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EP300-interacting inhibitor of differentiation 1 (21 kDa pRb-associated protein) (CREBBP/EP300 inhibitory protein 1) (E1A-like inhibitor of differentiation 1) (EID-1)

 EID1_HUMAN              Reviewed;         187 AA.
Q9Y6B2; B2RD11; Q8N7I4; Q9BZT9;
29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
12-SEP-2018, entry version 129.
RecName: Full=EP300-interacting inhibitor of differentiation 1;
AltName: Full=21 kDa pRb-associated protein;
AltName: Full=CREBBP/EP300 inhibitory protein 1;
AltName: Full=E1A-like inhibitor of differentiation 1;
Short=EID-1;
Name=EID1 {ECO:0000312|EMBL:AAI14947.1};
Synonyms=C15orf3, CRI1 {ECO:0000312|HGNC:HGNC:1191}, RBP21;
ORFNames=PNAS-22, PTD014;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305, ECO:0000312|EMBL:AAK29640.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH
EP300 AND RB1, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
MUTAGENESIS OF CYS-180.
PubMed=11073990; DOI=10.1128/MCB.20.23.8903-8915.2000;
MacLellan W.R., Xiao G., Abdellatif M., Schneider M.D.;
"A novel Rb- and p300-binding protein inhibits transactivation by
MyoD.";
Mol. Cell. Biol. 20:8903-8915(2000).
[2] {ECO:0000305, ECO:0000312|EMBL:AAG35179.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH RB1,
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF LEU-178;
CYS-180 AND GLU-182.
PubMed=11223246; DOI=10.1016/S0378-1119(00)00585-0;
Wen H., Ao S.;
"Identification and characterization of a novel human cDNA encoding a
21 kDa pRb-associated protein.";
Gene 263:85-92(2001).
[3] {ECO:0000305, ECO:0000312|EMBL:AAD40377.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Pituitary tumor {ECO:0000312|EMBL:AAD40377.1};
Huang Q., Peng Y., Dai M., Song H., Mao Y., Zhang Q., Mao M., Fu G.,
Luo M., Chen J., Hu R.;
"Human PTD014 mRNA, complete cds.";
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000305, ECO:0000312|EMBL:AAD40377.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Neonatal brain {ECO:0000312|EMBL:CAB52022.1}, and
Retina {ECO:0000312|EMBL:CAB93108.1};
The European IMAGE consortium;
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
[5] {ECO:0000305, ECO:0000312|EMBL:BAC05296.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain {ECO:0000312|EMBL:BAC05296.1};
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6] {ECO:0000305, ECO:0000312|EMBL:AAD40377.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7] {ECO:0000305, ECO:0000312|EMBL:AAI14945.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8] {ECO:0000305, ECO:0000312|EMBL:AAD40377.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 97-187.
TISSUE=Promyelocytic leukemia {ECO:0000312|EMBL:AAK07524.1};
Yu W.-Q., Sun B.-Z., Chai Y.-B., Zhu F., Liu X.-S., Li Z., Lu F.,
Yan W., Yang H., Zhao Z.-L.;
"Human acute promyelocytic leukemia cell line NB4's apoptosis related
genes.";
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
[9] {ECO:0000305}
FUNCTION, INTERACTION WITH EP300 AND RB1, UBIQUITINATION, AND
INDUCTION.
PubMed=11073989; DOI=10.1128/MCB.20.23.8889-8902.2000;
Miyake S., Sellers W.R., Safran M., Li X., Zhao W., Grossman S.R.,
Gan J., DeCaprio J.A., Adams P.D., Kaelin W.G. Jr.;
"Cells degrade a novel inhibitor of differentiation with E1A-like
properties upon exiting the cell cycle.";
Mol. Cell. Biol. 20:8889-8902(2000).
[10] {ECO:0000305}
INTERACTION WITH TRIM27.
PubMed=15837424; DOI=10.1016/j.molcel.2005.03.009;
Krutzfeldt M., Ellis M., Weekes D.B., Bull J.J., Eilers M.,
Vivanco M.D., Sellers W.R., Mittnacht S.;
"Selective ablation of retinoblastoma protein function by the RET
finger protein.";
Mol. Cell 18:213-224(2005).
-!- FUNCTION: Interacts with RB1 and EP300 and acts as a repressor of
MYOD1 transactivation. Inhibits EP300 and CBP histone
acetyltransferase activity. May be involved in coupling cell cycle
exit to the transcriptional activation of genes required for
cellular differentiation. May act as a candidate coinhibitory
factor for NR0B2 that can be directly linked to transcription
inhibitory mechanisms. {ECO:0000269|PubMed:11073989,
ECO:0000269|PubMed:11073990}.
-!- SUBUNIT: Interacts via its LXCXE motif with the entire pocket
region of RB1. Interacts with EP300, NR0B2 and TRIM27.
{ECO:0000250|UniProtKB:Q9DCR4, ECO:0000269|PubMed:11073989,
ECO:0000269|PubMed:11073990, ECO:0000269|PubMed:11223246,
ECO:0000269|PubMed:15837424}.
-!- INTERACTION:
P25233:Ndn (xeno); NbExp=5; IntAct=EBI-1049975, EBI-1801080;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11223246}.
Cytoplasm {ECO:0000269|PubMed:11223246}. Note=May shuttle between
nucleus and cytoplasm. {ECO:0000250|UniProtKB:Q9DCR4,
ECO:0000269|PubMed:11223246}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1 {ECO:0000269|PubMed:11073990, ECO:0000269|PubMed:11223246,
ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3};
IsoId=Q9Y6B2-1; Sequence=Displayed;
Name=2 {ECO:0000269|PubMed:14702039};
IsoId=Q9Y6B2-2; Sequence=VSP_052454;
Note=No experimental confirmation available. {ECO:0000305};
-!- TISSUE SPECIFICITY: Widely expressed. Most abundantly expressed in
heart, skeletal muscle, pancreas, brain and testis. Expressed at
much lower levels in placenta and peripheral blood leukocyte.
Barely detectable in lung. Also weakly expressed in lung carcinoma
A-549 and various leukemia cell lines.
{ECO:0000269|PubMed:11073990, ECO:0000269|PubMed:11223246}.
-!- DEVELOPMENTAL STAGE: Expression decreased with development in
ventricular tissue while remaining highly expressed in adult
atrial tissue. In primary cultures of human skeletal myocytes,
expression decreased during myogenic differentiation (at protein
level). {ECO:0000269|PubMed:11073990}.
-!- INDUCTION: Down-regulated in differentiating U-937 leukemia cells.
{ECO:0000269|PubMed:11073989}.
-!- PTM: Ubiquitinated in U2OS osteosarcoma cells and is rapidly
degraded by proteasome as cells exit the cell cycle exit.
{ECO:0000269|PubMed:11073989}.
-!- MISCELLANEOUS: Inhibition of MYOD1 may be partly due to the
ability of EID1 to bind and inhibit EP300 histone
acetyltransferase activity. {ECO:0000269|PubMed:11073990}.
-!- SEQUENCE CAUTION:
Sequence=AAK07524.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF349444; AAK29640.1; -; mRNA.
EMBL; AF109873; AAG35179.1; -; mRNA.
EMBL; AF092135; AAD40377.1; -; mRNA.
EMBL; AL109701; CAB52022.1; -; mRNA.
EMBL; AL357456; CAB93108.1; -; mRNA.
EMBL; AK098383; BAC05296.1; -; mRNA.
EMBL; AK315365; BAG37758.1; -; mRNA.
EMBL; CH471082; EAW77357.1; -; Genomic_DNA.
EMBL; BC114944; AAI14945.1; -; mRNA.
EMBL; BC114946; AAI14947.1; -; mRNA.
EMBL; AF274947; AAK07524.1; ALT_INIT; mRNA.
CCDS; CCDS53941.1; -. [Q9Y6B2-1]
RefSeq; NP_055150.1; NM_014335.2. [Q9Y6B2-1]
UniGene; Hs.255973; -.
ProteinModelPortal; Q9Y6B2; -.
BioGrid; 117243; 48.
ELM; Q9Y6B2; -.
IntAct; Q9Y6B2; 10.
MINT; Q9Y6B2; -.
STRING; 9606.ENSP00000431162; -.
iPTMnet; Q9Y6B2; -.
PhosphoSitePlus; Q9Y6B2; -.
BioMuta; EID1; -.
DMDM; 74721525; -.
PaxDb; Q9Y6B2; -.
PeptideAtlas; Q9Y6B2; -.
PRIDE; Q9Y6B2; -.
ProteomicsDB; 86644; -.
ProteomicsDB; 86645; -. [Q9Y6B2-2]
Ensembl; ENST00000530028; ENSP00000431162; ENSG00000255302. [Q9Y6B2-1]
GeneID; 23741; -.
KEGG; hsa:23741; -.
UCSC; uc001zxc.2; human. [Q9Y6B2-1]
CTD; 23741; -.
DisGeNET; 23741; -.
EuPathDB; HostDB:ENSG00000255302.3; -.
GeneCards; EID1; -.
H-InvDB; HIX0012222; -.
HGNC; HGNC:1191; EID1.
HPA; HPA051122; -.
HPA; HPA051123; -.
MIM; 605894; gene.
neXtProt; NX_Q9Y6B2; -.
OpenTargets; ENSG00000255302; -.
PharmGKB; PA26876; -.
eggNOG; ENOG410J09N; Eukaryota.
eggNOG; ENOG41118MI; LUCA.
GeneTree; ENSGT00500000045230; -.
HOVERGEN; HBG098825; -.
InParanoid; Q9Y6B2; -.
OMA; MAEPQGE; -.
OrthoDB; EOG091G0YVS; -.
PhylomeDB; Q9Y6B2; -.
TreeFam; TF337633; -.
SIGNOR; Q9Y6B2; -.
GeneWiki; EID1; -.
GenomeRNAi; 23741; -.
PRO; PR:Q9Y6B2; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000255302; Expressed in 236 organ(s), highest expression level in tendon of biceps brachii.
CleanEx; HS_EID1; -.
ExpressionAtlas; Q9Y6B2; baseline and differential.
Genevisible; Q9Y6B2; HS.
GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IPI:MGI.
GO; GO:0035035; F:histone acetyltransferase binding; IDA:UniProtKB.
GO; GO:0035034; F:histone acetyltransferase regulator activity; IDA:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0030154; P:cell differentiation; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0045595; P:regulation of cell differentiation; IEA:InterPro.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR033258; EID.
InterPro; IPR033255; EID-1.
PANTHER; PTHR15556; PTHR15556; 1.
PANTHER; PTHR15556:SF5; PTHR15556:SF5; 1.
1: Evidence at protein level;
Alternative splicing; Cell cycle; Complete proteome; Cytoplasm;
Differentiation; Nucleus; Reference proteome; Repressor;
Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 187 EP300-interacting inhibitor of
differentiation 1.
/FTId=PRO_0000289156.
REGION 54 120 Interaction with NR0B2.
{ECO:0000250|UniProtKB:Q9DCR4}.
MOTIF 178 182 LXCXE motif.
{ECO:0000269|PubMed:11073990}.
VAR_SEQ 65 87 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_052454.
MUTAGEN 178 178 L->S: Abolishes RB1 binding.
{ECO:0000269|PubMed:11223246}.
MUTAGEN 180 180 C->G: Abolishes RB1 binding.
{ECO:0000269|PubMed:11073990,
ECO:0000269|PubMed:11223246}.
MUTAGEN 182 182 E->Q: Abolishes RB1 binding.
{ECO:0000269|PubMed:11223246}.
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


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