| Tag | Content |
|---|
| CPLM ID | CPLM-010628 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Serine palmitoyltransferase 2 |
Protein Synonyms/Alias | Long chain base biosynthesis protein 2; LCB 2; Long chain base biosynthesis protein 2a; LCB2a; Serine-palmitoyl-CoA transferase 2; SPT 2 |
Gene Name | Sptlc2 |
Gene Synonyms/Alias | Lcb2 |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 536 | VGDLLQLKYSRHRLV | ubiquitination | [1] |
|
Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
Functional Description | Serine palmitoyltransferase (SPT). The heterodimer formed with LCB1/SPTLC1 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC2-SPTSSB complex displays a preference for C18-CoA substrate (By similarity). |
Sequence Annotation | MOD_RES 377 377 N6-(pyridoxal phosphate)lysine (By |
Keyword | Acyltransferase; Complete proteome; Endoplasmic reticulum; Lipid metabolism; Membrane; Pyridoxal phosphate; Reference proteome; Sphingolipid metabolism; Transferase; Transmembrane; Transmembrane helix. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 560 AA |
Protein Sequence | MRPEPGGCCC RRPMRANGCV KNGEVRNGYL RSSTATVAAA GQIHHVTENG GLYKRPFNEA 60
FEETPMLVAV LTYVGYGVLT LFGYLRDFLR HWRIEKCHHA TEREEQKDFV SLYQDFENFY 120
TRNLYMRIRD NWNRPICSVP GAKVDIMERK SHDYNWSFKY TGNIIKGVIN MGSYNYLGFA 180
RNTGSCQEAA AEVLKEYGAG VCSTRQEIGN LDKHEELEKL VARFLGVEAA MTYGMGFATN 240
SMNIPALVGK GCLILSDELN HASLVLGARL SGATIRIFKH NNMQSLEKLL KDAIVYGQPR 300
TRRPWKKILI LVEGIYSMEG SIVRLPEVIA LKKKYKAYLY LDEAHSIGAL GPSGRGVVDY 360
FGLDPEDVDV MMGTFTKSFG ASGGYIGGKK ELIDYLRTHS HSAVYATSMS PPVMEQIITS 420
MKCIMGQDGT SLGKECIQQL AENTRYFRRR LKEMGFIIYG NEDSPVVPLM LYMPAKIGAF 480
GREMLKRNIG VVVVGFPATP IIESRARFCL SAAHTKEILD TALKEIDEVG DLLQLKYSRH 540
RLVPLLDRPF DETTYEETED 560 |
Gene Ontology | GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. GO:0005739; C:mitochondrion; IDA:MGI. GO:0017059; C:serine C-palmitoyltransferase complex; ISA:MGI. GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. GO:0004758; F:serine C-palmitoyltransferase activity; IDA:MGI. GO:0046513; P:ceramide biosynthetic process; IMP:MGI. GO:0046511; P:sphinganine biosynthetic process; IDA:MGI. GO:0006686; P:sphingomyelin biosynthetic process; IMP:MGI. GO:0046512; P:sphingosine biosynthetic process; IMP:MGI. |
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Pfam | |
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