8V6V

Cryo-EM structure of doubly-bound SNF2h-nucleosome complex

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
W	0000183	biological_process	rDNA heterochromatin formation
W	0000785	cellular_component	chromatin
W	0000793	cellular_component	condensed chromosome
W	0001650	cellular_component	fibrillar center
W	0003677	molecular_function	DNA binding
W	0003682	molecular_function	chromatin binding
W	0004386	molecular_function	helicase activity
W	0005515	molecular_function	protein binding
W	0005524	molecular_function	ATP binding
W	0005634	cellular_component	nucleus
W	0005654	cellular_component	nucleoplasm
W	0005677	cellular_component	chromatin silencing complex
W	0005694	cellular_component	chromosome
W	0005721	cellular_component	pericentric heterochromatin
W	0005730	cellular_component	nucleolus
W	0006275	biological_process	regulation of DNA replication
W	0006281	biological_process	DNA repair
W	0006325	biological_process	chromatin organization
W	0006334	biological_process	nucleosome assembly
W	0006338	biological_process	chromatin remodeling
W	0006346	biological_process	DNA methylation-dependent constitutive heterochromatin formation
W	0006352	biological_process	DNA-templated transcription initiation
W	0006355	biological_process	regulation of DNA-templated transcription
W	0006357	biological_process	regulation of transcription by RNA polymerase II
W	0006974	biological_process	DNA damage response
W	0008623	cellular_component	CHRAC
W	0016479	biological_process	negative regulation of transcription by RNA polymerase I
W	0016589	cellular_component	NURF complex
W	0016590	cellular_component	ACF complex
W	0016787	molecular_function	hydrolase activity
W	0016887	molecular_function	ATP hydrolysis activity
W	0031010	cellular_component	ISWI-type complex
W	0031213	cellular_component	RSF complex
W	0031491	molecular_function	nucleosome binding
W	0031507	biological_process	heterochromatin formation
W	0035861	cellular_component	site of double-strand break
W	0042393	molecular_function	histone binding
W	0043596	cellular_component	nuclear replication fork
W	0045740	biological_process	positive regulation of DNA replication
W	0045943	biological_process	positive regulation of transcription by RNA polymerase I
W	0045944	biological_process	positive regulation of transcription by RNA polymerase II
W	0045945	biological_process	positive regulation of transcription by RNA polymerase III
W	0090535	cellular_component	WICH complex
W	0090536	cellular_component	NoRC complex
W	0090537	cellular_component	CERF complex
W	0110016	cellular_component	B-WICH complex
W	0140374	biological_process	antiviral innate immune response
W	0140658	molecular_function	ATP-dependent chromatin remodeler activity
W	0140750	molecular_function	nucleosome array spacer activity
W	0140751	molecular_function	histone octamer slider activity
W	1905213	biological_process	negative regulation of mitotic chromosome condensation
X	0000183	biological_process	rDNA heterochromatin formation
X	0000785	cellular_component	chromatin
X	0000793	cellular_component	condensed chromosome
X	0001650	cellular_component	fibrillar center
X	0003677	molecular_function	DNA binding
X	0003682	molecular_function	chromatin binding
X	0004386	molecular_function	helicase activity
X	0005515	molecular_function	protein binding
X	0005524	molecular_function	ATP binding
X	0005634	cellular_component	nucleus
X	0005654	cellular_component	nucleoplasm
X	0005677	cellular_component	chromatin silencing complex
X	0005694	cellular_component	chromosome
X	0005721	cellular_component	pericentric heterochromatin
X	0005730	cellular_component	nucleolus
X	0006275	biological_process	regulation of DNA replication
X	0006281	biological_process	DNA repair
X	0006325	biological_process	chromatin organization
X	0006334	biological_process	nucleosome assembly
X	0006338	biological_process	chromatin remodeling
X	0006346	biological_process	DNA methylation-dependent constitutive heterochromatin formation
X	0006352	biological_process	DNA-templated transcription initiation
X	0006355	biological_process	regulation of DNA-templated transcription
X	0006357	biological_process	regulation of transcription by RNA polymerase II
X	0006974	biological_process	DNA damage response
X	0008623	cellular_component	CHRAC
X	0016479	biological_process	negative regulation of transcription by RNA polymerase I
X	0016589	cellular_component	NURF complex
X	0016590	cellular_component	ACF complex
X	0016787	molecular_function	hydrolase activity
X	0016887	molecular_function	ATP hydrolysis activity
X	0031010	cellular_component	ISWI-type complex
X	0031213	cellular_component	RSF complex
X	0031491	molecular_function	nucleosome binding
X	0031507	biological_process	heterochromatin formation
X	0035861	cellular_component	site of double-strand break
X	0042393	molecular_function	histone binding
X	0043596	cellular_component	nuclear replication fork
X	0045740	biological_process	positive regulation of DNA replication
X	0045943	biological_process	positive regulation of transcription by RNA polymerase I
X	0045944	biological_process	positive regulation of transcription by RNA polymerase II
X	0045945	biological_process	positive regulation of transcription by RNA polymerase III
X	0090535	cellular_component	WICH complex
X	0090536	cellular_component	NoRC complex
X	0090537	cellular_component	CERF complex
X	0110016	cellular_component	B-WICH complex
X	0140374	biological_process	antiviral innate immune response
X	0140658	molecular_function	ATP-dependent chromatin remodeler activity
X	0140750	molecular_function	nucleosome array spacer activity
X	0140751	molecular_function	histone octamer slider activity
X	1905213	biological_process	negative regulation of mitotic chromosome condensation

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

Chain

Residue

Details

---

site_id	SWS_FT_FI2
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_FI3
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
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_FI5
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P84243","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
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_FI8
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_FI9
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_FI10
Number of Residues	8
Details	DNA binding: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	6
Details	Modified residue: {"description":"N6-propionyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	2
Details	Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI13
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_FI14
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_FI15
Number of Residues	4
Details	Modified residue: {"description":"Phosphotyrosine","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-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI17
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_FI18
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_FI19
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_FI20
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_FI21
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_FI22
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_FI23
Number of Residues	2
Details	Modified residue: {"description":"N5-methylglutamine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI24
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_FI25
Number of Residues	7
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	330
Details	Domain: {"description":"Helicase ATP-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI29
Number of Residues	6
Details	Motif: {"description":"DEAH box"}

Chain

Residue

Details

---

site_id	SWS_FT_FI30
Number of Residues	14
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI31
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---