3C99
Structural Basis of Histone H4 Recognition by p55
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000122 | biological_process | negative regulation of transcription by RNA polymerase II |
A | 0000976 | molecular_function | transcription cis-regulatory region binding |
A | 0005515 | molecular_function | protein binding |
A | 0005634 | cellular_component | nucleus |
A | 0005667 | cellular_component | transcription regulator complex |
A | 0005700 | cellular_component | polytene chromosome |
A | 0006325 | biological_process | chromatin organization |
A | 0006335 | biological_process | DNA replication-dependent chromatin assembly |
A | 0006338 | biological_process | chromatin remodeling |
A | 0006355 | biological_process | regulation of DNA-templated transcription |
A | 0007307 | biological_process | eggshell chorion gene amplification |
A | 0007346 | biological_process | regulation of mitotic cell cycle |
A | 0007379 | biological_process | segment specification |
A | 0016581 | cellular_component | NuRD complex |
A | 0016589 | cellular_component | NURF complex |
A | 0031491 | molecular_function | nucleosome binding |
A | 0031507 | biological_process | heterochromatin formation |
A | 0031523 | cellular_component | Myb complex |
A | 0033186 | cellular_component | CAF-1 complex |
A | 0034728 | biological_process | nucleosome organization |
A | 0035097 | cellular_component | histone methyltransferase complex |
A | 0035098 | cellular_component | ESC/E(Z) complex |
A | 0042393 | molecular_function | histone binding |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0042826 | molecular_function | histone deacetylase binding |
A | 0045892 | biological_process | negative regulation of DNA-templated transcription |
A | 0045893 | biological_process | positive regulation of DNA-templated transcription |
A | 0070822 | cellular_component | Sin3-type complex |
A | 0090575 | cellular_component | RNA polymerase II transcription regulator complex |
A | 0140718 | biological_process | facultative heterochromatin formation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CD A 431 |
Chain | Residue |
A | CYS116 |
A | ASN140 |
A | CYS142 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CD A 432 |
Chain | Residue |
A | CYS116 |
A | GLU120 |
A | CYS142 |
A | THR159 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CD A 433 |
Chain | Residue |
A | GLN326 |
A | ASP236 |
A | CYS282 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CD A 434 |
Chain | Residue |
A | HIS161 |
A | CYS171 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CD A 435 |
Chain | Residue |
A | GLU45 |
A | HIS82 |
A | LYS124 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CD A 436 |
Chain | Residue |
A | HIS75 |
A | SER77 |
A | GLU130 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CD A 437 |
Chain | Residue |
A | HIS82 |
A | ASN126 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE CD A 439 |
Chain | Residue |
A | HIS243 |
A | SER245 |
Functional Information from PROSITE/UniProt
site_id | PS00678 |
Number of Residues | 15 |
Details | WD_REPEATS_1 Trp-Asp (WD) repeats signature. LLSAsdDhTICLWDI |
Chain | Residue | Details |
A | LEU197-ILE211 | |
A | LEU293-LEU307 | |
A | LEU337-LEU351 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:17372656 |
Chain | Residue | Details |
A | SER11 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:18327897 |
Chain | Residue | Details |
A | SER100 |