3Q68

Structure of the Vps75-Rtt109 histone chaperone-lysine acetyltransferase complex (Full-length proteins in space group P212121)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000785	cellular_component	chromatin
A	0003682	molecular_function	chromatin binding
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005829	cellular_component	cytosol
A	0006303	biological_process	double-strand break repair via nonhomologous end joining
A	0006334	biological_process	nucleosome assembly
A	0010698	molecular_function	acetyltransferase activator activity
A	0015031	biological_process	protein transport
A	0036211	biological_process	protein modification process
A	0042393	molecular_function	histone binding
A	0042802	molecular_function	identical protein binding
A	0070775	cellular_component	H3 histone acetyltransferase complex
A	2000617	biological_process	obsolete positive regulation of histone H3-K9 acetylation
B	0000785	cellular_component	chromatin
B	0003682	molecular_function	chromatin binding
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005829	cellular_component	cytosol
B	0006303	biological_process	double-strand break repair via nonhomologous end joining
B	0006334	biological_process	nucleosome assembly
B	0010698	molecular_function	acetyltransferase activator activity
B	0015031	biological_process	protein transport
B	0036211	biological_process	protein modification process
B	0042393	molecular_function	histone binding
B	0042802	molecular_function	identical protein binding
B	0070775	cellular_component	H3 histone acetyltransferase complex
B	2000617	biological_process	obsolete positive regulation of histone H3-K9 acetylation
C	0000785	cellular_component	chromatin
C	0004402	molecular_function	histone acetyltransferase activity
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0006325	biological_process	chromatin organization
C	0006334	biological_process	nucleosome assembly
C	0006355	biological_process	regulation of DNA-templated transcription
C	0006357	biological_process	regulation of transcription by RNA polymerase II
C	0006974	biological_process	DNA damage response
C	0010468	biological_process	regulation of gene expression
C	0010484	molecular_function	histone H3 acetyltransferase activity
C	0010526	biological_process	retrotransposon silencing
C	0016740	molecular_function	transferase activity
C	0032931	molecular_function	histone H3K56 acetyltransferase activity
C	0036211	biological_process	protein modification process
C	0036408	molecular_function	histone H3K14 acetyltransferase activity
C	0043007	biological_process	maintenance of rDNA
C	0043992	molecular_function	histone H3K9 acetyltransferase activity
C	0043994	molecular_function	histone H3K23 acetyltransferase activity
C	0044017	molecular_function	histone H3K27 acetyltransferase activity
C	0061733	molecular_function	peptide-lysine-N-acetyltransferase activity
C	0070775	cellular_component	H3 histone acetyltransferase complex
C	1990414	biological_process	replication-born double-strand break repair via sister chromatid exchange
C	2001032	biological_process	regulation of double-strand break repair via nonhomologous end joining

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:18707894

Chain	Residue	Details
C	ASP288
B	SER3

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site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:18568037, ECO:0000269|PubMed:18707894, ECO:0000269|PubMed:18719104, ECO:0000269|PubMed:21256037, ECO:0007744|PDB:2ZFN, ECO:0007744|PDB:3CZ7, ECO:0007744|PDB:3Q33, ECO:0007744|PDB:3Q35, ECO:0007744|PDB:3QM0

Chain	Residue	Details
C	ALA88
C	ARG97
C	HIS211

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site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:18568037, ECO:0007744|PDB:3QM0

Chain	Residue	Details
C	PHE192

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site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:18568037, ECO:0000269|PubMed:21256037, ECO:0007744|PDB:3Q33, ECO:0007744|PDB:3Q35, ECO:0007744|PDB:3QM0

Chain	Residue	Details
C	ALA196

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site_id	SWS_FT_FI5
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:18707894, ECO:0000269|PubMed:18719104, ECO:0000269|PubMed:21256037, ECO:0007744|PDB:2ZFN, ECO:0007744|PDB:3CZ7, ECO:0007744|PDB:3Q33, ECO:0007744|PDB:3Q35

Chain	Residue	Details
C	TRP221

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site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: N6-acetyllysine; by autocatalysis => ECO:0000269|PubMed:18568037, ECO:0000269|PubMed:18707894, ECO:0000269|PubMed:18719104

Chain	Residue	Details
C	ALY290

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