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O75530

- EED_HUMAN

UniProt

O75530 - EED_HUMAN

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Protein
Polycomb protein EED
Gene
EED
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Polycomb group (PcG) protein. Component of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' and 'Lys-27' of histone H3, leading to transcriptional repression of the affected target gene. Also recognizes 'Lys-26' trimethylated histone H1 with the effect of inhibiting PRC2 complex methyltransferase activity on nucleosomal histone H3 'Lys-27', whereas H3 'Lys-27' recognition has the opposite effect, enabling the propagation of this repressive mark. The PRC2/EED-EZH2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems. Genes repressed by the PRC2/EED-EZH2 complex include HOXC8, HOXA9, MYT1 and CDKN2A.9 Publications

GO - Molecular functioni

  1. chromatin binding Source: Ensembl
  2. histone methyltransferase activity Source: MGI
  3. identical protein binding Source: IntAct
  4. protein binding Source: UniProtKB

GO - Biological processi

  1. negative regulation of transcription, DNA-templated Source: UniProtKB
  2. positive regulation of histone H3-K27 methylation Source: Ensembl
  3. regulation of gene expression by genetic imprinting Source: Ensembl
  4. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_169436. Oxidative Stress Induced Senescence.
REACT_200808. PRC2 methylates histones and DNA.
SignaLinkiO75530.

Names & Taxonomyi

Protein namesi
Recommended name:
Polycomb protein EED
Short name:
hEED
Alternative name(s):
WD protein associating with integrin cytoplasmic tails 1
Short name:
WAIT-1
Gene namesi
Name:EED
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:3188. EED.

Subcellular locationi

Nucleus. Chromosome
Note: Transiently colocalizes with XIST at inactive X chromosomes.5 Publications

GO - Cellular componenti

  1. ESC/E(Z) complex Source: UniProtKB
  2. cytoplasm Source: HPA
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProtKB
  5. pronucleus Source: Ensembl
  6. sex chromatin Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi97 – 971F → A: Abolishes binding to H3K27me3. 2 Publications
Mutagenesisi148 – 1481Y → A: Abolishes binding to H3K27me3. 2 Publications
Mutagenesisi193 – 1931I → N: Impairs interaction with EZH2. 2 Publications
Mutagenesisi196 – 1961L → P: Impairs interaction with EZH2. 2 Publications
Mutagenesisi300 – 3012ST → AA: Impairs interaction with the matrix protein MA of HIV-1. 1 Publication
Mutagenesisi305 – 3084HRNY → AAAA: Impairs interaction with the matrix protein MA of HIV-1. 1 Publication
Mutagenesisi364 – 3641W → A: Abolishes binding to H3K27me3. 2 Publications
Mutagenesisi364 – 3641W → L: Abolishes binding to H3K27me3. 2 Publications
Mutagenesisi365 – 3651Y → A: Abolishes binding to H3K27me3. 2 Publications

Organism-specific databases

PharmGKBiPA27624.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 441440Polycomb protein EED
PRO_0000343725Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei55 – 551Phosphothreonine1 Publication
Modified residuei66 – 661N6,N6,N6-trimethyllysine; alternate1 Publication
Modified residuei66 – 661N6,N6-dimethyllysine; alternate1 Publication
Modified residuei66 – 661N6-methyllysine; alternate1 Publication
Modified residuei197 – 1971N6,N6,N6-trimethyllysine; alternate1 Publication
Modified residuei197 – 1971N6,N6-dimethyllysine; alternate1 Publication
Modified residuei197 – 1971N6-methyllysine; alternate1 Publication
Modified residuei268 – 2681N6,N6,N6-trimethyllysine; alternate1 Publication
Modified residuei268 – 2681N6,N6-dimethyllysine; alternate1 Publication
Modified residuei268 – 2681N6-methyllysine; alternate1 Publication
Modified residuei284 – 2841N6,N6,N6-trimethyllysine; alternate1 Publication
Modified residuei284 – 2841N6,N6-dimethyllysine; alternate1 Publication
Modified residuei284 – 2841N6-methyllysine; alternate1 Publication

Post-translational modificationi

Methylated. Binding to histone H1 'Lys-26' promotes mono-, di-, and trimethylation of internal lysines.2 Publications

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

MaxQBiO75530.
PaxDbiO75530.
PRIDEiO75530.

PTM databases

PhosphoSiteiO75530.

Expressioni

Tissue specificityi

Expressed in brain, colon, heart, kidney, liver, lung, muscle, ovary, peripheral blood leukocytes, pancreas, placenta, prostate, spleen, small intestine, testis, thymus and uterus. Appears to be overexpressed in breast and colon cancer.5 Publications

Developmental stagei

Expression peaks at the G1/S phase boundary.1 Publication

Inductioni

Expression is induced by E2F1, E2F2 and E2F3.1 Publication

Gene expression databases

ArrayExpressiO75530.
BgeeiO75530.
CleanExiHS_EED.
GenevestigatoriO75530.

Organism-specific databases

HPAiCAB012211.
HPA046731.

Interactioni

Subunit structurei

Interacts with KMT2A/MLL1 By similarity. Component of the PRC2/EED-EZH2 complex, which includes EED, EZH2, SUZ12, RBBP4 and RBBP7 and possibly AEBP2. The minimum components required for methyltransferase activity of the PRC2/EED-EZH2 complex are EED, EZH2 and SUZ12. Component of the PRC2/EED-EZH1 complex, which includes EED, EZH1, SUZ12, RBBP4 and AEBP2. The PRC2 complex may also interact with DNMT1, DNMT3A, DNMT3B and PHF1 via the EZH2 subunit and with SIRT1 via the SUZ12 subunit. Interacts with HDAC, HDAC2, histone H1 and YY1. May interact with ITGA4, ITGAE and ITGB7. Interacts with CDYL. May interact with the MA protein of HIV-1. Interacts with ARNTL/BMAL1.14 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-923794,EBI-923794
ASXL1Q8IXJ95EBI-923794,EBI-1646500
DDB1Q165314EBI-923794,EBI-350322
DNMT1P263583EBI-923794,EBI-719459
DNMT3AQ9Y6K12EBI-923794,EBI-923653
DNMT3BQ9UBC34EBI-923794,EBI-80125
EZH2Q159107EBI-923794,EBI-530054
PINK1Q9BXM76EBI-923794,EBI-2846068
PML-RARQ151562EBI-923794,EBI-867256

Protein-protein interaction databases

BioGridi114265. 460 interactions.
DIPiDIP-36673N.
IntActiO75530. 35 interactions.
MINTiMINT-6630924.
STRINGi9606.ENSP00000263360.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi83 – 897
Beta strandi96 – 1016
Beta strandi111 – 1177
Beta strandi120 – 1267
Helixi128 – 1303
Beta strandi132 – 1398
Beta strandi147 – 1548
Turni156 – 1583
Beta strandi161 – 1677
Beta strandi171 – 1755
Turni177 – 1793
Beta strandi182 – 1887
Beta strandi193 – 1986
Beta strandi205 – 2106
Beta strandi215 – 2195
Turni220 – 2234
Beta strandi224 – 2296
Beta strandi231 – 2344
Beta strandi239 – 2446
Beta strandi248 – 2558
Beta strandi260 – 2656
Helixi268 – 27811
Helixi282 – 2843
Beta strandi292 – 2943
Beta strandi298 – 3014
Beta strandi311 – 3155
Beta strandi318 – 3225
Beta strandi324 – 33512
Helixi340 – 3423
Beta strandi350 – 3578
Beta strandi374 – 3807
Beta strandi386 – 3905
Beta strandi393 – 3953
Helixi396 – 3983
Beta strandi400 – 4045
Beta strandi413 – 4186
Beta strandi422 – 4298
Beta strandi432 – 4387

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IIWX-ray1.80A77-441[»]
3IIYX-ray2.65A77-441[»]
3IJ0X-ray2.45A77-441[»]
3IJ1X-ray2.10A77-441[»]
3IJCX-ray1.95A77-441[»]
3JPXX-ray2.05A40-441[»]
3JZGX-ray2.10A40-441[»]
3JZHX-ray2.05A40-441[»]
3JZNX-ray2.60A76-441[»]
3K26X-ray1.58A76-441[»]
3K27X-ray1.76A76-441[»]
ProteinModelPortaliO75530.
SMRiO75530. Positions 80-439.

Miscellaneous databases

EvolutionaryTraceiO75530.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati91 – 13444WD 1
Add
BLAST
Repeati142 – 18544WD 2
Add
BLAST
Repeati188 – 22841WD 3
Add
BLAST
Repeati234 – 27542WD 4
Add
BLAST
Repeati304 – 34138WD 5
Add
BLAST
Repeati359 – 39941WD 6
Add
BLAST
Repeati408 – 44134WD 7
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni81 – 441361Interaction with EZH2 By similarity
Add
BLAST
Regioni149 – 303155Required for interaction with the matrix protein MA of HIV-1
Add
BLAST
Regioni301 – 441141Required for interaction with the matrix protein MA of HIV-1
Add
BLAST

Domaini

The WD repeat domain mediates recognition of trimethylated histone peptides at the consensus sequence Ala-Arg-Lys-Ser. This is achieved through an aromatic cage encircling the methyllysine, and involving Phe-97, Tyr-148 and Tyr-365.1 Publication

Sequence similaritiesi

Belongs to the WD repeat ESC family.
Contains 7 WD repeats.

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiCOG2319.
HOVERGENiHBG052708.
KOiK11462.
OMAiCTTLTHP.
OrthoDBiEOG7WQ7S8.
PhylomeDBiO75530.
TreeFamiTF314451.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 2 hits.
[Graphical view]
SMARTiSM00320. WD40. 6 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 2 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing and alternative initiation. Align

Note: Additional isoforms may be produced by alternative initiation, both from non-canonical start codons upstream of the initiator methionine displayed and from other canonical start codons downstream of that displayed (PubMed:15099518 and PubMed:15684044). The precise sites of translation initiation have not been unambiguously identified.

Isoform 1 (identifier: O75530-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MSEREVSTAP AGTDMPAAKK QKLSSDENSN PDLSGDENDD AVSIESGTNT    50
ERPDTPTNTP NAPGRKSWGK GKWKSKKCKY SFKCVNSLKE DHNQPLFGVQ 100
FNWHSKEGDP LVFATVGSNR VTLYECHSQG EIRLLQSYVD ADADENFYTC 150
AWTYDSNTSH PLLAVAGSRG IIRIINPITM QCIKHYVGHG NAINELKFHP 200
RDPNLLLSVS KDHALRLWNI QTDTLVAIFG GVEGHRDEVL SADYDLLGEK 250
IMSCGMDHSL KLWRINSKRM MNAIKESYDY NPNKTNRPFI SQKIHFPDFS 300
TRDIHRNYVD CVRWLGDLIL SKSCENAIVC WKPGKMEDDI DKIKPSESNV 350
TILGRFDYSQ CDIWYMRFSM DFWQKMLALG NQVGKLYVWD LEVEDPHKAK 400
CTTLTHHKCG AAIRQTSFSR DSSILIAVCD DASIWRWDRL R 441
Length:441
Mass (Da):50,198
Last modified:July 22, 2008 - v2
Checksum:iD2E0A5BA27C0499A
GO
Isoform 2 (identifier: O75530-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     322-322: K → KSGRAILHSHQQCMRDPVSPNLRQHL

Show »
Length:466
Mass (Da):53,061
Checksum:i614B2E31B2A9D41F
GO
Isoform 3 (identifier: O75530-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     401-441: Missing.

Show »
Length:400
Mass (Da):45,524
Checksum:i45DD879776FF83D5
GO

Sequence cautioni

The sequence AAC23685.1 differs from that shown. Reason: Erroneous initiation.
The sequence AAC68675.1 differs from that shown. Reason: Erroneous initiation.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei322 – 3221K → KSGRAILHSHQQCMRDPVSP NLRQHL in isoform 2.
VSP_034691
Alternative sequencei401 – 44141Missing in isoform 3.
VSP_034692Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321D → E in AAC68675. 1 Publication
Sequence conflicti74 – 741K → S in AAD08714. 1 Publication
Sequence conflicti74 – 741K → S in AAD08815. 1 Publication
Sequence conflicti337 – 3371E → K in AAD08714. 1 Publication
Sequence conflicti337 – 3371E → K in AAD08815. 1 Publication
Sequence conflicti417 – 4171S → G in BAF84809. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF080227 mRNA. Translation: AAC95144.1.
AF070418 mRNA. Translation: AAC23685.1. Different initiation.
U90651 mRNA. Translation: AAD08714.1.
AF099032 mRNA. Translation: AAD08815.1.
AK292120 mRNA. Translation: BAF84809.1.
AP003084 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW75129.1.
CH471076 Genomic DNA. Translation: EAW75130.1.
BC047672 mRNA. Translation: AAH47672.1.
BC068995 mRNA. Translation: AAH68995.1.
AF078933 mRNA. Translation: AAC68675.1. Different initiation.
CCDSiCCDS8273.1. [O75530-1]
CCDS8274.1. [O75530-3]
RefSeqiNP_003788.2. NM_003797.3. [O75530-1]
NP_694536.1. NM_152991.2. [O75530-3]
UniGeneiHs.503510.

Genome annotation databases

EnsembliENST00000263360; ENSP00000263360; ENSG00000074266. [O75530-1]
ENST00000327320; ENSP00000315587; ENSG00000074266. [O75530-3]
ENST00000351625; ENSP00000338186; ENSG00000074266. [O75530-2]
GeneIDi8726.
KEGGihsa:8726.
UCSCiuc001pbp.3. human. [O75530-1]
uc001pbr.3. human. [O75530-2]

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF080227 mRNA. Translation: AAC95144.1 .
AF070418 mRNA. Translation: AAC23685.1 . Different initiation.
U90651 mRNA. Translation: AAD08714.1 .
AF099032 mRNA. Translation: AAD08815.1 .
AK292120 mRNA. Translation: BAF84809.1 .
AP003084 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW75129.1 .
CH471076 Genomic DNA. Translation: EAW75130.1 .
BC047672 mRNA. Translation: AAH47672.1 .
BC068995 mRNA. Translation: AAH68995.1 .
AF078933 mRNA. Translation: AAC68675.1 . Different initiation.
CCDSi CCDS8273.1. [O75530-1 ]
CCDS8274.1. [O75530-3 ]
RefSeqi NP_003788.2. NM_003797.3. [O75530-1 ]
NP_694536.1. NM_152991.2. [O75530-3 ]
UniGenei Hs.503510.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3IIW X-ray 1.80 A 77-441 [» ]
3IIY X-ray 2.65 A 77-441 [» ]
3IJ0 X-ray 2.45 A 77-441 [» ]
3IJ1 X-ray 2.10 A 77-441 [» ]
3IJC X-ray 1.95 A 77-441 [» ]
3JPX X-ray 2.05 A 40-441 [» ]
3JZG X-ray 2.10 A 40-441 [» ]
3JZH X-ray 2.05 A 40-441 [» ]
3JZN X-ray 2.60 A 76-441 [» ]
3K26 X-ray 1.58 A 76-441 [» ]
3K27 X-ray 1.76 A 76-441 [» ]
ProteinModelPortali O75530.
SMRi O75530. Positions 80-439.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114265. 460 interactions.
DIPi DIP-36673N.
IntActi O75530. 35 interactions.
MINTi MINT-6630924.
STRINGi 9606.ENSP00000263360.

PTM databases

PhosphoSitei O75530.

Proteomic databases

MaxQBi O75530.
PaxDbi O75530.
PRIDEi O75530.

Protocols and materials databases

DNASUi 8726.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000263360 ; ENSP00000263360 ; ENSG00000074266 . [O75530-1 ]
ENST00000327320 ; ENSP00000315587 ; ENSG00000074266 . [O75530-3 ]
ENST00000351625 ; ENSP00000338186 ; ENSG00000074266 . [O75530-2 ]
GeneIDi 8726.
KEGGi hsa:8726.
UCSCi uc001pbp.3. human. [O75530-1 ]
uc001pbr.3. human. [O75530-2 ]

Organism-specific databases

CTDi 8726.
GeneCardsi GC11P085955.
HGNCi HGNC:3188. EED.
HPAi CAB012211.
HPA046731.
MIMi 605984. gene.
neXtProti NX_O75530.
PharmGKBi PA27624.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2319.
HOVERGENi HBG052708.
KOi K11462.
OMAi CTTLTHP.
OrthoDBi EOG7WQ7S8.
PhylomeDBi O75530.
TreeFami TF314451.

Enzyme and pathway databases

Reactomei REACT_169436. Oxidative Stress Induced Senescence.
REACT_200808. PRC2 methylates histones and DNA.
SignaLinki O75530.

Miscellaneous databases

ChiTaRSi EED. human.
EvolutionaryTracei O75530.
GeneWikii EED.
GenomeRNAii 8726.
NextBioi 32733.
PROi O75530.
SOURCEi Search...

Gene expression databases

ArrayExpressi O75530.
Bgeei O75530.
CleanExi HS_EED.
Genevestigatori O75530.

Family and domain databases

Gene3Di 2.130.10.10. 1 hit.
InterProi IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view ]
Pfami PF00400. WD40. 2 hits.
[Graphical view ]
SMARTi SM00320. WD40. 6 hits.
[Graphical view ]
SUPFAMi SSF50978. SSF50978. 1 hit.
PROSITEi PS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 2 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The murine Polycomb-group gene eed and its human orthologue: functional implications of evolutionary conservation."
    Schumacher A., Lichtarge O., Schwartz S., Magnuson T.
    Genomics 54:79-88(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: Brain.
  2. "Characterization of interactions between the mammalian polycomb-group proteins Enx1/EZH2 and EED suggests the existence of different mammalian polycomb-group protein complexes."
    Sewalt R.G.A.B., van der Vlag J., Gunster M.J., Hamer K.M., den Blaauwen J.L., Satijn D.P.E., Hendrix T., van Driel R., Otte A.P.
    Mol. Cell. Biol. 18:3586-3595(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH EZH2, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF ILE-193 AND LEU-196, PUTATIVE ALTERNATIVE INITIATION.
  3. "HEED, the product of the human homolog of the murine eed gene, binds to the matrix protein of HIV-1."
    Peytavi R., Hong S.S., Gay B., d'Angeac A.D., Selig L., Benichou S., Benarous R., Boulanger P.
    J. Biol. Chem. 274:1635-1645(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), INTERACTION WITH THE HIV-1 MA PROTEIN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF 300-SER-THR-301 AND 305-HIS-TYR-308.
    Tissue: Spleen.
  4. "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.
    , 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 1).
    Tissue: Synovium.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. 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 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-441 (ISOFORM 1).
    Tissue: Eye and Lung.
  8. "The human WD repeat protein WAIT-1 specifically interacts with the cytoplasmic tails of beta7-integrins."
    Rietzler M., Bittner M., Kolanus W., Schuster A., Holzmann B.
    J. Biol. Chem. 273:27459-27466(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-441 (ISOFORM 1), INTERACTION WITH ITGA4; ITGAE AND ITGB7, TISSUE SPECIFICITY.
  9. "Transcriptional repression mediated by the human polycomb-group protein EED involves histone deacetylation."
    van der Vlag J., Otte A.P.
    Nat. Genet. 23:474-478(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EZH2; HDAC1 AND HDAC2.
  10. "The polycomb group protein EED interacts with YY1, and both proteins induce neural tissue in Xenopus embryos."
    Satijn D.P.E., Hamer K.M., den Blaauwen J., Otte A.P.
    Mol. Cell. Biol. 21:1360-1369(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EZH2 AND YY1.
  11. "Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein."
    Kuzmichev A., Nishioka K., Erdjument-Bromage H., Tempst P., Reinberg D.
    Genes Dev. 16:2893-2905(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE PRC2 COMPLEX WITH EZH2; RBBP4; RBBP7 AND SUZ12, METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX.
  12. "Selective interactions between vertebrate polycomb homologs and the SUV39H1 histone lysine methyltransferase suggest that histone H3-K9 methylation contributes to chromosomal targeting of Polycomb group proteins."
    Sewalt R.G.A.B., Lachner M., Vargas M., Hamer K.M., den Blaauwen J.L., Hendrix T., Melcher M., Schweizer D., Jenuwein T., Otte A.P.
    Mol. Cell. Biol. 22:5539-5553(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  13. "Role of histone H3 lysine 27 methylation in Polycomb-group silencing."
    Cao R., Wang L., Wang H., Xia L., Erdjument-Bromage H., Tempst P., Jones R.S., Zhang Y.
    Science 298:1039-1043(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE PRC2 COMPLEX WITH EZH2; RBBP4; RBBP7 AND SUZ12, METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX.
  14. "EZH2 is downstream of the pRB-E2F pathway, essential for proliferation and amplified in cancer."
    Bracken A.P., Pasini D., Capra M., Prosperini E., Colli E., Helin K.
    EMBO J. 22:5323-5335(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DEVELOPMENTAL STAGE, INDUCTION.
  15. Cited for: SUBCELLULAR LOCATION.
  16. "Suz12 is essential for mouse development and for EZH2 histone methyltransferase activity."
    Pasini D., Bracken A.P., Jensen M.R., Lazzerini Denchi E., Helin K.
    EMBO J. 23:4061-4071(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EZH2, METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX.
  17. "Silencing of human polycomb target genes is associated with methylation of histone H3 Lys 27."
    Kirmizis A., Bartley S.M., Kuzmichev A., Margueron R., Reinberg D., Green R., Farnham P.J.
    Genes Dev. 18:1592-1605(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  18. "Different EZH2-containing complexes target methylation of histone H1 or nucleosomal histone H3."
    Kuzmichev A., Jenuwein T., Tempst P., Reinberg D.
    Mol. Cell 14:183-193(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF THE PRC2 AND PRC3 COMPLEXES INCLUDING EED; EZH2; RBBP4; RBBP7 AND SUZ12, METHYLTRANSFERASE ACTIVITY OF THE PRC2 AND PRC3 COMPLEXES, PUTATIVE ALTERNATIVE INITIATION.
  19. "SUZ12 is required for both the histone methyltransferase activity and the silencing function of the EED-EZH2 complex."
    Cao R., Zhang Y.
    Mol. Cell 15:57-67(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CHARACTERIZATION OF THE PRC2 COMPLEX INCLUDING AEBP2; EED; EZH2; RBBP4 AND SUZ12, METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX.
  20. "Composition and histone substrates of polycomb repressive group complexes change during cellular differentiation."
    Kuzmichev A., Margueron R., Vaquero A., Preissner T.S., Scher M., Kirmizis A., Ouyang X., Brockdorff N., Abate-Shen C., Farnham P.J., Reinberg D.
    Proc. Natl. Acad. Sci. U.S.A. 102:1859-1864(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF THE PRC4 COMPLEX INCLUDING EED; EZH2; RBBP4; RBBP7; SUZ12 AND SIRT1, METHYLTRANSFERASE ACTIVITY OF THE PRC4 COMPLEX, TISSUE SPECIFICITY.
  21. "Substrate preferences of the EZH2 histone methyltransferase complex."
    Martin C., Cao R., Zhang Y.
    J. Biol. Chem. 281:8365-8370(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX, INTERACTION WITH HISTONE H1.
  22. Cited for: FUNCTION, INTERACTION OF THE PRC2 COMPLEX WITH DNMT1; DNMT3A AND DNMT3B.
  23. "Polycomb-mediated methylation on Lys27 of histone H3 pre-marks genes for de novo methylation in cancer."
    Schlesinger Y., Straussman R., Keshet I., Farkash S., Hecht M., Zimmerman J., Eden E., Yakhini Z., Ben-Shushan E., Reubinoff B.E., Bergman Y., Simon I., Cedar H.
    Nat. Genet. 39:232-236(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: DE NOVO DNA METHYLATION OF PRC2 TARGET GENES.
  24. "Ezh1 and Ezh2 maintain repressive chromatin through different mechanisms."
    Margueron R., Li G., Sarma K., Blais A., Zavadil J., Woodcock C.L., Dynlacht B.D., Reinberg D.
    Mol. Cell 32:503-518(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE PRC2/EED-EZH1 COMPLEX.
  25. "Role of hPHF1 in H3K27 methylation and Hox gene silencing."
    Cao R., Wang H., He J., Erdjument-Bromage H., Tempst P., Zhang Y.
    Mol. Cell. Biol. 28:1862-1872(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION OF THE PRC2 COMPLEX WITH PHF1, METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX.
  26. "Ezh2 requires PHF1 to efficiently catalyze H3 lysine 27 trimethylation in vivo."
    Sarma K., Margueron R., Ivanov A., Pirrotta V., Reinberg D.
    Mol. Cell. Biol. 28:2718-2731(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH EZH2 AND SUZ12, INTERACTION OF THE PRC2 COMPLEX WITH PHF1, METHYLTRANSFERASE ACTIVITY OF THE PRC2 COMPLEX.
  27. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-55, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  28. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  29. "Corepressor protein CDYL functions as a molecular bridge between polycomb repressor complex 2 and repressive chromatin mark trimethylated histone lysine 27."
    Zhang Y., Yang X., Gui B., Xie G., Zhang D., Shang Y., Liang J.
    J. Biol. Chem. 286:42414-42425(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CDYL.
  30. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  31. "Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2)."
    Xu C., Bian C., Yang W., Galka M., Ouyang H., Chen C., Qiu W., Liu H., Jones A.E., MacKenzie F., Pan P., Li S.S., Wang H., Min J.
    Proc. Natl. Acad. Sci. U.S.A. 107:19266-19271(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 40-441 ALONE AND IN COMPLEX WITH METHYLATED HISTONE PEPTIDES, FUNCTION, DOMAIN WD REPEATS, METHYLATION AT LYS-66; LYS-197; LYS-268 AND LYS-284, MUTAGENESIS OF PHE-97; TYR-148; TRP-364 AND TYR-365.

Entry informationi

Entry nameiEED_HUMAN
AccessioniPrimary (citable) accession number: O75530
Secondary accession number(s): A8K7V5
, O00149, Q6NTH2, Q7LDA5, Q7LDG8, Q86VV2, Q9UNY7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: July 22, 2008
Last modified: September 3, 2014
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Caution

Two variants of the PRC2 complex have been described, termed PRC3 and PRC4. Each of the three complexes may include a different complement of EED isoforms, although the precise sequences of the isoforms in each complex have not been determined. The PRC2 and PRC4 complexes may also methylate 'Lys-26' of histone H1 in addition to 'Lys-27' of histone H3 (1 Publication and 1 Publication), although other studies have demonstrated no methylation of 'Lys-26' of histone H1 by PRC2 (1 Publication).

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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