRS; EID1; human.
DR GeneWiki; EID1; -.
DR GenomeRNAi; 23741; -.
DR Pharos; Q9Y6B2; Tbio.
DR PRO; PR:Q9Y6B2; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9Y6B2; protein.
DR Bgee; ENSG00000255302; Expressed in tendon of biceps brachii and 215 other tissues.
DR ExpressionAtlas; Q9Y6B2; baseline and differential.
DR Genevisible; Q9Y6B2; HS.
DR GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IPI:MGI.
DR GO; GO:0035035; F:histone acetyltransferase binding; IDA:UniProtKB.
DR GO; GO:0035034; F:histone acetyltransferase regulator activity; IDA:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0045595; P:regulation of cell differentiation; IEA:InterPro.
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 Alternative splicing; Cell cycle; Cytoplasm; Differentiation; Nucleus;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..187
FT /note="EP300-interacting inhibitor of differentiation 1"
FT /id="PRO_0000289156"
FT REGION 1..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..120
FT /note="Interaction with NR0B2"
FT /evidence="ECO:0000250|UniProtKB:Q9DCR4"
FT MOTIF 178..182
FT /note="LXCXE motif"
FT /evidence="ECO:0000269|PubMed:11073990"
FT COMPBIAS 93..114
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 65..87
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_052454"
FT MUTAGEN 178
FT /note="L->S: Abolishes RB1 binding."
FT /evidence="ECO:0000269|PubMed:11223246"
FT MUTAGEN 180
FT /note="C->G: Abolishes RB1 binding."
FT /evidence="ECO:0000269|PubMed:11073990,
FT ECO:0000269|PubMed:11223246"
FT MUTAGEN 182
FT /note="E->Q: Abolishes RB1 binding."
FT /evidence="ECO:0000269|PubMed:11223246"
SQ SEQUENCE 187 AA; 20876 MW; A2815FA78ED0736D CRC64;
MSEMAELSEL YEESSDLQMD VMPGEGDLPQ MEVGSGSREL SLRPSRSGAQ QLEEEGPMEE
EEAQPMAAPE GKRSLANGPN AGEQPGQVAG ADFESEDEGE EFDDWEDDYD YPEEEQLSGA
GYRVSAALEE ADKMFLRTRE PALDGGFQMH YEKTPFDQLA FIEELFSLMV VNRLTEELGC
DEIIDRE
