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7VVU

NuA4 HAT module bound to the nucleosome

Functional Information from GO Data
ChainGOidnamespacecontents
A0000786cellular_componentnucleosome
A0003677molecular_functionDNA binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005694cellular_componentchromosome
A0030527molecular_functionstructural constituent of chromatin
A0031492molecular_functionnucleosomal DNA binding
A0031507biological_processheterochromatin formation
A0046982molecular_functionprotein heterodimerization activity
B0000786cellular_componentnucleosome
B0003677molecular_functionDNA binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005694cellular_componentchromosome
B0006334biological_processnucleosome assembly
B0030527molecular_functionstructural constituent of chromatin
B0031507biological_processheterochromatin formation
B0046982molecular_functionprotein heterodimerization activity
D0000786cellular_componentnucleosome
D0002227biological_processinnate immune response in mucosa
D0003677molecular_functionDNA binding
D0005515molecular_functionprotein binding
D0005615cellular_componentextracellular space
D0005634cellular_componentnucleus
D0005694cellular_componentchromosome
D0006325biological_processchromatin organization
D0019731biological_processantibacterial humoral response
D0030527molecular_functionstructural constituent of chromatin
D0031507biological_processheterochromatin formation
D0046982molecular_functionprotein heterodimerization activity
D0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
N0000786cellular_componentnucleosome
N0003677molecular_functionDNA binding
N0005634cellular_componentnucleus
N0005694cellular_componentchromosome
N0030527molecular_functionstructural constituent of chromatin
N0031507biological_processheterochromatin formation
N0046982molecular_functionprotein heterodimerization activity
O0000786cellular_componentnucleosome
O0003677molecular_functionDNA binding
O0005515molecular_functionprotein binding
O0005634cellular_componentnucleus
O0005654cellular_componentnucleoplasm
O0005694cellular_componentchromosome
O0030527molecular_functionstructural constituent of chromatin
O0031492molecular_functionnucleosomal DNA binding
O0031507biological_processheterochromatin formation
O0046982molecular_functionprotein heterodimerization activity
P0000183biological_processrDNA heterochromatin formation
P0000785cellular_componentchromatin
P0003682molecular_functionchromatin binding
P0003712molecular_functiontranscription coregulator activity
P0004402molecular_functionhistone acetyltransferase activity
P0005515molecular_functionprotein binding
P0005634cellular_componentnucleus
P0006281biological_processDNA repair
P0006325biological_processchromatin organization
P0006351biological_processDNA-templated transcription
P0006354biological_processDNA-templated transcription elongation
P0006355biological_processregulation of DNA-templated transcription
P0006357biological_processregulation of transcription by RNA polymerase II
P0006974biological_processDNA damage response
P0008270molecular_functionzinc ion binding
P0010485molecular_functionhistone H4 acetyltransferase activity
P0010629biological_processnegative regulation of gene expression
P0010867biological_processpositive regulation of triglyceride biosynthetic process
P0016239biological_processpositive regulation of macroautophagy
P0016740molecular_functiontransferase activity
P0032777cellular_componentpiccolo histone acetyltransferase complex
P0032968biological_processpositive regulation of transcription elongation by RNA polymerase II
P0033554biological_processcellular response to stress
P0035267cellular_componentNuA4 histone acetyltransferase complex
P0051726biological_processregulation of cell cycle
P0061733molecular_functionprotein-lysine-acetyltransferase activity
P0106226molecular_functionpeptide 2-hydroxyisobutyryltransferase activity
P0140064molecular_functionpeptide crotonyltransferase activity
P0140068molecular_functionhistone crotonyltransferase activity
Q0000786cellular_componentnucleosome
Q0003677molecular_functionDNA binding
Q0005515molecular_functionprotein binding
Q0005634cellular_componentnucleus
Q0005694cellular_componentchromosome
Q0006334biological_processnucleosome assembly
Q0030527molecular_functionstructural constituent of chromatin
Q0031507biological_processheterochromatin formation
Q0046982molecular_functionprotein heterodimerization activity
S0000786cellular_componentnucleosome
S0003677molecular_functionDNA binding
S0005634cellular_componentnucleus
S0005694cellular_componentchromosome
S0030527molecular_functionstructural constituent of chromatin
S0031507biological_processheterochromatin formation
S0046982molecular_functionprotein heterodimerization activity
T0004402molecular_functionhistone acetyltransferase activity
T0005515molecular_functionprotein binding
T0005634cellular_componentnucleus
T0006281biological_processDNA repair
T0006325biological_processchromatin organization
T0006338biological_processchromatin remodeling
T0006351biological_processDNA-templated transcription
T0006357biological_processregulation of transcription by RNA polymerase II
T0006974biological_processDNA damage response
T0016239biological_processpositive regulation of macroautophagy
T0030674molecular_functionprotein-macromolecule adaptor activity
T0032777cellular_componentpiccolo histone acetyltransferase complex
T0035267cellular_componentNuA4 histone acetyltransferase complex
U0000786cellular_componentnucleosome
U0002227biological_processinnate immune response in mucosa
U0003677molecular_functionDNA binding
U0005515molecular_functionprotein binding
U0005615cellular_componentextracellular space
U0005634cellular_componentnucleus
U0005694cellular_componentchromosome
U0006325biological_processchromatin organization
U0019731biological_processantibacterial humoral response
U0030527molecular_functionstructural constituent of chromatin
U0031507biological_processheterochromatin formation
U0046982molecular_functionprotein heterodimerization activity
U0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
V0004402molecular_functionhistone acetyltransferase activity
V0005515molecular_functionprotein binding
V0005634cellular_componentnucleus
V0005829cellular_componentcytosol
V0006281biological_processDNA repair
V0006325biological_processchromatin organization
V0006338biological_processchromatin remodeling
V0006351biological_processDNA-templated transcription
V0006355biological_processregulation of DNA-templated transcription
V0006974biological_processDNA damage response
V0008270molecular_functionzinc ion binding
V0032777cellular_componentpiccolo histone acetyltransferase complex
V0035267cellular_componentNuA4 histone acetyltransferase complex
V0046872molecular_functionmetal ion binding
V0051321biological_processmeiotic cell cycle
V0140002molecular_functionhistone H3K4me3 reader activity
X0004402molecular_functionhistone acetyltransferase activity
X0005515molecular_functionprotein binding
X0005634cellular_componentnucleus
X0006281biological_processDNA repair
X0006325biological_processchromatin organization
X0006338biological_processchromatin remodeling
X0006351biological_processDNA-templated transcription
X0006357biological_processregulation of transcription by RNA polymerase II
X0006974biological_processDNA damage response
X0016239biological_processpositive regulation of macroautophagy
X0030674molecular_functionprotein-macromolecule adaptor activity
X0032777cellular_componentpiccolo histone acetyltransferase complex
X0035267cellular_componentNuA4 histone acetyltransferase complex
Y0000123cellular_componenthistone acetyltransferase complex
Y0004402molecular_functionhistone acetyltransferase activity
Y0005515molecular_functionprotein binding
Y0005634cellular_componentnucleus
Y0006281biological_processDNA repair
Y0006325biological_processchromatin organization
Y0006338biological_processchromatin remodeling
Y0006351biological_processDNA-templated transcription
Y0006974biological_processDNA damage response
Y0033100cellular_componentNuA3 histone acetyltransferase complex
Y0035267cellular_componentNuA4 histone acetyltransferase complex
Y1990467cellular_componentNuA3a histone acetyltransferase complex
Y1990468cellular_componentNuA3b histone acetyltransferase complex
Functional Information from PROSITE/UniProt
site_idPS00046
Number of Residues7
DetailsHISTONE_H2A Histone H2A signature. AGLqFPV
ChainResidueDetails
SALA21-VAL27

site_idPS00047
Number of Residues5
DetailsHISTONE_H4 Histone H4 signature. GAKRH
ChainResidueDetails
QGLY14-HIS18

site_idPS00322
Number of Residues7
DetailsHISTONE_H3_1 Histone H3 signature 1. KAPRKQL
ChainResidueDetails
OLYS14-LEU20

site_idPS00357
Number of Residues23
DetailsHISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG
ChainResidueDetails
UARG92-GLY114

site_idPS00959
Number of Residues9
DetailsHISTONE_H3_2 Histone H3 signature 2. PFqRLVREI
ChainResidueDetails
OPRO66-ILE74

site_idPS01359
Number of Residues44
DetailsZF_PHD_1 Zinc finger PHD-type signature. Cf.Cqrvsfgem.....................................VaCdgpnCkyewFHydCvnlkeppkgt...................................WyCpeC
ChainResidueDetails
VCYS225-CYS268

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues93
DetailsCoiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P84228","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P84243","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsLipidation: {"description":"S-palmitoyl cysteine","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":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues5
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 Residues4
DetailsDNA binding: {}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues1
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues2
DetailsModified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine; alternate","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI22
Number of Residues4
DetailsModified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI23
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI24
Number of Residues2
DetailsModified residue: {"description":"N5-methylglutamine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI25
Number of Residues6
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI26
Number of Residues2
DetailsGlycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"source":"UniProtKB","id":"P62807","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI27
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

site_idSWS_FT_FI28
Number of Residues25
DetailsZinc finger: {"description":"C2HC MYST-type; degenerate","evidences":[{"source":"PROSITE-ProRule","id":"PRU01063","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI29
Number of Residues21
DetailsMotif: {"description":"ESA1-RPD3 motif"}
ChainResidueDetails

site_idSWS_FT_FI30
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"12368900","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"17223684","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"18245364","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22020126","evidenceCode":"ECO:0000303"},{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI31
Number of Residues11
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11106757","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12368900","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22020126","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI32
Number of Residues1
DetailsSite: {"description":"Important for catalytic activity","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI33
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"PubMed","id":"22020126","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 525
ChainResidueDetails

246905

PDB entries from 2025-12-31

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