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6UPK

Structure of FACT_subnucleosome complex 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
A0010467biological_processgene expression
A0016020cellular_componentmembrane
A0030527molecular_functionstructural constituent of chromatin
A0032200biological_processtelomere organization
A0032991cellular_componentprotein-containing complex
A0040029biological_processepigenetic regulation of gene expression
A0043229cellular_componentintracellular organelle
A0045296molecular_functioncadherin binding
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
C0003674molecular_functionmolecular_function
C0003677molecular_functionDNA binding
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005694cellular_componentchromosome
C0008285biological_processnegative regulation of cell population proliferation
C0030527molecular_functionstructural constituent of chromatin
C0031492molecular_functionnucleosomal DNA binding
C0031507biological_processheterochromatin formation
C0043229cellular_componentintracellular organelle
C0046982molecular_functionprotein heterodimerization activity
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
D0006334biological_processnucleosome assembly
D0019731biological_processantibacterial humoral response
D0030527molecular_functionstructural constituent of chromatin
D0042742biological_processdefense response to bacterium
D0042802molecular_functionidentical protein binding
D0043229cellular_componentintracellular organelle
D0046982molecular_functionprotein heterodimerization activity
D0050830biological_processdefense response to Gram-positive bacterium
D0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
D0070062cellular_componentextracellular exosome
E0000786cellular_componentnucleosome
E0003677molecular_functionDNA binding
E0005515molecular_functionprotein binding
E0005576cellular_componentextracellular region
E0005634cellular_componentnucleus
E0005654cellular_componentnucleoplasm
E0005694cellular_componentchromosome
E0006325biological_processchromatin organization
E0006334biological_processnucleosome assembly
E0010467biological_processgene expression
E0016020cellular_componentmembrane
E0030527molecular_functionstructural constituent of chromatin
E0032200biological_processtelomere organization
E0032991cellular_componentprotein-containing complex
E0040029biological_processepigenetic regulation of gene expression
E0043229cellular_componentintracellular organelle
E0045296molecular_functioncadherin binding
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
G0035101cellular_componentFACT complex
H0003677molecular_functionDNA binding
H0003682molecular_functionchromatin binding
H0003723molecular_functionRNA binding
H0005515molecular_functionprotein binding
H0005634cellular_componentnucleus
H0005654cellular_componentnucleoplasm
H0005694cellular_componentchromosome
H0005730cellular_componentnucleolus
H0006260biological_processDNA replication
H0006281biological_processDNA repair
H0006334biological_processnucleosome assembly
H0006337biological_processnucleosome disassembly
H0031491molecular_functionnucleosome binding
H0035101cellular_componentFACT complex
H0042393molecular_functionhistone binding
H1902275biological_processregulation of chromatin organization
Functional Information from PROSITE/UniProt
site_idPS00047
Number of Residues5
DetailsHISTONE_H4 Histone H4 signature. GAKRH
ChainResidueDetails
BGLY14-HIS18

site_idPS00046
Number of Residues7
DetailsHISTONE_H2A Histone H2A signature. AGLqFPV
ChainResidueDetails
CALA21-VAL27

site_idPS00357
Number of Residues23
DetailsHISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG
ChainResidueDetails
DARG92-GLY114

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

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 Residues68
DetailsDNA_BIND: HMG box => ECO:0000255|PROSITE-ProRule:PRU00267
ChainResidueDetails
HPRO547-GLU615
FLYS16-LYS20

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Cleavage; by caspase-3 and/or caspase-7
ChainResidueDetails
HASP450
GLYS196
GLYS223
GLYS732
GLYS786
GLYS904

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0000269|Ref.3, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378
ChainResidueDetails
HALA2
DLYS11
DLYS15
DLYS16
DLYS20
DLYS23
DLYS43
DLYS85

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231
ChainResidueDetails
HTHR170
GSER658

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
HLYS233
HLYS413
BLYS44
FLYS8
FLYS16
FLYS44

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648
ChainResidueDetails
HSER437
BLYS31
BLYS77
BLYS91
FLYS12
FLYS31
FLYS77
FLYS91

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q08943
ChainResidueDetails
HTYR441
HTYR452

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
HSER444
DLYS116
DLYS120

site_idSWS_FT_FI9
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
HSER471
CLYS119
CLYS125

site_idSWS_FT_FI10
Number of Residues1
DetailsMOD_RES: Phosphoserine; by CK2 => ECO:0000305|PubMed:15659405
ChainResidueDetails
HSER510
GLYS647
ELYS14
ELYS56

site_idSWS_FT_FI11
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q08943
ChainResidueDetails
HLYS542
DLYS108

site_idSWS_FT_FI12
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
HLYS90
CLYS119
HLYS296
HLYS364

site_idSWS_FT_FI13
Number of Residues1
DetailsMOD_RES: Dimethylated arginine => ECO:0000250|UniProtKB:Q96A08
ChainResidueDetails
DARG79
FTYR88

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08
ChainResidueDetails
DARG86
DARG92

site_idSWS_FT_FI15
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q00729
ChainResidueDetails
DTHR115
BLYS91
FLYS91

site_idSWS_FT_FI16
Number of Residues1
DetailsCARBOHYD: O-linked (GlcNAc) serine => ECO:0000269|PubMed:22121020
ChainResidueDetails
DSER112
BLYS59
BLYS79
FLYS20
FLYS59
FLYS79

site_idSWS_FT_FI17
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P58876
ChainResidueDetails
DLYS5
FLYS31

site_idSWS_FT_FI18
Number of Residues2
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, ECO:0000269|PubMed:22121020
ChainResidueDetails
ALYS37
DLYS120

site_idSWS_FT_FI19
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:Q5QNW6
ChainResidueDetails
DLYS20
ETYR41

site_idSWS_FT_FI20
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:21726816
ChainResidueDetails
DLYS34
ESER57

site_idSWS_FT_FI21
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:29211711
ChainResidueDetails
ALYS79
ELYS79

site_idSWS_FT_FI22
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:20850016
ChainResidueDetails
ATHR80
ETHR80

site_idSWS_FT_FI23
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P84243
ChainResidueDetails
ASER86
ESER86

site_idSWS_FT_FI24
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ATHR107
ETHR107

site_idSWS_FT_FI25
Number of Residues2
DetailsMOD_RES: N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297
ChainResidueDetails
ALYS115
ELYS115

site_idSWS_FT_FI26
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:27436229
ChainResidueDetails
ALYS122
ELYS122

site_idSWS_FT_FI27
Number of Residues2
DetailsLIPID: N6-decanoyllysine => ECO:0000269|PubMed:35939806
ChainResidueDetails
ALYS18
ELYS18

219140

PDB entries from 2024-05-01

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