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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7KSO

Cryo-EM structure of PRC2:EZH1-AEBP2-JARID2

Functional Information from GO Data
ChainGOidnamespacecontents
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0000781cellular_componentchromosome, telomeric region
A0000792cellular_componentheterochromatin
A0003677molecular_functionDNA binding
A0003682molecular_functionchromatin binding
A0003714molecular_functiontranscription corepressor activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0006325biological_processchromatin organization
A0006338biological_processchromatin remodeling
A0006351biological_processDNA-templated transcription
A0008168molecular_functionmethyltransferase activity
A0009653biological_processanatomical structure morphogenesis
A0016279molecular_functionprotein-lysine N-methyltransferase activity
A0016740molecular_functiontransferase activity
A0021766biological_processhippocampus development
A0031491molecular_functionnucleosome binding
A0031507biological_processheterochromatin formation
A0031509biological_processsubtelomeric heterochromatin formation
A0032259biological_processmethylation
A0035098cellular_componentESC/E(Z) complex
A0042054molecular_functionhistone methyltransferase activity
A0042393molecular_functionhistone binding
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0046976molecular_functionhistone H3K27 methyltransferase activity
A0140693molecular_functionmolecular condensate scaffold activity
A0140951molecular_functionhistone H3K27 trimethyltransferase activity
B0000122biological_processnegative regulation of transcription by RNA polymerase II
B0001222molecular_functiontranscription corepressor binding
B0001739cellular_componentsex chromatin
B0003682molecular_functionchromatin binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005677cellular_componentchromatin silencing complex
B0005694cellular_componentchromosome
B0006325biological_processchromatin organization
B0006351biological_processDNA-templated transcription
B0008047molecular_functionenzyme activator activity
B0021510biological_processspinal cord development
B0031491molecular_functionnucleosome binding
B0031507biological_processheterochromatin formation
B0035098cellular_componentESC/E(Z) complex
B0042802molecular_functionidentical protein binding
B0045120cellular_componentpronucleus
B0045892biological_processnegative regulation of DNA-templated transcription
B0140718biological_processfacultative heterochromatin formation
B1990841molecular_functionpromoter-specific chromatin binding
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
D0000118cellular_componenthistone deacetylase complex
D0000122biological_processnegative regulation of transcription by RNA polymerase II
D0000781cellular_componentchromosome, telomeric region
D0000785cellular_componentchromatin
D0000978molecular_functionRNA polymerase II cis-regulatory region sequence-specific DNA binding
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0006260biological_processDNA replication
D0006281biological_processDNA repair
D0006325biological_processchromatin organization
D0006334biological_processnucleosome assembly
D0006335biological_processDNA replication-dependent chromatin assembly
D0006338biological_processchromatin remodeling
D0006351biological_processDNA-templated transcription
D0006355biological_processregulation of DNA-templated transcription
D0006974biological_processDNA damage response
D0007420biological_processbrain development
D0008094molecular_functionATP-dependent activity, acting on DNA
D0008285biological_processnegative regulation of cell population proliferation
D0016581cellular_componentNuRD complex
D0016589cellular_componentNURF complex
D0030336biological_processnegative regulation of cell migration
D0030512biological_processnegative regulation of transforming growth factor beta receptor signaling pathway
D0031492molecular_functionnucleosomal DNA binding
D0031507biological_processheterochromatin formation
D0032991cellular_componentprotein-containing complex
D0033186cellular_componentCAF-1 complex
D0035098cellular_componentESC/E(Z) complex
D0042393molecular_functionhistone binding
D0042659biological_processregulation of cell fate specification
D0042826molecular_functionhistone deacetylase binding
D0045892biological_processnegative regulation of DNA-templated transcription
D0045893biological_processpositive regulation of DNA-templated transcription
D0045944biological_processpositive regulation of transcription by RNA polymerase II
D0070822cellular_componentSin3-type complex
D1902455biological_processnegative regulation of stem cell population maintenance
D1902459biological_processpositive regulation of stem cell population maintenance
D2000736biological_processregulation of stem cell differentiation
F0000122biological_processnegative regulation of transcription by RNA polymerase II
F0000785cellular_componentchromatin
F0003677molecular_functionDNA binding
F0003682molecular_functionchromatin binding
F0005634cellular_componentnucleus
F0005654cellular_componentnucleoplasm
F0006325biological_processchromatin organization
F0006338biological_processchromatin remodeling
F0006351biological_processDNA-templated transcription
F0007417biological_processcentral nervous system development
F0010468biological_processregulation of gene expression
F0030154biological_processcell differentiation
F0031507biological_processheterochromatin formation
F0032452molecular_functionhistone demethylase activity
F0035097cellular_componenthistone methyltransferase complex
F0035098cellular_componentESC/E(Z) complex
F0043130molecular_functionubiquitin binding
F0046976molecular_functionhistone H3K27 methyltransferase activity
F0048731biological_processsystem development
F0048863biological_processstem cell differentiation
F0061649molecular_functionubiquitin-modified histone reader activity
F0140718biological_processfacultative heterochromatin formation
F1990904cellular_componentribonucleoprotein complex
Functional Information from PROSITE/UniProt
site_idPS00028
Number of Residues24
DetailsZINC_FINGER_C2H2_1 Zinc finger C2H2 type domain signature. CcwdqCqacFnsspdladHirsi.H
ChainResidueDetails
ECYS263-HIS286
ECYS330-HIS352
CCYS450-HIS471
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LLSAsdDhTICLWDI
ChainResidueDetails
DLEU193-ILE207
DLEU289-LEU303
DLEU333-LEU347
BLEU206-ILE220
site_idPS00729
Number of Residues9
DetailsAP_NUCLEASE_F2_1 AP endonucleases family 2 signature 1. HGtYFNNFC
ChainResidueDetails
AHIS446-CYS454
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues43
DetailsRepeat: {"description":"WD 1"}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues43
DetailsRepeat: {"description":"WD 2"}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues40
DetailsRepeat: {"description":"WD 3"}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues41
DetailsRepeat: {"description":"WD 4"}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues37
DetailsRepeat: {"description":"WD 5"}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues40
DetailsRepeat: {"description":"WD 6"}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues154
DetailsRegion: {"description":"Required for interaction with the matrix protein MA of HIV-1"}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues3
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"20974918","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues23
DetailsZinc finger: {"description":"C2H2-type"}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues27
DetailsRegion: {"description":"Interaction with JARID2 and EPOP","evidences":[{"source":"PubMed","id":"29499137","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues76
DetailsRegion: {"description":"VEFS-box"}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsSite: {"description":"Breakpoint for translocation to form JAZF1-SUZ12 oncogene"}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18220336","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues49
DetailsRepeat: {"description":"WD 2","evidences":[{"source":"PubMed","id":"39460621","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8TX8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues47
DetailsRepeat: {"description":"WD 3","evidences":[{"source":"PubMed","id":"39460621","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8TX8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues45
DetailsRepeat: {"description":"WD 4","evidences":[{"source":"PubMed","id":"39460621","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8TX8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues43
DetailsRepeat: {"description":"WD 5","evidences":[{"source":"PubMed","id":"39460621","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8TX8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues56
DetailsRepeat: {"description":"WD 6","evidences":[{"source":"PubMed","id":"39460621","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8TX8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues32
DetailsRepeat: {"description":"WD 7","evidences":[{"source":"PubMed","id":"39460621","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8TX8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q60972","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"25755297","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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