CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000421
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serine palmitoyltransferase 1 
Protein Synonyms/Alias
 Long chain base biosynthesis protein 1; LCB 1; Serine-palmitoyl-CoA transferase 1; SPT 1; SPT1 
Gene Name
 SPTLC1 
Gene Synonyms/Alias
 LCB1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
45LLFSKTYKLQERSDLubiquitination[1]
55ERSDLTVKEKEELIEubiquitination[2, 3]
57SDLTVKEKEELIEEWubiquitination[2, 3, 4, 5, 6, 7]
75PLVPPVPKDHPALNYubiquitination[3]
92VSGPPSHKTVVNGKEubiquitination[2, 3, 4, 6]
118LLDNPRVKAAALASLubiquitination[6]
126AAALASLKKYGVGTCubiquitination[3, 6]
127AALASLKKYGVGTCGubiquitination[6]
197AACFAIQKGLQASRSubiquitination[4, 5, 6, 7]
207QASRSDIKLFKHNDMubiquitination[2, 3, 6]
210RSDIKLFKHNDMADLubiquitination[2, 3, 6, 7]
222ADLERLLKEQEIEDQubiquitination[2, 3, 6]
230EQEIEDQKNPRKARVubiquitination[2, 3, 7]
375EKCGQIHKALQGISGubiquitination[4, 6, 7]
384LQGISGLKVVGESLSubiquitination[2, 3]
465ERAASTIKEVAQAVLubiquitination[2, 3, 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] 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]
 [3] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [4] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [5] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [6] 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]
 [7] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
Functional Description
 Serine palmitoyltransferase (SPT). The heterodimer formed with SPTLC2 or SPTLC3 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-SPTLC3-SPTSSA isozyme uses both C14-CoA and C16-CoA as substrates, with a slight preference for C14-CoA. The SPTLC1- SPTLC2-SPTSSB complex shows a strong preference for C18-CoA substrate, while the SPTLC1-SPTLC3-SPTSSB isozyme displays an ability to use a broader range of acyl-CoAs, without apparent preference. 
Sequence Annotation
  
Keyword
 Acyltransferase; Alternative splicing; Complete proteome; Disease mutation; Endoplasmic reticulum; Lipid metabolism; Membrane; Neuropathy; Polymorphism; Pyridoxal phosphate; Reference proteome; Sphingolipid metabolism; Transferase; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 473 AA 
Protein Sequence
MATATEQWVL VEMVQALYEA PAYHLILEGI LILWIIRLLF SKTYKLQERS DLTVKEKEEL 60
IEEWQPEPLV PPVPKDHPAL NYNIVSGPPS HKTVVNGKEC INFASFNFLG LLDNPRVKAA 120
ALASLKKYGV GTCGPRGFYG TFDVHLDLED RLAKFMKTEE AIIYSYGFAT IASAIPAYSK 180
RGDIVFVDRA ACFAIQKGLQ ASRSDIKLFK HNDMADLERL LKEQEIEDQK NPRKARVTRR 240
FIVVEGLYMN TGTICPLPEL VKLKYKYKAR IFLEESLSFG VLGEHGRGVT EHYGINIDDI 300
DLISANMENA LASIGGFCCG RSFVIDHQRL SGQGYCFSAS LPPLLAAAAI EALNIMEENP 360
GIFAVLKEKC GQIHKALQGI SGLKVVGESL SPAFHLQLEE STGSREQDVR LLQEIVDQCM 420
NRSIALTQAR YLEKEEKCLP PPSIRVVVTV EQTEEELERA ASTIKEVAQA VLL 473 
Gene Ontology
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0035339; C:SPOTS 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
 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