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Q8N6I1 (EID2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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 2

Short name=EID-2
Alternative name(s):
CREBBP/EP300 inhibitor 2
EID-1-like inhibitor of differentiation 2
Gene names
Name:EID2
Synonyms:CRI2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length236 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Interacts with EP300 and acts as a repressor of MYOD-dependent transcription and muscle differentiation. Inhibits EP300 histone acetyltransferase activity. Acts as a repressor of TGFB/SMAD transcriptional responses. May act as a repressor of the TGFB/SMAD3-dependent signaling by selectively blocking formation of TGFB-induced SMAD3-SMAD4 complex. Ref.1 Ref.5 Ref.6

Subunit structure

Heterodimer with EID2B. Interacts with the C-terminus of EP300. Interacts with HDAC1 and HDAC2. Interacts with SMAD2, SMAD4 and with the MH2 domain of SMAD3. Ref.1 Ref.5 Ref.6 Ref.7

Subcellular location

Nucleus Ref.1.

Tissue specificity

Most abundantly expressed in placenta. Highly expressed in liver, brain, heart, skeletal muscle, and kidney. Ref.1

Domain

The N-terminal portion of EID2 is required for nuclear localization. Ref.1

Ontologies

Keywords
   Biological processDifferentiation
Myogenesis
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   Molecular functionDevelopmental protein
Repressor
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processSMAD protein complex assembly

Inferred from direct assay Ref.6. Source: HGNC

cell differentiation

Inferred from electronic annotation. Source: UniProtKB-KW

muscle organ development

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.6. Source: HGNC

negative regulation of transforming growth factor beta receptor signaling pathway

Inferred from direct assay Ref.6. Source: HGNC

regulation of cell proliferation

Inferred from direct assay Ref.6. Source: HGNC

regulation of transforming growth factor beta receptor signaling pathway

Inferred from direct assay Ref.6. Source: HGNC

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transforming growth factor beta receptor complex assembly

Inferred from direct assay Ref.6. Source: HGNC

   Cellular_componentintracellular

Inferred by curator Ref.6. Source: HGNC

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionSMAD binding

Inferred from direct assay Ref.6. Source: HGNC

protein binding

Inferred from physical interaction Ref.7. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

EID3Q8N1403EBI-5525894,EBI-744483

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.1 Ref.3 Ref.4 (identifier: Q8N6I1-1)

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.2 (identifier: Q8N6I1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     43-91: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 236236EP300-interacting inhibitor of differentiation 2
PRO_0000315901

Regions

Coiled coil170 – 19021 Potential
Compositional bias35 – 10975Ala-rich

Natural variations

Alternative sequence43 – 9149Missing in isoform 2. Ref.2
VSP_052648
Natural variant61A → T. Ref.2
Corresponds to variant rs7252027 [ dbSNP | Ensembl ].
VAR_038351
Natural variant601E → A.
Corresponds to variant rs3746086 [ dbSNP | Ensembl ].
VAR_050964

Sequences

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

Last modified July 19, 2005. Version 3.
Checksum: A69BD5AA098EDC95

FASTA23625,190
        10         20         30         40         50         60 
MSKLPADSSV PQTGAANGDR DVPQAEVGRG RREPAPAQPE EAGEGAMAAA RGGPVPAARE 

        70         80         90        100        110        120 
GRMAAARAAP AAAARGAPVA AAALARAAAA GRESPAAAAA REARMAEVAR LLGEPVDEEG 

       130        140        150        160        170        180 
PEGRPRSRHG NGGLAALPYL RLRHPLSVLG INYQQFLRHY LENYPIAPGR IQELEERRRR 

       190        200        210        220        230 
FVEACRAREA AFDAEYQRNP HRVDLDILTF TIALTASEVI NPLIEELGCD KFINRE 

« Hide

Isoform 2 [UniParc].

Checksum: F2A01DD44EFF45B2
Show »

FASTA18720,856

References

« Hide 'large scale' references
[1]"EID-2, a novel member of the EID family of p300-binding proteins inhibits transactivation by MyoD."
Ji A., Dao D., Chen J., MacLellan W.R.
Gene 318:35-43(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH EP300, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DOMAIN.
[2]"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] (ISOFORM 2), VARIANT THR-6.
Tissue: Kidney.
[3]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].
[4]"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).
Tissue: Lung and Skin.
[5]"A novel EID-1 family member, EID-2, associates with histone deacetylases and inhibits muscle differentiation."
Miyake S., Yanagisawa Y., Yuasa Y.
J. Biol. Chem. 278:17060-17065(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HDAC1 AND HDAC2.
[6]"A novel E1A-like inhibitor of differentiation (EID) family member, EID-2, suppresses transforming growth factor (TGF)-beta signaling by blocking TGF-beta-induced formation of Smad3-Smad4 complexes."
Lee H.-J., Lee J.K., Miyake S., Kim S.-J.
J. Biol. Chem. 279:2666-2672(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SMAD2; SMAD3 AND SMAD4.
[7]"A novel EID family member, EID-3, inhibits differentiation and forms a homodimer or heterodimer with EID-2."
Sasajima Y., Tanaka H., Miyake S., Yuasa Y.
Biochem. Biophys. Res. Commun. 333:969-975(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY251272 mRNA. Translation: AAP12559.1.
AK128468 mRNA. Translation: BAC87454.1.
CH471126 Genomic DNA. Translation: EAW56909.1.
BC030137 mRNA. Translation: AAH30137.3.
BC099899 mRNA. Translation: AAH99899.1.
CCDSCCDS12540.2. [Q8N6I1-1]
RefSeqNP_694964.3. NM_153232.3. [Q8N6I1-1]
UniGeneHs.18949.

3D structure databases

ProteinModelPortalQ8N6I1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid127852. 14 interactions.
IntActQ8N6I1. 4 interactions.
STRING9606.ENSP00000375073.

PTM databases

PhosphoSiteQ8N6I1.

Polymorphism databases

DMDM74762532.

Proteomic databases

MaxQBQ8N6I1.
PaxDbQ8N6I1.
PRIDEQ8N6I1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000390658; ENSP00000375073; ENSG00000176396. [Q8N6I1-1]
GeneID163126.
KEGGhsa:163126.
UCSCuc002oma.3. human. [Q8N6I1-1]

Organism-specific databases

CTD163126.
GeneCardsGC19M040028.
H-InvDBHIX0015123.
HGNCHGNC:28292. EID2.
HPAHPA045477.
MIM609773. gene.
neXtProtNX_Q8N6I1.
PharmGKBPA162384544.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG124477.
HOGENOMHOG000054219.
InParanoidQ8N6I1.
OMAPQRVDFD.
OrthoDBEOG73FQPX.
PhylomeDBQ8N6I1.
TreeFamTF337633.

Gene expression databases

BgeeQ8N6I1.
CleanExHS_EID2.
GenevestigatorQ8N6I1.

Family and domain databases

ProtoNetSearch...

Other

GenomeRNAi163126.
NextBio88309.
PROQ8N6I1.
SOURCESearch...

Entry information

Entry nameEID2_HUMAN
AccessionPrimary (citable) accession number: Q8N6I1
Secondary accession number(s): A7YQ71, Q6X7T0, Q6ZR61
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 19, 2005
Last modified: July 9, 2014
This is version 83 of the entry and version 3 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

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM