3P5J

The structure of the human RNase H2 complex defines key interaction interfaces relevant to enzyme function and human disease

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003676	molecular_function	nucleic acid binding
A	0003723	molecular_function	RNA binding
A	0004518	molecular_function	nuclease activity
A	0004519	molecular_function	endonuclease activity
A	0004523	molecular_function	RNA-DNA hybrid ribonuclease activity
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005829	cellular_component	cytosol
A	0006298	biological_process	mismatch repair
A	0006401	biological_process	RNA catabolic process
A	0016070	biological_process	RNA metabolic process
A	0016787	molecular_function	hydrolase activity
A	0032299	cellular_component	ribonuclease H2 complex
A	0043137	biological_process	DNA replication, removal of RNA primer
A	0046872	molecular_function	metal ion binding
A	0090304	biological_process	nucleic acid metabolic process
B	0001701	biological_process	in utero embryonic development
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0006298	biological_process	mismatch repair
B	0006401	biological_process	RNA catabolic process
B	0009259	biological_process	ribonucleotide metabolic process
B	0010389	biological_process	regulation of G2/M transition of mitotic cell cycle
B	0010467	biological_process	gene expression
B	0010629	biological_process	negative regulation of gene expression
B	0032299	cellular_component	ribonuclease H2 complex
B	0048144	biological_process	fibroblast proliferation
B	0048146	biological_process	positive regulation of fibroblast proliferation
B	2000001	biological_process	regulation of DNA damage checkpoint
C	0005634	cellular_component	nucleus
C	0006298	biological_process	mismatch repair
C	0006401	biological_process	RNA catabolic process
C	0032299	cellular_component	ribonuclease H2 complex

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	MOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:Q8TDP1

Chain	Residue	Details
C	MET1
A	GLU35
A	ASP142

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site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q5TBB1

Chain	Residue	Details
B	LYS292

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q5TBB1

Chain	Residue	Details
B	SER293

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079

Chain	Residue	Details
A	SER258

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