Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

9PGC

Trident submodule from human SRCAP-nucleosome complex in the fully-engaged state (focused refinement)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000786	cellular_component	nucleosome
A	0000812	cellular_component	Swr1 complex
A	0003713	molecular_function	transcription coactivator activity
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0006338	biological_process	chromatin remodeling
A	0006355	biological_process	regulation of DNA-templated transcription
A	0010468	biological_process	regulation of gene expression
A	0016604	cellular_component	nuclear body
A	0016887	molecular_function	ATP hydrolysis activity
A	0032991	cellular_component	protein-containing complex
A	0042393	molecular_function	histone binding
A	0045944	biological_process	positive regulation of transcription by RNA polymerase II
A	0048471	cellular_component	perinuclear region of cytoplasm
A	0140658	molecular_function	ATP-dependent chromatin remodeler activity
A	0141156	biological_process	cAMP/PKA signal transduction
B	0000122	biological_process	negative regulation of transcription by RNA polymerase II
B	0000786	cellular_component	nucleosome
B	0000812	cellular_component	Swr1 complex
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0006338	biological_process	chromatin remodeling
B	0006355	biological_process	regulation of DNA-templated transcription
B	0016607	cellular_component	nuclear speck
B	0032991	cellular_component	protein-containing complex
B	0035267	cellular_component	NuA4 histone acetyltransferase complex
B	0042393	molecular_function	histone binding
B	0042981	biological_process	regulation of apoptotic process
B	0045815	biological_process	transcription initiation-coupled chromatin remodeling
B	0045893	biological_process	positive regulation of DNA-templated transcription
B	0051726	biological_process	regulation of cell cycle
B	0140713	molecular_function	histone chaperone activity
B	1905168	biological_process	positive regulation of double-strand break repair via homologous recombination
B	2000779	biological_process	regulation of double-strand break repair
K	0000723	biological_process	telomere maintenance
K	0000776	cellular_component	kinetochore
K	0000785	cellular_component	chromatin
K	0000786	cellular_component	nucleosome
K	0003407	biological_process	neural retina development
K	0003682	molecular_function	chromatin binding
K	0003713	molecular_function	transcription coactivator activity
K	0005515	molecular_function	protein binding
K	0005634	cellular_component	nucleus
K	0005654	cellular_component	nucleoplasm
K	0005886	cellular_component	plasma membrane
K	0006275	biological_process	regulation of DNA replication
K	0006282	biological_process	regulation of DNA repair
K	0006338	biological_process	chromatin remodeling
K	0006355	biological_process	regulation of DNA-templated transcription
K	0006357	biological_process	regulation of transcription by RNA polymerase II
K	0007165	biological_process	signal transduction
K	0007399	biological_process	nervous system development
K	0008284	biological_process	positive regulation of cell population proliferation
K	0016363	cellular_component	nuclear matrix
K	0016514	cellular_component	SWI/SNF complex
K	0016586	cellular_component	RSC-type complex
K	0021510	biological_process	spinal cord development
K	0030071	biological_process	regulation of mitotic metaphase/anaphase transition
K	0031011	cellular_component	Ino80 complex
K	0031492	molecular_function	nucleosomal DNA binding
K	0032991	cellular_component	protein-containing complex
K	0033044	biological_process	regulation of chromosome organization
K	0035060	cellular_component	brahma complex
K	0035267	cellular_component	NuA4 histone acetyltransferase complex
K	0042981	biological_process	regulation of apoptotic process
K	0045582	biological_process	positive regulation of T cell differentiation
K	0045596	biological_process	negative regulation of cell differentiation
K	0045597	biological_process	positive regulation of cell differentiation
K	0045663	biological_process	positive regulation of myoblast differentiation
K	0045739	biological_process	positive regulation of DNA repair
K	0045893	biological_process	positive regulation of DNA-templated transcription
K	0045995	biological_process	regulation of embryonic development
K	0048731	biological_process	system development
K	0051726	biological_process	regulation of cell cycle
K	0060382	biological_process	regulation of DNA strand elongation
K	0070316	biological_process	regulation of G0 to G1 transition
K	0071564	cellular_component	npBAF complex
K	0140288	cellular_component	GBAF complex
K	0160108	biological_process	animal gross anatomical part developmental process
K	1902459	biological_process	positive regulation of stem cell population maintenance
K	1904507	biological_process	positive regulation of telomere maintenance in response to DNA damage
K	1905168	biological_process	positive regulation of double-strand break repair via homologous recombination
K	2000045	biological_process	regulation of G1/S transition of mitotic cell cycle
K	2000779	biological_process	regulation of double-strand break repair
K	2000781	biological_process	positive regulation of double-strand break repair
K	2000819	biological_process	regulation of nucleotide-excision repair

Functional Information from PROSITE/UniProt

site_id	PS00141
Number of Residues	12
Details	ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. LILDSGATHTTA

Chain	Residue	Details
K	LEU168-ALA179

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

Chain	Residue	Details
K	TRP410-GLU418

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	165
Details	Domain: {"description":"Helicase ATP-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	153
Details	Domain: {"description":"Helicase C-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU00542","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17081983","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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