Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

4R8P

Crystal structure of the Ring1B/Bmi1/UbcH5c PRC1 ubiquitylation module bound to the nucleosome core particle

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
C0000786cellular_componentnucleosome
C0003677molecular_functionDNA binding
C0005634cellular_componentnucleus
C0005694cellular_componentchromosome
C0030527molecular_functionstructural constituent of chromatin
C0031507biological_processheterochromatin formation
C0046982molecular_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
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
G0003677molecular_functionDNA binding
G0005634cellular_componentnucleus
G0005694cellular_componentchromosome
G0030527molecular_functionstructural constituent of chromatin
G0031507biological_processheterochromatin formation
G0046982molecular_functionprotein heterodimerization activity
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
L0000122biological_processnegative regulation of transcription by RNA polymerase II
L0000151cellular_componentubiquitin ligase complex
L0000166molecular_functionnucleotide binding
L0000209biological_processprotein polyubiquitination
L0004842molecular_functionubiquitin-protein transferase activity
L0005515molecular_functionprotein binding
L0005524molecular_functionATP binding
L0005634cellular_componentnucleus
L0005654cellular_componentnucleoplasm
L0005829cellular_componentcytosol
L0005886cellular_componentplasma membrane
L0006281biological_processDNA repair
L0006511biological_processubiquitin-dependent protein catabolic process
L0006513biological_processprotein monoubiquitination
L0006915biological_processapoptotic process
L0006974biological_processDNA damage response
L0010008cellular_componentendosome membrane
L0016567biological_processprotein ubiquitination
L0016740molecular_functiontransferase activity
L0030514biological_processnegative regulation of BMP signaling pathway
L0036211biological_processprotein modification process
L0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
L0051865biological_processprotein autoubiquitination
L0061630molecular_functionubiquitin protein ligase activity
L0061631molecular_functionubiquitin conjugating enzyme activity
L0070062cellular_componentextracellular exosome
L0070936biological_processprotein K48-linked ubiquitination
L0070979biological_processprotein K11-linked ubiquitination
L0085020biological_processprotein K6-linked ubiquitination
L1903955biological_processpositive regulation of protein targeting to mitochondrion
N0000122biological_processnegative regulation of transcription by RNA polymerase II
N0000151cellular_componentubiquitin ligase complex
N0000166molecular_functionnucleotide binding
N0000209biological_processprotein polyubiquitination
N0004842molecular_functionubiquitin-protein transferase activity
N0005515molecular_functionprotein binding
N0005524molecular_functionATP binding
N0005634cellular_componentnucleus
N0005654cellular_componentnucleoplasm
N0005829cellular_componentcytosol
N0005886cellular_componentplasma membrane
N0006281biological_processDNA repair
N0006511biological_processubiquitin-dependent protein catabolic process
N0006513biological_processprotein monoubiquitination
N0006915biological_processapoptotic process
N0006974biological_processDNA damage response
N0010008cellular_componentendosome membrane
N0016567biological_processprotein ubiquitination
N0016740molecular_functiontransferase activity
N0030514biological_processnegative regulation of BMP signaling pathway
N0036211biological_processprotein modification process
N0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
N0051865biological_processprotein autoubiquitination
N0061630molecular_functionubiquitin protein ligase activity
N0061631molecular_functionubiquitin conjugating enzyme activity
N0070062cellular_componentextracellular exosome
N0070936biological_processprotein K48-linked ubiquitination
N0070979biological_processprotein K11-linked ubiquitination
N0085020biological_processprotein K6-linked ubiquitination
N1903955biological_processpositive regulation of protein targeting to mitochondrion
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN K 201
ChainResidue
KCYS18
KCYS21
KCYS39
KCYS42

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN K 202
ChainResidue
KCYS34
KHIS36
KCYS53
KCYS56

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN L 401
ChainResidue
LCYS54
LCYS72
LCYS75
LCYS51

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN L 402
ChainResidue
LCYS67
LHIS69
LCYS87
LTHR89
LCYS90

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN M 201
ChainResidue
MCYS18
MCYS21
MCYS39
MCYS42

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN M 202
ChainResidue
MCYS34
MHIS36
MCYS53
MCYS56

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN N 401
ChainResidue
NCYS51
NCYS54
NCYS72
NCYS75
NARG121

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN N 402
ChainResidue
NCYS67
NHIS69
NCYS87
NTHR89
NCYS90

Functional Information from PROSITE/UniProt
site_idPS00046
Number of Residues7
DetailsHISTONE_H2A Histone H2A signature. AGLqFPV
ChainResidueDetails
CALA21-VAL27

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

site_idPS00183
Number of Residues16
DetailsUBC_1 Ubiquitin-conjugating (UBC) active site signature. YHPNInsn.GsICLdiL
ChainResidueDetails
LTYR274-LEU289

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_idPS00518
Number of Residues10
DetailsZF_RING_1 Zinc finger RING-type signature. ClHrFCadCI
ChainResidueDetails
LCYS67-ILE76
KCYS34-ILE43

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 Residues1
DetailsModified residue: {"description":"N6-methyllysine","evidences":[{"source":"UniProtKB","id":"P68431","evidenceCode":"ECO:0000250"}]}
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 Residues1
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

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

site_idSWS_FT_FI13
Number of Residues4
DetailsModified residue: {"description":"N6-propionyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by PAK2","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

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

site_idSWS_FT_FI17
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI18
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_FI19
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_FI20
Number of Residues2
DetailsModified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine; alternate","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues4
DetailsModified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI22
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI23
Number of Residues2
DetailsModified residue: {"description":"N5-methylglutamine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI24
Number of Residues2
DetailsModified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI25
Number of Residues5
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 Residues158
DetailsZinc finger: {"description":"RING-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00175","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI29
Number of Residues28
DetailsMotif: {"description":"Nuclear localization signal","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI30
Number of Residues2
DetailsActive site: {"description":"Glycyl thioester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00388","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10133","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI31
Number of Residues10
DetailsRegion: {"description":"Interaction with nucleosomes via an acidic patch on histone H2A and histone H2B","evidences":[{"source":"PubMed","id":"25355358","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI32
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"25519132","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI33
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"Q9CQJ4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

PDB statisticsPDBj update infoContact PDBjnumon