CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017742
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Phosphatidylcholine:ceramide cholinephosphotransferase 2 
Protein Synonyms/Alias
 Sphingomyelin synthase 2 
Gene Name
 SGMS2 
Gene Synonyms/Alias
 SMS2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
55GLRKGTKKYPDYIQIubiquitination[1]
71MPTESRNKFPLEWWKubiquitination[1]
116LSPPLPDKFFDYIDRubiquitination[2]
363KIGEDNEKST*****ubiquitination[2]
Reference
 [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [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
Functional Description
 Sphingomyelin synthases synthesize the sphingolipid, sphingomyelin, through transfer of the phosphatidyl head group, phosphatidylcholine, on to the primary hydroxyl of ceramide. The reaction is bidirectional depending on the respective levels of the sphingolipid and ceramide. Plasma membrane SMS2 can also convert phosphatidylethanolamine (PE) to ceramide phosphatidylethanolamine (CPE). Major form in liver. Required for cell growth in certain cell types. Regulator of cell surface levels of ceramide, an important mediator of signal transduction and apoptosis. Regulation of sphingomyelin (SM) levels at the cell surface affects insulin sensitivity. 
Sequence Annotation
 ACT_SITE 229 229
 ACT_SITE 272 272
 ACT_SITE 276 276
 LIPID 331 331 S-palmitoyl cysteine.
 LIPID 332 332 S-palmitoyl cysteine.
 LIPID 343 343 S-palmitoyl cysteine.
 LIPID 348 348 S-palmitoyl cysteine.  
Keyword
 Cell membrane; Complete proteome; Golgi apparatus; Kinase; Lipid metabolism; Lipoprotein; Membrane; Palmitate; Polymorphism; Reference proteome; Sphingolipid metabolism; Transferase; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 365 AA 
Protein Sequence
MDIIETAKLE EHLENQPSDP TNTYARPAEP VEEENKNGNG KPKSLSSGLR KGTKKYPDYI 60
QIAMPTESRN KFPLEWWKTG IAFIYAVFNL VLTTVMITVV HERVPPKELS PPLPDKFFDY 120
IDRVKWAFSV SEINGIILVG LWITQWLFLR YKSIVGRRFC FIIGTLYLYR CITMYVTTLP 180
VPGMHFQCAP KLNGDSQAKV QRILRLISGG GLSITGSHIL CGDFLFSGHT VTLTLTYLFI 240
KEYSPRHFWW YHLICWLLSA AGIICILVAH EHYTIDVIIA YYITTRLFWW YHSMANEKNL 300
KVSSQTNFLS RAWWFPIFYF FEKNVQGSIP CCFSWPLSWP PGCFKSSCKK YSRVQKIGED 360
NEKST 365 
Gene Ontology
 GO:0045203; C:integral to cell outer membrane; IEA:Compara.
 GO:0030173; C:integral to Golgi membrane; IDA:UniProtKB.
 GO:0005887; C:integral to plasma membrane; IDA:UniProtKB.
 GO:0047493; F:ceramide cholinephosphotransferase activity; IDA:UniProtKB.
 GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
 GO:0033188; F:sphingomyelin synthase activity; IEA:EC.
 GO:0030148; P:sphingolipid biosynthetic process; TAS:Reactome.
 GO:0006686; P:sphingomyelin biosynthetic process; IDA:UniProtKB. 
Interpro
 IPR025749; Sphingomyelin_synth-like_dom. 
Pfam
 PF14360; PAP2_C 
SMART
  
PROSITE
  
PRINTS