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Q9Y6B2 (EID1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
EP300-interacting inhibitor of differentiation 1
Alternative name(s):
21 kDa pRb-associated protein
CREBBP/EP300 inhibitory protein 1
E1A-like inhibitor of differentiation 1
Short name=EID-1
Gene names
Name:EID1
Synonyms:C15orf3, CRI1, RBP21
ORF Names:PNAS-22, PTD014
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length187 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.1 Ref.9 UniProtKB Q9DCR4

Subunit structure

Interacts via its LXCXE motif with the entire pocket region of RB1. Interacts with EP300, NR0B2 and TRIM27. Ref.1 Ref.2 Ref.9 Ref.10 UniProtKB Q9DCR4

Subcellular location

Nucleus. Cytoplasm. Note: May shuttle between nucleus and cytoplasm. Ref.2 UniProtKB Q9DCR4

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. Ref.1 Ref.2

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). Ref.1

Induction

Down-regulated in differentiating U-937 leukemia cells. Ref.9

Post-translational modification

Ubiquitinated in U2OS osteosarcoma cells and is rapidly degraded by proteasome as cells exit the cell cycle exit. Ref.9

Miscellaneous

Inhibition of MYOD1 may be partly due to the ability of EID1 to bind and inhibit EP300 histone acetyltransferase activity. Ref.1

Sequence caution

The sequence AAK07524.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NdnP252335EBI-1049975,EBI-1801080From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.1 Ref.2 Ref.3 Ref.4 Ref.7 (identifier: Q9Y6B2-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 Ref.5 (identifier: Q9Y6B2-2)

The sequence of this isoform differs from the canonical sequence as follows:
     65-87: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 187187EP300-interacting inhibitor of differentiation 1
PRO_0000289156

Regions

Region54 – 12067Interaction with NR0B2 By similarity UniProtKB Q9DCR4
Motif178 – 1825LXCXE motif Ref.1

Natural variations

Alternative sequence65 – 8723Missing in isoform 2. Ref.5
VSP_052454

Experimental info

Mutagenesis1781L → S: Abolishes RB1 binding. Ref.2
Mutagenesis1801C → G: Abolishes RB1 binding. Ref.1 Ref.2
Mutagenesis1821E → Q: Abolishes RB1 binding. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: A2815FA78ED0736D

FASTA18720,876
        10         20         30         40         50         60 
MSEMAELSEL YEESSDLQMD VMPGEGDLPQ MEVGSGSREL SLRPSRSGAQ QLEEEGPMEE 

        70         80         90        100        110        120 
EEAQPMAAPE GKRSLANGPN AGEQPGQVAG ADFESEDEGE EFDDWEDDYD YPEEEQLSGA 

       130        140        150        160        170        180 
GYRVSAALEE ADKMFLRTRE PALDGGFQMH YEKTPFDQLA FIEELFSLMV VNRLTEELGC 


DEIIDRE 

« Hide

Isoform 2 [UniParc].

Checksum: FB44C04D87381C53
Show »

FASTA16418,616

References

« Hide 'large scale' references
[1]"A novel Rb- and p300-binding protein inhibits transactivation by MyoD."
MacLellan W.R., Xiao G., Abdellatif M., Schneider M.D.
Mol. Cell. Biol. 20:8903-8915(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH EP300 AND RB1, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, MUTAGENESIS OF CYS-180.
[2]"Identification and characterization of a novel human cDNA encoding a 21 kDa pRb-associated protein."
Wen H., Ao S.
Gene 263:85-92(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH RB1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF LEU-178; CYS-180 AND GLU-182.
[3]"Human PTD014 mRNA, complete cds."
Huang Q., Peng Y., Dai M., Song H., Mao Y., Zhang Q., Mao M., Fu G., Luo M., Chen J., Hu R.
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Pituitary tumor.
[4]The European IMAGE consortium
Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Neonatal brain and Retina.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Brain.
[6]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[8]"Human acute promyelocytic leukemia cell line NB4's apoptosis related genes."
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.
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 97-187.
Tissue: Promyelocytic leukemia.
[9]"Cells degrade a novel inhibitor of differentiation with E1A-like properties upon exiting the cell cycle."
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.
Mol. Cell. Biol. 20:8889-8902(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH EP300 AND RB1, UBIQUITINATION, INDUCTION.
[10]"Selective ablation of retinoblastoma protein function by the RET finger protein."
Krutzfeldt M., Ellis M., Weekes D.B., Bull J.J., Eilers M., Vivanco M.D., Sellers W.R., Mittnacht S.
Mol. Cell 18:213-224(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRIM27.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF349444 mRNA. Translation: AAK29640.1.
AF109873 mRNA. Translation: AAG35179.1.
AF092135 mRNA. Translation: AAD40377.1.
AL109701 mRNA. Translation: CAB52022.1.
AL357456 mRNA. Translation: CAB93108.1.
AK098383 mRNA. Translation: BAC05296.1.
AK315365 mRNA. Translation: BAG37758.1.
CH471082 Genomic DNA. Translation: EAW77357.1.
BC114944 mRNA. Translation: AAI14945.1.
BC114946 mRNA. Translation: AAI14947.1.
AF274947 mRNA. Translation: AAK07524.1. Different initiation.
IPIIPI00295287.
IPI00847728.
RefSeqNP_055150.1. NM_014335.2.
UniGeneHs.255973.

3D structure databases

ProteinModelPortalQ9Y6B2.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9Y6B2. 6 interactions.

PTM databases

PhosphoSiteQ9Y6B2.

Polymorphism databases

DMDM74721525.

Proteomic databases

PRIDEQ9Y6B2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000530028; ENSP00000431162; ENSG00000255302.
GeneID23741.
KEGGhsa:23741.
UCSCuc001zxc.1. human.

Organism-specific databases

CTD23741.
GeneCardsGC15P049171.
H-InvDBHIX0012222.
HGNCHGNC:1191. EID1.
HPAHPA051122.
HPA051123.
MIM605894. gene.
neXtProtNX_Q9Y6B2.
PharmGKBPA26876.
GenAtlasSearch...

Phylogenomic databases

HOVERGENHBG098825.
InParanoidQ9Y6B2.
OMANDLQMDV.
OrthoDBEOG4X97JM.

Gene expression databases

ArrayExpressQ9Y6B2.
BgeeQ9Y6B2.
CleanExHS_EID1.
GenevestigatorQ9Y6B2.

Family and domain databases

ProtoNetSearch...

Other

GenomeRNAi23741.
NextBio46655.
SOURCESearch...

Entry information

Entry nameEID1_HUMAN
AccessionPrimary (citable) accession number: Q9Y6B2
Secondary accession number(s): B2RD11, Q8N7I4, Q9BZT9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: November 1, 1999
Last modified: May 1, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot