5BT1
histone chaperone Hif1 playing with histone H2A-H2B dimer
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000123 | cellular_component | histone acetyltransferase complex |
A | 0000781 | cellular_component | chromosome, telomeric region |
A | 0005515 | molecular_function | protein binding |
A | 0005634 | cellular_component | nucleus |
A | 0006325 | biological_process | chromatin organization |
A | 0006334 | biological_process | nucleosome assembly |
A | 0031509 | biological_process | subtelomeric heterochromatin formation |
A | 0042393 | molecular_function | histone binding |
A | 0042803 | molecular_function | protein homodimerization activity |
B | 0000123 | cellular_component | histone acetyltransferase complex |
B | 0000781 | cellular_component | chromosome, telomeric region |
B | 0005515 | molecular_function | protein binding |
B | 0005634 | cellular_component | nucleus |
B | 0006325 | biological_process | chromatin organization |
B | 0006334 | biological_process | nucleosome assembly |
B | 0031509 | biological_process | subtelomeric heterochromatin formation |
B | 0042393 | molecular_function | histone binding |
B | 0042803 | molecular_function | protein homodimerization activity |
C | 0000122 | biological_process | negative regulation of transcription by RNA polymerase II |
C | 0000786 | cellular_component | nucleosome |
C | 0003677 | molecular_function | DNA binding |
C | 0005515 | molecular_function | protein binding |
C | 0005634 | cellular_component | nucleus |
C | 0005694 | cellular_component | chromosome |
C | 0006281 | biological_process | DNA repair |
C | 0006325 | biological_process | chromatin organization |
C | 0006974 | biological_process | DNA damage response |
C | 0030527 | molecular_function | structural constituent of chromatin |
C | 0031298 | cellular_component | replication fork protection complex |
C | 0031492 | molecular_function | nucleosomal DNA binding |
C | 0032991 | cellular_component | protein-containing complex |
C | 0046982 | molecular_function | protein heterodimerization activity |
C | 0070828 | biological_process | heterochromatin organization |
D | 0000122 | biological_process | negative regulation of transcription by RNA polymerase II |
D | 0000786 | cellular_component | nucleosome |
D | 0003677 | molecular_function | DNA binding |
D | 0005515 | molecular_function | protein binding |
D | 0005634 | cellular_component | nucleus |
D | 0005694 | cellular_component | chromosome |
D | 0006301 | biological_process | postreplication repair |
D | 0006325 | biological_process | chromatin organization |
D | 0006355 | biological_process | regulation of DNA-templated transcription |
D | 0030527 | molecular_function | structural constituent of chromatin |
D | 0031298 | cellular_component | replication fork protection complex |
D | 0032991 | cellular_component | protein-containing complex |
D | 0046982 | molecular_function | protein heterodimerization activity |
Functional Information from PROSITE/UniProt
site_id | PS00014 |
Number of Residues | 4 |
Details | ER_TARGET Endoplasmic reticulum targeting sequence. SQEL |
Chain | Residue | Details |
C | SER128-LEU131 |
site_id | PS00046 |
Number of Residues | 7 |
Details | HISTONE_H2A Histone H2A signature. AGLtFPV |
Chain | Residue | Details |
C | ALA22-VAL28 |
site_id | PS00357 |
Number of Residues | 23 |
Details | HISTONE_H2B Histone H2B signature. REIQTavRlILpGELaKHAVSEG |
Chain | Residue | Details |
D | ARG95-GLY117 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000269|PubMed:16598039 |
Chain | Residue | Details |
D | LYS6 | |
D | LYS7 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:15652479, ECO:0000269|PubMed:15970663 |
Chain | Residue | Details |
D | SER10 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:11545749, ECO:0000269|PubMed:15186774 |
Chain | Residue | Details |
D | LYS11 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000269|PubMed:11545749, ECO:0000269|PubMed:15186774, ECO:0000269|PubMed:16598039, ECO:0000269|PubMed:19113941 |
Chain | Residue | Details |
D | LYS16 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000269|PubMed:19113941 |
Chain | Residue | Details |
D | LYS17 | |
C | LYS21 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: N6-butyryllysine; alternate => ECO:0000269|PubMed:19113941 |
Chain | Residue | Details |
D | LYS21 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:19113941 |
Chain | Residue | Details |
D | LYS22 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine => ECO:0000269|PubMed:22389435 |
Chain | Residue | Details |
D | LYS34 | |
D | LYS46 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: N6,N6-dimethyllysine => ECO:0000269|PubMed:19113941 |
Chain | Residue | Details |
D | LYS37 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate |
Chain | Residue | Details |
D | LYS6 | |
D | LYS7 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:10642555, ECO:0000269|PubMed:12535538, ECO:0000269|PubMed:12535539, ECO:0000269|PubMed:14660635, ECO:0000269|PubMed:15280549, ECO:0000269|PubMed:16432255 |
Chain | Residue | Details |
D | LYS123 |
site_id | SWS_FT_FI12 |
Number of Residues | 2 |
Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate => ECO:0000305 |
Chain | Residue | Details |
D | LYS16 | |
D | LYS17 |