7K0J

Human serine palmitoyltransferase complex SPTLC1/SPLTC2/ssSPTa protomer

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004758	molecular_function	serine C-palmitoyltransferase activity
A	0005515	molecular_function	protein binding
A	0005783	cellular_component	endoplasmic reticulum
A	0005789	cellular_component	endoplasmic reticulum membrane
A	0006629	biological_process	lipid metabolic process
A	0006665	biological_process	sphingolipid metabolic process
A	0006686	biological_process	sphingomyelin biosynthetic process
A	0009058	biological_process	biosynthetic process
A	0016020	cellular_component	membrane
A	0016740	molecular_function	transferase activity
A	0016746	molecular_function	acyltransferase activity
A	0017059	cellular_component	serine palmitoyltransferase complex
A	0030148	biological_process	sphingolipid biosynthetic process
A	0030170	molecular_function	pyridoxal phosphate binding
A	0043604	biological_process	amide biosynthetic process
A	0046511	biological_process	sphinganine biosynthetic process
A	0046512	biological_process	sphingosine biosynthetic process
A	0046513	biological_process	ceramide biosynthetic process
A	1904504	biological_process	positive regulation of lipophagy
A	1904649	biological_process	regulation of fat cell apoptotic process
B	0004758	molecular_function	serine C-palmitoyltransferase activity
B	0005515	molecular_function	protein binding
B	0005783	cellular_component	endoplasmic reticulum
B	0005789	cellular_component	endoplasmic reticulum membrane
B	0006629	biological_process	lipid metabolic process
B	0006665	biological_process	sphingolipid metabolic process
B	0006686	biological_process	sphingomyelin biosynthetic process
B	0009058	biological_process	biosynthetic process
B	0016020	cellular_component	membrane
B	0016740	molecular_function	transferase activity
B	0016746	molecular_function	acyltransferase activity
B	0017059	cellular_component	serine palmitoyltransferase complex
B	0030148	biological_process	sphingolipid biosynthetic process
B	0030170	molecular_function	pyridoxal phosphate binding
B	0046511	biological_process	sphinganine biosynthetic process
B	0046512	biological_process	sphingosine biosynthetic process
B	0046513	biological_process	ceramide biosynthetic process
B	0060612	biological_process	adipose tissue development
B	1904504	biological_process	positive regulation of lipophagy
C	0004758	molecular_function	serine C-palmitoyltransferase activity
C	0005515	molecular_function	protein binding
C	0005783	cellular_component	endoplasmic reticulum
C	0005789	cellular_component	endoplasmic reticulum membrane
C	0006629	biological_process	lipid metabolic process
C	0006665	biological_process	sphingolipid metabolic process
C	0008104	biological_process	protein localization
C	0016020	cellular_component	membrane
C	0017059	cellular_component	serine palmitoyltransferase complex
C	0030148	biological_process	sphingolipid biosynthetic process
C	0046512	biological_process	sphingosine biosynthetic process
C	0046513	biological_process	ceramide biosynthetic process

Functional Information from PROSITE/UniProt

site_id	PS00599
Number of Residues	10
Details	AA_TRANSFER_CLASS_2 Aminotransferases class-II pyridoxal-phosphate attachment site. TFTKSFGASG

Chain	Residue	Details
B	THR376-GLY385

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Modified residue: {"description":"Phosphotyrosine; by ABL","evidences":[{"source":"PubMed","id":"23629659","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	58
Details	Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	4
Details	Topological domain: {"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	1
Details	Site: {"description":"Within the serine palmitoyltransferase (SPT) complex, defines the length of the acyl chain-binding pocket, determining the acyl-CoA substrate preference"}

Chain

Residue

Details

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