CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020661
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Very-long-chain enoyl-CoA reductase 
Protein Synonyms/Alias
 Synaptic glycoprotein SC2; Trans-2,3-enoyl-CoA reductase; TER 
Gene Name
 Tecr 
Gene Synonyms/Alias
 Gpsn2 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
2******MKHYEVEIRubiquitination[1]
16RDAKTREKLCFLDKVubiquitination[1]
22EKLCFLDKVEPQATIacetylation[2]
22EKLCFLDKVEPQATIubiquitination[1]
38EIKTLFTKTHPQWYPubiquitination[1]
57LRLDPKGKSLKDEDVubiquitination[1]
60DPKGKSLKDEDVLQKacetylation[2]
60DPKGKSLKDEDVLQKubiquitination[1]
67KDEDVLQKLPVGTTAubiquitination[1]
116VPFIYGRKYDFTSSRacetylation[3]
291GKHRSYLKEFRDYPPubiquitination[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]
 [2] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [3] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647
Functional Description
 Reduces trans-2,3-stearoyl-CoA to stearoyl-CoA of long and very long chain fatty acids (By similarity). 
Sequence Annotation
 MOD_RES 22 22 N6-acetyllysine (By similarity).
 MOD_RES 116 116 N6-acetyllysine.
 CARBOHYD 164 164 N-linked (GlcNAc...) (Potential).
 CARBOHYD 247 247 N-linked (GlcNAc...) (Potential).  
Keyword
 Acetylation; Complete proteome; Endoplasmic reticulum; Glycoprotein; Lipid biosynthesis; Lipid metabolism; Membrane; NADP; Oxidoreductase; Reference proteome; Steroid biosynthesis; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 308 AA 
Protein Sequence
MKHYEVEIRD AKTREKLCFL DKVEPQATIS EIKTLFTKTH PQWYPARQSL RLDPKGKSLK 60
DEDVLQKLPV GTTATLYFRD LGAQISWVTV FLTEYAGPLF IYLLFYFRVP FIYGRKYDFT 120
SSRHTVVHLA CMCHSFHYIK RLLETLFVHR FSHGTMPLRN IFKNCTYYWG FAAWMAYYIN 180
HPLYTPPTYG VQQVKLALAV FVICQLGNFS IHMALRDLRP AGSKTRKIPY PTKNPFTWLF 240
LLVSCPNYTY EVGSWIGFAI LTQCVPVALF SLVGFTQMTI WAKGKHRSYL KEFRDYPPLR 300
MPIIPFLL 308 
Gene Ontology
 GO:0030176; C:integral to endoplasmic reticulum membrane; ISS:UniProtKB.
 GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
 GO:0030497; P:fatty acid elongation; ISS:UniProtKB.
 GO:0006694; P:steroid biosynthetic process; IEA:UniProtKB-KW.
 GO:0042761; P:very long-chain fatty acid biosynthetic process; ISS:UniProtKB. 
Interpro
 IPR001104; 3-oxo-5_a-steroid_4-DH_C. 
Pfam
 PF02544; Steroid_dh 
SMART
  
PROSITE
 PS50244; S5A_REDUCTASE 
PRINTS