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8VMJ

H3K4me3 nucleosome bound to PRC2_AJ119-450

Functional Information from GO Data
ChainGOidnamespacecontents
I0000122biological_processnegative regulation of transcription by RNA polymerase II
I0000785cellular_componentchromatin
I0000786cellular_componentnucleosome
I0003677molecular_functionDNA binding
I0003682molecular_functionchromatin binding
I0005515molecular_functionprotein binding
I0005576cellular_componentextracellular region
I0005634cellular_componentnucleus
I0005654cellular_componentnucleoplasm
I0005694cellular_componentchromosome
I0006325biological_processchromatin organization
I0006334biological_processnucleosome assembly
I0010467biological_processgene expression
I0030527molecular_functionstructural constituent of chromatin
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
J0043505cellular_componentCENP-A containing nucleosome
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
O0000122biological_processnegative regulation of transcription by RNA polymerase II
O0000785cellular_componentchromatin
O0000786cellular_componentnucleosome
O0003677molecular_functionDNA binding
O0003682molecular_functionchromatin binding
O0005515molecular_functionprotein binding
O0005576cellular_componentextracellular region
O0005634cellular_componentnucleus
O0005654cellular_componentnucleoplasm
O0005694cellular_componentchromosome
O0006325biological_processchromatin organization
O0006334biological_processnucleosome assembly
O0010467biological_processgene expression
O0030527molecular_functionstructural constituent of chromatin
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
Q0043505cellular_componentCENP-A containing nucleosome
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 Residues8
DetailsDNA_BIND:
ChainResidueDetails
JLYS16-LYS20
QLYS16-LYS20

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:17967882
ChainResidueDetails
JSER1
QSER1

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Symmetric dimethylarginine; by PRMT5 and PRMT7; alternate => ECO:0000250|UniProtKB:P62806
ChainResidueDetails
JARG3
QARG3
ILYS64
OM3L4
OLYS18
OLYS64

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732
ChainResidueDetails
JLYS5
QLYS5

site_idSWS_FT_FI5
Number of Residues6
DetailsMOD_RES: N6-propionyllysine; alternate => ECO:0000269|PubMed:17267393
ChainResidueDetails
JLYS8
JLYS16
JLYS44
QLYS8
QLYS16
QLYS44

site_idSWS_FT_FI6
Number of Residues8
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435
ChainResidueDetails
JLYS12
JLYS31
JLYS77
JLYS91
QLYS12
QLYS31
QLYS77
QLYS91

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:12086618, ECO:0000269|PubMed:15964846, ECO:0000269|PubMed:17967882, ECO:0000269|PubMed:27338793
ChainResidueDetails
JLYS20
QLYS20

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PAK2 => ECO:0000269|PubMed:21724829, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
JSER47
QSER47

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:20068231
ChainResidueDetails
JTYR51
QTYR51

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297
ChainResidueDetails
JLYS59
QLYS59
OLYS14
OLYS56

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62806
ChainResidueDetails
JLYS79
QLYS79

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P62806
ChainResidueDetails
JTHR80
QTHR80

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:24275569
ChainResidueDetails
JTYR88
QTYR88

site_idSWS_FT_FI14
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25218447
ChainResidueDetails
JLYS12
QLYS12
OLYS27
OLYS36

site_idSWS_FT_FI15
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:19818714
ChainResidueDetails
ISER28
JLYS91
QLYS91

site_idSWS_FT_FI16
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
ChainResidueDetails
JLYS20
JLYS59
JLYS79
QLYS20
QLYS59
QLYS79

site_idSWS_FT_FI17
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate => ECO:0000269|PubMed:30886146
ChainResidueDetails
JLYS31
QLYS31

site_idSWS_FT_FI18
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:20850016
ChainResidueDetails
ISER57
OSER57

site_idSWS_FT_FI19
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:29211711
ChainResidueDetails
ILYS79
OLYS79

site_idSWS_FT_FI20
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:20850016
ChainResidueDetails
ITHR80
OTHR80

site_idSWS_FT_FI21
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P84243
ChainResidueDetails
ISER86
OSER86

site_idSWS_FT_FI22
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332
ChainResidueDetails
ITHR107
OTHR107

site_idSWS_FT_FI23
Number of Residues2
DetailsMOD_RES: N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297
ChainResidueDetails
ILYS115
OLYS115

site_idSWS_FT_FI24
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:27436229
ChainResidueDetails
ILYS122
OLYS122

site_idSWS_FT_FI25
Number of Residues2
DetailsLIPID: N6-decanoyllysine => ECO:0000269|PubMed:35939806
ChainResidueDetails
ILYS18
OLYS18

site_idSWS_FT_FI26
Number of Residues2
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:21076176
ChainResidueDetails
ICYS110
OCYS110

237423

PDB entries from 2025-06-11

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