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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8OFF

Structure of BARD1 ARD-BRCTs in complex with H2AKc15ub nucleosomes (Map1)

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
Aa0000786cellular_componentnucleosome
Aa0003677molecular_functionDNA binding
Aa0005515molecular_functionprotein binding
Aa0005634cellular_componentnucleus
Aa0005694cellular_componentchromosome
Aa0019899molecular_functionenzyme binding
Aa0030527molecular_functionstructural constituent of chromatin
Aa0031507biological_processheterochromatin formation
Aa0046982molecular_functionprotein heterodimerization activity
Aa0070062cellular_componentextracellular exosome
Ab0000786cellular_componentnucleosome
Ab0003677molecular_functionDNA binding
Ab0005515molecular_functionprotein binding
Ab0005634cellular_componentnucleus
Ab0005694cellular_componentchromosome
Ab0019899molecular_functionenzyme binding
Ab0030527molecular_functionstructural constituent of chromatin
Ab0031507biological_processheterochromatin formation
Ab0046982molecular_functionprotein heterodimerization activity
Ab0070062cellular_componentextracellular exosome
Ba0000786cellular_componentnucleosome
Ba0002227biological_processinnate immune response in mucosa
Ba0003677molecular_functionDNA binding
Ba0005515molecular_functionprotein binding
Ba0005615cellular_componentextracellular space
Ba0005634cellular_componentnucleus
Ba0005654cellular_componentnucleoplasm
Ba0005694cellular_componentchromosome
Ba0005829cellular_componentcytosol
Ba0006334biological_processnucleosome assembly
Ba0019731biological_processantibacterial humoral response
Ba0030527molecular_functionstructural constituent of chromatin
Ba0042742biological_processdefense response to bacterium
Ba0042802molecular_functionidentical protein binding
Ba0046982molecular_functionprotein heterodimerization activity
Ba0050830biological_processdefense response to Gram-positive bacterium
Ba0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
Ba0070062cellular_componentextracellular exosome
Bb0000786cellular_componentnucleosome
Bb0002227biological_processinnate immune response in mucosa
Bb0003677molecular_functionDNA binding
Bb0005515molecular_functionprotein binding
Bb0005615cellular_componentextracellular space
Bb0005634cellular_componentnucleus
Bb0005654cellular_componentnucleoplasm
Bb0005694cellular_componentchromosome
Bb0005829cellular_componentcytosol
Bb0006334biological_processnucleosome assembly
Bb0019731biological_processantibacterial humoral response
Bb0030527molecular_functionstructural constituent of chromatin
Bb0042742biological_processdefense response to bacterium
Bb0042802molecular_functionidentical protein binding
Bb0046982molecular_functionprotein heterodimerization activity
Bb0050830biological_processdefense response to Gram-positive bacterium
Bb0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
Bb0070062cellular_componentextracellular exosome
Ca0000786cellular_componentnucleosome
Ca0003677molecular_functionDNA binding
Ca0005515molecular_functionprotein binding
Ca0005576cellular_componentextracellular region
Ca0005634cellular_componentnucleus
Ca0005654cellular_componentnucleoplasm
Ca0005694cellular_componentchromosome
Ca0006325biological_processchromatin organization
Ca0006334biological_processnucleosome assembly
Ca0010467biological_processgene expression
Ca0016020cellular_componentmembrane
Ca0030527molecular_functionstructural constituent of chromatin
Ca0032200biological_processtelomere organization
Ca0032991cellular_componentprotein-containing complex
Ca0040029biological_processepigenetic regulation of gene expression
Ca0045296molecular_functioncadherin binding
Ca0046982molecular_functionprotein heterodimerization activity
Ca0070062cellular_componentextracellular exosome
Cb0000786cellular_componentnucleosome
Cb0003677molecular_functionDNA binding
Cb0005515molecular_functionprotein binding
Cb0005576cellular_componentextracellular region
Cb0005634cellular_componentnucleus
Cb0005654cellular_componentnucleoplasm
Cb0005694cellular_componentchromosome
Cb0006325biological_processchromatin organization
Cb0006334biological_processnucleosome assembly
Cb0010467biological_processgene expression
Cb0016020cellular_componentmembrane
Cb0030527molecular_functionstructural constituent of chromatin
Cb0032200biological_processtelomere organization
Cb0032991cellular_componentprotein-containing complex
Cb0040029biological_processepigenetic regulation of gene expression
Cb0045296molecular_functioncadherin binding
Cb0046982molecular_functionprotein heterodimerization activity
Cb0070062cellular_componentextracellular exosome
Da0000781cellular_componentchromosome, telomeric region
Da0000786cellular_componentnucleosome
Da0003677molecular_functionDNA binding
Da0003723molecular_functionRNA binding
Da0005515molecular_functionprotein binding
Da0005576cellular_componentextracellular region
Da0005634cellular_componentnucleus
Da0005654cellular_componentnucleoplasm
Da0005694cellular_componentchromosome
Da0006325biological_processchromatin organization
Da0006334biological_processnucleosome assembly
Da0016020cellular_componentmembrane
Da0030527molecular_functionstructural constituent of chromatin
Da0032200biological_processtelomere organization
Da0032991cellular_componentprotein-containing complex
Da0043505cellular_componentCENP-A containing nucleosome
Da0045653biological_processnegative regulation of megakaryocyte differentiation
Da0046982molecular_functionprotein heterodimerization activity
Da0061644biological_processprotein localization to CENP-A containing chromatin
Da0070062cellular_componentextracellular exosome
Db0000781cellular_componentchromosome, telomeric region
Db0000786cellular_componentnucleosome
Db0003677molecular_functionDNA binding
Db0003723molecular_functionRNA binding
Db0005515molecular_functionprotein binding
Db0005576cellular_componentextracellular region
Db0005634cellular_componentnucleus
Db0005654cellular_componentnucleoplasm
Db0005694cellular_componentchromosome
Db0006325biological_processchromatin organization
Db0006334biological_processnucleosome assembly
Db0016020cellular_componentmembrane
Db0030527molecular_functionstructural constituent of chromatin
Db0032200biological_processtelomere organization
Db0032991cellular_componentprotein-containing complex
Db0043505cellular_componentCENP-A containing nucleosome
Db0045653biological_processnegative regulation of megakaryocyte differentiation
Db0046982molecular_functionprotein heterodimerization activity
Db0061644biological_processprotein localization to CENP-A containing chromatin
Db0070062cellular_componentextracellular exosome
Ea0004842molecular_functionubiquitin-protein transferase activity
Ea0005634cellular_componentnucleus
Ea0006281biological_processDNA repair
Ea0006974biological_processDNA damage response
Ea0008270molecular_functionzinc ion binding
Ea0016740molecular_functiontransferase activity
Ea0031436cellular_componentBRCA1-BARD1 complex
Ea0046872molecular_functionmetal ion binding
Ea0070531cellular_componentBRCA1-A complex
Ea0085020biological_processprotein K6-linked ubiquitination
Eb0004842molecular_functionubiquitin-protein transferase activity
Eb0005634cellular_componentnucleus
Eb0006281biological_processDNA repair
Eb0006974biological_processDNA damage response
Eb0008270molecular_functionzinc ion binding
Eb0016740molecular_functiontransferase activity
Eb0031436cellular_componentBRCA1-BARD1 complex
Eb0046872molecular_functionmetal ion binding
Eb0070531cellular_componentBRCA1-A complex
Eb0085020biological_processprotein K6-linked ubiquitination
Functional Information from PROSITE/UniProt
site_idPS00046
Number of Residues7
DetailsHISTONE_H2A Histone H2A signature. AGLqFPV
ChainResidueDetails
AaALA22-VAL28
site_idPS00047
Number of Residues5
DetailsHISTONE_H4 Histone H4 signature. GAKRH
ChainResidueDetails
DaGLY15-HIS19
site_idPS00299
Number of Residues26
DetailsUBIQUITIN_1 Ubiquitin domain signature. KakIqDkegIPpdqQrLIFaGkqleD
ChainResidueDetails
FaLYS27-ASP52
site_idPS00322
Number of Residues7
DetailsHISTONE_H3_1 Histone H3 signature 1. KAPRKQL
ChainResidueDetails
CaLYS15-LEU21
site_idPS00357
Number of Residues23
DetailsHISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG
ChainResidueDetails
BaARG93-GLY115
site_idPS00518
Number of Residues10
DetailsZF_RING_1 Zinc finger RING-type signature. CeHiFCsnCV
ChainResidueDetails
EaCYS61-VAL70
site_idPS00959
Number of Residues9
DetailsHISTONE_H3_2 Histone H3 signature 2. PFqRLVREI
ChainResidueDetails
CaPRO67-ILE75
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 Residues16
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":"UniProtKB","id":"P84243","evidenceCode":"ECO:0000250"}]}
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 Residues5
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 Residues2
DetailsModified residue: {"description":"PolyADP-ribosyl glutamic acid","evidences":[{"source":"UniProtKB","id":"Q64475","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by AMPK","evidences":[{"source":"UniProtKB","id":"Q6ZWY9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues4
DetailsModified residue: {"description":"N6-lactoyllysine; alternate","evidences":[{"source":"PubMed","id":"31645732","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues4
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"16627869","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues2
DetailsModified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine; alternate","evidences":[{"source":"PubMed","id":"24681537","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues2
DetailsModified residue: {"description":"Dimethylated arginine","evidences":[{"source":"UniProtKB","id":"Q96A08","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues4
DetailsModified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"Q96A08","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q00729","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues2
DetailsGlycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"source":"PubMed","id":"22121020","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"PubMed","id":"21726816","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"PubMed","id":"16307923","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16627869","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16713563","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22121020","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues2
DetailsModified residue: {"description":"N6-(beta-hydroxybutyryl)lysine; alternate","evidences":[{"source":"PubMed","id":"27105115","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues2
DetailsModified residue: {"description":"N6-crotonyllysine; alternate","evidences":[{"source":"PubMed","id":"21925322","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues4
DetailsModified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"PubMed","id":"24681537","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues2
DetailsModified residue: {"description":"N6-glutaryllysine","evidences":[{"source":"PubMed","id":"31542297","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues2
DetailsModified residue: {"description":"N5-methylglutamine","evidences":[{"source":"PubMed","id":"24352239","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"PubMed","id":"22713238","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22980979","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22713238","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22980979","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues2
DetailsModified residue: {"description":"N6-propionyllysine; alternate","evidences":[{"source":"PubMed","id":"17267393","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI30
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_FI31
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_FI32
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62806","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI33
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P62806","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI34
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI35
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_FI36
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_FI37
Number of Residues5
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_FI38
Number of Residues1
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

238895

PDB entries from 2025-07-16

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