PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
11589694-10	2001	Recently, the structure of human cytosolic PLA(2) (cPLA(2)) was solved, showing a novel Ser-Asp active site dyad [1].	Aspartic Acid	92-95	phospholipase A2 group IVA	Homo sapiens	33-49	
16814865-3	2006	However, a number of other serine acylhydrolases (patatin, Group VI PLA2s, Pseudomonas aeruginosa ExoU and NTE) contain the Ser/Asp catalytic dyad characteristic of Group IV PLA2s, and recent structural analysis of patatin has confirmed its structural similarity to cPLA2alpha.	Aspartic Acid	128-131	phospholipase A2 group IVA	Homo sapiens	266-276	
28063500-3	2017	cPLA2alpha is composed of an N-terminal C2 domain and a C-terminal catalytic domain that contains the Ser-Asp catalytic dyad.	Aspartic Acid	106-109	phospholipase A2 group IVA	Homo sapiens	0-10	
15249229-3	2004	Comparison of this catalytic domain with those of the mouse homologue, human cytosolic PLA(2) (cPLA(2)), and the plant PLA(2) patatin reveals that an amino acid sequence of a short segment around Asp-627 of iPLA(2)gamma is conserved among these PLA(2)s, in addition to the Ser-483-containing lipase motif; the corresponding serine and aspartate in cPLA(2) and patatin are known to form a catalytic dyad.	Aspartic Acid	196-199	phospholipase A2 group IVA	Homo sapiens	77-93	
15249229-3	2004	Comparison of this catalytic domain with those of the mouse homologue, human cytosolic PLA(2) (cPLA(2)), and the plant PLA(2) patatin reveals that an amino acid sequence of a short segment around Asp-627 of iPLA(2)gamma is conserved among these PLA(2)s, in addition to the Ser-483-containing lipase motif; the corresponding serine and aspartate in cPLA(2) and patatin are known to form a catalytic dyad.	Aspartic Acid	196-199	phospholipase A2 group IVA	Homo sapiens	95-102	
15249229-3	2004	Comparison of this catalytic domain with those of the mouse homologue, human cytosolic PLA(2) (cPLA(2)), and the plant PLA(2) patatin reveals that an amino acid sequence of a short segment around Asp-627 of iPLA(2)gamma is conserved among these PLA(2)s, in addition to the Ser-483-containing lipase motif; the corresponding serine and aspartate in cPLA(2) and patatin are known to form a catalytic dyad.	Aspartic Acid	196-199	phospholipase A2 group IVA	Homo sapiens	348-355	
15249229-3	2004	Comparison of this catalytic domain with those of the mouse homologue, human cytosolic PLA(2) (cPLA(2)), and the plant PLA(2) patatin reveals that an amino acid sequence of a short segment around Asp-627 of iPLA(2)gamma is conserved among these PLA(2)s, in addition to the Ser-483-containing lipase motif; the corresponding serine and aspartate in cPLA(2) and patatin are known to form a catalytic dyad.	Aspartic Acid	335-344	phospholipase A2 group IVA	Homo sapiens	77-93	
15249229-3	2004	Comparison of this catalytic domain with those of the mouse homologue, human cytosolic PLA(2) (cPLA(2)), and the plant PLA(2) patatin reveals that an amino acid sequence of a short segment around Asp-627 of iPLA(2)gamma is conserved among these PLA(2)s, in addition to the Ser-483-containing lipase motif; the corresponding serine and aspartate in cPLA(2) and patatin are known to form a catalytic dyad.	Aspartic Acid	335-344	phospholipase A2 group IVA	Homo sapiens	95-102	
11589694-10	2001	Recently, the structure of human cytosolic PLA(2) (cPLA(2)) was solved, showing a novel Ser-Asp active site dyad [1].	Aspartic Acid	92-95	phospholipase A2 group IVA	Homo sapiens	51-58	
8702602-6	1996	cPLA2 contains a catalytic aspartic acid motif common to the subtilisin family of serine proteases.	Aspartic Acid	27-40	phospholipase A2 group IVA	Homo sapiens	0-5	
8702602-12	1996	Arg-200, Ser-228, and Asp-549 are conserved in cPLA2 from six species and also in four nonmammalian phospholipase B enzymes.	Aspartic Acid	22-25	phospholipase A2 group IVA	Homo sapiens	47-52	
8702602-13	1996	Our results, supported by circular dichroism, provide evidence that Asp-549 and Arg-200 are critical to the enzyme"s function and suggest that the cPLA2 catalytic center is novel.	Aspartic Acid	68-71	phospholipase A2 group IVA	Homo sapiens	147-152	
10747887-2	2000	Cytosolic phospholipase A(2)alpha (cPLA(2)alpha; type IVA), an essential initiator of stimulus-dependent arachidonic acid (AA) metabolism, underwent caspase-mediated cleavage at Asp(522) during apoptosis.	Aspartic Acid	178-181	phospholipase A2 group IVA	Homo sapiens	35-47