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 | 0006351 | biological_process | DNA-templated transcription |
| 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 | 0006351 | biological_process | DNA-templated transcription |
| 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 | 0031507 | biological_process | heterochromatin formation |
| C | 0046982 | molecular_function | protein heterodimerization activity |
| 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 | DNA damage tolerance |
| D | 0006325 | biological_process | chromatin organization |
| D | 0006355 | biological_process | regulation of DNA-templated transcription |
| D | 0030527 | molecular_function | structural constituent of chromatin |
| 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 | 68 |
| Details | Repeat: {"description":"TPR 1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 66 |
| Details | Repeat: {"description":"TPR 2","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 66 |
| Details | Repeat: {"description":"TPR 3","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 168 |
| Details | Region: {"description":"Interaction with dimeric histone H2A and H2B","evidences":[{"source":"PubMed","id":"27618665","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"22389435","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6,N6-dimethyllysine","evidences":[{"source":"PubMed","id":"19113941","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"10642555","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12535538","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12535539","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14660635","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15280549","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16432255","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
