Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5BT1

histone chaperone Hif1 playing with histone H2A-H2B dimer

Functional Information from GO Data
ChainGOidnamespacecontents
A0000123cellular_componenthistone acetyltransferase complex
A0000781cellular_componentchromosome, telomeric region
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0006325biological_processchromatin organization
A0006334biological_processnucleosome assembly
A0031509biological_processsubtelomeric heterochromatin formation
A0042393molecular_functionhistone binding
A0042803molecular_functionprotein homodimerization activity
B0000123cellular_componenthistone acetyltransferase complex
B0000781cellular_componentchromosome, telomeric region
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0006325biological_processchromatin organization
B0006334biological_processnucleosome assembly
B0031509biological_processsubtelomeric heterochromatin formation
B0042393molecular_functionhistone binding
B0042803molecular_functionprotein homodimerization activity
C0000122biological_processnegative regulation of transcription by RNA polymerase II
C0000786cellular_componentnucleosome
C0003677molecular_functionDNA binding
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005694cellular_componentchromosome
C0006281biological_processDNA repair
C0006325biological_processchromatin organization
C0006974biological_processDNA damage response
C0030527molecular_functionstructural constituent of chromatin
C0031298cellular_componentreplication fork protection complex
C0031492molecular_functionnucleosomal DNA binding
C0032991cellular_componentprotein-containing complex
C0046982molecular_functionprotein heterodimerization activity
C0070828biological_processheterochromatin organization
D0000122biological_processnegative regulation of transcription by RNA polymerase II
D0000786cellular_componentnucleosome
D0003677molecular_functionDNA binding
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005694cellular_componentchromosome
D0006301biological_processpostreplication repair
D0006325biological_processchromatin organization
D0006355biological_processregulation of DNA-templated transcription
D0030527molecular_functionstructural constituent of chromatin
D0031298cellular_componentreplication fork protection complex
D0032991cellular_componentprotein-containing complex
D0046982molecular_functionprotein heterodimerization activity
Functional Information from PROSITE/UniProt
site_idPS00014
Number of Residues4
DetailsER_TARGET Endoplasmic reticulum targeting sequence. SQEL
ChainResidueDetails
CSER128-LEU131

site_idPS00046
Number of Residues7
DetailsHISTONE_H2A Histone H2A signature. AGLtFPV
ChainResidueDetails
CALA22-VAL28

site_idPS00357
Number of Residues23
DetailsHISTONE_H2B Histone H2B signature. REIQTavRlILpGELaKHAVSEG
ChainResidueDetails
DARG95-GLY117

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000269|PubMed:16598039
ChainResidueDetails
DLYS6
DLYS7

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:15652479, ECO:0000269|PubMed:15970663
ChainResidueDetails
DSER10

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:11545749, ECO:0000269|PubMed:15186774
ChainResidueDetails
DLYS11

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000269|PubMed:11545749, ECO:0000269|PubMed:15186774, ECO:0000269|PubMed:16598039, ECO:0000269|PubMed:19113941
ChainResidueDetails
DLYS16

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000269|PubMed:19113941
ChainResidueDetails
DLYS17
CLYS21

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-butyryllysine; alternate => ECO:0000269|PubMed:19113941
ChainResidueDetails
DLYS21

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:19113941
ChainResidueDetails
DLYS22

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000269|PubMed:22389435
ChainResidueDetails
DLYS34
DLYS46

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: N6,N6-dimethyllysine => ECO:0000269|PubMed:19113941
ChainResidueDetails
DLYS37

site_idSWS_FT_FI10
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
ChainResidueDetails
DLYS6
DLYS7

site_idSWS_FT_FI11
Number of Residues2
DetailsCROSSLNK: 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
ChainResidueDetails
DLYS123

site_idSWS_FT_FI12
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate => ECO:0000305
ChainResidueDetails
DLYS16
DLYS17

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon