CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020263
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Elongation of very long chain fatty acids protein 1 
Protein Synonyms/Alias
 3-keto acyl-CoA synthase ELOVL1; ELOVL fatty acid elongase 1; ELOVL FA elongase 1; Very-long-chain 3-oxoacyl-CoA synthase 1 
Gene Name
 ELOVL1 
Gene Synonyms/Alias
 SSC1; CGI-88 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
54PRIMANRKPFQLRGFubiquitination[1, 2]
275NGAPGIAKVKAN***ubiquitination[3]
277APGIAKVKAN*****ubiquitination[3]
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
Functional Description
 Condensing enzyme that catalyzes the synthesis of both saturated and monounsaturated very long chain fatty acids. Exhibits activity toward saturated C18 to C26 acyl-CoA substrates, with the highest activity towards C22:0 acyl-CoA. Important for saturated C24:0 and monounsaturated C24:1 sphingolipid synthesis. 
Sequence Annotation
 MOTIF 275 279 Di-lysine motif (Potential).  
Keyword
 Alternative splicing; Complete proteome; Endoplasmic reticulum; Fatty acid biosynthesis; Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism; Membrane; Reference proteome; Transferase; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 279 AA 
Protein Sequence
MEAVVNLYQE VMKHADPRIQ GYPLMGSPLL MTSILLTYVY FVLSLGPRIM ANRKPFQLRG 60
FMIVYNFSLV ALSLYIVYEF LMSGWLSTYT WRCDPVDYSN SPEALRMVRV AWLFLFSKFI 120
ELMDTVIFIL RKKDGQVTFL HVFHHSVLPW SWWWGVKIAP GGMGSFHAMI NSSVHVIMYL 180
YYGLSAFGPV AQPYLWWKKH MTAIQLIQFV LVSLHISQYY FMSSCNYQYP VIIHLIWMYG 240
TIFFMLFSNF WYHSYTKGKR LPRALQQNGA PGIAKVKAN 279 
Gene Ontology
 GO:0030176; C:integral to endoplasmic reticulum membrane; NAS:UniProtKB.
 GO:0009922; F:fatty acid elongase activity; IDA:UniProtKB.
 GO:0034625; P:fatty acid elongation, monounsaturated fatty acid; IDA:UniProtKB.
 GO:0019367; P:fatty acid elongation, saturated fatty acid; IDA:UniProtKB.
 GO:0035338; P:long-chain fatty-acyl-CoA biosynthetic process; TAS:Reactome.
 GO:0030148; P:sphingolipid biosynthetic process; IMP:UniProtKB.
 GO:0019432; P:triglyceride biosynthetic process; TAS:Reactome.
 GO:0042761; P:very long-chain fatty acid biosynthetic process; IDA:UniProtKB. 
Interpro
 IPR002076; GNS1_SUR4. 
Pfam
 PF01151; ELO 
SMART
  
PROSITE
 PS01188; ELO 
PRINTS