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

8AAG

H1-bound palindromic nucleosome, state 1

Functional Information from GO Data
ChainGOidnamespacecontents
A0000786cellular_componentnucleosome
A0003677molecular_functionDNA binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005694cellular_componentchromosome
A0006325biological_processchromatin organization
A0006334biological_processnucleosome assembly
A0030527molecular_functionstructural constituent of chromatin
A0046982molecular_functionprotein heterodimerization activity
A0070062cellular_componentextracellular exosome
B0000781cellular_componentchromosome, telomeric region
B0000786cellular_componentnucleosome
B0003677molecular_functionDNA binding
B0003723molecular_functionRNA binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005694cellular_componentchromosome
B0006325biological_processchromatin organization
B0006334biological_processnucleosome assembly
B0016020cellular_componentmembrane
B0030527molecular_functionstructural constituent of chromatin
B0032200biological_processtelomere organization
B0032991cellular_componentprotein-containing complex
B0043505cellular_componentCENP-A containing nucleosome
B0045653biological_processnegative regulation of megakaryocyte differentiation
B0046982molecular_functionprotein heterodimerization activity
B0061644biological_processprotein localization to CENP-A containing chromatin
B0070062cellular_componentextracellular exosome
C0000786cellular_componentnucleosome
C0003677molecular_functionDNA binding
C0005634cellular_componentnucleus
C0005694cellular_componentchromosome
C0030527molecular_functionstructural constituent of chromatin
C0046982molecular_functionprotein heterodimerization activity
D0000786cellular_componentnucleosome
D0003677molecular_functionDNA binding
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005694cellular_componentchromosome
D0030527molecular_functionstructural constituent of chromatin
D0046982molecular_functionprotein heterodimerization activity
E0000786cellular_componentnucleosome
E0003677molecular_functionDNA binding
E0005515molecular_functionprotein binding
E0005576cellular_componentextracellular region
E0005634cellular_componentnucleus
E0005654cellular_componentnucleoplasm
E0005694cellular_componentchromosome
E0006325biological_processchromatin organization
E0006334biological_processnucleosome assembly
E0030527molecular_functionstructural constituent of chromatin
E0046982molecular_functionprotein heterodimerization activity
E0070062cellular_componentextracellular exosome
F0000781cellular_componentchromosome, telomeric region
F0000786cellular_componentnucleosome
F0003677molecular_functionDNA binding
F0003723molecular_functionRNA binding
F0005515molecular_functionprotein binding
F0005576cellular_componentextracellular region
F0005634cellular_componentnucleus
F0005654cellular_componentnucleoplasm
F0005694cellular_componentchromosome
F0006325biological_processchromatin organization
F0006334biological_processnucleosome assembly
F0016020cellular_componentmembrane
F0030527molecular_functionstructural constituent of chromatin
F0032200biological_processtelomere organization
F0032991cellular_componentprotein-containing complex
F0043505cellular_componentCENP-A containing nucleosome
F0045653biological_processnegative regulation of megakaryocyte differentiation
F0046982molecular_functionprotein heterodimerization activity
F0061644biological_processprotein localization to CENP-A containing chromatin
F0070062cellular_componentextracellular exosome
G0000786cellular_componentnucleosome
G0003677molecular_functionDNA binding
G0005634cellular_componentnucleus
G0005694cellular_componentchromosome
G0030527molecular_functionstructural constituent of chromatin
G0046982molecular_functionprotein heterodimerization activity
H0000786cellular_componentnucleosome
H0003677molecular_functionDNA binding
H0005515molecular_functionprotein binding
H0005634cellular_componentnucleus
H0005694cellular_componentchromosome
H0030527molecular_functionstructural constituent of chromatin
H0046982molecular_functionprotein heterodimerization activity
Z0000786cellular_componentnucleosome
Z0003677molecular_functionDNA binding
Z0003690molecular_functiondouble-stranded DNA binding
Z0005634cellular_componentnucleus
Z0005694cellular_componentchromosome
Z0006334biological_processnucleosome assembly
Z0030261biological_processchromosome condensation
Z0030527molecular_functionstructural constituent of chromatin
Z0031492molecular_functionnucleosomal DNA binding
Z0045910biological_processnegative regulation of DNA recombination
Functional Information from PROSITE/UniProt
site_idPS00046
Number of Residues7
DetailsHISTONE_H2A Histone H2A signature. AGLqFPV
ChainResidueDetails
CALA21-VAL27

site_idPS00047
Number of Residues5
DetailsHISTONE_H4 Histone H4 signature. GAKRH
ChainResidueDetails
BGLY14-HIS18

site_idPS00322
Number of Residues7
DetailsHISTONE_H3_1 Histone H3 signature 1. KAPRKQL
ChainResidueDetails
ALYS14-LEU20

site_idPS00357
Number of Residues23
DetailsHISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG
ChainResidueDetails
DARG89-GLY111

site_idPS00959
Number of Residues9
DetailsHISTONE_H3_2 Histone H3 signature 2. PFqRLVREI
ChainResidueDetails
APRO66-ILE74

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P0C1H4
ChainResidueDetails
DLYS2
DLYS9
DLYS12
DLYS17
HLYS2
HLYS9
HLYS12
HLYS17

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:12757711
ChainResidueDetails
DSER11
HSER11

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807
ChainResidueDetails
DSER109
HSER109
GLYS9
GLYS95
ELYS18
ELYS64

site_idSWS_FT_FI4
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0C1H4
ChainResidueDetails
DLYS117
GLYS36
HLYS117

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8
ChainResidueDetails
CLYS74
CLYS75
GLYS74
GLYS75
FLYS16
FLYS44

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N5-methylglutamine => ECO:0000250
ChainResidueDetails
CGLN104
GGLN104
BLYS77
BLYS91
FLYS12
FLYS31
FLYS77
FLYS91

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8
ChainResidueDetails
CLYS118
GLYS118

site_idSWS_FT_FI8
Number of Residues8
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250
ChainResidueDetails
CLYS13
ESER10
CLYS15
CLYS119
GLYS13
GLYS15
GLYS119

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by PKC => ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:18066052, ECO:0000269|PubMed:22901803
ChainResidueDetails
ATHR11
ETHR11

site_idSWS_FT_FI10
Number of Residues4
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435
ChainResidueDetails
ALYS14
ALYS56
ELYS14
ELYS56

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Citrulline; alternate => ECO:0000269|PubMed:15345777, ECO:0000269|PubMed:16497732, ECO:0000269|PubMed:16567635
ChainResidueDetails
AARG17
EARG17

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:17194708
ChainResidueDetails
ALYS23
ELYS23

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: Citrulline => ECO:0000269|PubMed:16567635
ChainResidueDetails
AARG26
EARG26

site_idSWS_FT_FI14
Number of Residues4
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16627869, ECO:0000269|PubMed:17194708
ChainResidueDetails
ALYS27
ALYS36
ELYS27
ELYS36

site_idSWS_FT_FI15
Number of Residues2
DetailsMOD_RES: Phosphoserine; alternate; by AURKB, AURKC and RPS6KA5 => ECO:0000269|PubMed:10464286, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:15684425, ECO:0000269|PubMed:16185088
ChainResidueDetails
ASER28
ESER28
FLYS91

site_idSWS_FT_FI16
Number of Residues2
DetailsMOD_RES: N6-methyllysine => ECO:0000250|UniProtKB:P68431
ChainResidueDetails
ALYS37
ELYS37
BLYS79
FLYS20
FLYS59
FLYS79

site_idSWS_FT_FI17
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000269|PubMed:19783980
ChainResidueDetails
ATYR41
ETYR41

site_idSWS_FT_FI18
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:20850016
ChainResidueDetails
ASER57
ESER57

site_idSWS_FT_FI19
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:29211711
ChainResidueDetails
ALYS79
ELYS79

site_idSWS_FT_FI20
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:20850016
ChainResidueDetails
ATHR80
ETHR80

site_idSWS_FT_FI21
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P84243
ChainResidueDetails
ASER86
ESER86

site_idSWS_FT_FI22
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332
ChainResidueDetails
ATHR107
ETHR107

site_idSWS_FT_FI23
Number of Residues2
DetailsMOD_RES: N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297
ChainResidueDetails
ALYS115
ELYS115

site_idSWS_FT_FI24
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:27436229
ChainResidueDetails
ALYS122
ELYS122

site_idSWS_FT_FI25
Number of Residues2
DetailsLIPID: N6-decanoyllysine => ECO:0000269|PubMed:35939806
ChainResidueDetails
ALYS18
ELYS18

site_idSWS_FT_FI26
Number of Residues2
DetailsLIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:21076176
ChainResidueDetails
ACYS110
ECYS110

224201

PDB entries from 2024-08-28

PDB statisticsPDBj update infoContact PDBjnumon