9B6C

Human asparagine synthetase Arg-142 to Ile-142 (R142I) variant

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004066	molecular_function	asparagine synthase (glutamine-hydrolyzing) activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005829	cellular_component	cytosol
A	0006529	biological_process	asparagine biosynthetic process
A	0008652	biological_process	amino acid biosynthetic process
A	0016874	molecular_function	ligase activity
A	0042149	biological_process	cellular response to glucose starvation
A	0043066	biological_process	negative regulation of apoptotic process
A	0045931	biological_process	positive regulation of mitotic cell cycle
A	0070981	biological_process	L-asparagine biosynthetic process
B	0000166	molecular_function	nucleotide binding
B	0004066	molecular_function	asparagine synthase (glutamine-hydrolyzing) activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005829	cellular_component	cytosol
B	0006529	biological_process	asparagine biosynthetic process
B	0008652	biological_process	amino acid biosynthetic process
B	0016874	molecular_function	ligase activity
B	0042149	biological_process	cellular response to glucose starvation
B	0043066	biological_process	negative regulation of apoptotic process
B	0045931	biological_process	positive regulation of mitotic cell cycle
B	0070981	biological_process	L-asparagine biosynthetic process

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"For GATase activity","evidences":[{"source":"PubMed","id":"2564390","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2573597","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	12
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	2
Details	Site: {"description":"Important for beta-aspartyl-AMP intermediate formation","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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