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

3CFS

Structural basis of the interaction of RbAp46/RbAp48 with histone H4

Functional Information from GO Data
ChainGOidnamespacecontents
B0000118cellular_componenthistone deacetylase complex
B0000122biological_processnegative regulation of transcription by RNA polymerase II
B0000123cellular_componenthistone acetyltransferase complex
B0000781cellular_componentchromosome, telomeric region
B0003723molecular_functionRNA binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0006260biological_processDNA replication
B0006325biological_processchromatin organization
B0006338biological_processchromatin remodeling
B0006355biological_processregulation of DNA-templated transcription
B0007420biological_processbrain development
B0016581cellular_componentNuRD complex
B0016589cellular_componentNURF complex
B0030308biological_processnegative regulation of cell growth
B0030336biological_processnegative regulation of cell migration
B0030512biological_processnegative regulation of transforming growth factor beta receptor signaling pathway
B0031507biological_processheterochromatin formation
B0035098cellular_componentESC/E(Z) complex
B0042393molecular_functionhistone binding
B0042659biological_processregulation of cell fate specification
B0045892biological_processnegative regulation of DNA-templated transcription
B0045893biological_processpositive regulation of DNA-templated transcription
B0048545biological_processresponse to steroid hormone
B0070370biological_processcellular heat acclimation
B0070822cellular_componentSin3-type complex
B1902455biological_processnegative regulation of stem cell population maintenance
B1902459biological_processpositive regulation of stem cell population maintenance
B1904949cellular_componentATPase complex
B2000736biological_processregulation of stem cell differentiation
E0046982molecular_functionprotein heterodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE ARS B 412
ChainResidue
BCYS116

Functional Information from PROSITE/UniProt
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LLSAsdDhTVCLWDI
ChainResidueDetails
BLEU192-ILE206
BLEU288-LEU302
BLEU332-LEU346

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues45
DetailsRepeat: {"description":"WD 2"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues36
DetailsRepeat: {"description":"WD 3"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues41
DetailsRepeat: {"description":"WD 4"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues37
DetailsRepeat: {"description":"WD 5"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues51
DetailsRepeat: {"description":"WD 6"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q60973","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q60973","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
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_FI11
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"25772364","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"22389435","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI14
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

246031

PDB entries from 2025-12-10

PDB statisticsPDBj update infoContact PDBjnumon