Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6NQ3

Crystal Structure of a SUZ12-RBBP4-PHF19-JARID2 Heterotetrameric Complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000118	cellular_component	histone deacetylase complex
A	0000122	biological_process	negative regulation of transcription by RNA polymerase II
A	0000781	cellular_component	chromosome, telomeric region
A	0000785	cellular_component	chromatin
A	0000978	molecular_function	RNA polymerase II cis-regulatory region sequence-specific DNA binding
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005829	cellular_component	cytosol
A	0006260	biological_process	DNA replication
A	0006281	biological_process	DNA repair
A	0006325	biological_process	chromatin organization
A	0006334	biological_process	nucleosome assembly
A	0006335	biological_process	DNA replication-dependent chromatin assembly
A	0006338	biological_process	chromatin remodeling
A	0006355	biological_process	regulation of DNA-templated transcription
A	0006974	biological_process	DNA damage response
A	0007420	biological_process	brain development
A	0008094	molecular_function	ATP-dependent activity, acting on DNA
A	0008285	biological_process	negative regulation of cell population proliferation
A	0016581	cellular_component	NuRD complex
A	0016589	cellular_component	NURF complex
A	0030336	biological_process	negative regulation of cell migration
A	0030512	biological_process	negative regulation of transforming growth factor beta receptor signaling pathway
A	0031492	molecular_function	nucleosomal DNA binding
A	0032991	cellular_component	protein-containing complex
A	0033186	cellular_component	CAF-1 complex
A	0035098	cellular_component	ESC/E(Z) complex
A	0042393	molecular_function	histone binding
A	0042659	biological_process	regulation of cell fate specification
A	0042826	molecular_function	histone deacetylase binding
A	0045892	biological_process	negative regulation of DNA-templated transcription
A	0045893	biological_process	positive regulation of DNA-templated transcription
A	0070822	cellular_component	Sin3-type complex
A	1902455	biological_process	negative regulation of stem cell population maintenance
A	1902459	biological_process	positive regulation of stem cell population maintenance
A	1904949	cellular_component	ATPase complex
A	2000736	biological_process	regulation of stem cell differentiation
E	0000118	cellular_component	histone deacetylase complex
E	0000122	biological_process	negative regulation of transcription by RNA polymerase II
E	0000781	cellular_component	chromosome, telomeric region
E	0000785	cellular_component	chromatin
E	0000978	molecular_function	RNA polymerase II cis-regulatory region sequence-specific DNA binding
E	0005515	molecular_function	protein binding
E	0005634	cellular_component	nucleus
E	0005654	cellular_component	nucleoplasm
E	0005829	cellular_component	cytosol
E	0006260	biological_process	DNA replication
E	0006281	biological_process	DNA repair
E	0006325	biological_process	chromatin organization
E	0006334	biological_process	nucleosome assembly
E	0006335	biological_process	DNA replication-dependent chromatin assembly
E	0006338	biological_process	chromatin remodeling
E	0006355	biological_process	regulation of DNA-templated transcription
E	0006974	biological_process	DNA damage response
E	0007420	biological_process	brain development
E	0008094	molecular_function	ATP-dependent activity, acting on DNA
E	0008285	biological_process	negative regulation of cell population proliferation
E	0016581	cellular_component	NuRD complex
E	0016589	cellular_component	NURF complex
E	0030336	biological_process	negative regulation of cell migration
E	0030512	biological_process	negative regulation of transforming growth factor beta receptor signaling pathway
E	0031492	molecular_function	nucleosomal DNA binding
E	0032991	cellular_component	protein-containing complex
E	0033186	cellular_component	CAF-1 complex
E	0035098	cellular_component	ESC/E(Z) complex
E	0042393	molecular_function	histone binding
E	0042659	biological_process	regulation of cell fate specification
E	0042826	molecular_function	histone deacetylase binding
E	0045892	biological_process	negative regulation of DNA-templated transcription
E	0045893	biological_process	positive regulation of DNA-templated transcription
E	0070822	cellular_component	Sin3-type complex
E	1902455	biological_process	negative regulation of stem cell population maintenance
E	1902459	biological_process	positive regulation of stem cell population maintenance
E	1904949	cellular_component	ATPase complex
E	2000736	biological_process	regulation of stem cell differentiation

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue ZN B 1001

Chain	Residue
B	CYS450
B	CYS453
B	HIS466
B	HIS471

site_id	AC2
Number of Residues	4
Details	binding site for residue ZN F 1001

Chain	Residue
F	CYS450
F	CYS453
F	HIS466
F	HIS471

Functional Information from PROSITE/UniProt

site_id	PS00028
Number of Residues	22
Details	ZINC_FINGER_C2H2_1 Zinc finger C2H2 type domain signature. Cpw..CtlnCrklysllkHlklc.H

Chain	Residue	Details
B	CYS450-HIS471

site_id	PS00678
Number of Residues	15
Details	WD_REPEATS_1 Trp-Asp (WD) repeats signature. LLSAsdDhTICLWDI

Chain	Residue	Details
A	LEU193-ILE207
A	LEU289-LEU303
A	LEU333-LEU347

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	98
Details	Repeat: {"description":"WD 2","evidences":[{"source":"PubMed","id":"39460621","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8TX8","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	90
Details	Repeat: {"description":"WD 4","evidences":[{"source":"PubMed","id":"39460621","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8TX8","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	86
Details	Repeat: {"description":"WD 5","evidences":[{"source":"PubMed","id":"39460621","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8TX8","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	112
Details	Repeat: {"description":"WD 6","evidences":[{"source":"PubMed","id":"39460621","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8TX8","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	64
Details	Repeat: {"description":"WD 7","evidences":[{"source":"PubMed","id":"39460621","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8TX8","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q60972","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"25755297","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	46
Details	Zinc finger: {"description":"C2H2-type"}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	27
Details	Region: {"description":"Interaction with JARID2 and EPOP","evidences":[{"source":"PubMed","id":"29499137","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	2
Details	Site: {"description":"Breakpoint for translocation to form JAZF1-SUZ12 oncogene"}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	98
Details	Region: {"description":"Interaction with SUZ12","evidences":[{"source":"PubMed","id":"29499137","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	26
Details	Region: {"description":"Important for PRC2 dimer stability","evidences":[{"source":"PubMed","id":"31959557","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)