Polycomb protein EED

EED
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	3IIW, 3IIY, 3IJ0, 3IJ1, 3IJC, 3JPX, 3JZG, 3JZH, 3JZN, 3K26, 3K27, 4X3E, 5IJ7, 5IJ8, 5HYN Contents Function ; Clinical significance ; Interactions ; References ; External links ; Further reading ;
Identifiers
Aliases	EED , HWAIT1, embryonic ectoderm development, COGIS
External IDs	OMIM: 605984 MGI: 95286 HomoloGene: 2814 GeneCards: EED
Gene location (Human)
Chr.	Chromosome 11 (human)
End	86,278,813 bp
Gene location (Mouse)
Chr.	Chromosome 7 (mouse)
End	89,980,983 bp
RNA expression pattern
	; ;
	More reference expression data
Gene ontology
Molecular function	• chromatin binding ; • GO:0001948 protein binding ; • identical protein binding ; • GO:0000980 RNA polymerase II cis-regulatory region sequence-specific DNA binding ; • histone methyltransferase activity ; • histone methyltransferase activity (H3-K27 specific) ; • nucleosome binding ;
Cellular component	• sex chromatin ; • ESC/E(Z) complex ; • chromosome ; • pronucleus ; • cell nucleus ; • nucleoplasm ; • cytosol ;
Biological process	• regulation of gene expression by genetic imprinting ; • regulation of transcription, DNA-templated ; • negative regulation of transcription from RNA polymerase II promoter ; • transcription, DNA-templated ; • negative regulation of gene expression, epigenetic ; • spinal cord development ; • positive regulation of histone H3-K27 methylation ; • histone methylation ; • negative regulation of transcription, DNA-templated ; • regulation of adaxial/abaxial pattern formation ; • histone H3-K27 methylation ; • cellular response to leukemia inhibitory factor ; • negative regulation of G0 to G1 transition ; • chromatin organization ; • chromatin silencing ;
	Sources:Amigo / QuickGO
Orthologs
	8726
	13626
	ENSG00000074266
	ENSMUSG00000030619
	O75530
	Q921E6
	NM_001308007 ; NM_003797 ; NM_152991 ; NM_001330334
	NM_021876
	NP_001294936 ; NP_001317263 ; NP_003788
	NP_068676
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated March 30, 2021

Polycomb protein EED is a protein that in humans is encoded by the EED gene.^[5]^[6]^[7]

Function

Polycomb protein EED is a member of the Polycomb-group (PcG) family. PcG family members form multimeric protein complexes, which are involved in maintaining the transcriptional repressive state of genes over successive cell generations. This protein interacts with enhancer of zeste 2, the cytoplasmic tail of integrin β7, immunodeficiency virus type 1 (HIV-1) MA protein, and histone deacetylase proteins. This protein mediates repression of gene activity through histone deacetylation, and may act as a specific regulator of integrin function. Two transcript variants encoding distinct isoforms have been identified for this gene.^[7]

Clinical significance

In humans, a de-novo mutation in EED has been reported in an individual displaying symptoms similar to those of Weaver syndrome.^[8]

Interactions

EED has been shown to interact with:

Related Research Articles

Methyl-CpG-binding domain protein 1 is a protein that in humans is encoded by the MBD1 gene. The protein encoded by MBD1 binds to methylated sequences in DNA, and thereby influences transcription. It binds to a variety of methylated sequences, and appears to mediate repression of gene expression. It has been shown to play a role in chromatin modification through interaction with the histone H3K9 methyltransferase SETDB1. H3K9me3 is a repressive modification.

Enhancer of zeste homolog 2 (EZH2) is a histone-lysine N-methyltransferase enzyme encoded by EZH2 gene, that participates in histone methylation and, ultimately, transcriptional repression. EZH2 catalyzes the addition of methyl groups to histone H3 at lysine 27, by using the cofactor S-adenosyl-L-methionine. Methylation activity of EZH2 facilitates heterochromatin formation thereby silences gene function. Remodeling of chromosomal heterochromatin by EZH2 is also required during cell mitosis.

Polycomb complex protein BMI-1 also known as polycomb group RING finger protein 4 (PCGF4) or RING finger protein 51 (RNF51) is a protein that in humans is encoded by the BMI1 gene. BMI1 is a polycomb ring finger oncogene.

Histone-lysine N-methyltransferase SUV39H1 is an enzyme that in humans is encoded by the SUV39H1 gene.

Histone acetyltransferase KAT2A is an enzyme that in humans is encoded by the KAT2A gene.

Nuclear inhibitor of protein phosphatase 1 is an enzyme that in humans is encoded by the PPP1R8 gene.

Chromatin assembly factor 1 subunit A is a protein that in humans is encoded by the CHAF1A gene.

Histone H2B type 1-K is a protein that in humans is encoded by the HIST1H2BK gene.

DNA methyltransferase 1-associated protein 1 is an enzyme that in humans is encoded by the DMAP1 gene.

E3 ubiquitin-protein ligase RING2 is an enzyme that in humans is encoded by the RNF2 gene.

Polycomb protein SUZ12 is a protein that in humans is encoded by the SUZ12 gene.

Histone H3.1 is a protein in humans that is encoded by the HIST1H3A gene.

WD repeat-containing protein 5 is a protein that in humans is encoded by the WDR5 gene.

Histone H3.1 is a protein that in humans is encoded by the HIST1H3F gene.

Enhancer of polycomb homolog 1 is a protein that in humans is encoded by the EPC1 gene.

Histone H4 is a protein that in humans is encoded by the HIST1H4A gene.

Set1/Ash2 histone methyltransferase complex subunit ASH2 is an enzyme that in humans is encoded by the ASH2L gene.

Histone-lysine N-methyltransferase EZH1 is an enzyme that in humans is encoded by the EZH1 gene.

Trithorax-group proteins (TrxG) are a heterogeneous collection of proteins whose main action is to maintain gene expression. They can be categorized into three general classes based on molecular function:

histone-modifying TrxG proteins
chromatin-remodeling TrxG proteins
DNA-binding TrxG proteins,

PRC2 is one of the two classes of polycomb-group proteins or (PcG). The other component of this group of proteins is PRC1.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000074266 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000030619 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
1 2 Rietzler M, Bittner M, Kolanus W, Schuster A, Holzmann B (Nov 1998). "The human WD repeat protein WAIT-1 specifically interacts with the cytoplasmic tails of beta7-integrins". J. Biol. Chem. 273 (42): 27459–66. doi: 10.1074/jbc.273.42.27459 . PMID 9765275.
↑ Schumacher A, Lichtarge O, Schwartz S, Magnuson T (Jan 1999). "The murine Polycomb-group gene eed and its human orthologue: functional implications of evolutionary conservation". Genomics. 54 (1): 79–88. doi:10.1006/geno.1998.5509. PMID 9806832.
1 2 "Entrez Gene: EED embryonic ectoderm development".
↑ Cohen AS, Tuysuz B, Shen Y, Bhalla SK, Jones SJ, Gibson WT (Mar 2015). "A novel mutation in EED associated with overgrowth". Journal of Human Genetics. 60 (6): 339–342. doi: 10.1038/jhg.2015.26 . PMID 25787343. S2CID 22055237.
1 2 3 van der Vlag J, Otte AP (Dec 1999). "Transcriptional repression mediated by the human polycomb-group protein EED involves histone deacetylation". Nat. Genet. 23 (4): 474–8. doi:10.1038/70602. PMID 10581039. S2CID 6748531.
↑ van Lohuizen M, Tijms M, Voncken JW, Schumacher A, Magnuson T, Wientjens E (Jun 1998). "Interaction of mouse polycomb-group (Pc-G) proteins Enx1 and Enx2 with Eed: indication for separate Pc-G complexes". Mol. Cell. Biol. 18 (6): 3572–9. doi:10.1128/MCB.18.6.3572. PMC 108938 . PMID 9584197.
↑ Denisenko O, Shnyreva M, Suzuki H, Bomsztyk K (Oct 1998). "Point mutations in the WD40 domain of Eed block its interaction with Ezh2". Mol. Cell. Biol. 18 (10): 5634–42. doi:10.1128/MCB.18.10.5634. PMC 109149 . PMID 9742080.
↑ Jin Q, van Eynde A, Beullens M, Roy N, Thiel G, Stalmans W, Bollen M (Aug 2003). "The protein phosphatase-1 (PP1) regulator, nuclear inhibitor of PP1 (NIPP1), interacts with the polycomb group protein, embryonic ectoderm development (EED), and functions as a transcriptional repressor". J. Biol. Chem. 278 (33): 30677–85. doi: 10.1074/jbc.M302273200 . PMID 12788942.
↑ Enünlü I, Pápai G, Cserpán I, Udvardy A, Jeang KT, Boros I (Sep 2003). "Different isoforms of PRIP-interacting protein with methyltransferase domain/trimethylguanosine synthase localizes to the cytoplasm and nucleus". Biochem. Biophys. Res. Commun. 309 (1): 44–51. doi:10.1016/s0006-291x(03)01514-6. PMID 12943661.

External links

Overview of all the structural information available in the PDB for UniProt : O75530 (Polycomb protein EED) at the PDBe-KB .

Joseph AM, Kumar M, Mitra D (2005). "Nef: "necessary and enforcing factor" in HIV infection". Curr. HIV Res. 3 (1): 87–94. doi:10.2174/1570162052773013. PMID 15638726.
Van Maele B, Debyser Z (2005). "HIV-1 integration: an interplay between HIV-1 integrase, cellular and viral proteins". AIDS Rev. 7 (1): 26–43. PMID 15875659.
Jones CA, Ng J, Peterson AJ, Morgan K, Simon J, Jones RS (1998). "The Drosophila esc and E(z) proteins are direct partners in polycomb group-mediated repression". Mol. Cell. Biol. 18 (5): 2825–34. doi:10.1128/mcb.18.5.2825. PMC 110661 . PMID 9566901.
van Lohuizen M, Tijms M, Voncken JW, Schumacher A, Magnuson T, Wientjens E (1998). "Interaction of mouse polycomb-group (Pc-G) proteins Enx1 and Enx2 with Eed: indication for separate Pc-G complexes". Mol. Cell. Biol. 18 (6): 3572–9. doi:10.1128/MCB.18.6.3572. PMC 108938 . PMID 9584197.
Sewalt RG, van der Vlag J, Gunster MJ, Hamer KM, den Blaauwen JL, Satijn DP, Hendrix T, van Driel R, Otte AP (1998). "Characterization of interactions between the mammalian polycomb-group proteins Enx1/EZH2 and EED suggests the existence of different mammalian polycomb-group protein complexes". Mol. Cell. Biol. 18 (6): 3586–95. doi:10.1128/mcb.18.6.3586. PMC 108940 . PMID 9584199.
Denisenko O, Shnyreva M, Suzuki H, Bomsztyk K (1998). "Point mutations in the WD40 domain of Eed block its interaction with Ezh2". Mol. Cell. Biol. 18 (10): 5634–42. doi:10.1128/MCB.18.10.5634. PMC 109149 . PMID 9742080.
Peytavi R, Hong SS, Gay B, d'Angeac AD, Selig L, Bénichou S, Benarous R, Boulanger P (1999). "HEED, the product of the human homolog of the murine eed gene, binds to the matrix protein of HIV-1". J. Biol. Chem. 274 (3): 1635–45. doi: 10.1074/jbc.274.3.1635 . PMID 9880543.
van der Vlag J, Otte AP (1999). "Transcriptional repression mediated by the human polycomb-group protein EED involves histone deacetylation". Nat. Genet. 23 (4): 474–8. doi:10.1038/70602. PMID 10581039. S2CID 6748531.
Satijn DP, Hamer KM, den Blaauwen J, Otte AP (2001). "The polycomb group protein EED interacts with YY1, and both proteins induce neural tissue in Xenopus embryos". Mol. Cell. Biol. 21 (4): 1360–9. doi:10.1128/MCB.21.4.1360-1369.2001. PMC 99588 . PMID 11158321.
Kuzmichev A, Nishioka K, Erdjument-Bromage H, Tempst P, Reinberg D (2002). "Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein". Genes Dev. 16 (22): 2893–905. doi:10.1101/gad.1035902. PMC 187479 . PMID 12435631.
Jin Q, van Eynde A, Beullens M, Roy N, Thiel G, Stalmans W, Bollen M (2003). "The protein phosphatase-1 (PP1) regulator, nuclear inhibitor of PP1 (NIPP1), interacts with the polycomb group protein, embryonic ectoderm development (EED), and functions as a transcriptional repressor". J. Biol. Chem. 278 (33): 30677–85. doi: 10.1074/jbc.M302273200 . PMID 12788942.
Enünlü I, Pápai G, Cserpán I, Udvardy A, Jeang KT, Boros I (2003). "Different isoforms of PRIP-interacting protein with methyltransferase domain/trimethylguanosine synthase localizes to the cytoplasm and nucleus". Biochem. Biophys. Res. Commun. 309 (1): 44–51. doi:10.1016/S0006-291X(03)01514-6. PMID 12943661.
Violot S, Hong SS, Rakotobe D, Petit C, Gay B, Moreau K, Billaud G, Priet S, Sire J, Schwartz O, Mouscadet JF, Boulanger P (2003). "The human polycomb group EED protein interacts with the integrase of human immunodeficiency virus type 1". J. Virol. 77 (23): 12507–22. doi:10.1128/JVI.77.23.12507-12522.2003. PMC 262565 . PMID 14610174.
Witte V, Laffert B, Rosorius O, Lischka P, Blume K, Galler G, Stilper A, Willbold D, D'Aloja P, Sixt M, Kolanus J, Ott M, Kolanus W, Schuler G, Baur AS (2004). "HIV-1 Nef mimics an integrin receptor signal that recruits the polycomb group protein Eed to the plasma membrane". Mol. Cell. 13 (2): 179–90. doi:10.1016/S1097-2765(04)00004-8. PMID 14759364.
Cao R, Zhang Y (2004). "SUZ12 is required for both the histone methyltransferase activity and the silencing function of the EED-EZH2 complex". Mol. Cell. 15 (1): 57–67. doi:10.1016/j.molcel.2004.06.020. PMID 15225548.
Pasini D, Bracken AP, Jensen MR, Lazzerini Denchi E, Helin K (2004). "Suz12 is essential for mouse development and for EZH2 histone methyltransferase activity". EMBO J. 23 (20): 4061–71. doi:10.1038/sj.emboj.7600402. PMC 524339 . PMID 15385962.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000074266 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000030619 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid9765275-5] 1 2 Rietzler M, Bittner M, Kolanus W, Schuster A, Holzmann B (Nov 1998). "The human WD repeat protein WAIT-1 specifically interacts with the cytoplasmic tails of beta7-integrins". J. Biol. Chem. 273 (42): 27459–66. doi: 10.1074/jbc.273.42.27459 . PMID 9765275.

[pmid9806832-6] Schumacher A, Lichtarge O, Schwartz S, Magnuson T (Jan 1999). "The murine Polycomb-group gene eed and its human orthologue: functional implications of evolutionary conservation". Genomics. 54 (1): 79–88. doi:10.1006/geno.1998.5509. PMID 9806832.

[entrez-7] 1 2 "Entrez Gene: EED embryonic ectoderm development".

[8] Cohen AS, Tuysuz B, Shen Y, Bhalla SK, Jones SJ, Gibson WT (Mar 2015). "A novel mutation in EED associated with overgrowth". Journal of Human Genetics. 60 (6): 339–342. doi: 10.1038/jhg.2015.26 . PMID 25787343. S2CID 22055237.

[pmid10581039-9] 1 2 3 van der Vlag J, Otte AP (Dec 1999). "Transcriptional repression mediated by the human polycomb-group protein EED involves histone deacetylation". Nat. Genet. 23 (4): 474–8. doi:10.1038/70602. PMID 10581039. S2CID 6748531.

[pmid9584197-10] van Lohuizen M, Tijms M, Voncken JW, Schumacher A, Magnuson T, Wientjens E (Jun 1998). "Interaction of mouse polycomb-group (Pc-G) proteins Enx1 and Enx2 with Eed: indication for separate Pc-G complexes". Mol. Cell. Biol. 18 (6): 3572–9. doi:10.1128/MCB.18.6.3572. PMC 108938 . PMID 9584197.

[pmid9742080-11] Denisenko O, Shnyreva M, Suzuki H, Bomsztyk K (Oct 1998). "Point mutations in the WD40 domain of Eed block its interaction with Ezh2". Mol. Cell. Biol. 18 (10): 5634–42. doi:10.1128/MCB.18.10.5634. PMC 109149 . PMID 9742080.

[pmid12788942-12] Jin Q, van Eynde A, Beullens M, Roy N, Thiel G, Stalmans W, Bollen M (Aug 2003). "The protein phosphatase-1 (PP1) regulator, nuclear inhibitor of PP1 (NIPP1), interacts with the polycomb group protein, embryonic ectoderm development (EED), and functions as a transcriptional repressor". J. Biol. Chem. 278 (33): 30677–85. doi: 10.1074/jbc.M302273200 . PMID 12788942.

[pmid12943661-13] Enünlü I, Pápai G, Cserpán I, Udvardy A, Jeang KT, Boros I (Sep 2003). "Different isoforms of PRIP-interacting protein with methyltransferase domain/trimethylguanosine synthase localizes to the cytoplasm and nucleus". Biochem. Biophys. Res. Commun. 309 (1): 44–51. doi:10.1016/s0006-291x(03)01514-6. PMID 12943661.

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