Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8OF4

Nucleosome Bound human SIRT6 (Composite)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000786	cellular_component	nucleosome
A	0003677	molecular_function	DNA binding
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005694	cellular_component	chromosome
A	0030527	molecular_function	structural constituent of chromatin
A	0046982	molecular_function	protein heterodimerization activity
B	0000786	cellular_component	nucleosome
B	0003677	molecular_function	DNA binding
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005694	cellular_component	chromosome
B	0006334	biological_process	nucleosome assembly
B	0030527	molecular_function	structural constituent of chromatin
B	0046982	molecular_function	protein heterodimerization activity
C	0000786	cellular_component	nucleosome
C	0003677	molecular_function	DNA binding
C	0005634	cellular_component	nucleus
C	0005694	cellular_component	chromosome
C	0030527	molecular_function	structural constituent of chromatin
C	0046982	molecular_function	protein heterodimerization activity
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	0030527	molecular_function	structural constituent of chromatin
D	0046982	molecular_function	protein heterodimerization activity
E	0000786	cellular_component	nucleosome
E	0003677	molecular_function	DNA binding
E	0005515	molecular_function	protein binding
E	0005634	cellular_component	nucleus
E	0005654	cellular_component	nucleoplasm
E	0005694	cellular_component	chromosome
E	0030527	molecular_function	structural constituent of chromatin
E	0046982	molecular_function	protein heterodimerization activity
F	0000786	cellular_component	nucleosome
F	0003677	molecular_function	DNA binding
F	0005515	molecular_function	protein binding
F	0005634	cellular_component	nucleus
F	0005694	cellular_component	chromosome
F	0006334	biological_process	nucleosome assembly
F	0030527	molecular_function	structural constituent of chromatin
F	0046982	molecular_function	protein heterodimerization activity
G	0000786	cellular_component	nucleosome
G	0003677	molecular_function	DNA binding
G	0005634	cellular_component	nucleus
G	0005694	cellular_component	chromosome
G	0030527	molecular_function	structural constituent of chromatin
G	0046982	molecular_function	protein heterodimerization activity
H	0000786	cellular_component	nucleosome
H	0003677	molecular_function	DNA binding
H	0005515	molecular_function	protein binding
H	0005634	cellular_component	nucleus
H	0005694	cellular_component	chromosome
H	0030527	molecular_function	structural constituent of chromatin
H	0046982	molecular_function	protein heterodimerization activity
L	0000122	biological_process	negative regulation of transcription by RNA polymerase II
L	0000781	cellular_component	chromosome, telomeric region
L	0000785	cellular_component	chromatin
L	0003677	molecular_function	DNA binding
L	0003682	molecular_function	chromatin binding
L	0003684	molecular_function	damaged DNA binding
L	0003714	molecular_function	transcription corepressor activity
L	0003723	molecular_function	RNA binding
L	0003950	molecular_function	NAD+ ADP-ribosyltransferase activity
L	0005515	molecular_function	protein binding
L	0005634	cellular_component	nucleus
L	0005654	cellular_component	nucleoplasm
L	0005694	cellular_component	chromosome
L	0005721	cellular_component	pericentric heterochromatin
L	0005730	cellular_component	nucleolus
L	0005783	cellular_component	endoplasmic reticulum
L	0006281	biological_process	DNA repair
L	0006284	biological_process	base-excision repair
L	0006302	biological_process	double-strand break repair
L	0006325	biological_process	chromatin organization
L	0006338	biological_process	chromatin remodeling
L	0006476	biological_process	protein deacetylation
L	0008270	molecular_function	zinc ion binding
L	0008285	biological_process	negative regulation of cell population proliferation
L	0008340	biological_process	determination of adult lifespan
L	0009411	biological_process	response to UV
L	0010526	biological_process	retrotransposon silencing
L	0010569	biological_process	regulation of double-strand break repair via homologous recombination
L	0016746	molecular_function	acyltransferase activity
L	0016757	molecular_function	glycosyltransferase activity
L	0016779	molecular_function	nucleotidyltransferase activity
L	0017136	molecular_function	NAD-dependent histone deacetylase activity
L	0019216	biological_process	regulation of lipid metabolic process
L	0031490	molecular_function	chromatin DNA binding
L	0031491	molecular_function	nucleosome binding
L	0031508	biological_process	pericentric heterochromatin formation
L	0031509	biological_process	subtelomeric heterochromatin formation
L	0031648	biological_process	protein destabilization
L	0032024	biological_process	positive regulation of insulin secretion
L	0032206	biological_process	positive regulation of telomere maintenance
L	0032436	biological_process	positive regulation of proteasomal ubiquitin-dependent protein catabolic process
L	0032922	biological_process	circadian regulation of gene expression
L	0033558	molecular_function	protein lysine deacetylase activity
L	0034244	biological_process	negative regulation of transcription elongation by RNA polymerase II
L	0034979	molecular_function	NAD-dependent protein lysine deacetylase activity
L	0035861	cellular_component	site of double-strand break
L	0042181	biological_process	ketone biosynthetic process
L	0042308	biological_process	negative regulation of protein import into nucleus
L	0042593	biological_process	glucose homeostasis
L	0042752	biological_process	regulation of circadian rhythm
L	0042803	molecular_function	protein homodimerization activity
L	0043231	cellular_component	intracellular membrane-bounded organelle
L	0043687	biological_process	post-translational protein modification
L	0045600	biological_process	positive regulation of fat cell differentiation
L	0045721	biological_process	negative regulation of gluconeogenesis
L	0045814	biological_process	negative regulation of gene expression, epigenetic
L	0045820	biological_process	negative regulation of glycolytic process
L	0045892	biological_process	negative regulation of DNA-templated transcription
L	0046325	biological_process	negative regulation of glucose import
L	0046827	biological_process	positive regulation of protein export from nucleus
L	0046872	molecular_function	metal ion binding
L	0046969	molecular_function	NAD-dependent histone H3K9 deacetylase activity
L	0048146	biological_process	positive regulation of fibroblast proliferation
L	0050708	biological_process	regulation of protein secretion
L	0050994	biological_process	regulation of lipid catabolic process
L	0051697	biological_process	protein delipidation
L	0055007	biological_process	cardiac muscle cell differentiation
L	0070403	molecular_function	NAD+ binding
L	0090734	cellular_component	site of DNA damage
L	0097372	molecular_function	NAD-dependent histone H3K18 deacetylase activity
L	0099115	cellular_component	chromosome, subtelomeric region
L	0106222	molecular_function	lncRNA binding
L	0106274	molecular_function	NAD+-protein-arginine ADP-ribosyltransferase activity
L	0120162	biological_process	positive regulation of cold-induced thermogenesis
L	0120186	biological_process	negative regulation of protein localization to chromatin
L	0120187	biological_process	positive regulation of protein localization to chromatin
L	0140612	molecular_function	DNA damage sensor activity
L	0140765	molecular_function	NAD-dependent histone H3K56 deacetylase activity
L	0140773	molecular_function	NAD-dependent protein demyristoylase activity
L	0140774	molecular_function	NAD-dependent protein depalmitoylase activity
L	0140804	molecular_function	NAD+- protein-lysine ADP-ribosyltransferase activity
L	0140861	biological_process	DNA repair-dependent chromatin remodeling
L	1902459	biological_process	positive regulation of stem cell population maintenance
L	1902732	biological_process	positive regulation of chondrocyte proliferation
L	1903076	biological_process	regulation of protein localization to plasma membrane
L	1904841	molecular_function	TORC2 complex binding
L	1905555	biological_process	positive regulation of blood vessel branching
L	1905564	biological_process	positive regulation of vascular endothelial cell proliferation
L	1990166	biological_process	protein localization to site of double-strand break
L	1990404	molecular_function	NAD+-protein ADP-ribosyltransferase activity
L	2000648	biological_process	positive regulation of stem cell proliferation
L	2000738	biological_process	positive regulation of stem cell differentiation
L	2000773	biological_process	negative regulation of cellular senescence
L	2000781	biological_process	positive regulation of double-strand break repair

Functional Information from PROSITE/UniProt

site_id	PS00046
Number of Residues	7
Details	HISTONE_H2A Histone H2A signature. AGLqFPV

Chain	Residue	Details
C	ALA21-VAL27

site_id	PS00047
Number of Residues	5
Details	HISTONE_H4 Histone H4 signature. GAKRH

Chain	Residue	Details
B	GLY14-HIS18

site_id	PS00322
Number of Residues	7
Details	HISTONE_H3_1 Histone H3 signature 1. KAPRKQL

Chain	Residue	Details
A	LYS14-LEU20

site_id	PS00357
Number of Residues	23
Details	HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG

Chain	Residue	Details
D	ARG89-GLY111

site_id	PS00959
Number of Residues	9
Details	HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI

Chain	Residue	Details
A	PRO66-ILE74

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:P0C1H4

Chain	Residue	Details
D	LYS2
D	LYS9
D	LYS12
D	LYS17
H	LYS2
H	LYS9
H	LYS12
H	LYS17

site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000269\|PubMed:12757711

Chain	Residue	Details
D	SER11
H	SER11

site_id	SWS_FT_FI3
Number of Residues	2
Details	CARBOHYD: O-linked (GlcNAc) serine => ECO:0000250\|UniProtKB:P62807

Chain	Residue	Details
D	SER109
L	GLN242
L	VAL258
H	SER109
L	ARG65
L	TRP71
L	GLN113
L	HIS133
L	GLY214
L	SER216
L	ASN240

site_id	SWS_FT_FI4
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250\|UniProtKB:P0C1H4

Chain	Residue	Details
D	LYS117
L	CYS144
H	LYS117
L	CYS177

site_id	SWS_FT_FI5
Number of Residues	1
Details	SITE: Formation of an covalent adduct with nitro-fatty acid activators => ECO:0000269\|PubMed:33122195

Chain	Residue	Details
L	CYS18
C	LYS75
G	LYS74
G	LYS75
F	LYS8
F	LYS16
F	LYS44
F	LYS79

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: N-acetylserine => ECO:0007744\|PubMed:19413330

Chain	Residue	Details
L	SER2
G	GLN104
F	LYS12
F	LYS20

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphoserine; by MAPK8 => ECO:0000269\|PubMed:27568560, ECO:0007744\|PubMed:23186163

Chain	Residue	Details
L	SER10
G	LYS118
F	LYS31
F	LYS91

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0000269\|PubMed:32538779

Chain	Residue	Details
L	LYS33
F	SER47
C	LYS15
C	LYS119
G	LYS13
G	LYS15
G	LYS119

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744\|PubMed:24275569

Chain	Residue	Details
L	THR294
B	TYR88
F	TYR51
F	TYR88

site_id	SWS_FT_FI10
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18669648, ECO:0007744\|PubMed:23186163

Chain	Residue	Details
L	SER303
E	LYS64
F	LYS59
A	LYS27
A	LYS36
A	LYS64
E	LYS18
E	LYS23
E	LYS27
E	LYS36

site_id	SWS_FT_FI11
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
L	SER330
F	LYS77

site_id	SWS_FT_FI12
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269\|PubMed:24043303

Chain	Residue	Details
L	LYS170
F	LYS31

site_id	SWS_FT_FI13
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250\|UniProtKB:P62805

Chain	Residue	Details
A	LYS37
B	LYS91
F	LYS91

site_id	SWS_FT_FI14
Number of Residues	2
Details	MOD_RES: Phosphotyrosine => ECO:0000250\|UniProtKB:Q71DI3

Chain	Residue	Details
A	TYR41
E	TYR41

site_id	SWS_FT_FI15
Number of Residues	4
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250\|UniProtKB:P84228

Chain	Residue	Details
A	LYS56
A	LYS79
E	LYS56
E	LYS79

site_id	SWS_FT_FI16
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:Q71DI3

Chain	Residue	Details
A	SER57
E	SER57

site_id	SWS_FT_FI17
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0000250\|UniProtKB:Q71DI3

Chain	Residue	Details
A	THR80
A	THR107
E	THR80
E	THR107

site_id	SWS_FT_FI18
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P84243

Chain	Residue	Details
A	SER86
E	SER86

site_id	SWS_FT_FI19
Number of Residues	2
Details	MOD_RES: N6-glutaryllysine; alternate => ECO:0000250\|UniProtKB:Q71DI3

Chain	Residue	Details
A	LYS115
E	LYS115

site_id	SWS_FT_FI20
Number of Residues	2
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250\|UniProtKB:Q71DI3

Chain	Residue	Details
A	LYS122
E	LYS122

site_id	SWS_FT_FI21
Number of Residues	2
Details	LIPID: S-palmitoyl cysteine => ECO:0000250\|UniProtKB:Q71DI3

Chain	Residue	Details
A	CYS110
E	CYS110

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)