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9B3P

The cryo-EM structure of the H2A.Z-H3.3 double-variant nucleosome

Functional Information from GO Data
ChainGOidnamespacecontents
A0000775cellular_componentchromosome, centromeric region
A0000781cellular_componentchromosome, telomeric region
A0000785cellular_componentchromatin
A0000786cellular_componentnucleosome
A0000939cellular_componentinner kinetochore
A0000978molecular_functionRNA polymerase II cis-regulatory region sequence-specific DNA binding
A0000979molecular_functionRNA polymerase II core promoter sequence-specific DNA binding
A0001556biological_processoocyte maturation
A0001649biological_processosteoblast differentiation
A0001740cellular_componentBarr body
A0003677molecular_functionDNA binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005694cellular_componentchromosome
A0006334biological_processnucleosome assembly
A0006997biological_processnucleus organization
A0007283biological_processspermatogenesis
A0007286biological_processspermatid development
A0007338biological_processsingle fertilization
A0007566biological_processembryo implantation
A0008283biological_processcell population proliferation
A0008584biological_processmale gonad development
A0030307biological_processpositive regulation of cell growth
A0030527molecular_functionstructural constituent of chromatin
A0031492molecular_functionnucleosomal DNA binding
A0031508biological_processpericentric heterochromatin formation
A0031509biological_processsubtelomeric heterochromatin formation
A0032200biological_processtelomere organization
A0032991cellular_componentprotein-containing complex
A0035264biological_processmulticellular organism growth
A0042692biological_processmuscle cell differentiation
A0046982molecular_functionprotein heterodimerization activity
A0048477biological_processoogenesis
A0070062cellular_componentextracellular exosome
A0090230biological_processregulation of centromere complex assembly
A1902340biological_processnegative regulation of chromosome condensation
B0000786cellular_componentnucleosome
B0003677molecular_functionDNA binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005694cellular_componentchromosome
B0006334biological_processnucleosome assembly
B0030527molecular_functionstructural constituent of chromatin
B0046982molecular_functionprotein heterodimerization activity
C0000786cellular_componentnucleosome
C0000791cellular_componenteuchromatin
C0000792cellular_componentheterochromatin
C0000978molecular_functionRNA polymerase II cis-regulatory region sequence-specific DNA binding
C0000979molecular_functionRNA polymerase II core promoter sequence-specific DNA binding
C0001740cellular_componentBarr body
C0003677molecular_functionDNA binding
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005694cellular_componentchromosome
C0006325biological_processchromatin organization
C0030527molecular_functionstructural constituent of chromatin
C0031490molecular_functionchromatin DNA binding
C0031492molecular_functionnucleosomal DNA binding
C0031507biological_processheterochromatin formation
C0045944biological_processpositive regulation of transcription by RNA polymerase II
C0046982molecular_functionprotein heterodimerization activity
C0071392biological_processcellular response to estradiol stimulus
D0000786cellular_componentnucleosome
D0003677molecular_functionDNA binding
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005694cellular_componentchromosome
D0030527molecular_functionstructural constituent of chromatin
D0046982molecular_functionprotein heterodimerization activity
E0000775cellular_componentchromosome, centromeric region
E0000781cellular_componentchromosome, telomeric region
E0000785cellular_componentchromatin
E0000786cellular_componentnucleosome
E0000939cellular_componentinner kinetochore
E0000978molecular_functionRNA polymerase II cis-regulatory region sequence-specific DNA binding
E0000979molecular_functionRNA polymerase II core promoter sequence-specific DNA binding
E0001556biological_processoocyte maturation
E0001649biological_processosteoblast differentiation
E0001740cellular_componentBarr body
E0003677molecular_functionDNA binding
E0005515molecular_functionprotein binding
E0005576cellular_componentextracellular region
E0005634cellular_componentnucleus
E0005654cellular_componentnucleoplasm
E0005694cellular_componentchromosome
E0006334biological_processnucleosome assembly
E0006997biological_processnucleus organization
E0007283biological_processspermatogenesis
E0007286biological_processspermatid development
E0007338biological_processsingle fertilization
E0007566biological_processembryo implantation
E0008283biological_processcell population proliferation
E0008584biological_processmale gonad development
E0030307biological_processpositive regulation of cell growth
E0030527molecular_functionstructural constituent of chromatin
E0031492molecular_functionnucleosomal DNA binding
E0031508biological_processpericentric heterochromatin formation
E0031509biological_processsubtelomeric heterochromatin formation
E0032200biological_processtelomere organization
E0032991cellular_componentprotein-containing complex
E0035264biological_processmulticellular organism growth
E0042692biological_processmuscle cell differentiation
E0046982molecular_functionprotein heterodimerization activity
E0048477biological_processoogenesis
E0070062cellular_componentextracellular exosome
E0090230biological_processregulation of centromere complex assembly
E1902340biological_processnegative regulation of chromosome condensation
F0000786cellular_componentnucleosome
F0003677molecular_functionDNA binding
F0005515molecular_functionprotein binding
F0005634cellular_componentnucleus
F0005694cellular_componentchromosome
F0006334biological_processnucleosome assembly
F0030527molecular_functionstructural constituent of chromatin
F0046982molecular_functionprotein heterodimerization activity
G0000786cellular_componentnucleosome
G0000791cellular_componenteuchromatin
G0000792cellular_componentheterochromatin
G0000978molecular_functionRNA polymerase II cis-regulatory region sequence-specific DNA binding
G0000979molecular_functionRNA polymerase II core promoter sequence-specific DNA binding
G0001740cellular_componentBarr body
G0003677molecular_functionDNA binding
G0005515molecular_functionprotein binding
G0005634cellular_componentnucleus
G0005694cellular_componentchromosome
G0006325biological_processchromatin organization
G0030527molecular_functionstructural constituent of chromatin
G0031490molecular_functionchromatin DNA binding
G0031492molecular_functionnucleosomal DNA binding
G0031507biological_processheterochromatin formation
G0045944biological_processpositive regulation of transcription by RNA polymerase II
G0046982molecular_functionprotein heterodimerization activity
G0071392biological_processcellular response to estradiol stimulus
H0000786cellular_componentnucleosome
H0003677molecular_functionDNA binding
H0005515molecular_functionprotein binding
H0005634cellular_componentnucleus
H0005694cellular_componentchromosome
H0030527molecular_functionstructural constituent of chromatin
H0046982molecular_functionprotein heterodimerization activity
Functional Information from PROSITE/UniProt
site_idPS00046
Number of Residues7
DetailsHISTONE_H2A Histone H2A signature. AGLqFPV
ChainResidueDetails
CALA23-VAL29

site_idPS00047
Number of Residues5
DetailsHISTONE_H4 Histone H4 signature. GAKRH
ChainResidueDetails
BGLY14-HIS18

site_idPS00322
Number of Residues7
DetailsHISTONE_H3_1 Histone H3 signature 1. KAPRKQL
ChainResidueDetails
ALYS14-LEU20

site_idPS00357
Number of Residues23
DetailsHISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG
ChainResidueDetails
DARG92-GLY114

site_idPS00959
Number of Residues9
DetailsHISTONE_H3_2 Histone H3 signature 2. PFqRLVREI
ChainResidueDetails
APRO66-ILE74

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19783980","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"22389435","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20850016","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
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_FI5
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_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20850016","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"PubMed","id":"31542297","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
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_FI11
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues4
DetailsModified residue: {"description":"N6-propionyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by PAK2","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues2
DetailsModified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI17
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_FI18
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_FI19
Number of Residues22
DetailsRegion: {"description":"M6 cassette","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues20
DetailsRegion: {"description":"Required for interaction with INCENP","evidences":[{"source":"PubMed","id":"12660166","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues1
DetailsModified residue: {"description":"N6-lactoyllysine","evidences":[{"source":"PubMed","id":"31645732","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI22
Number of Residues2
DetailsGlycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"source":"UniProtKB","id":"P62807","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI23
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

238582

PDB entries from 2025-07-09

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