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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8VMJ

H3K4me3 nucleosome bound to PRC2_AJ119-450

Functional Information from GO Data
ChainGOidnamespacecontents
I0000786cellular_componentnucleosome
I0003677molecular_functionDNA binding
I0005515molecular_functionprotein binding
I0005576cellular_componentextracellular region
I0005634cellular_componentnucleus
I0005654cellular_componentnucleoplasm
I0005694cellular_componentchromosome
I0006325biological_processchromatin organization
I0006334biological_processnucleosome assembly
I0030527molecular_functionstructural constituent of chromatin
I0031492molecular_functionnucleosomal DNA binding
I0031507biological_processheterochromatin formation
I0046982molecular_functionprotein heterodimerization activity
I0070062cellular_componentextracellular exosome
J0000781cellular_componentchromosome, telomeric region
J0000786cellular_componentnucleosome
J0003677molecular_functionDNA binding
J0003723molecular_functionRNA binding
J0005515molecular_functionprotein binding
J0005576cellular_componentextracellular region
J0005634cellular_componentnucleus
J0005654cellular_componentnucleoplasm
J0005694cellular_componentchromosome
J0006325biological_processchromatin organization
J0006334biological_processnucleosome assembly
J0016020cellular_componentmembrane
J0030527molecular_functionstructural constituent of chromatin
J0032200biological_processtelomere organization
J0032991cellular_componentprotein-containing complex
J0045653biological_processnegative regulation of megakaryocyte differentiation
J0046982molecular_functionprotein heterodimerization activity
J0061644biological_processprotein localization to CENP-A containing chromatin
J0070062cellular_componentextracellular exosome
K0000786cellular_componentnucleosome
K0003677molecular_functionDNA binding
K0030527molecular_functionstructural constituent of chromatin
K0046982molecular_functionprotein heterodimerization activity
M0000786cellular_componentnucleosome
M0003677molecular_functionDNA binding
M0030527molecular_functionstructural constituent of chromatin
M0046982molecular_functionprotein heterodimerization activity
O0000786cellular_componentnucleosome
O0003677molecular_functionDNA binding
O0005515molecular_functionprotein binding
O0005576cellular_componentextracellular region
O0005634cellular_componentnucleus
O0005654cellular_componentnucleoplasm
O0005694cellular_componentchromosome
O0006325biological_processchromatin organization
O0006334biological_processnucleosome assembly
O0030527molecular_functionstructural constituent of chromatin
O0031492molecular_functionnucleosomal DNA binding
O0031507biological_processheterochromatin formation
O0046982molecular_functionprotein heterodimerization activity
O0070062cellular_componentextracellular exosome
Q0000781cellular_componentchromosome, telomeric region
Q0000786cellular_componentnucleosome
Q0003677molecular_functionDNA binding
Q0003723molecular_functionRNA binding
Q0005515molecular_functionprotein binding
Q0005576cellular_componentextracellular region
Q0005634cellular_componentnucleus
Q0005654cellular_componentnucleoplasm
Q0005694cellular_componentchromosome
Q0006325biological_processchromatin organization
Q0006334biological_processnucleosome assembly
Q0016020cellular_componentmembrane
Q0030527molecular_functionstructural constituent of chromatin
Q0032200biological_processtelomere organization
Q0032991cellular_componentprotein-containing complex
Q0045653biological_processnegative regulation of megakaryocyte differentiation
Q0046982molecular_functionprotein heterodimerization activity
Q0061644biological_processprotein localization to CENP-A containing chromatin
Q0070062cellular_componentextracellular exosome
R0000786cellular_componentnucleosome
R0003677molecular_functionDNA binding
R0030527molecular_functionstructural constituent of chromatin
R0046982molecular_functionprotein heterodimerization activity
S0000786cellular_componentnucleosome
S0003677molecular_functionDNA binding
S0030527molecular_functionstructural constituent of chromatin
S0046982molecular_functionprotein heterodimerization activity
Functional Information from PROSITE/UniProt
site_idPS00046
Number of Residues7
DetailsHISTONE_H2A Histone H2A signature. AGLqFPV
ChainResidueDetails
KALA21-VAL27
site_idPS00047
Number of Residues5
DetailsHISTONE_H4 Histone H4 signature. GAKRH
ChainResidueDetails
JGLY14-HIS18
site_idPS00322
Number of Residues7
DetailsHISTONE_H3_1 Histone H3 signature 1. KAPRKQL
ChainResidueDetails
ILYS14-LEU20
site_idPS00357
Number of Residues23
DetailsHISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG
ChainResidueDetails
MARG89-GLY111
site_idPS00959
Number of Residues9
DetailsHISTONE_H3_2 Histone H3 signature 2. PFqRLVREI
ChainResidueDetails
IPRO66-ILE74
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"16185088","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16267050","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16627869","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17194708","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68431","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19783980","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues8
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"22389435","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20850016","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"16267050","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17194708","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"22389435","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29211711","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20850016","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P84243","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues4
DetailsModified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"PubMed","id":"31542297","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"22389435","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27436229","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues2
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"PubMed","id":"21076176","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues2
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"12086618","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15964846","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17967882","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27338793","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues3
DetailsModified residue: {"description":"N6-propionyllysine; alternate","evidences":[{"source":"PubMed","id":"17267393","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by PAK2","evidences":[{"source":"PubMed","id":"21724829","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17081983","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18669648","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"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62806","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P62806","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues6
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"PubMed","id":"19818714","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate","evidences":[{"source":"PubMed","id":"30886146","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues4
DetailsDNA binding: {}
ChainResidueDetails

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PDB entries from 2025-12-24

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