CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008032
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Lanosterol synthase 
Protein Synonyms/Alias
 2,3-epoxysqualene--lanosterol cyclase; Oxidosqualene--lanosterol cyclase; OSC; hOSC 
Gene Name
 LSS 
Gene Synonyms/Alias
 OSC 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
15RRRGGPYKTEPATDLubiquitination[1, 2, 3]
61YALGLDTKNYFKDLPubiquitination[1, 3]
65LDTKNYFKDLPKAHTubiquitination[1, 2, 3]
148WGLHIEDKSTVFGTAubiquitination[3]
318LRQRAVQKLYEHIVAubiquitination[1, 3, 4]
331VADDRFTKSISIGPIubiquitination[1, 3, 4, 5]
340ISIGPISKTINMLVRubiquitination[3]
432DNPPDYQKYYRQMRKubiquitination[1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11]
439KYYRQMRKGGFSFSTubiquitination[3, 4]
470AVLLLQEKCPHVTEHubiquitination[3, 4]
506GFATYETKRGGHLLEubiquitination[1, 2, 3, 4, 5, 8, 9]
680GVRCLLEKQLPNGDWubiquitination[2, 3, 4, 8, 9]
698NIAGVFNKSCAISYTubiquitination[3, 4, 8]
Reference
 [1] 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]
 [2] 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]
 [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]
 [4] 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]
 [5] 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]
 [6] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] 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]
 [11] 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
 Catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol nucleus. 
Sequence Annotation
 REPEAT 124 165 PFTB 1.
 REPEAT 483 528 PFTB 2.
 REPEAT 560 600 PFTB 3.
 REPEAT 612 653 PFTB 4.
 ACT_SITE 232 232 Proton acceptor.
 ACT_SITE 455 455 Proton donor (Probable).  
Keyword
 3D-structure; Alternative splicing; Complete proteome; Direct protein sequencing; Endoplasmic reticulum; Isomerase; Lipid biosynthesis; Lipid metabolism; Membrane; Polymorphism; Reference proteome; Repeat; Steroid biosynthesis. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 732 AA 
Protein Sequence
MTEGTCLRRR GGPYKTEPAT DLGRWRLNCE RGRQTWTYLQ DERAGREQTG LEAYALGLDT 60
KNYFKDLPKA HTAFEGALNG MTFYVGLQAE DGHWTGDYGG PLFLLPGLLI TCHVARIPLP 120
AGYREEIVRY LRSVQLPDGG WGLHIEDKST VFGTALNYVS LRILGVGPDD PDLVRARNIL 180
HKKGGAVAIP SWGKFWLAVL NVYSWEGLNT LFPEMWLFPD WAPAHPSTLW CHCRQVYLPM 240
SYCYAVRLSA AEDPLVQSLR QELYVEDFAS IDWLAQRNNV APDELYTPHS WLLRVVYALL 300
NLYEHHHSAH LRQRAVQKLY EHIVADDRFT KSISIGPISK TINMLVRWYV DGPASTAFQE 360
HVSRIPDYLW MGLDGMKMQG TNGSQIWDTA FAIQALLEAG GHHRPEFSSC LQKAHEFLRL 420
SQVPDNPPDY QKYYRQMRKG GFSFSTLDCG WIVSDCTAEA LKAVLLLQEK CPHVTEHIPR 480
ERLCDAVAVL LNMRNPDGGF ATYETKRGGH LLELLNPSEV FGDIMIDYTY VECTSAVMQA 540
LKYFHKRFPE HRAAEIRETL TQGLEFCRRQ QRADGSWEGS WGVCFTYGTW FGLEAFACMG 600
QTYRDGTACA EVSRACDFLL SRQMADGGWG EDFESCEERR YLQSAQSQIH NTCWAMMGLM 660
AVRHPDIEAQ ERGVRCLLEK QLPNGDWPQE NIAGVFNKSC AISYTSYRNI FPIWALGRFS 720
QLYPERALAG HP 732 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
 GO:0005811; C:lipid particle; IDA:UniProtKB.
 GO:0000250; F:lanosterol synthase activity; TAS:ProtInc.
 GO:0006695; P:cholesterol biosynthetic process; IMP:BHF-UCL. 
Interpro
 IPR001330; Prenyltrans.
 IPR018333; Squalene_cyclase.
 IPR002365; Terpene_synthase_CS.
 IPR008930; Terpenoid_cyclase/PrenylTrfase. 
Pfam
 PF00432; Prenyltrans 
SMART
  
PROSITE
 PS01074; TERPENE_SYNTHASES 
PRINTS