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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8UXQ

Structure of Heterochromatin Protein 1 (HP1) alpha in complex with an H2A.Z nucleosome

Functional Information from GO Data
ChainGOidnamespacecontents
A0000118cellular_componenthistone deacetylase complex
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0000775cellular_componentchromosome, centromeric region
A0000776cellular_componentkinetochore
A0000781cellular_componentchromosome, telomeric region
A0000792cellular_componentheterochromatin
A0003682molecular_functionchromatin binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005635cellular_componentnuclear envelope
A0005654cellular_componentnucleoplasm
A0005694cellular_componentchromosome
A0005721cellular_componentpericentric heterochromatin
A0005730cellular_componentnucleolus
A0006974biological_processDNA damage response
A0010369cellular_componentchromocenter
A0016605cellular_componentPML body
A0017053cellular_componenttranscription repressor complex
A0030261biological_processchromosome condensation
A0030674molecular_functionprotein-macromolecule adaptor activity
A0031507biological_processheterochromatin formation
A0032991cellular_componentprotein-containing complex
A0035097cellular_componenthistone methyltransferase complex
A0042802molecular_functionidentical protein binding
A0042826molecular_functionhistone deacetylase binding
A0043021molecular_functionribonucleoprotein complex binding
A0044877molecular_functionprotein-containing complex binding
A0045892biological_processnegative regulation of DNA-templated transcription
A0062072molecular_functionhistone H3K9me2/3 reader activity
A0070828biological_processheterochromatin organization
A0090734cellular_componentsite of DNA damage
A0097355biological_processprotein localization to heterochromatin
A0140297molecular_functionDNA-binding transcription factor binding
A0140566molecular_functionhistone reader activity
A0160267molecular_functionhistone H1K26me1 reader activity
A0160268molecular_functionhistone H1K26me2 reader activity
A1990904cellular_componentribonucleoprotein complex
C0000118cellular_componenthistone deacetylase complex
C0000122biological_processnegative regulation of transcription by RNA polymerase II
C0000775cellular_componentchromosome, centromeric region
C0000776cellular_componentkinetochore
C0000781cellular_componentchromosome, telomeric region
C0000792cellular_componentheterochromatin
C0003682molecular_functionchromatin binding
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005635cellular_componentnuclear envelope
C0005654cellular_componentnucleoplasm
C0005694cellular_componentchromosome
C0005721cellular_componentpericentric heterochromatin
C0005730cellular_componentnucleolus
C0006974biological_processDNA damage response
C0010369cellular_componentchromocenter
C0016605cellular_componentPML body
C0017053cellular_componenttranscription repressor complex
C0030261biological_processchromosome condensation
C0030674molecular_functionprotein-macromolecule adaptor activity
C0031507biological_processheterochromatin formation
C0032991cellular_componentprotein-containing complex
C0035097cellular_componenthistone methyltransferase complex
C0042802molecular_functionidentical protein binding
C0042826molecular_functionhistone deacetylase binding
C0043021molecular_functionribonucleoprotein complex binding
C0044877molecular_functionprotein-containing complex binding
C0045892biological_processnegative regulation of DNA-templated transcription
C0062072molecular_functionhistone H3K9me2/3 reader activity
C0070828biological_processheterochromatin organization
C0090734cellular_componentsite of DNA damage
C0097355biological_processprotein localization to heterochromatin
C0140297molecular_functionDNA-binding transcription factor binding
C0140566molecular_functionhistone reader activity
C0160267molecular_functionhistone H1K26me1 reader activity
C0160268molecular_functionhistone H1K26me2 reader activity
C1990904cellular_componentribonucleoprotein complex
E0000786cellular_componentnucleosome
E0003677molecular_functionDNA binding
E0005515molecular_functionprotein binding
E0005634cellular_componentnucleus
E0005654cellular_componentnucleoplasm
E0005694cellular_componentchromosome
E0030527molecular_functionstructural constituent of chromatin
E0031492molecular_functionnucleosomal DNA binding
E0031507biological_processheterochromatin formation
E0046982molecular_functionprotein heterodimerization activity
F0000786cellular_componentnucleosome
F0003677molecular_functionDNA binding
F0005515molecular_functionprotein binding
F0005634cellular_componentnucleus
F0005694cellular_componentchromosome
F0006334biological_processnucleosome assembly
F0030527molecular_functionstructural constituent of chromatin
F0031507biological_processheterochromatin formation
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
G0003677molecular_functionDNA binding
G0005515molecular_functionprotein binding
G0005634cellular_componentnucleus
G0005654cellular_componentnucleoplasm
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
H0002227biological_processinnate immune response in mucosa
H0003677molecular_functionDNA binding
H0005515molecular_functionprotein binding
H0005615cellular_componentextracellular space
H0005634cellular_componentnucleus
H0005694cellular_componentchromosome
H0006325biological_processchromatin organization
H0019731biological_processantibacterial humoral response
H0030527molecular_functionstructural constituent of chromatin
H0031507biological_processheterochromatin formation
H0046982molecular_functionprotein heterodimerization activity
H0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
K0000786cellular_componentnucleosome
K0003677molecular_functionDNA binding
K0005515molecular_functionprotein binding
K0005634cellular_componentnucleus
K0005654cellular_componentnucleoplasm
K0005694cellular_componentchromosome
K0030527molecular_functionstructural constituent of chromatin
K0031492molecular_functionnucleosomal DNA binding
K0031507biological_processheterochromatin formation
K0046982molecular_functionprotein heterodimerization activity
L0000786cellular_componentnucleosome
L0003677molecular_functionDNA binding
L0005515molecular_functionprotein binding
L0005634cellular_componentnucleus
L0005694cellular_componentchromosome
L0006334biological_processnucleosome assembly
L0030527molecular_functionstructural constituent of chromatin
L0031507biological_processheterochromatin formation
L0046982molecular_functionprotein heterodimerization activity
M0000786cellular_componentnucleosome
M0000791cellular_componenteuchromatin
M0000792cellular_componentheterochromatin
M0000978molecular_functionRNA polymerase II cis-regulatory region sequence-specific DNA binding
M0000979molecular_functionRNA polymerase II core promoter sequence-specific DNA binding
M0003677molecular_functionDNA binding
M0005515molecular_functionprotein binding
M0005634cellular_componentnucleus
M0005654cellular_componentnucleoplasm
M0005694cellular_componentchromosome
M0006325biological_processchromatin organization
M0030527molecular_functionstructural constituent of chromatin
M0031490molecular_functionchromatin DNA binding
M0031492molecular_functionnucleosomal DNA binding
M0031507biological_processheterochromatin formation
M0045944biological_processpositive regulation of transcription by RNA polymerase II
M0046982molecular_functionprotein heterodimerization activity
M0071392biological_processcellular response to estradiol stimulus
N0000786cellular_componentnucleosome
N0002227biological_processinnate immune response in mucosa
N0003677molecular_functionDNA binding
N0005515molecular_functionprotein binding
N0005615cellular_componentextracellular space
N0005634cellular_componentnucleus
N0005694cellular_componentchromosome
N0006325biological_processchromatin organization
N0019731biological_processantibacterial humoral response
N0030527molecular_functionstructural constituent of chromatin
N0031507biological_processheterochromatin formation
N0046982molecular_functionprotein heterodimerization activity
N0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
Functional Information from PROSITE/UniProt
site_idPS00322
Number of Residues7
DetailsHISTONE_H3_1 Histone H3 signature 1. KAPRKQL
ChainResidueDetails
ELYS302-LEU308
site_idPS00959
Number of Residues9
DetailsHISTONE_H3_2 Histone H3 signature 2. PFqRLVREI
ChainResidueDetails
EPRO354-ILE362
site_idPS00357
Number of Residues23
DetailsHISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG
ChainResidueDetails
HARG678-GLY700
site_idPS00598
Number of Residues21
DetailsCHROMO_1 Chromo domain signature. YlLKWkGFseehn.TWEPeknL
ChainResidueDetails
ATYR16-LEU36
site_idPS00047
Number of Residues5
DetailsHISTONE_H4 Histone H4 signature. GAKRH
ChainResidueDetails
FGLY421-HIS425
site_idPS00046
Number of Residues7
DetailsHISTONE_H2A Histone H2A signature. AGLqFPV
ChainResidueDetails
GALA517-VAL523
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues58
DetailsDomain: {"description":"Chromo 2; shadow subtype","evidences":[{"source":"PROSITE-ProRule","id":"PRU00053","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues94
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues32
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q13185","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"25218447","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25755297","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25772364","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues9
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues3
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68431","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P84228","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P84243","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues2
DetailsModified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues2
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
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 Residues4
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues4
DetailsModified residue: {"description":"N6-propionyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by PAK2","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues2
DetailsModified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI27
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_FI28
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_FI29
Number of Residues22
DetailsRegion: {"description":"M6 cassette","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues20
DetailsRegion: {"description":"Required for interaction with INCENP","evidences":[{"source":"PubMed","id":"12660166","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI31
Number of Residues2
DetailsModified residue: {"description":"N6-lactoyllysine","evidences":[{"source":"PubMed","id":"31645732","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI32
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P0C0S5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI33
Number of Residues2
DetailsGlycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"source":"UniProtKB","id":"P62807","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI34
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

246905

PDB entries from 2025-12-31

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