PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
28902413-10	2017	In one patient, the plasma sphingolipid profile could functionally prove the pathogenicity of a mutation in SPTLC2.	Sphingolipids	27-39	serine palmitoyltransferase long chain base subunit 2	Homo sapiens	108-114	
21618344-2	2011	Mutations in SPTLC1 and SPTLC2, encoding the two subunits of serine palmitoyltransferase (SPT), the enzyme catalyzing the first and rate-limiting step in the de novo synthesis of sphingolipids, have been reported to cause HSAN-I.	Sphingolipids	179-192	serine palmitoyltransferase long chain base subunit 2	Homo sapiens	24-30	
12445191-3	2002	The key enzyme for de novo sphingolipid synthesis is serine palmitoyltransferase, which consists of two different subunits, named LCB1 and LCB2 proteins.	Sphingolipids	27-39	serine palmitoyltransferase long chain base subunit 2	Homo sapiens	139-143	
17070807-1	2006	A series of luciferase reporter constructs was prepared from a 1035-bp fragment of mouse genomic DNA flanking the 5"-coding sequence for the SPTLC2 subunit of serine palmitoyltransferase, the initial enzyme of de novo sphingolipid biosynthesis.	Sphingolipids	218-230	serine palmitoyltransferase long chain base subunit 2	Homo sapiens	141-147	
8921873-0	1996	Sphingolipid synthesis: identification and characterization of mammalian cDNAs encoding the Lcb2 subunit of serine palmitoyltransferase.	Sphingolipids	0-12	serine palmitoyltransferase long chain base subunit 2	Homo sapiens	92-96	
9788249-9	1998	Together, these results demonstrate that CHKs respond to UVB by increasing sphingolipid synthesis, primarily through increases in both LCB2 mRNA and protein levels, leading to increased SPT activity.	Sphingolipids	75-87	serine palmitoyltransferase long chain base subunit 2	Homo sapiens	135-139	
34785538-3	2022	Here, we show that SPTLC2, a subunit of the serine palmitoyltransferase (SPT) complex, catalyzing the first step in de novo sphingolipid synthesis, localizes dually to the ER and the outer mitochondrial membrane.	Sphingolipids	124-136	serine palmitoyltransferase long chain base subunit 2	Homo sapiens	19-25	
34785538-5	2022	Loss of SPTLC2 prevents the synthesis of mitochondrial sphingolipids and protects from palmitate-induced mitochondrial toxicity, a process dependent on mitochondrial ceramides.	Sphingolipids	55-68	serine palmitoyltransferase long chain base subunit 2	Homo sapiens	8-14	
34302797-5	2021	In the former, the selectivity of sphingolipid synthesis relies on a hydrogen bond interaction between Lys379 of SPTLC2 and the l-serine sidechain hydroxyl moiety.	Sphingolipids	34-46	serine palmitoyltransferase long chain base subunit 2	Homo sapiens	113-119	
30952607-6	2019	Protective CD8+ T cell responses in HSAN-I patient PBMCs and Sptlc2-deficient mice were restored by supplementing with sphingolipids and pharmacologically inhibiting ER stress-induced cell death.	Sphingolipids	119-132	serine palmitoyltransferase long chain base subunit 2	Homo sapiens	61-67	
34563520-2	2021	HSAN1 is caused by several missense mutations in the SPTLC1 and SPTLC2 subunit of the enzyme serine-palmitoyltransferase (SPT) -the key enzyme for the synthesis of sphingolipids.	Sphingolipids	164-177	serine palmitoyltransferase long chain base subunit 2	Homo sapiens	64-70	
33558761-2	2021	In humans, the first and rate-limiting step of sphingolipid synthesis is catalyzed by the serine palmitoyltransferase holocomplex, which consists of catalytic components (SPTLC1 and SPTLC2) and regulatory components (ssSPTa and ORMDL3).	Sphingolipids	47-59	serine palmitoyltransferase long chain base subunit 2	Homo sapiens	182-188