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7PEX

Nucleosome 2 of the 4x177 nucleosome array containing H1

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
c0005515molecular_functionprotein binding
c0005634cellular_componentnucleus
c0005694cellular_componentchromosome
c0006325biological_processchromatin organization
c0008285biological_processnegative regulation of cell population proliferation
c0030527molecular_functionstructural constituent of chromatin
c0031507biological_processheterochromatin formation
c0043505cellular_componentCENP-A containing nucleosome
c0046982molecular_functionprotein heterodimerization activity
c0061644biological_processprotein localization to CENP-A containing chromatin
c0070062cellular_componentextracellular exosome
d0000786cellular_componentnucleosome
d0002227biological_processinnate immune response in mucosa
d0003677molecular_functionDNA binding
d0005515molecular_functionprotein binding
d0005615cellular_componentextracellular space
d0005634cellular_componentnucleus
d0005654cellular_componentnucleoplasm
d0005694cellular_componentchromosome
d0005829cellular_componentcytosol
d0019731biological_processantibacterial humoral response
d0030527molecular_functionstructural constituent of chromatin
d0031640biological_processkilling of cells of another organism
d0042742biological_processdefense response to bacterium
d0046982molecular_functionprotein heterodimerization activity
d0050829biological_processdefense response to Gram-negative bacterium
d0050830biological_processdefense response to Gram-positive bacterium
d0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
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
g0005515molecular_functionprotein binding
g0005634cellular_componentnucleus
g0005694cellular_componentchromosome
g0006325biological_processchromatin organization
g0008285biological_processnegative regulation of cell population proliferation
g0030527molecular_functionstructural constituent of chromatin
g0031507biological_processheterochromatin formation
g0043505cellular_componentCENP-A containing nucleosome
g0046982molecular_functionprotein heterodimerization activity
g0061644biological_processprotein localization to CENP-A containing chromatin
g0070062cellular_componentextracellular exosome
h0000786cellular_componentnucleosome
h0002227biological_processinnate immune response in mucosa
h0003677molecular_functionDNA binding
h0005515molecular_functionprotein binding
h0005615cellular_componentextracellular space
h0005634cellular_componentnucleus
h0005654cellular_componentnucleoplasm
h0005694cellular_componentchromosome
h0005829cellular_componentcytosol
h0019731biological_processantibacterial humoral response
h0030527molecular_functionstructural constituent of chromatin
h0031640biological_processkilling of cells of another organism
h0042742biological_processdefense response to bacterium
h0046982molecular_functionprotein heterodimerization activity
h0050829biological_processdefense response to Gram-negative bacterium
h0050830biological_processdefense response to Gram-positive bacterium
h0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
u0000122biological_processnegative regulation of transcription by RNA polymerase II
u0000786cellular_componentnucleosome
u0000791cellular_componenteuchromatin
u0000792cellular_componentheterochromatin
u0003677molecular_functionDNA binding
u0003690molecular_functiondouble-stranded DNA binding
u0003723molecular_functionRNA binding
u0005515molecular_functionprotein binding
u0005634cellular_componentnucleus
u0005694cellular_componentchromosome
u0006325biological_processchromatin organization
u0006334biological_processnucleosome assembly
u0006357biological_processregulation of transcription by RNA polymerase II
u0030261biological_processchromosome condensation
u0030527molecular_functionstructural constituent of chromatin
u0031490molecular_functionchromatin DNA binding
u0031492molecular_functionnucleosomal DNA binding
u0042826molecular_functionhistone deacetylase binding
u0045910biological_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
dARG92-GLY114

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 Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P15865
ChainResidueDetails
uSER1
hPRO1

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P43274
ChainResidueDetails
uLYS16
hGLU2

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
uTHR17
hLYS11
hLYS15
hLYS16
hLYS20
hLYS23
hLYS43
hLYS85
dLYS11
dLYS15
dLYS16
dLYS20
dLYS23
dLYS43
dLYS85
hLYS5

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:3782055
ChainResidueDetails
uLYS25
hSER6
gLYS9
gLYS95

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P43274
ChainResidueDetails
uLYS33
hLYS12
bLYS44
fLYS8
fLYS16
fLYS44

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P43274
ChainResidueDetails
uSER35
hSER14
bLYS77
bLYS91
fLYS12
fLYS31
fLYS77
fLYS91

site_idSWS_FT_FI7
Number of Residues5
DetailsMOD_RES: N6-(beta-hydroxybutyryl)lysine => ECO:0000250|UniProtKB:P43277
ChainResidueDetails
uLYS51
uLYS63
uLYS84
uLYS89
uLYS105

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Citrulline => ECO:0000250|UniProtKB:P43274
ChainResidueDetails
uARG53
dLYS116
dLYS120
hLYS34
hLYS116
hLYS120

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:20068231
ChainResidueDetails
uTHR145
hGLU35
cLYS125
gLYS118
gLYS119
gLYS125

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: ADP-ribosylserine => ECO:0000269|PubMed:27723750
ChainResidueDetails
uSER149
hSER36
eLYS14
eLYS56

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692
ChainResidueDetails
uSER186
dLYS108
hLYS46
hLYS108

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000269|PubMed:24681537
ChainResidueDetails
dLYS57
hLYS57
gLYS119

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: Dimethylated arginine => ECO:0000250|UniProtKB:Q96A08
ChainResidueDetails
dARG79
hARG79

site_idSWS_FT_FI14
Number of Residues4
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08
ChainResidueDetails
dARG86
dARG92
hARG86
hARG92

site_idSWS_FT_FI15
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q00729
ChainResidueDetails
dTHR115
hTHR115
fLYS91

site_idSWS_FT_FI16
Number of Residues2
DetailsCARBOHYD: O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807
ChainResidueDetails
dSER112
hSER112
bLYS79
fLYS20
fLYS59
fLYS79

site_idSWS_FT_FI17
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P58876
ChainResidueDetails
dLYS5
hLYS5

site_idSWS_FT_FI18
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:16627869, ECO:0000269|PubMed:16713563
ChainResidueDetails
aSER57
dLYS120
hLYS120

site_idSWS_FT_FI19
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:Q5QNW6
ChainResidueDetails
dLYS20
hLYS20

site_idSWS_FT_FI20
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:21726816
ChainResidueDetails
dLYS34
hLYS34

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
aALA110
eALA110

227111

PDB entries from 2024-11-06

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