CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000422
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
 KIAA0526; LCB2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
161HDYNWSFKYTGNIIKubiquitination[1, 2]
194SCQEAAAKVLEEYGAubiquitination[3]
215QEIGNLDKHEELEELubiquitination[3]
293QSLEKLLKDAIVYGQubiquitination[3]
391SGGYIGGKKELIDYLubiquitination[3]
392GGYIGGKKELIDYLRubiquitination[3]
436QDGTSLGKECVQQLAubiquitination[3]
538VGDLLQLKYSRHRLVubiquitination[4]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983] 
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. 
Sequence Annotation
 MOD_RES 379 379 N6-(pyridoxal phosphate)lysine (By  
Keyword
 Acyltransferase; Complete proteome; Disease mutation; Endoplasmic reticulum; Lipid metabolism; Membrane; Neuropathy; Pyridoxal phosphate; Reference proteome; Sphingolipid metabolism; Transferase; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 562 AA 
Protein Sequence
MRPEPGGCCC RRTVRANGCV ANGEVRNGYV RSSAAAAAAA AAGQIHHVTQ NGGLYKRPFN 60
EAFEETPMLV AVLTYVGYGV LTLFGYLRDF LRYWRIEKCH HATEREEQKD FVSLYQDFEN 120
FYTRNLYMRI RDNWNRPICS VPGARVDIME RQSHDYNWSF KYTGNIIKGV INMGSYNYLG 180
FARNTGSCQE AAAKVLEEYG AGVCSTRQEI GNLDKHEELE ELVARFLGVE AAMAYGMGFA 240
TNSMNIPALV GKGCLILSDE LNHASLVLGA RLSGATIRIF KHNNMQSLEK LLKDAIVYGQ 300
PRTRRPWKKI LILVEGIYSM EGSIVRLPEV IALKKKYKAY LYLDEAHSIG ALGPTGRGVV 360
EYFGLDPEDV DVMMGTFTKS FGASGGYIGG KKELIDYLRT HSHSAVYATS LSPPVVEQII 420
TSMKCIMGQD GTSLGKECVQ QLAENTRYFR RRLKEMGFII YGNEDSPVVP LMLYMPAKIG 480
AFGREMLKRN IGVVVVGFPA TPIIESRARF CLSAAHTKEI LDTALKEIDE VGDLLQLKYS 540
RHRLVPLLDR PFDETTYEET ED 562 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0017059; C:serine C-palmitoyltransferase complex; IDA:UniProtKB.
 GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
 GO:0004758; F:serine C-palmitoyltransferase activity; IDA:UniProtKB.
 GO:0046513; P:ceramide biosynthetic process; IEA:Compara.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome.
 GO:0046511; P:sphinganine biosynthetic process; IEA:Compara.
 GO:0030148; P:sphingolipid biosynthetic process; TAS:UniProtKB.
 GO:0006686; P:sphingomyelin biosynthetic process; IEA:Compara.
 GO:0046512; P:sphingosine biosynthetic process; IEA:Compara. 
Interpro
 IPR001917; Aminotrans_II_pyridoxalP_BS.
 IPR004839; Aminotransferase_I/II.
 IPR015424; PyrdxlP-dep_Trfase.
 IPR015421; PyrdxlP-dep_Trfase_major_sub1.
 IPR015422; PyrdxlP-dep_Trfase_major_sub2. 
Pfam
 PF00155; Aminotran_1_2 
SMART
  
PROSITE
 PS00599; AA_TRANSFER_CLASS_2 
PRINTS