CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012551
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Delta(24)-sterol reductase 
Protein Synonyms/Alias
 24-dehydrocholesterol reductase; 3-beta-hydroxysterol delta-24-reductase; Diminuto/dwarf1 homolog; Seladin-1 
Gene Name
 DHCR24 
Gene Synonyms/Alias
 KIAA0018 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
76QRVRDIQKQVREWKEubiquitination[1, 2]
87EWKEQGSKTFMCTGRubiquitination[2]
254GLEAICAKFTHESQRubiquitination[2, 3, 4, 5, 6]
301NSIGNYYKPWFFKHVubiquitination[2, 3, 6, 7]
313KHVENYLKTNREGLEubiquitination[1, 2, 4, 6, 7, 8]
367PPKISLLKLTQGETLubiquitination[1, 2, 3, 4, 5, 6, 7]
376TQGETLRKLYEQHHVubiquitination[2, 3, 6]
459SCMRQLEKFVRSVHGubiquitination[2]
492FDGSLYHKLREKLGCubiquitination[1, 3, 6]
496LYHKLREKLGCQDAFubiquitination[2, 5]
509AFPEVYDKICKAARHubiquitination[2]
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] 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] 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]
 [4] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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
Functional Description
 Catalyzes the reduction of the delta-24 double bond of sterol intermediates. Protects cells from oxidative stress by reducing caspase 3 activity during apoptosis induced by oxidative stress. Also protects against amyloid-beta peptide-induced apoptosis. 
Sequence Annotation
 DOMAIN 58 234 FAD-binding PCMH-type.
 NP_BIND 163 175 FAD (Potential).  
Keyword
 Cholesterol biosynthesis; Cholesterol metabolism; Complete proteome; Disease mutation; Endoplasmic reticulum; FAD; Golgi apparatus; Lipid biosynthesis; Lipid metabolism; Membrane; NADP; Oxidoreductase; Reference proteome; Signal; Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis; Sterol metabolism; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 516 AA 
Protein Sequence
MEPAVSLAVC ALLFLLWVRL KGLEFVLIHQ RWVFVCLFLL PLSLIFDIYY YVRAWVVFKL 60
SSAPRLHEQR VRDIQKQVRE WKEQGSKTFM CTGRPGWLTV SLRVGKYKKT HKNIMINLMD 120
ILEVDTKKQI VRVEPLVTMG QVTALLTSIG WTLPVLPELD DLTVGGLIMG TGIESSSHKY 180
GLFQHICTAY ELVLADGSFV RCTPSENSDL FYAVPWSCGT LGFLVAAEIR IIPAKKYVKL 240
RFEPVRGLEA ICAKFTHESQ RQENHFVEGL LYSLDEAVIM TGVMTDEAEP SKLNSIGNYY 300
KPWFFKHVEN YLKTNREGLE YIPLRHYYHR HTRSIFWELQ DIIPFGNNPI FRYLFGWMVP 360
PKISLLKLTQ GETLRKLYEQ HHVVQDMLVP MKCLQQALHT FQNDIHVYPI WLCPFILPSQ 420
PGLVHPKGNE AELYIDIGAY GEPRVKHFEA RSCMRQLEKF VRSVHGFQML YADCYMNREE 480
FWEMFDGSLY HKLREKLGCQ DAFPEVYDKI CKAARH 516 
Gene Ontology
 GO:0005856; C:cytoskeleton; IEA:Compara.
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0005789; C:endoplasmic reticulum membrane; NAS:UniProtKB.
 GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0050614; F:delta24-sterol reductase activity; IEA:EC.
 GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
 GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IDA:MGI.
 GO:0042605; F:peptide antigen binding; IPI:UniProtKB.
 GO:0008762; F:UDP-N-acetylmuramate dehydrogenase activity; IEA:InterPro.
 GO:0042987; P:amyloid precursor protein catabolic process; IEA:Compara.
 GO:0007050; P:cell cycle arrest; NAS:UniProtKB.
 GO:0016044; P:cellular membrane organization; IEA:Compara.
 GO:0006695; P:cholesterol biosynthetic process; ISS:UniProtKB.
 GO:0030539; P:male genitalia development; IEA:Compara.
 GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
 GO:0008285; P:negative regulation of cell proliferation; IEA:Compara.
 GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
 GO:0031639; P:plasminogen activation; IEA:Compara.
 GO:0008104; P:protein localization; IEA:Compara.
 GO:0007265; P:Ras protein signal transduction; IEA:Compara.
 GO:1901214; P:regulation of neuron death; NAS:UniProtKB.
 GO:0009725; P:response to hormone stimulus; IEA:Compara.
 GO:0006979; P:response to oxidative stress; IEP:UniProtKB.
 GO:0043588; P:skin development; ISS:UniProtKB. 
Interpro
 IPR016169; CO_DH_flavot_FAD-bd_sub2.
 IPR016166; FAD-bd_2.
 IPR006094; Oxid_FAD_bind_N. 
Pfam
 PF01565; FAD_binding_4 
SMART
  
PROSITE
 PS51387; FAD_PCMH 
PRINTS