CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006729
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Squalene synthase 
Protein Synonyms/Alias
 SQS; SS; FPP:FPP farnesyltransferase; Farnesyl-diphosphate farnesyltransferase 
Gene Name
 FDFT1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
5***MEFVKCLGHPEEubiquitination[1, 2]
30GKRKVMPKMDQDSLSubiquitination[2]
41DSLSSSLKTCYKYLNubiquitination[1, 2, 3]
45SSLKTCYKYLNQTSRubiquitination[1, 2]
92DMTISVEKKVPLLHNubiquitination[4]
93MTISVEKKVPLLHNFubiquitination[2]
115DWRFMESKEKDRQVLubiquitination[2]
117RFMESKEKDRQVLEDubiquitination[2]
138EFRNLAEKYQTVIADubiquitination[2, 5]
160GMAEFLDKHVTSEQEubiquitination[4]
213SMGLFLQKTNIIRDYubiquitination[1, 2, 3, 4, 6, 7, 8, 9]
318KGAVKIRKGQAVTLMubiquitination[2, 4]
335ATNMPAVKAIIYQYMubiquitination[8]
358DSDPSSSKTRQIISTubiquitination[1, 2, 4, 8]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [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]
 [5] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [6] 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]
 [7] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [8] 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]
 [9] 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] 
Functional Description
  
Sequence Annotation
  
Keyword
 3D-structure; Cholesterol biosynthesis; Cholesterol metabolism; Complete proteome; Endoplasmic reticulum; Isoprene biosynthesis; Lipid biosynthesis; Lipid metabolism; Magnesium; Membrane; Multifunctional enzyme; NADP; Oxidoreductase; Polymorphism; Reference proteome; Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis; Sterol metabolism; Transferase; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 417 AA 
Protein Sequence
MEFVKCLGHP EEFYNLVRFR IGGKRKVMPK MDQDSLSSSL KTCYKYLNQT SRSFAAVIQA 60
LDGEMRNAVC IFYLVLRALD TLEDDMTISV EKKVPLLHNF HSFLYQPDWR FMESKEKDRQ 120
VLEDFPTISL EFRNLAEKYQ TVIADICRRM GIGMAEFLDK HVTSEQEWDK YCHYVAGLVG 180
IGLSRLFSAS EFEDPLVGED TERANSMGLF LQKTNIIRDY LEDQQGGREF WPQEVWSRYV 240
KKLGDFAKPE NIDLAVQCLN ELITNALHHI PDVITYLSRL RNQSVFNFCA IPQVMAIATL 300
AACYNNQQVF KGAVKIRKGQ AVTLMMDATN MPAVKAIIYQ YMEEIYHRIP DSDPSSSKTR 360
QIISTIRTQN LPNCQLISRS HYSPIYLSFV MLLAALSWQY LTTLSQVTED YVQTGEH 417 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
 GO:0016021; C:integral to membrane; TAS:ProtInc.
 GO:0004310; F:farnesyl-diphosphate farnesyltransferase activity; TAS:Reactome.
 GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
 GO:0051996; F:squalene synthase activity; IEA:EC.
 GO:0044255; P:cellular lipid metabolic process; TAS:Reactome.
 GO:0006695; P:cholesterol biosynthetic process; TAS:Reactome.
 GO:0045338; P:farnesyl diphosphate metabolic process; IEA:Compara.
 GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW. 
Interpro
 IPR002060; Squ/phyt_synthse.
 IPR006449; Squal_synth.
 IPR019845; Squalene/phytoene_synthase_CS.
 IPR008949; Terpenoid_synth. 
Pfam
 PF00494; SQS_PSY 
SMART
  
PROSITE
 PS01044; SQUALEN_PHYTOEN_SYN_1
 PS01045; SQUALEN_PHYTOEN_SYN_2 
PRINTS