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Protein

Polycomb protein EED

Gene

EED

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

  • chromatin binding Source: Ensembl
  • histone methyltransferase activity Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

BioCyciZFISH:ENSG00000074266-MONOMER.
ReactomeiR-HSA-212300. PRC2 methylates histones and DNA.
R-HSA-2559580. Oxidative Stress Induced Senescence.
R-HSA-3214841. PKMTs methylate histone lysines.
R-HSA-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
SignaLinkiO75530.
SIGNORiO75530.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:3188. EED.

Subcellular locationi

GO - Cellular componenti

  • ESC/E(Z) complex Source: UniProtKB
  • nucleolus Source: HPA
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • pronucleus Source: Ensembl
  • sex chromatin Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi97F → A: Abolishes binding to H3K27me3. 1 Publication1
Mutagenesisi148Y → A: Abolishes binding to H3K27me3. 1 Publication1
Mutagenesisi193I → N: Impairs interaction with EZH2. 1 Publication1
Mutagenesisi196L → P: Impairs interaction with EZH2. 1 Publication1
Mutagenesisi300 – 301ST → AA: Impairs interaction with the matrix protein MA of HIV-1. 1 Publication2
Mutagenesisi305 – 308HRNY → AAAA: Impairs interaction with the matrix protein MA of HIV-1. 1 Publication4
Mutagenesisi364W → A: Abolishes binding to H3K27me3. 1 Publication1
Mutagenesisi364W → L: Abolishes binding to H3K27me3. 1 Publication1
Mutagenesisi365Y → A: Abolishes binding to H3K27me3. 1 Publication1

Organism-specific databases

DisGeNETi8726.
OpenTargetsiENSG00000074266.
PharmGKBiPA27624.

Chemistry databases

ChEMBLiCHEMBL2189117.

Polymorphism and mutation databases

BioMutaiEED.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00003437252 – 441Polycomb protein EEDAdd BLAST440

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1
Modified residuei2PhosphoserineCombined sources1
Modified residuei34PhosphoserineBy similarity1
Modified residuei55PhosphothreonineCombined sources1
Modified residuei66N6,N6,N6-trimethyllysine; alternate1 Publication1
Modified residuei66N6,N6-dimethyllysine; alternate1 Publication1
Modified residuei66N6-methyllysine; alternate1 Publication1
Modified residuei197N6,N6,N6-trimethyllysine; alternate1 Publication1
Modified residuei197N6,N6-dimethyllysine; alternate1 Publication1
Modified residuei197N6-methyllysine; alternate1 Publication1
Modified residuei268N6,N6,N6-trimethyllysine; alternate1 Publication1
Modified residuei268N6,N6-dimethyllysine; alternate1 Publication1
Modified residuei268N6-methyllysine; alternate1 Publication1
Modified residuei284N6,N6,N6-trimethyllysine; alternate1 Publication1
Modified residuei284N6,N6-dimethyllysine; alternate1 Publication1
Modified residuei284N6-methyllysine; alternate1 Publication1

Post-translational modificationi

Methylated. Binding to histone H1 'Lys-26' promotes mono-, di-, and trimethylation of internal lysines.1 Publication

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

EPDiO75530.
MaxQBiO75530.
PaxDbiO75530.
PeptideAtlasiO75530.
PRIDEiO75530.

PTM databases

iPTMnetiO75530.
PhosphoSitePlusiO75530.

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

BgeeiENSG00000074266.
CleanExiHS_EED.
ExpressionAtlasiO75530. baseline and differential.
GenevisibleiO75530. HS.

Organism-specific databases

HPAiCAB012211.
HPA060089.
HPA061140.

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.By similarity15 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
EZH2Q1591011EBI-923794,EBI-530054
PINK1Q9BXM76EBI-923794,EBI-2846068
PML-RARQ151562EBI-923794,EBI-867256

Protein-protein interaction databases

BioGridi114265. 480 interactors.
DIPiDIP-36673N.
IntActiO75530. 66 interactors.
MINTiMINT-6630924.
STRINGi9606.ENSP00000263360.

Chemistry databases

BindingDBiO75530.

Structurei

Secondary structure

1441
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi83 – 89Combined sources7
Beta strandi96 – 101Combined sources6
Beta strandi103 – 105Combined sources3
Beta strandi111 – 117Combined sources7
Beta strandi120 – 126Combined sources7
Helixi128 – 130Combined sources3
Beta strandi132 – 139Combined sources8
Beta strandi147 – 154Combined sources8
Turni156 – 158Combined sources3
Beta strandi161 – 167Combined sources7
Beta strandi171 – 175Combined sources5
Turni177 – 179Combined sources3
Beta strandi182 – 188Combined sources7
Beta strandi193 – 198Combined sources6
Beta strandi205 – 210Combined sources6
Beta strandi215 – 219Combined sources5
Turni220 – 223Combined sources4
Beta strandi224 – 229Combined sources6
Beta strandi231 – 234Combined sources4
Beta strandi239 – 244Combined sources6
Beta strandi248 – 255Combined sources8
Beta strandi260 – 265Combined sources6
Helixi268 – 278Combined sources11
Helixi282 – 284Combined sources3
Beta strandi292 – 294Combined sources3
Beta strandi298 – 301Combined sources4
Beta strandi311 – 315Combined sources5
Beta strandi318 – 322Combined sources5
Beta strandi324 – 335Combined sources12
Helixi340 – 342Combined sources3
Beta strandi350 – 357Combined sources8
Beta strandi363 – 365Combined sources3
Beta strandi368 – 370Combined sources3
Beta strandi374 – 380Combined sources7
Beta strandi386 – 390Combined sources5
Beta strandi393 – 395Combined sources3
Helixi396 – 398Combined sources3
Beta strandi400 – 404Combined sources5
Beta strandi413 – 418Combined sources6
Beta strandi422 – 429Combined sources8
Beta strandi432 – 438Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4X3EX-ray2.30A77-441[»]
5HYNX-ray2.95B/G/L/R77-441[»]
5IJ7X-ray2.62E/F81-441[»]
5IJ8X-ray2.99E/F81-441[»]
ProteinModelPortaliO75530.
SMRiO75530.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75530.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati91 – 134WD 1Add BLAST44
Repeati142 – 185WD 2Add BLAST44
Repeati188 – 228WD 3Add BLAST41
Repeati234 – 275WD 4Add BLAST42
Repeati304 – 341WD 5Add BLAST38
Repeati359 – 399WD 6Add BLAST41
Repeati408 – 441WD 7Add BLAST34

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni81 – 441Interaction with EZH2By similarityAdd BLAST361
Regioni149 – 303Required for interaction with the matrix protein MA of HIV-1Add BLAST155
Regioni301 – 441Required for interaction with the matrix protein MA of HIV-1Add BLAST141

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.Curated
Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG1034. Eukaryota.
ENOG410XRQI. LUCA.
GeneTreeiENSGT00510000047334.
HOVERGENiHBG052708.
InParanoidiO75530.
KOiK11462.
OMAiCTTLTHP.
OrthoDBiEOG091G082Z.
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. AlignAdd to basket

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

        10         20         30         40         50
MSEREVSTAP AGTDMPAAKK QKLSSDENSN PDLSGDENDD AVSIESGTNT
60 70 80 90 100
ERPDTPTNTP NAPGRKSWGK GKWKSKKCKY SFKCVNSLKE DHNQPLFGVQ
110 120 130 140 150
FNWHSKEGDP LVFATVGSNR VTLYECHSQG EIRLLQSYVD ADADENFYTC
160 170 180 190 200
AWTYDSNTSH PLLAVAGSRG IIRIINPITM QCIKHYVGHG NAINELKFHP
210 220 230 240 250
RDPNLLLSVS KDHALRLWNI QTDTLVAIFG GVEGHRDEVL SADYDLLGEK
260 270 280 290 300
IMSCGMDHSL KLWRINSKRM MNAIKESYDY NPNKTNRPFI SQKIHFPDFS
310 320 330 340 350
TRDIHRNYVD CVRWLGDLIL SKSCENAIVC WKPGKMEDDI DKIKPSESNV
360 370 380 390 400
TILGRFDYSQ CDIWYMRFSM DFWQKMLALG NQVGKLYVWD LEVEDPHKAK
410 420 430 440
CTTLTHHKCG AAIRQTSFSR DSSILIAVCD DASIWRWDRL R
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 differs from that shown. Reason: Erroneous initiation.Curated
The sequence AAC68675 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti32D → E in AAC68675 (PubMed:9765275).Curated1
Sequence conflicti74K → S in AAD08714 (PubMed:9880543).Curated1
Sequence conflicti74K → S in AAD08815 (PubMed:9880543).Curated1
Sequence conflicti337E → K in AAD08714 (PubMed:9880543).Curated1
Sequence conflicti337E → K in AAD08815 (PubMed:9880543).Curated1
Sequence conflicti417S → G in BAF84809 (PubMed:14702039).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_034691322K → KSGRAILHSHQQCMRDPVSP NLRQHL in isoform 2. 1 Publication1
Alternative sequenceiVSP_034692401 – 441Missing in isoform 3. 1 PublicationAdd BLAST41

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
CCDSiCCDS76463.1. [O75530-2]
CCDS8273.1. [O75530-1]
RefSeqiNP_001294936.1. NM_001308007.1. [O75530-2]
NP_003788.2. NM_003797.4. [O75530-1]
UniGeneiHs.503510.
Hs.528103.

Genome annotation databases

EnsembliENST00000263360; ENSP00000263360; ENSG00000074266. [O75530-1]
ENST00000327320; ENSP00000315587; ENSG00000074266. [O75530-3]
ENST00000351625; ENSP00000338186; ENSG00000074266. [O75530-2]
GeneIDi8726.
KEGGihsa:8726.
UCSCiuc001pbp.4. human. [O75530-1]

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
CCDSiCCDS76463.1. [O75530-2]
CCDS8273.1. [O75530-1]
RefSeqiNP_001294936.1. NM_001308007.1. [O75530-2]
NP_003788.2. NM_003797.4. [O75530-1]
UniGeneiHs.503510.
Hs.528103.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4X3EX-ray2.30A77-441[»]
5HYNX-ray2.95B/G/L/R77-441[»]
5IJ7X-ray2.62E/F81-441[»]
5IJ8X-ray2.99E/F81-441[»]
ProteinModelPortaliO75530.
SMRiO75530.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114265. 480 interactors.
DIPiDIP-36673N.
IntActiO75530. 66 interactors.
MINTiMINT-6630924.
STRINGi9606.ENSP00000263360.

Chemistry databases

BindingDBiO75530.
ChEMBLiCHEMBL2189117.

PTM databases

iPTMnetiO75530.
PhosphoSitePlusiO75530.

Polymorphism and mutation databases

BioMutaiEED.

Proteomic databases

EPDiO75530.
MaxQBiO75530.
PaxDbiO75530.
PeptideAtlasiO75530.
PRIDEiO75530.

Protocols and materials databases

DNASUi8726.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263360; ENSP00000263360; ENSG00000074266. [O75530-1]
ENST00000327320; ENSP00000315587; ENSG00000074266. [O75530-3]
ENST00000351625; ENSP00000338186; ENSG00000074266. [O75530-2]
GeneIDi8726.
KEGGihsa:8726.
UCSCiuc001pbp.4. human. [O75530-1]

Organism-specific databases

CTDi8726.
DisGeNETi8726.
GeneCardsiEED.
HGNCiHGNC:3188. EED.
HPAiCAB012211.
HPA060089.
HPA061140.
MIMi605984. gene.
neXtProtiNX_O75530.
OpenTargetsiENSG00000074266.
PharmGKBiPA27624.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1034. Eukaryota.
ENOG410XRQI. LUCA.
GeneTreeiENSGT00510000047334.
HOVERGENiHBG052708.
InParanoidiO75530.
KOiK11462.
OMAiCTTLTHP.
OrthoDBiEOG091G082Z.
PhylomeDBiO75530.
TreeFamiTF314451.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000074266-MONOMER.
ReactomeiR-HSA-212300. PRC2 methylates histones and DNA.
R-HSA-2559580. Oxidative Stress Induced Senescence.
R-HSA-3214841. PKMTs methylate histone lysines.
R-HSA-5617472. Activation of anterior HOX genes in hindbrain development during early embryogenesis.
SignaLinkiO75530.
SIGNORiO75530.

Miscellaneous databases

ChiTaRSiEED. human.
EvolutionaryTraceiO75530.
GeneWikiiEED.
GenomeRNAii8726.
PROiO75530.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000074266.
CleanExiHS_EED.
ExpressionAtlasiO75530. baseline and differential.
GenevisibleiO75530. HS.

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]
ProtoNetiSearch...

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: November 30, 2016
This is version 142 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 (PubMed:15099518 and PubMed:15684044), although other studies have demonstrated no methylation of 'Lys-26' of histone H1 by PRC2 (PubMed:16431907).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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.