CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012747
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Lanosterol 14-alpha demethylase 
Protein Synonyms/Alias
 LDM; CYPLI; Cytochrome P450 51A1; Cytochrome P450-14DM; Cytochrome P45014DM; Cytochrome P450LI; Sterol 14-alpha demethylase 
Gene Name
 CYP51A1 
Gene Synonyms/Alias
 CYP51 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
91FLENAYEKYGPVFSFubiquitination[1]
121AALLFNSKNEDLNAEubiquitination[1, 2, 3]
141LTTPVFGKGVAYDVPubiquitination[1, 2, 3, 4, 5, 6, 7, 8, 9]
156NPVFLEQKKMLKSGLubiquitination[1, 2, 3, 5, 9, 10]
157PVFLEQKKMLKSGLNubiquitination[8]
160LEQKKMLKSGLNIAHubiquitination[1, 5, 7, 9]
177QHVSIIEKETKEYFEubiquitination[1]
180SIIEKETKEYFESWGubiquitination[1, 3]
213ASHCLHGKEIRSQLNubiquitination[1]
261DRAHREIKDIFYKAIubiquitination[1, 5, 9]
266EIKDIFYKAIQKRRQubiquitination[1, 5, 9]
277KRRQSQEKIDDILQTubiquitination[1]
342KKCYLEQKTVCGENLubiquitination[1]
358PLTYDQLKDLNLLDRubiquitination[1, 10]
368NLLDRCIKETLRLRPubiquitination[8]
412PTVNQRLKDSWVERLubiquitination[1, 3, 8]
436DNPASGEKFAYVPFGubiquitination[1, 2, 4, 5, 6, 7, 8, 9, 10, 11]
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] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [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]
 [10] 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]
 [11] 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
Functional Description
 Catalyzes C14-demethylation of lanosterol; it transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol. 
Sequence Annotation
 METAL 449 449 Iron (heme axial ligand).  
Keyword
 3D-structure; Alternative splicing; Cholesterol biosynthesis; Cholesterol metabolism; Complete proteome; Endoplasmic reticulum; Heme; Iron; Lipid biosynthesis; Lipid metabolism; Membrane; Metal-binding; Microsome; Monooxygenase; NADP; Oxidoreductase; Polymorphism; Reference proteome; Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis; Sterol metabolism; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 503 AA 
Protein Sequence
MLLLGLLQAG GSVLGQAMEK VTGGNLLSML LIACAFTLSL VYLIRLAAGH LVQLPAGVKS 60
PPYIFSPIPF LGHAIAFGKS PIEFLENAYE KYGPVFSFTM VGKTFTYLLG SDAAALLFNS 120
KNEDLNAEDV YSRLTTPVFG KGVAYDVPNP VFLEQKKMLK SGLNIAHFKQ HVSIIEKETK 180
EYFESWGESG EKNVFEALSE LIILTASHCL HGKEIRSQLN EKVAQLYADL DGGFSHAAWL 240
LPGWLPLPSF RRRDRAHREI KDIFYKAIQK RRQSQEKIDD ILQTLLDATY KDGRPLTDDE 300
VAGMLIGLLL AGQHTSSTTS AWMGFFLARD KTLQKKCYLE QKTVCGENLP PLTYDQLKDL 360
NLLDRCIKET LRLRPPIMIM MRMARTPQTV AGYTIPPGHQ VCVSPTVNQR LKDSWVERLD 420
FNPDRYLQDN PASGEKFAYV PFGAGRHRCI GENFAYVQIK TIWSTMLRLY EFDLIDGYFP 480
TVNYTTMIHT PENPVIRYKR RSK 503 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0009055; F:electron carrier activity; IEA:InterPro.
 GO:0020037; F:heme binding; IDA:UniProtKB.
 GO:0005506; F:iron ion binding; IEA:InterPro.
 GO:0008398; F:sterol 14-demethylase activity; IDA:UniProtKB.
 GO:0006695; P:cholesterol biosynthetic process; TAS:Reactome.
 GO:0033488; P:cholesterol biosynthetic process via 24,25-dihydrolanosterol; IEA:Compara.
 GO:0006805; P:xenobiotic metabolic process; TAS:Reactome. 
Interpro
 IPR001128; Cyt_P450.
 IPR017972; Cyt_P450_CS.
 IPR002403; Cyt_P450_E_grp-IV. 
Pfam
 PF00067; p450 
SMART
  
PROSITE
 PS00086; CYTOCHROME_P450 
PRINTS
 PR00465; EP450IV.
 PR00385; P450.