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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9M77

The activated state of human UHRF1 bound to a mononucleosome, with the finger loop ordered and linker 4 disordered.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000786cellular_componentnucleosome
A0005634cellular_componentnucleus
A0005694cellular_componentchromosome
A0030527molecular_functionstructural constituent of chromatin
A0031492molecular_functionnucleosomal DNA binding
A0031507biological_processheterochromatin formation
B0000786cellular_componentnucleosome
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005694cellular_componentchromosome
B0006334biological_processnucleosome assembly
B0030527molecular_functionstructural constituent of chromatin
B0031507biological_processheterochromatin formation
C0000786cellular_componentnucleosome
C0005634cellular_componentnucleus
C0005694cellular_componentchromosome
C0030527molecular_functionstructural constituent of chromatin
C0031507biological_processheterochromatin formation
D0000786cellular_componentnucleosome
D0002227biological_processinnate immune response in mucosa
D0003677molecular_functionDNA binding
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005694cellular_componentchromosome
D0006325biological_processchromatin organization
D0019731biological_processantibacterial humoral response
D0030527molecular_functionstructural constituent of chromatin
D0031507biological_processheterochromatin formation
D0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
E0000786cellular_componentnucleosome
E0005634cellular_componentnucleus
E0005694cellular_componentchromosome
E0030527molecular_functionstructural constituent of chromatin
E0031492molecular_functionnucleosomal DNA binding
E0031507biological_processheterochromatin formation
F0000786cellular_componentnucleosome
F0005515molecular_functionprotein binding
F0005634cellular_componentnucleus
F0005694cellular_componentchromosome
F0006334biological_processnucleosome assembly
F0030527molecular_functionstructural constituent of chromatin
F0031507biological_processheterochromatin formation
G0000786cellular_componentnucleosome
G0005634cellular_componentnucleus
G0005694cellular_componentchromosome
G0030527molecular_functionstructural constituent of chromatin
G0031507biological_processheterochromatin formation
H0000786cellular_componentnucleosome
H0002227biological_processinnate immune response in mucosa
H0003677molecular_functionDNA binding
H0005515molecular_functionprotein binding
H0005634cellular_componentnucleus
H0005694cellular_componentchromosome
H0006325biological_processchromatin organization
H0019731biological_processantibacterial humoral response
H0030527molecular_functionstructural constituent of chromatin
H0031507biological_processheterochromatin formation
H0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
K0000122biological_processnegative regulation of transcription by RNA polymerase II
K0000724biological_processdouble-strand break repair via homologous recombination
K0000785cellular_componentchromatin
K0000791cellular_componenteuchromatin
K0000792cellular_componentheterochromatin
K0000987molecular_functioncis-regulatory region sequence-specific DNA binding
K0003676molecular_functionnucleic acid binding
K0004842molecular_functionubiquitin-protein transferase activity
K0005515molecular_functionprotein binding
K0005634cellular_componentnucleus
K0005654cellular_componentnucleoplasm
K0005657cellular_componentreplication fork
K0005694cellular_componentchromosome
K0005819cellular_componentspindle
K0006511biological_processubiquitin-dependent protein catabolic process
K0006950biological_processresponse to stress
K0006974biological_processDNA damage response
K0008270molecular_functionzinc ion binding
K0008327molecular_functionmethyl-CpG binding
K0016363cellular_componentnuclear matrix
K0016567biological_processprotein ubiquitination
K0031507biological_processheterochromatin formation
K0035825biological_processhomologous recombination
K0040029biological_processepigenetic regulation of gene expression
K0042393molecular_functionhistone binding
K0042802molecular_functionidentical protein binding
K0044027biological_processnegative regulation of gene expression via chromosomal CpG island methylation
K0044729molecular_functionhemi-methylated DNA-binding
K0045944biological_processpositive regulation of transcription by RNA polymerase II
K0050678biological_processregulation of epithelial cell proliferation
K0051247biological_processpositive regulation of protein metabolic process
K0051865biological_processprotein autoubiquitination
K0061630molecular_functionubiquitin protein ligase activity
K0062072molecular_functionhistone H3K9me2/3 reader activity
K0071168biological_processprotein localization to chromatin
K0090307biological_processmitotic spindle assembly
K0140006molecular_functionhistone H3 reader activity
K0140234molecular_functionhistone H3K23 ubiquitin ligase activity
K0140248molecular_functionhistone H3K18 ubiquitin ligase activity
K0140612molecular_functionDNA damage sensor activity
K0140851molecular_functionhistone H3K14 ubiquitin ligase activity
K0141055molecular_functionhistone H3 ubiquitin ligase activity
K0141119biological_processchromosomal DNA methylation maintenance following DNA replication
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_idPS00322
Number of Residues7
DetailsHISTONE_H3_1 Histone H3 signature 1. KAPRKQL
ChainResidueDetails
ELYS14-LEU20
site_idPS00357
Number of Residues23
DetailsHISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG
ChainResidueDetails
DARG89-GLY111
site_idPS00518
Number of Residues10
DetailsZF_RING_1 Zinc finger RING-type signature. CqHnVCkdCL
ChainResidueDetails
KCYS739-LEU748
site_idPS00959
Number of Residues9
DetailsHISTONE_H3_2 Histone H3 signature 2. PFqRLVREI
ChainResidueDetails
EPRO66-ILE74
site_idPS01359
Number of Residues62
DetailsZF_PHD_1 Zinc finger PHD-type signature. CkhCkddvnrlcrvcachlcggrqdpdkq....................LmCde..Cdma.FHiyCldpplssvpsede................................WyCpeC
ChainResidueDetails
KCYS302-CYS363
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues4
DetailsModified residue: {"description":"N6-propionyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by PAK2","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"N6-methacryllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
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_FI9
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_FI10
Number of Residues4
DetailsModified residue: {"description":"N6-isonicotinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q93079","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues6
DetailsModified residue: {"description":"N6-methacryllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q93079","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues2
DetailsGlycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"source":"UniProtKB","id":"P62807","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
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_FI16
Number of Residues163
DetailsDomain: {"description":"YDG","evidences":[{"source":"PROSITE-ProRule","id":"PRU00358","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues56
DetailsZinc finger: {"description":"PHD-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00146","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues67
DetailsRegion: {"description":"Tudor-like 2","evidences":[{"source":"PubMed","id":"21489993","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues5
DetailsRegion: {"description":"Linker","evidences":[{"source":"PubMed","id":"22837395","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues6
DetailsRegion: {"description":"Histone H3R2me0 binding","evidences":[{"source":"PubMed","id":"21777816","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues1
DetailsRegion: {"description":"Required to promote base flipping","evidences":[{"source":"UniProtKB","id":"Q8VDF2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues6
DetailsRegion: {"description":"Required for formation of a 5-methylcytosine-binding pocket","evidences":[{"source":"PubMed","id":"18772889","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21777816","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22837395","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3ASK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ASL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SOU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21777816","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22837395","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3ASL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SOU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22837395","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3ASK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ASL","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22837395","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3ASL","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18772889","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues1
DetailsSite: {"description":"Histone H3K4me0 binding","evidences":[{"source":"PubMed","id":"21777816","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues2
DetailsSite: {"description":"Histone H3R2me0 binding","evidences":[{"source":"PubMed","id":"21777816","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues1
DetailsSite: {"description":"Required to confer preferential recognition of cytosine over thymine","evidences":[{"source":"PubMed","id":"18772889","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI31
Number of Residues1
DetailsSite: {"description":"Required to discriminate between hemimethylated DNA versus symmetrically methylated DNA","evidences":[{"source":"PubMed","id":"18772889","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI32
Number of Residues1
DetailsSite: {"description":"Required for affinity and specificity for 5-mCpG sequence","evidences":[{"source":"PubMed","id":"18772889","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI33
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17081983","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18220336","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"}]}
ChainResidueDetails
site_idSWS_FT_FI34
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by PKA","evidences":[{"source":"PubMed","id":"15178447","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22837395","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI35
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI36
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI37
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI38
Number of Residues1
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_FI39
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"25218447","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

253091

PDB entries from 2026-05-06

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