Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7VVZ

NuA4 bound to the 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
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	0003674	molecular_function	molecular_function
E	0003682	molecular_function	chromatin binding
E	0005515	molecular_function	protein binding
E	0005634	cellular_component	nucleus
E	0006281	biological_process	DNA repair
E	0006325	biological_process	chromatin organization
E	0006351	biological_process	DNA-templated transcription
E	0006974	biological_process	DNA damage response
E	0019865	molecular_function	immunoglobulin binding
E	0035267	cellular_component	NuA4 histone acetyltransferase complex
E	0036228	biological_process	protein localization to nuclear inner membrane
E	0065003	biological_process	protein-containing complex assembly
F	0000785	cellular_component	chromatin
F	0000812	cellular_component	Swr1 complex
F	0003682	molecular_function	chromatin binding
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0005634	cellular_component	nucleus
F	0006281	biological_process	DNA repair
F	0006325	biological_process	chromatin organization
F	0006338	biological_process	chromatin remodeling
F	0006351	biological_process	DNA-templated transcription
F	0006355	biological_process	regulation of DNA-templated transcription
F	0006357	biological_process	regulation of transcription by RNA polymerase II
F	0006974	biological_process	DNA damage response
F	0010468	biological_process	regulation of gene expression
F	0016514	cellular_component	SWI/SNF complex
F	0031011	cellular_component	Ino80 complex
F	0035267	cellular_component	NuA4 histone acetyltransferase complex
F	0042393	molecular_function	histone binding
F	0051382	biological_process	kinetochore assembly
G	0000011	biological_process	vacuole inheritance
G	0000142	cellular_component	cellular bud neck contractile ring
G	0000166	molecular_function	nucleotide binding
G	0000785	cellular_component	chromatin
G	0000812	cellular_component	Swr1 complex
G	0005200	molecular_function	structural constituent of cytoskeleton
G	0005515	molecular_function	protein binding
G	0005524	molecular_function	ATP binding
G	0005634	cellular_component	nucleus
G	0005737	cellular_component	cytoplasm
G	0005856	cellular_component	cytoskeleton
G	0005884	cellular_component	actin filament
G	0006281	biological_process	DNA repair
G	0006338	biological_process	chromatin remodeling
G	0006351	biological_process	DNA-templated transcription
G	0006355	biological_process	regulation of DNA-templated transcription
G	0006897	biological_process	endocytosis
G	0009306	biological_process	protein secretion
G	0015629	cellular_component	actin cytoskeleton
G	0016787	molecular_function	hydrolase activity
G	0016887	molecular_function	ATP hydrolysis activity
G	0030010	biological_process	establishment of cell polarity
G	0030476	biological_process	ascospore wall assembly
G	0030479	cellular_component	actin cortical patch
G	0031011	cellular_component	Ino80 complex
G	0032432	cellular_component	actin filament bundle
G	0035267	cellular_component	NuA4 histone acetyltransferase complex
G	0042802	molecular_function	identical protein binding
G	0071944	cellular_component	cell periphery
G	1902404	biological_process	mitotic actomyosin contractile ring contraction
H	0004402	molecular_function	histone acetyltransferase activity
H	0005515	molecular_function	protein binding
H	0005634	cellular_component	nucleus
H	0006281	biological_process	DNA repair
H	0006325	biological_process	chromatin organization
H	0006338	biological_process	chromatin remodeling
H	0006351	biological_process	DNA-templated transcription
H	0006357	biological_process	regulation of transcription by RNA polymerase II
H	0006974	biological_process	DNA damage response
H	0016239	biological_process	positive regulation of macroautophagy
H	0030674	molecular_function	protein-macromolecule adaptor activity
H	0032777	cellular_component	piccolo histone acetyltransferase complex
H	0035267	cellular_component	NuA4 histone acetyltransferase complex
K	0000122	biological_process	negative regulation of transcription by RNA polymerase II
K	0000785	cellular_component	chromatin
K	0000812	cellular_component	Swr1 complex
K	0003714	molecular_function	transcription corepressor activity
K	0005515	molecular_function	protein binding
K	0005634	cellular_component	nucleus
K	0005694	cellular_component	chromosome
K	0006281	biological_process	DNA repair
K	0006325	biological_process	chromatin organization
K	0006338	biological_process	chromatin remodeling
K	0006351	biological_process	DNA-templated transcription
K	0006355	biological_process	regulation of DNA-templated transcription
K	0006974	biological_process	DNA damage response
K	0035267	cellular_component	NuA4 histone acetyltransferase complex
K	0051276	biological_process	chromosome organization
L	0000124	cellular_component	SAGA complex
L	0004402	molecular_function	histone acetyltransferase activity
L	0004672	molecular_function	protein kinase activity
L	0005515	molecular_function	protein binding
L	0005634	cellular_component	nucleus
L	0006281	biological_process	DNA repair
L	0006325	biological_process	chromatin organization
L	0006351	biological_process	DNA-templated transcription
L	0006355	biological_process	regulation of DNA-templated transcription
L	0006357	biological_process	regulation of transcription by RNA polymerase II
L	0033554	biological_process	cellular response to stress
L	0035267	cellular_component	NuA4 histone acetyltransferase complex
L	0045944	biological_process	positive regulation of transcription by RNA polymerase II
L	0046695	cellular_component	SLIK (SAGA-like) complex
L	0110078	cellular_component	TTT Hsp90 cochaperone complex
L	0140861	biological_process	DNA repair-dependent chromatin remodeling
N	0000786	cellular_component	nucleosome
N	0003677	molecular_function	DNA binding
N	0005634	cellular_component	nucleus
N	0005694	cellular_component	chromosome
N	0030527	molecular_function	structural constituent of chromatin
N	0031507	biological_process	heterochromatin formation
N	0046982	molecular_function	protein heterodimerization activity
O	0000786	cellular_component	nucleosome
O	0003677	molecular_function	DNA binding
O	0005515	molecular_function	protein binding
O	0005634	cellular_component	nucleus
O	0005654	cellular_component	nucleoplasm
O	0005694	cellular_component	chromosome
O	0030527	molecular_function	structural constituent of chromatin
O	0031492	molecular_function	nucleosomal DNA binding
O	0031507	biological_process	heterochromatin formation
O	0046982	molecular_function	protein heterodimerization activity
P	0000183	biological_process	rDNA heterochromatin formation
P	0000785	cellular_component	chromatin
P	0003682	molecular_function	chromatin binding
P	0003712	molecular_function	transcription coregulator activity
P	0004402	molecular_function	histone acetyltransferase activity
P	0005515	molecular_function	protein binding
P	0005634	cellular_component	nucleus
P	0006281	biological_process	DNA repair
P	0006325	biological_process	chromatin organization
P	0006351	biological_process	DNA-templated transcription
P	0006354	biological_process	DNA-templated transcription elongation
P	0006355	biological_process	regulation of DNA-templated transcription
P	0006357	biological_process	regulation of transcription by RNA polymerase II
P	0006974	biological_process	DNA damage response
P	0008270	molecular_function	zinc ion binding
P	0010485	molecular_function	histone H4 acetyltransferase activity
P	0010629	biological_process	negative regulation of gene expression
P	0010867	biological_process	positive regulation of triglyceride biosynthetic process
P	0016239	biological_process	positive regulation of macroautophagy
P	0016740	molecular_function	transferase activity
P	0032777	cellular_component	piccolo histone acetyltransferase complex
P	0032968	biological_process	positive regulation of transcription elongation by RNA polymerase II
P	0033554	biological_process	cellular response to stress
P	0035267	cellular_component	NuA4 histone acetyltransferase complex
P	0051726	biological_process	regulation of cell cycle
P	0061733	molecular_function	protein-lysine-acetyltransferase activity
P	0106226	molecular_function	peptide 2-hydroxyisobutyryltransferase activity
P	0140064	molecular_function	peptide crotonyltransferase activity
P	0140068	molecular_function	histone crotonyltransferase activity
Q	0000786	cellular_component	nucleosome
Q	0003677	molecular_function	DNA binding
Q	0005515	molecular_function	protein binding
Q	0005634	cellular_component	nucleus
Q	0005694	cellular_component	chromosome
Q	0006334	biological_process	nucleosome assembly
Q	0030527	molecular_function	structural constituent of chromatin
Q	0031507	biological_process	heterochromatin formation
Q	0046982	molecular_function	protein heterodimerization activity
S	0000786	cellular_component	nucleosome
S	0003677	molecular_function	DNA binding
S	0005634	cellular_component	nucleus
S	0005694	cellular_component	chromosome
S	0030527	molecular_function	structural constituent of chromatin
S	0031507	biological_process	heterochromatin formation
S	0046982	molecular_function	protein heterodimerization activity
T	0004402	molecular_function	histone acetyltransferase activity
T	0005515	molecular_function	protein binding
T	0005634	cellular_component	nucleus
T	0006281	biological_process	DNA repair
T	0006325	biological_process	chromatin organization
T	0006338	biological_process	chromatin remodeling
T	0006351	biological_process	DNA-templated transcription
T	0006357	biological_process	regulation of transcription by RNA polymerase II
T	0006974	biological_process	DNA damage response
T	0016239	biological_process	positive regulation of macroautophagy
T	0030674	molecular_function	protein-macromolecule adaptor activity
T	0032777	cellular_component	piccolo histone acetyltransferase complex
T	0035267	cellular_component	NuA4 histone acetyltransferase complex
U	0000786	cellular_component	nucleosome
U	0002227	biological_process	innate immune response in mucosa
U	0003677	molecular_function	DNA binding
U	0005515	molecular_function	protein binding
U	0005615	cellular_component	extracellular space
U	0005634	cellular_component	nucleus
U	0005694	cellular_component	chromosome
U	0006325	biological_process	chromatin organization
U	0019731	biological_process	antibacterial humoral response
U	0030527	molecular_function	structural constituent of chromatin
U	0031507	biological_process	heterochromatin formation
U	0046982	molecular_function	protein heterodimerization activity
U	0061844	biological_process	antimicrobial humoral immune response mediated by antimicrobial peptide
V	0004402	molecular_function	histone acetyltransferase activity
V	0005515	molecular_function	protein binding
V	0005634	cellular_component	nucleus
V	0005829	cellular_component	cytosol
V	0006281	biological_process	DNA repair
V	0006325	biological_process	chromatin organization
V	0006338	biological_process	chromatin remodeling
V	0006351	biological_process	DNA-templated transcription
V	0006355	biological_process	regulation of DNA-templated transcription
V	0006974	biological_process	DNA damage response
V	0008270	molecular_function	zinc ion binding
V	0032777	cellular_component	piccolo histone acetyltransferase complex
V	0035267	cellular_component	NuA4 histone acetyltransferase complex
V	0046872	molecular_function	metal ion binding
V	0051321	biological_process	meiotic cell cycle
V	0140002	molecular_function	histone H3K4me3 reader activity
Y	0000123	cellular_component	histone acetyltransferase complex
Y	0004402	molecular_function	histone acetyltransferase activity
Y	0005515	molecular_function	protein binding
Y	0005634	cellular_component	nucleus
Y	0006281	biological_process	DNA repair
Y	0006325	biological_process	chromatin organization
Y	0006338	biological_process	chromatin remodeling
Y	0006351	biological_process	DNA-templated transcription
Y	0006974	biological_process	DNA damage response
Y	0033100	cellular_component	NuA3 histone acetyltransferase complex
Y	0035267	cellular_component	NuA4 histone acetyltransferase complex
Y	1990467	cellular_component	NuA3a histone acetyltransferase complex
Y	1990468	cellular_component	NuA3b histone acetyltransferase complex

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
S	ALA21-VAL27

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

Chain	Residue	Details
Q	GLY14-HIS18

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

Chain	Residue	Details
O	LYS14-LEU20

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

Chain	Residue	Details
U	ARG92-GLY114

site_id	PS00406
Number of Residues	11
Details	ACTINS_1 Actins signature 1. YVGDEAQs.KRG

Chain	Residue	Details
G	TYR53-GLY63

site_id	PS00432
Number of Residues	9
Details	ACTINS_2 Actins signature 2. WISKqEYDE

Chain	Residue	Details
G	TRP356-GLU364

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

Chain	Residue	Details
O	PRO66-ILE74

site_id	PS01132
Number of Residues	13
Details	ACTINS_ACT_LIKE Actins and actin-related proteins signature. LLTEApMNPksNR

Chain	Residue	Details
G	LEU104-ARG116
F	LEU109-ARG121

site_id	PS01359
Number of Residues	44
Details	ZF_PHD_1 Zinc finger PHD-type signature. Cf.Cqrvsfgem.....................................VaCdgpnCkyewFHydCvnlkeppkgt...................................WyCpeC

Chain	Residue	Details
V	CYS225-CYS268

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	93
Details	Coiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
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_FI4
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
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_FI6
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P84243","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
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_FI9
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_FI10
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_FI11
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_FI12
Number of Residues	5
Details	Modified residue: {"description":"N6-propionyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
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_FI14
Number of Residues	4
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
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_FI16
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_FI17
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_FI18
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_FI19
Number of Residues	4
Details	DNA binding: {}

Chain

Residue

Details

site_id	SWS_FT_FI20
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_FI21
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_FI22
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_FI23
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_FI24
Number of Residues	2
Details	Modified residue: {"description":"N5-methylglutamine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI25
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_FI26
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_FI27
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_FI28
Number of Residues	25
Details	Zinc finger: {"description":"C2HC MYST-type; degenerate","evidences":[{"source":"PROSITE-ProRule","id":"PRU01063","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI29
Number of Residues	21
Details	Motif: {"description":"ESA1-RPD3 motif"}

Chain

Residue

Details

site_id	SWS_FT_FI30
Number of Residues	1
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"12368900","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"17223684","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"18245364","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"22020126","evidenceCode":"ECO:0000303"},{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI31
Number of Residues	11
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11106757","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12368900","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22020126","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI32
Number of Residues	1
Details	Site: {"description":"Important for catalytic activity","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI33
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine; by autocatalysis","evidences":[{"source":"PubMed","id":"22020126","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI34
Number of Residues	62
Details	Domain: {"description":"Myb-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00133","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI35
Number of Residues	1
Details	Site: {"description":"Not methylated","evidences":[{"source":"PubMed","id":"10496983","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI36
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22106047","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI37
Number of Residues	38
Details	Repeat: {"description":"HEAT 1","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI38
Number of Residues	46
Details	Repeat: {"description":"HEAT 2","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI39
Number of Residues	37
Details	Repeat: {"description":"HEAT 3","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI40
Number of Residues	38
Details	Repeat: {"description":"HEAT 6","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI41
Number of Residues	40
Details	Repeat: {"description":"HEAT 7","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI42
Number of Residues	40
Details	Repeat: {"description":"HEAT 8","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI43
Number of Residues	37
Details	Repeat: {"description":"HEAT 9","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI44
Number of Residues	42
Details	Repeat: {"description":"HEAT 10","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI45
Number of Residues	38
Details	Repeat: {"description":"HEAT 11","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI46
Number of Residues	40
Details	Repeat: {"description":"HEAT 12","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI47
Number of Residues	39
Details	Repeat: {"description":"HEAT 13","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI48
Number of Residues	38
Details	Repeat: {"description":"HEAT 14","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI49
Number of Residues	37
Details	Repeat: {"description":"HEAT 15","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI50
Number of Residues	37
Details	Repeat: {"description":"HEAT 16","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI51
Number of Residues	39
Details	Repeat: {"description":"HEAT 17","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI52
Number of Residues	37
Details	Repeat: {"description":"HEAT 18","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI53
Number of Residues	36
Details	Repeat: {"description":"HEAT 19","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI54
Number of Residues	41
Details	Repeat: {"description":"HEAT 20","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI55
Number of Residues	37
Details	Repeat: {"description":"HEAT 21","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI56
Number of Residues	37
Details	Repeat: {"description":"HEAT 22","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI57
Number of Residues	37
Details	Repeat: {"description":"HEAT 24","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI58
Number of Residues	37
Details	Repeat: {"description":"HEAT 25","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI59
Number of Residues	38
Details	Repeat: {"description":"HEAT 26","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI60
Number of Residues	37
Details	Repeat: {"description":"HEAT 27","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI61
Number of Residues	358
Details	Domain: {"description":"PI3K/PI4K catalytic","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI62
Number of Residues	32
Details	Domain: {"description":"FATC","evidences":[{"source":"PROSITE-ProRule","id":"PRU00534","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU00535","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI63
Number of Residues	6
Details	Region: {"description":"G-loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI64
Number of Residues	8
Details	Region: {"description":"Catalytic loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI65
Number of Residues	25
Details	Region: {"description":"Activation loop","evidences":[{"source":"PROSITE-ProRule","id":"PRU00269","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI66
Number of Residues	1
Details	Modified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	2
Details	M-CSA 525

Chain	Residue	Details
L	PHE304	covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor
L	SER338	activator, proton acceptor, proton donor

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