Protein detail
SPTC2
Serine palmitoyltransferase 2 (EC 2.3.1.50) (Long chain base biosynthesis protein 2) (LCB 2) (Long chain base biosynthesis protein 2a) (LCB2a) (Serine-palmitoyl-CoA transferase 2) (SPT 2)
Entry name SPTC2 | UniProt ID | EVMP confidence score 0.50 |
Supporting publications (n) 2 | Transmembrane count 1 | Protein classification |
EVMP confidence score
Annotation confidence score; open for threshold definitions.
Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40Basic Information8
Protein Names
Serine palmitoyltransferase 2 (EC 2.3.1.50) (Long chain base biosynthesis protein 2) (LCB 2) (Long chain base biosynthesis protein 2a) (LCB2a) (Serine-palmitoyl-CoA transferase 2) (SPT 2)
Protein Function (5)
- Human disease related genes:Nervous system diseases:Other nervous and sensory system diseases
- ENZYME proteins:Transferases
- Potential drug targets
- Enzymes
- Disease related genes
Transmembrane
67..87; Helical
Transmembrane Count
1
Ensembl
Entrez Gene Symbol
Supporting publications (n)
2
EVMP confidence score
0.50
Function & Pathway7
Protein Function (5)
- Human disease related genes:Nervous system diseases:Other nervous and sensory system diseases
- ENZYME proteins:Transferases
- Potential drug targets
- Enzymes
- Disease related genes
Cellular Component (2)
Molecular Function (3)
Biological Process (3)
KEGG (4)
Reactome (3)
Mediation Categories
Metabolism mediation
Relations & Evidence25
Ligand-Receptor Signaling (14)
14 records.
| Category | Parent | Database | Transmitter | Receiver | Secreted | Plasma Membrane (Transmembrane) | Plasma Membrane (Peripheral) |
|---|---|---|---|---|---|---|---|
| transmembrane | transmembrane | Ramilowski_location | No | No | No | No | No |
| transmembrane | transmembrane | OmniPath | No | No | No | No | No |
| receptor | receptor | scConnect | No | Yes | No | No | No |
| transmembrane | transmembrane_predicted | Phobius | No | No | No | No | No |
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Protein Complex Composition (10)
10 records.
| Component Name | Component Gene Symbols | Component UniProt ID | Stoichiometry | Database | Database IDs | References |
|---|---|---|---|---|---|---|
| Serine-palmitoyltransferase (SPTLC1SPTLC2) complex | SPTLC1SPTLC2 | O15269O15270 | 0:0 | CORUMhu.MAPhu.MAP2 | CORUM:6968 | 17023427 |
| Serine-palmitoyltransferase (SPTLC1SPTLC2SPTLC3) complex | SPTLC1SPTLC2SPTLC3 | O15269O15270Q9NUV7 | 1:1:1 | CompleatCORUM | Compleat:HC759CORUM:6969 | 173310738058731 |
| Serine-palmitoyltransferase (SPTLC1SPTLC2ssSPTa) complex | SPTLC1SPTLC2SPTSSA | O15269O15270Q969W0 | 2:2:2 | CORUMComplexPortalPDB | PDB:7K0IPDB:7k0lintact:EBI-26964783PDB:7k0iCORUM:6974PDB:7k0jPDB:7k0k | 194168511475529233558761 |
| Serine-palmitoyltransferase (SPTLC1SPTLC2ssSPTb) complex | SPTLC1SPTLC2SPTSSB | O15269O15270Q8NFR3 | 2:2:2 | CORUMComplexPortal | intact:EBI-26967735CORUM:6973 | 194168511475529233558761 |
| serine C-palmitoyltransferase complex | SPTLC1SPTLC2SPTLC3SPTSSASPTSSB | O15269O15270Q8NFR3Q969W0Q9NUV7 | 1:1:1:1:1 | Compleat | Compleat:HC1101 | 1733107319416851 |
| HSPA1LORMDL3PIGOSPTLC1SPTLC2UBC | O15269O15270P0CG48P34931Q8N138Q8TEQ8 | 1:1:1:1:1:1 | NetworkBlastCompleat | Compleat:HC9359 | ||
| ORMDL3PIGFPIGOSPTLC1SPTLC2UBC | O15269O15270P0CG48Q07326Q8N138Q8TEQ8 | 1:1:1:1:1:1 | NetworkBlastCompleat | Compleat:HC5296 | ||
| ORMDL2ORMDL3PIGOSPTLC1SPTLC2UBC | O15269O15270P0CG48Q53FV1Q8N138Q8TEQ8 | 1:1:1:1:1:1 | NetworkBlastCompleat | Compleat:HC4708 | ||
| ORMDL1ORMDL3PIGOSPTLC1SPTLC2UBC | O15269O15270P0CG48Q8N138Q8TEQ8Q9P0S3 | 1:1:1:1:1:1 | NetworkBlastCompleat | Compleat:HC7774 | ||
| ORMDL3SPTLC1SPTLC2SPTSSA | O15269O15270Q8N138Q969W0 | 2:2:2:2 | PDB | PDB:7k0mPDB:7cqkPDB:7k0pPDB:7k0qPDB:7yiuPDB:6m4oPDB:7cqiPDB:7k0oPDB:7yj1PDB:7yj2PDB:7yiyPDB:6m4nPDB:7k0n |
Isolation & Detection Technology (1)
1 record.
| EV Isolation Method | Detection Method | Number of References | References |
|---|---|---|---|
| Differential UltracentrifugationSize Exclusion Chromatography | Mass spectrometry | 1 | 40689422 |
Sequence, Structure & Domains9
Sequences
Length
562
Mass
62,924
Sequence
MRPEPGGCCCRRTVRANGCVANGEVRNGYVRSSAAAAAAAAAGQIHHVTQNGGLYKRPFNEAFEETPMLVAVLTYVGYGVLTLFGYLRDFLRYWRIEKCHHATEREEQKDFVSLYQDFENFYTRNLYMRIRDNWNRPICSVPGARVDIMERQSHDYNWSFKYTGNIIKGVINMGSYNYLGFARNTGSCQEAAAKVLEEYGAGVCSTRQEIGNLDKHEELEELVARFLGVEAAMAYGMGFATNSMNIPALVGKGCLILSDELNHASLVLGARLSGATIRIFKHNNMQSLEKLLKDAIVYGQPRTRRPWKKILILVEGIYSMEGSIVRLPEVIALKKKYKAYLYLDEAHSIGALGPTGRGVVEYFGLDPEDVDVMMGTFTKSFGASGGYIGGKKELIDYLRTHSHSAVYATSLSPPVVEQIITSMKCIMGQDGTSLGKECVQQLAENTRYFRRRLKEMGFIIYGNEDSPVVPLMLYMPAKIGAFGREMLKRNIGVVVVGFPATPIIESRARFCLSAAHTKEILDTALKEIDEVGDLLQLKYSRHRLVPLLDRPFDETTYEETED
3D Structural Models
Turn
92..94; 117..120; 207..210; 301..303; 319..322; 346..351; 428..430; 455..457; 498..500; 503..505
Helix
68..91; 106..108; 121..125; 127..129; 131..133; 178..180; 187..198; 214..227; 238..243; 246..248; 264..273; 285..298; 327..336; 358..362; 367..369; 392..401; 403..407; 413..427; 434..454; 476..488; 518..535
Beta Strand
50..52; 54..57; 100..102; 109..111; 137..140; 143..152; 154..159; 161..172; 184..186; 204..206; 229..234; 254..259; 276..280; 308..318; 340..344; 352..356; 371..383; 386..390; 431..433; 467..472; 494..496; 507..511; 513..515
3D Structure
Electron microscopy (17)
Domain & Motif Annotations
Protein Families
Class-II pyridoxal-phosphate-dependent aminotransferase family
Sequence Similarities
Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family.
Clinical Relevance3
Interaction Protein (2)
ENSG00000054356ENSG00000090054
Interaction Count
2
Interaction Dataset (2)
biogrid_bioplexintact_biogrid_opencell
Supporting Publications2
| PMID | Title | Abstract |
|---|---|---|
| 33709510 | Unbiased proteomic profiling of host cell extracellular vesicle composition and dynamics upon HIV-1 infection. | No abstract available |
| 38731868 | The Deep Proteomics Approach Identified Extracellular Vesicular Proteins Correlated to Extracellular Matrix in Type One and Two Endometrial Cancer. | No abstract available |