8F86

SIRT6 bound to an H3K9Ac nucleosome

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	0031492	molecular_function	nucleosomal DNA binding
A	0031507	biological_process	heterochromatin formation
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	0031507	biological_process	heterochromatin formation
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	0031507	biological_process	heterochromatin formation
C	0046982	molecular_function	protein heterodimerization activity
D	0000786	cellular_component	nucleosome
D	0002227	biological_process	innate immune response in mucosa
D	0003677	molecular_function	DNA binding
D	0005515	molecular_function	protein binding
D	0005615	cellular_component	extracellular space
D	0005634	cellular_component	nucleus
D	0005694	cellular_component	chromosome
D	0006325	biological_process	chromatin organization
D	0019731	biological_process	antibacterial humoral response
D	0030527	molecular_function	structural constituent of chromatin
D	0031507	biological_process	heterochromatin formation
D	0046982	molecular_function	protein heterodimerization activity
D	0061844	biological_process	antimicrobial humoral immune response mediated by antimicrobial peptide
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	0031492	molecular_function	nucleosomal DNA binding
E	0031507	biological_process	heterochromatin formation
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	0031507	biological_process	heterochromatin formation
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	0031507	biological_process	heterochromatin formation
G	0046982	molecular_function	protein heterodimerization activity
H	0000786	cellular_component	nucleosome
H	0002227	biological_process	innate immune response in mucosa
H	0003677	molecular_function	DNA binding
H	0005515	molecular_function	protein binding
H	0005615	cellular_component	extracellular space
H	0005634	cellular_component	nucleus
H	0005694	cellular_component	chromosome
H	0006325	biological_process	chromatin organization
H	0019731	biological_process	antibacterial humoral response
H	0030527	molecular_function	structural constituent of chromatin
H	0031507	biological_process	heterochromatin formation
H	0046982	molecular_function	protein heterodimerization activity
H	0061844	biological_process	antimicrobial humoral immune response mediated by antimicrobial peptide
K	0000122	biological_process	negative regulation of transcription by RNA polymerase II
K	0000781	cellular_component	chromosome, telomeric region
K	0000785	cellular_component	chromatin
K	0003677	molecular_function	DNA binding
K	0003682	molecular_function	chromatin binding
K	0003684	molecular_function	damaged DNA binding
K	0003714	molecular_function	transcription corepressor activity
K	0003723	molecular_function	RNA binding
K	0003950	molecular_function	NAD+ poly-ADP-ribosyltransferase activity
K	0005515	molecular_function	protein binding
K	0005634	cellular_component	nucleus
K	0005654	cellular_component	nucleoplasm
K	0005694	cellular_component	chromosome
K	0005721	cellular_component	pericentric heterochromatin
K	0005730	cellular_component	nucleolus
K	0005783	cellular_component	endoplasmic reticulum
K	0006111	biological_process	regulation of gluconeogenesis
K	0006281	biological_process	DNA repair
K	0006282	biological_process	regulation of DNA repair
K	0006284	biological_process	base-excision repair
K	0006302	biological_process	double-strand break repair
K	0006325	biological_process	chromatin organization
K	0006338	biological_process	chromatin remodeling
K	0006476	biological_process	protein deacetylation
K	0006606	biological_process	protein import into nucleus
K	0006974	biological_process	DNA damage response
K	0008270	molecular_function	zinc ion binding
K	0008285	biological_process	negative regulation of cell population proliferation
K	0008340	biological_process	determination of adult lifespan
K	0009411	biological_process	response to UV
K	0010526	biological_process	transposable element silencing
K	0010569	biological_process	regulation of double-strand break repair via homologous recombination
K	0016740	molecular_function	transferase activity
K	0016746	molecular_function	acyltransferase activity
K	0016757	molecular_function	glycosyltransferase activity
K	0016779	molecular_function	nucleotidyltransferase activity
K	0017136	molecular_function	histone deacetylase activity, NAD-dependent
K	0019216	biological_process	regulation of lipid metabolic process
K	0031490	molecular_function	chromatin DNA binding
K	0031491	molecular_function	nucleosome binding
K	0031508	biological_process	pericentric heterochromatin formation
K	0031509	biological_process	subtelomeric heterochromatin formation
K	0031648	biological_process	protein destabilization
K	0032024	biological_process	positive regulation of insulin secretion
K	0032129	molecular_function	histone H3K9 deacetylase activity, hydrolytic mechanism
K	0032206	biological_process	positive regulation of telomere maintenance
K	0032436	biological_process	positive regulation of proteasomal ubiquitin-dependent protein catabolic process
K	0032922	biological_process	circadian regulation of gene expression
K	0034244	biological_process	negative regulation of transcription elongation by RNA polymerase II
K	0034979	molecular_function	NAD-dependent protein lysine deacetylase activity
K	0035861	cellular_component	site of double-strand break
K	0042181	biological_process	ketone biosynthetic process
K	0042308	biological_process	negative regulation of protein import into nucleus
K	0042593	biological_process	glucose homeostasis
K	0042752	biological_process	regulation of circadian rhythm
K	0042803	molecular_function	protein homodimerization activity
K	0043687	biological_process	post-translational protein modification
K	0045600	biological_process	positive regulation of fat cell differentiation
K	0045721	biological_process	negative regulation of gluconeogenesis
K	0045814	biological_process	negative regulation of gene expression, epigenetic
K	0045820	biological_process	negative regulation of glycolytic process
K	0045892	biological_process	negative regulation of DNA-templated transcription
K	0046325	biological_process	negative regulation of D-glucose import
K	0046827	biological_process	positive regulation of protein export from nucleus
K	0046872	molecular_function	metal ion binding
K	0046969	molecular_function	histone H3K9 deacetylase activity, NAD-dependent
K	0048146	biological_process	positive regulation of fibroblast proliferation
K	0050708	biological_process	regulation of protein secretion
K	0050994	biological_process	regulation of lipid catabolic process
K	0051697	biological_process	protein delipidation
K	0055007	biological_process	cardiac muscle cell differentiation
K	0070403	molecular_function	NAD+ binding
K	0090734	cellular_component	site of DNA damage
K	0097372	molecular_function	histone H3K18 deacetylase activity, NAD-dependent
K	0099115	cellular_component	chromosome, subtelomeric region
K	0106222	molecular_function	lncRNA binding
K	0106274	molecular_function	NAD+-protein-arginine ADP-ribosyltransferase activity
K	0120162	biological_process	positive regulation of cold-induced thermogenesis
K	0120186	biological_process	negative regulation of protein localization to chromatin
K	0120187	biological_process	positive regulation of protein localization to chromatin
K	0140612	molecular_function	DNA damage sensor activity
K	0140765	molecular_function	histone H3K56 deacetylase activity, NAD-dependent
K	0140773	molecular_function	NAD-dependent protein demyristoylase activity
K	0140774	molecular_function	NAD-dependent protein depalmitoylase activity
K	0140804	molecular_function	NAD+-protein-lysine ADP-ribosyltransferase activity
K	0140861	biological_process	DNA repair-dependent chromatin remodeling
K	1902459	biological_process	positive regulation of stem cell population maintenance
K	1902732	biological_process	positive regulation of chondrocyte proliferation
K	1903076	biological_process	regulation of protein localization to plasma membrane
K	1904841	molecular_function	TORC2 complex binding
K	1905555	biological_process	positive regulation of blood vessel branching
K	1905564	biological_process	positive regulation of vascular endothelial cell proliferation
K	1990166	biological_process	protein localization to site of double-strand break
K	1990404	molecular_function	NAD+-protein mono-ADP-ribosyltransferase activity
K	2000648	biological_process	positive regulation of stem cell proliferation
K	2000738	biological_process	positive regulation of stem cell differentiation
K	2000773	biological_process	negative regulation of cellular senescence
K	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	1
Details	Modified residue: {"description":"Phosphothreonine; by HASPIN and VRK1","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"12138181","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"5-glutamyl serotonin; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine; by PKC","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Symmetric dimethylarginine; by PRMT5; alternate","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"12138181","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	4
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P84228","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	2
Details	Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI13
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P84243","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI14
Number of Residues	2
Details	Modified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI15
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI16
Number of Residues	2
Details	Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI17
Number of Residues	1
Details	Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI18
Number of Residues	4
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI19
Number of Residues	4
Details	Modified residue: {"description":"N6-propionyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI20
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine; by PAK2","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI21
Number of Residues	4
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI22
Number of Residues	2
Details	Modified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI23
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI24
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI25
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI26
Number of Residues	2
Details	Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine; alternate","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI27
Number of Residues	4
Details	Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI28
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI29
Number of Residues	2
Details	Modified residue: {"description":"N5-methylglutamine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI30
Number of Residues	2
Details	Modified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI31
Number of Residues	6
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI32
Number of Residues	2
Details	Glycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"source":"UniProtKB","id":"P62807","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI33
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P0C1H4","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI34
Number of Residues	245
Details	Domain: {"description":"Deacetylase sirtuin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00236","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI35
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00236","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18337721","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23552949","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"23892288","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"27322069","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"28406396","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI36
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"21362626","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3K35","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ZG6","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI37
Number of Residues	11
Details	Binding site: {"evidences":[{"source":"PubMed","id":"23552949","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21362626","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3K35","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ZG6","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI38
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00236","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21362626","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23552949","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27990725","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3K35","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3PKI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3PKJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3ZG6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MF6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MFP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MFZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5MGN","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI39
Number of Residues	1
Details	Site: {"description":"Formation of an covalent adduct with nitro-fatty acid activators","evidences":[{"source":"PubMed","id":"33122195","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI40
Number of Residues	1
Details	Modified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI41
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by MAPK8","evidences":[{"source":"PubMed","id":"27568560","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI42
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"32538779","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI43
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"24043303","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---