EID1_PONAB
ID EID1_PONAB Reviewed; 188 AA.
AC Q5RDL6;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 56.
DE RecName: Full=EP300-interacting inhibitor of differentiation 1;
DE AltName: Full=E1A-like inhibitor of differentiation 1;
DE Short=EID-1;
GN Name=EID1 {ECO:0000250|UniProtKB:Q9Y6B2};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1] {ECO:0000312|EMBL:CAH90141.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex {ECO:0000312|EMBL:CAH90141.1};
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts via its LXCXE motif with the entire pocket region of
CC RB1. Interacts with EP300, NR0B2 and TRIM27 (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y6B2}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y6B2}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9Y6B2}. Note=May shuttle between nucleus and
CC cytoplasm. {ECO:0000250|UniProtKB:Q9Y6B2}.
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:0000250|UniProtKB:Q9Y6B2}.
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DR EMBL; CR857888; CAH90141.1; -; mRNA.
DR RefSeq; NP_001125034.1; NM_001131562.1.
DR AlphaFoldDB; Q5RDL6; -.
DR STRING; 9601.ENSPPYP00000007318; -.
DR GeneID; 100171915; -.
DR KEGG; pon:100171915; -.
DR CTD; 23741; -.
DR eggNOG; ENOG502RQIS; Eukaryota.
DR InParanoid; Q5RDL6; -.
DR OrthoDB; 1497086at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:InterPro.
DR GO; GO:0045595; P:regulation of cell differentiation; IEA:InterPro.
DR GO; GO:0035065; P:regulation of histone acetylation; IEA:InterPro.
DR InterPro; IPR033258; EID.
DR InterPro; IPR033255; EID-1.
DR PANTHER; PTHR15556; PTHR15556; 1.
DR PANTHER; PTHR15556:SF5; PTHR15556:SF5; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cytoplasm; Differentiation; Nucleus; Reference proteome;
KW Repressor; Transcription; Transcription regulation.
FT CHAIN 1..188
FT /note="EP300-interacting inhibitor of differentiation 1"
FT /id="PRO_0000289158"
FT REGION 1..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..121
FT /note="Interaction with NR0B2"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6B2"
FT MOTIF 179..183
FT /note="LXCXE motif"
FT COMPBIAS 94..115
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 188 AA; 20973 MW; 5E5FFD0E997BCDD8 CRC64;
MSEMAELSEL YEESSDLQMD VMPGEGDLPQ MEVGSGSREL SLRPSRNGAQ PQLEEEGPME
EEEAQPMAAP EGKRSLASGP NAGEQPGQVA GADFESEDEG EEFDDWEDDY DYPEEEQLSG
AGYRVSAALE EADKMFLRTR EPALDGGFQM HYEKTPFDQL AFIEELFSLM VVNRLTEELG
CDEIIDRE
