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3C9C

Structural Basis of Histone H4 Recognition by p55

Functional Information from GO Data
ChainGOidnamespacecontents
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0000976molecular_functiontranscription cis-regulatory region binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005667cellular_componenttranscription regulator complex
A0005700cellular_componentpolytene chromosome
A0006325biological_processchromatin organization
A0006335biological_processDNA replication-dependent chromatin assembly
A0006338biological_processchromatin remodeling
A0006355biological_processregulation of DNA-templated transcription
A0007307biological_processeggshell chorion gene amplification
A0007346biological_processregulation of mitotic cell cycle
A0007379biological_processsegment specification
A0016581cellular_componentNuRD complex
A0016589cellular_componentNURF complex
A0031491molecular_functionnucleosome binding
A0031507biological_processheterochromatin formation
A0031523cellular_componentMyb complex
A0033186cellular_componentCAF-1 complex
A0034728biological_processnucleosome organization
A0035097cellular_componenthistone methyltransferase complex
A0035098cellular_componentESC/E(Z) complex
A0042393molecular_functionhistone binding
A0042803molecular_functionprotein homodimerization activity
A0042826molecular_functionhistone deacetylase binding
A0045892biological_processnegative regulation of DNA-templated transcription
A0045893biological_processpositive regulation of DNA-templated transcription
A0070822cellular_componentSin3-type complex
A0090575cellular_componentRNA polymerase II transcription regulator complex
A0140718biological_processfacultative heterochromatin formation
B0003677molecular_functionDNA binding
B0030527molecular_functionstructural constituent of chromatin
B0046982molecular_functionprotein heterodimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CD A 431
ChainResidue
ACYS116
AASN140
ACYS142

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD A 432
ChainResidue
ACYS116
AGLU120
ACYS142
ATHR159

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CD A 433
ChainResidue
AHIS161
ACYS171

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CD A 434
ChainResidue
AASP236
ACYS282
AGLN326

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CD A 436
ChainResidue
AGLU45
AHIS82

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CD A 437
ChainResidue
ACYS116
AASN140

Functional Information from PROSITE/UniProt
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. LLSAsdDhTICLWDI
ChainResidueDetails
ALEU197-ILE211
ALEU293-LEU307
ALEU337-LEU351

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues33
DetailsRepeat: {"description":"WD 1"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues31
DetailsRepeat: {"description":"WD 2"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues31
DetailsRepeat: {"description":"WD 3"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues31
DetailsRepeat: {"description":"WD 4"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues31
DetailsRepeat: {"description":"WD 5"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues31
DetailsRepeat: {"description":"WD 6"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17372656","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"22389435","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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