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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7AT8

Histone H3 recognition by nucleosome-bound PRC2 subunit EZH2.

Functional Information from GO Data
ChainGOidnamespacecontents
A0006338biological_processchromatin remodeling
A0042054molecular_functionhistone methyltransferase activity
A0046976molecular_functionhistone H3K27 methyltransferase activity
C0000122biological_processnegative regulation of transcription by RNA polymerase II
C0000978molecular_functionRNA polymerase II cis-regulatory region sequence-specific DNA binding
C0001222molecular_functiontranscription corepressor binding
C0001739cellular_componentsex chromatin
C0003682molecular_functionchromatin binding
C0003723molecular_functionRNA binding
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005677cellular_componentchromatin silencing complex
C0005730cellular_componentnucleolus
C0006325biological_processchromatin organization
C0006351biological_processDNA-templated transcription
C0008047molecular_functionenzyme activator activity
C0008270molecular_functionzinc ion binding
C0016586cellular_componentRSC-type complex
C0016604cellular_componentnuclear body
C0031490molecular_functionchromatin DNA binding
C0031507biological_processheterochromatin formation
C0031519cellular_componentPcG protein complex
C0032993cellular_componentprotein-DNA complex
C0035098cellular_componentESC/E(Z) complex
C0043565molecular_functionsequence-specific DNA binding
C0045596biological_processnegative regulation of cell differentiation
C0046872molecular_functionmetal ion binding
C0062072molecular_functionhistone H3K9me2/3 reader activity
C0106222molecular_functionlncRNA binding
C0140718biological_processfacultative heterochromatin formation
C1990841molecular_functionpromoter-specific chromatin binding
C1990904cellular_componentribonucleoprotein complex
D0000786cellular_componentnucleosome
D0003677molecular_functionDNA binding
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005694cellular_componentchromosome
D0030527molecular_functionstructural constituent of chromatin
D0031492molecular_functionnucleosomal DNA binding
D0031507biological_processheterochromatin formation
D0046982molecular_functionprotein heterodimerization activity
E0000786cellular_componentnucleosome
E0003677molecular_functionDNA binding
E0005515molecular_functionprotein binding
E0005634cellular_componentnucleus
E0005694cellular_componentchromosome
E0006334biological_processnucleosome assembly
E0030527molecular_functionstructural constituent of chromatin
E0031507biological_processheterochromatin formation
E0046982molecular_functionprotein heterodimerization activity
F0000786cellular_componentnucleosome
F0003677molecular_functionDNA binding
F0005634cellular_componentnucleus
F0005694cellular_componentchromosome
F0030527molecular_functionstructural constituent of chromatin
F0031507biological_processheterochromatin formation
F0046982molecular_functionprotein heterodimerization activity
G0000786cellular_componentnucleosome
G0002227biological_processinnate immune response in mucosa
G0003677molecular_functionDNA binding
G0005515molecular_functionprotein binding
G0005615cellular_componentextracellular space
G0005634cellular_componentnucleus
G0005694cellular_componentchromosome
G0006325biological_processchromatin organization
G0019731biological_processantibacterial humoral response
G0030527molecular_functionstructural constituent of chromatin
G0031507biological_processheterochromatin formation
G0046982molecular_functionprotein heterodimerization activity
G0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
H0000786cellular_componentnucleosome
H0003677molecular_functionDNA binding
H0005515molecular_functionprotein binding
H0005634cellular_componentnucleus
H0005654cellular_componentnucleoplasm
H0005694cellular_componentchromosome
H0030527molecular_functionstructural constituent of chromatin
H0031492molecular_functionnucleosomal DNA binding
H0031507biological_processheterochromatin formation
H0046982molecular_functionprotein heterodimerization activity
I0000786cellular_componentnucleosome
I0003677molecular_functionDNA binding
I0005515molecular_functionprotein binding
I0005634cellular_componentnucleus
I0005694cellular_componentchromosome
I0006334biological_processnucleosome assembly
I0030527molecular_functionstructural constituent of chromatin
I0031507biological_processheterochromatin formation
I0046982molecular_functionprotein heterodimerization activity
J0000786cellular_componentnucleosome
J0003677molecular_functionDNA binding
J0005634cellular_componentnucleus
J0005694cellular_componentchromosome
J0030527molecular_functionstructural constituent of chromatin
J0031507biological_processheterochromatin formation
J0046982molecular_functionprotein heterodimerization activity
K0000786cellular_componentnucleosome
K0002227biological_processinnate immune response in mucosa
K0003677molecular_functionDNA binding
K0005515molecular_functionprotein binding
K0005615cellular_componentextracellular space
K0005634cellular_componentnucleus
K0005694cellular_componentchromosome
K0006325biological_processchromatin organization
K0019731biological_processantibacterial humoral response
K0030527molecular_functionstructural constituent of chromatin
K0031507biological_processheterochromatin formation
K0046982molecular_functionprotein heterodimerization activity
K0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
Functional Information from PROSITE/UniProt
site_idPS00028
Number of Residues22
DetailsZINC_FINGER_C2H2_1 Zinc finger C2H2 type domain signature. Cpw..CtlnCrklysllkHlklc.H
ChainResidueDetails
CCYS450-HIS471
site_idPS00046
Number of Residues7
DetailsHISTONE_H2A Histone H2A signature. AGLqFPV
ChainResidueDetails
FALA21-VAL27
site_idPS00047
Number of Residues5
DetailsHISTONE_H4 Histone H4 signature. GAKRH
ChainResidueDetails
EGLY14-HIS18
site_idPS00322
Number of Residues7
DetailsHISTONE_H3_1 Histone H3 signature 1. KAPRKQL
ChainResidueDetails
DLYS14-LEU20
site_idPS00357
Number of Residues23
DetailsHISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG
ChainResidueDetails
GARG89-GLY111
site_idPS00959
Number of Residues9
DetailsHISTONE_H3_2 Histone H3 signature 2. PFqRLVREI
ChainResidueDetails
DPRO66-ILE74
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues102
DetailsDomain: {"description":"CXC","evidences":[{"source":"PROSITE-ProRule","id":"PRU00970","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"16964243","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"17081983","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18220336","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues76
DetailsRegion: {"description":"VEFS-box"}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18220336","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues5
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Citrulline","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68431","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P84228","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P84243","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues2
DetailsModified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues2
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues4
DetailsModified residue: {"description":"N6-propionyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by PAK2","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues2
DetailsModified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues2
DetailsModified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine; alternate","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues4
DetailsModified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues2
DetailsModified residue: {"description":"N5-methylglutamine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues2
DetailsModified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI31
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI32
Number of Residues2
DetailsGlycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"source":"UniProtKB","id":"P62807","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI33
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P0C1H4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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