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7K0I

Human serine palmitoyltransferase complex SPTLC1/SPLTC2/ssSPTa

Functional Information from GO Data
ChainGOidnamespacecontents
A0004758molecular_functionserine C-palmitoyltransferase activity
A0005515molecular_functionprotein binding
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0006629biological_processlipid metabolic process
A0006665biological_processsphingolipid metabolic process
A0006686biological_processsphingomyelin biosynthetic process
A0009058biological_processbiosynthetic process
A0016020cellular_componentmembrane
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0017059cellular_componentserine palmitoyltransferase complex
A0030148biological_processsphingolipid biosynthetic process
A0030170molecular_functionpyridoxal phosphate binding
A0043604biological_processamide biosynthetic process
A0046511biological_processsphinganine biosynthetic process
A0046512biological_processsphingosine biosynthetic process
A0046513biological_processceramide biosynthetic process
A1904504biological_processpositive regulation of lipophagy
A1904649biological_processregulation of fat cell apoptotic process
B0004758molecular_functionserine C-palmitoyltransferase activity
B0005515molecular_functionprotein binding
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0006629biological_processlipid metabolic process
B0006665biological_processsphingolipid metabolic process
B0006686biological_processsphingomyelin biosynthetic process
B0009058biological_processbiosynthetic process
B0016020cellular_componentmembrane
B0016740molecular_functiontransferase activity
B0016746molecular_functionacyltransferase activity
B0017059cellular_componentserine palmitoyltransferase complex
B0030148biological_processsphingolipid biosynthetic process
B0030170molecular_functionpyridoxal phosphate binding
B0046511biological_processsphinganine biosynthetic process
B0046512biological_processsphingosine biosynthetic process
B0046513biological_processceramide biosynthetic process
B0060612biological_processadipose tissue development
B1904504biological_processpositive regulation of lipophagy
C0004758molecular_functionserine C-palmitoyltransferase activity
C0005515molecular_functionprotein binding
C0005783cellular_componentendoplasmic reticulum
C0005789cellular_componentendoplasmic reticulum membrane
C0006629biological_processlipid metabolic process
C0006665biological_processsphingolipid metabolic process
C0008104biological_processprotein localization
C0016020cellular_componentmembrane
C0017059cellular_componentserine palmitoyltransferase complex
C0030148biological_processsphingolipid biosynthetic process
C0046512biological_processsphingosine biosynthetic process
C0046513biological_processceramide biosynthetic process
D0004758molecular_functionserine C-palmitoyltransferase activity
D0005515molecular_functionprotein binding
D0005783cellular_componentendoplasmic reticulum
D0005789cellular_componentendoplasmic reticulum membrane
D0006629biological_processlipid metabolic process
D0006665biological_processsphingolipid metabolic process
D0006686biological_processsphingomyelin biosynthetic process
D0009058biological_processbiosynthetic process
D0016020cellular_componentmembrane
D0016740molecular_functiontransferase activity
D0016746molecular_functionacyltransferase activity
D0017059cellular_componentserine palmitoyltransferase complex
D0030148biological_processsphingolipid biosynthetic process
D0030170molecular_functionpyridoxal phosphate binding
D0043604biological_processamide biosynthetic process
D0046511biological_processsphinganine biosynthetic process
D0046512biological_processsphingosine biosynthetic process
D0046513biological_processceramide biosynthetic process
D1904504biological_processpositive regulation of lipophagy
D1904649biological_processregulation of fat cell apoptotic process
E0004758molecular_functionserine C-palmitoyltransferase activity
E0005515molecular_functionprotein binding
E0005783cellular_componentendoplasmic reticulum
E0005789cellular_componentendoplasmic reticulum membrane
E0006629biological_processlipid metabolic process
E0006665biological_processsphingolipid metabolic process
E0006686biological_processsphingomyelin biosynthetic process
E0009058biological_processbiosynthetic process
E0016020cellular_componentmembrane
E0016740molecular_functiontransferase activity
E0016746molecular_functionacyltransferase activity
E0017059cellular_componentserine palmitoyltransferase complex
E0030148biological_processsphingolipid biosynthetic process
E0030170molecular_functionpyridoxal phosphate binding
E0046511biological_processsphinganine biosynthetic process
E0046512biological_processsphingosine biosynthetic process
E0046513biological_processceramide biosynthetic process
E0060612biological_processadipose tissue development
E1904504biological_processpositive regulation of lipophagy
F0004758molecular_functionserine C-palmitoyltransferase activity
F0005515molecular_functionprotein binding
F0005783cellular_componentendoplasmic reticulum
F0005789cellular_componentendoplasmic reticulum membrane
F0006629biological_processlipid metabolic process
F0006665biological_processsphingolipid metabolic process
F0008104biological_processprotein localization
F0016020cellular_componentmembrane
F0017059cellular_componentserine palmitoyltransferase complex
F0030148biological_processsphingolipid biosynthetic process
F0046512biological_processsphingosine biosynthetic process
F0046513biological_processceramide biosynthetic process
Functional Information from PROSITE/UniProt
site_idPS00599
Number of Residues10
DetailsAA_TRANSFER_CLASS_2 Aminotransferases class-II pyridoxal-phosphate attachment site. TFTKSFGASG
ChainResidueDetails
BTHR376-GLY385

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine; by ABL","evidences":[{"source":"PubMed","id":"23629659","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues116
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsTopological domain: {"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsSite: {"description":"Within the serine palmitoyltransferase (SPT) complex, defines the length of the acyl chain-binding pocket, determining the acyl-CoA substrate preference"}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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