Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

8ATF

Nucleosome-bound Ino80 ATPase

Functional Information from GO Data

Chain	GOid	namespace	contents
G	0003677	molecular_function	DNA binding
G	0005524	molecular_function	ATP binding
G	0005634	cellular_component	nucleus
G	0006281	biological_process	DNA repair
G	0006338	biological_process	chromatin remodeling
G	0006351	biological_process	DNA-templated transcription
G	0031011	cellular_component	Ino80 complex
G	0140658	molecular_function	ATP-dependent chromatin remodeler activity
H	0006338	biological_process	chromatin remodeling
H	0031011	cellular_component	Ino80 complex
M	0000786	cellular_component	nucleosome
M	0003677	molecular_function	DNA binding
M	0005515	molecular_function	protein binding
M	0005576	cellular_component	extracellular region
M	0005634	cellular_component	nucleus
M	0005654	cellular_component	nucleoplasm
M	0005694	cellular_component	chromosome
M	0006325	biological_process	chromatin organization
M	0006334	biological_process	nucleosome assembly
M	0030527	molecular_function	structural constituent of chromatin
M	0043229	cellular_component	intracellular organelle
M	0046982	molecular_function	protein heterodimerization activity
M	0070062	cellular_component	extracellular exosome
N	0000781	cellular_component	chromosome, telomeric region
N	0000786	cellular_component	nucleosome
N	0003677	molecular_function	DNA binding
N	0003723	molecular_function	RNA binding
N	0005515	molecular_function	protein binding
N	0005576	cellular_component	extracellular region
N	0005634	cellular_component	nucleus
N	0005654	cellular_component	nucleoplasm
N	0005694	cellular_component	chromosome
N	0006325	biological_process	chromatin organization
N	0006334	biological_process	nucleosome assembly
N	0016020	cellular_component	membrane
N	0030527	molecular_function	structural constituent of chromatin
N	0032200	biological_process	telomere organization
N	0032991	cellular_component	protein-containing complex
N	0043505	cellular_component	CENP-A containing nucleosome
N	0045653	biological_process	negative regulation of megakaryocyte differentiation
N	0046982	molecular_function	protein heterodimerization activity
N	0061644	biological_process	protein localization to CENP-A containing chromatin
N	0070062	cellular_component	extracellular exosome
O	0000786	cellular_component	nucleosome
O	0003677	molecular_function	DNA binding
O	0005515	molecular_function	protein binding
O	0005634	cellular_component	nucleus
O	0005694	cellular_component	chromosome
O	0008150	biological_process	biological_process
O	0019899	molecular_function	enzyme binding
O	0030527	molecular_function	structural constituent of chromatin
O	0031492	molecular_function	nucleosomal DNA binding
O	0031507	biological_process	heterochromatin formation
O	0043229	cellular_component	intracellular organelle
O	0046982	molecular_function	protein heterodimerization activity
O	0070062	cellular_component	extracellular exosome
P	0000786	cellular_component	nucleosome
P	0002227	biological_process	innate immune response in mucosa
P	0003677	molecular_function	DNA binding
P	0005515	molecular_function	protein binding
P	0005615	cellular_component	extracellular space
P	0005634	cellular_component	nucleus
P	0005654	cellular_component	nucleoplasm
P	0005694	cellular_component	chromosome
P	0005829	cellular_component	cytosol
P	0006334	biological_process	nucleosome assembly
P	0019731	biological_process	antibacterial humoral response
P	0030527	molecular_function	structural constituent of chromatin
P	0042742	biological_process	defense response to bacterium
P	0042802	molecular_function	identical protein binding
P	0043229	cellular_component	intracellular organelle
P	0046982	molecular_function	protein heterodimerization activity
P	0050830	biological_process	defense response to Gram-positive bacterium
P	0061844	biological_process	antimicrobial humoral immune response mediated by antimicrobial peptide
P	0070062	cellular_component	extracellular exosome
Q	0000786	cellular_component	nucleosome
Q	0003677	molecular_function	DNA binding
Q	0005515	molecular_function	protein binding
Q	0005576	cellular_component	extracellular region
Q	0005634	cellular_component	nucleus
Q	0005654	cellular_component	nucleoplasm
Q	0005694	cellular_component	chromosome
Q	0006325	biological_process	chromatin organization
Q	0006334	biological_process	nucleosome assembly
Q	0030527	molecular_function	structural constituent of chromatin
Q	0043229	cellular_component	intracellular organelle
Q	0046982	molecular_function	protein heterodimerization activity
Q	0070062	cellular_component	extracellular exosome
R	0000781	cellular_component	chromosome, telomeric region
R	0000786	cellular_component	nucleosome
R	0003677	molecular_function	DNA binding
R	0003723	molecular_function	RNA binding
R	0005515	molecular_function	protein binding
R	0005576	cellular_component	extracellular region
R	0005634	cellular_component	nucleus
R	0005654	cellular_component	nucleoplasm
R	0005694	cellular_component	chromosome
R	0006325	biological_process	chromatin organization
R	0006334	biological_process	nucleosome assembly
R	0016020	cellular_component	membrane
R	0030527	molecular_function	structural constituent of chromatin
R	0032200	biological_process	telomere organization
R	0032991	cellular_component	protein-containing complex
R	0043505	cellular_component	CENP-A containing nucleosome
R	0045653	biological_process	negative regulation of megakaryocyte differentiation
R	0046982	molecular_function	protein heterodimerization activity
R	0061644	biological_process	protein localization to CENP-A containing chromatin
R	0070062	cellular_component	extracellular exosome
S	0000786	cellular_component	nucleosome
S	0003677	molecular_function	DNA binding
S	0005515	molecular_function	protein binding
S	0005634	cellular_component	nucleus
S	0005694	cellular_component	chromosome
S	0008150	biological_process	biological_process
S	0019899	molecular_function	enzyme binding
S	0030527	molecular_function	structural constituent of chromatin
S	0031492	molecular_function	nucleosomal DNA binding
S	0031507	biological_process	heterochromatin formation
S	0043229	cellular_component	intracellular organelle
S	0046982	molecular_function	protein heterodimerization activity
S	0070062	cellular_component	extracellular exosome
T	0000786	cellular_component	nucleosome
T	0002227	biological_process	innate immune response in mucosa
T	0003677	molecular_function	DNA binding
T	0005515	molecular_function	protein binding
T	0005615	cellular_component	extracellular space
T	0005634	cellular_component	nucleus
T	0005654	cellular_component	nucleoplasm
T	0005694	cellular_component	chromosome
T	0005829	cellular_component	cytosol
T	0006334	biological_process	nucleosome assembly
T	0019731	biological_process	antibacterial humoral response
T	0030527	molecular_function	structural constituent of chromatin
T	0042742	biological_process	defense response to bacterium
T	0042802	molecular_function	identical protein binding
T	0043229	cellular_component	intracellular organelle
T	0046982	molecular_function	protein heterodimerization activity
T	0050830	biological_process	defense response to Gram-positive bacterium
T	0061844	biological_process	antimicrobial humoral immune response mediated by antimicrobial peptide
T	0070062	cellular_component	extracellular exosome

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
O	ALA21-VAL27

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

Chain	Residue	Details
N	GLY14-HIS18

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

Chain	Residue	Details
M	LYS14-LEU20

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

Chain	Residue	Details
P	ARG92-GLY114

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

Chain	Residue	Details
M	PRO66-ILE74

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	MOD_RES: Phosphoserine; by RPS6KA5 => ECO:0000269\|PubMed:11709551, ECO:0000269\|PubMed:15010469

Chain	Residue	Details
O	SER1
S	SER1

site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250\|UniProtKB:P22752

Chain	Residue	Details
O	ARG3
S	ARG3

site_id	SWS_FT_FI3
Number of Residues	6
Details	MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269\|PubMed:24681537

Chain	Residue	Details
O	LYS5
T	LYS11
T	LYS15
T	LYS16
T	LYS20
T	LYS23
T	LYS43
T	LYS85
O	LYS74
O	LYS75
S	LYS5
S	LYS74
S	LYS75
P	LYS43
P	LYS85
T	LYS5

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000269\|PubMed:22389435

Chain	Residue	Details
O	LYS9
O	LYS95
S	LYS9
S	LYS95

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: N6-(beta-hydroxybutyryl)lysine; alternate => ECO:0000269\|PubMed:27105115

Chain	Residue	Details
O	LYS13
S	LYS13
N	LYS44
R	LYS8
R	LYS16
R	LYS44

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: N6-crotonyllysine; alternate => ECO:0000269\|PubMed:21925322

Chain	Residue	Details
O	LYS36
S	LYS36
N	LYS77
N	LYS91
R	LYS12
R	LYS31
R	LYS77
R	LYS91

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: N6-glutaryllysine => ECO:0000269\|PubMed:31542297

Chain	Residue	Details
O	LYS99
S	LYS99

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: N5-methylglutamine => ECO:0000269\|PubMed:24352239

Chain	Residue	Details
O	GLN104
S	GLN104
P	LYS120
T	LYS34
T	LYS116
T	LYS120

site_id	SWS_FT_FI9
Number of Residues	6
Details	MOD_RES: N6-glutaryllysine; alternate => ECO:0000269\|PubMed:31542297

Chain	Residue	Details
O	LYS118
O	LYS119
O	LYS125
S	LYS118
S	LYS119
S	LYS125

site_id	SWS_FT_FI10
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by DCAF1 => ECO:0000269\|PubMed:15078818, ECO:0000269\|PubMed:24140421

Chain	Residue	Details
O	THR120
S	THR120
Q	LYS14
Q	LYS56

site_id	SWS_FT_FI11
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269\|PubMed:22713238, ECO:0000269\|PubMed:22980979

Chain	Residue	Details
O	LYS13
S	LYS13
T	LYS46
T	LYS108

site_id	SWS_FT_FI12
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269\|PubMed:15386022, ECO:0000269\|PubMed:16359901, ECO:0000269\|PubMed:16702407, ECO:0000269\|PubMed:25470042

Chain	Residue	Details
P	LYS57
O	LYS119
S	LYS119

site_id	SWS_FT_FI13
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269\|PubMed:22713238, ECO:0000269\|PubMed:22980979

Chain	Residue	Details
O	LYS15
S	LYS15

site_id	SWS_FT_FI14
Number of Residues	4
Details	MOD_RES: Omega-N-methylarginine => ECO:0000250\|UniProtKB:Q96A08

Chain	Residue	Details
P	ARG86
P	ARG92
T	ARG86
T	ARG92

site_id	SWS_FT_FI15
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000250\|UniProtKB:Q00729

Chain	Residue	Details
P	THR115
T	THR115
R	LYS91

site_id	SWS_FT_FI16
Number of Residues	2
Details	CARBOHYD: O-linked (GlcNAc) serine => ECO:0000269\|PubMed:22121020

Chain	Residue	Details
P	SER112
T	SER112
N	LYS79
R	LYS20
R	LYS59
R	LYS79

site_id	SWS_FT_FI17
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250\|UniProtKB:P58876

Chain	Residue	Details
P	LYS5
T	LYS5

site_id	SWS_FT_FI18
Number of Residues	4
Details	CROSSLNK: 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

Chain	Residue	Details
M	SER57
P	LYS120
T	LYS120

site_id	SWS_FT_FI19
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250\|UniProtKB:Q5QNW6

Chain	Residue	Details
P	LYS20
T	LYS20

site_id	SWS_FT_FI20
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269\|PubMed:21726816

Chain	Residue	Details
P	LYS34
T	LYS34

site_id	SWS_FT_FI21
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P84243

Chain	Residue	Details
M	SER86
Q	SER86

site_id	SWS_FT_FI22
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744\|PubMed:19690332

Chain	Residue	Details
M	THR107
Q	THR107

site_id	SWS_FT_FI23
Number of Residues	2
Details	MOD_RES: N6-glutaryllysine; alternate => ECO:0000269\|PubMed:31542297

Chain	Residue	Details
M	LYS115
Q	LYS115

site_id	SWS_FT_FI24
Number of Residues	2
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000269\|PubMed:22389435, ECO:0000269\|PubMed:27436229

Chain	Residue	Details
M	LYS122
Q	LYS122

site_id	SWS_FT_FI25
Number of Residues	2
Details	LIPID: N6-decanoyllysine => ECO:0000269\|PubMed:35939806

Chain	Residue	Details
M	LYS18
Q	LYS18

site_id	SWS_FT_FI26
Number of Residues	2
Details	LIPID: S-palmitoyl cysteine => ECO:0000269\|PubMed:21076176

Chain	Residue	Details
M	CYS110
Q	CYS110

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