CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004481
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 NADPH--cytochrome P450 reductase 
Protein Synonyms/Alias
 CPR; P450R 
Gene Name
 NCP1 
Gene Synonyms/Alias
 CPR1; NCPR1; PRD1; YHR042W 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
169GAAKKAEKHLSAAGAacetylation[1]
181AGAIRLGKLGEADDGubiquitination[2]
219HLDEQEAKFTSQFQYubiquitination[3]
666VGILSRGKSITTDEAubiquitination[2, 3, 4, 5, 6]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [3] Identification, analysis, and prediction of protein ubiquitination sites.
 Radivojac P, Vacic V, Haynes C, Cocklin RR, Mohan A, Heyen JW, Goebl MG, Iakoucheva LM.
 Proteins. 2010 Feb 1;78(2):365-80. [PMID: 19722269]
 [4] A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery.
 Hitchcock AL, Auld K, Gygi SP, Silver PA.
 Proc Natl Acad Sci U S A. 2003 Oct 28;100(22):12735-40. [PMID: 14557538]
 [5] Computational identification of ubiquitylation sites from protein sequences.
 Tung CW, Ho SY.
 BMC Bioinformatics. 2008 Jul 15;9:310. [PMID: 18625080]
 [6] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047] 
Functional Description
 This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5. Involved in ergosterol biosynthesis. Has NADPH-dependent ferrireductase activity on the plasma membrane. 
Sequence Annotation
 DOMAIN 61 204 Flavodoxin-like.
 DOMAIN 266 529 FAD-binding FR-type.
 NP_BIND 71 78 FMN; alternate.
 NP_BIND 116 119 FMN.
 NP_BIND 610 621 NADP.
 BINDING 67 67 FMN.
 BINDING 187 187 FMN; alternate.
 BINDING 441 441 FAD.
 BINDING 478 478 FAD.
 BINDING 646 646 NADP.
 CROSSLNK 666 666 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Cell membrane; Complete proteome; Direct protein sequencing; Endoplasmic reticulum; FAD; Flavoprotein; FMN; Isopeptide bond; Lipid biosynthesis; Lipid metabolism; Membrane; Microsome; Mitochondrion; Mitochondrion outer membrane; NADP; Oxidoreductase; Phosphoprotein; Reference proteome; Steroid biosynthesis; Steroid metabolism; Sterol biosynthesis; Sterol metabolism; Transmembrane; Transmembrane helix; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 691 AA 
Protein Sequence
MPFGIDNTDF TVLAGLVLAV LLYVKRNSIK ELLMSDDGDI TAVSSGNRDI AQVVTENNKN 60
YLVLYASQTG TAEDYAKKFS KELVAKFNLN VMCADVENYD FESLNDVPVI VSIFISTYGE 120
GDFPDGAVNF EDFICNAEAG ALSNLRYNMF GLGNSTYEFF NGAAKKAEKH LSAAGAIRLG 180
KLGEADDGAG TTDEDYMAWK DSILEVLKDE LHLDEQEAKF TSQFQYTVLN EITDSMSLGE 240
PSAHYLPSHQ LNRNADGIQL GPFDLSQPYI APIVKSRELF SSNDRNCIHS EFDLSGSNIK 300
YSTGDHLAVW PSNPLEKVEQ FLSIFNLDPE TIFDLKPLDP TVKVPFPTPT TIGAAIKHYL 360
EITGPVSRQL FSSLIQFAPN ADVKEKLTLL SKDKDQFAVE ITSKYFNIAD ALKYLSDGAK 420
WDTVPMQFLV ESVPQMTPRY YSISSSSLSE KQTVHVTSIV ENFPNPELPD APPVVGVTTN 480
LLRNIQLAQN NVNIAETNLP VHYDLNGPRK LFANYKLPVH VRRSNFRLPS NPSTPVIMIG 540
PGTGVAPFRG FIRERVAFLE SQKKGGNNVS LGKHILFYGS RNTDDFLYQD EWPEYAKKLD 600
GSFEMVVAHS RLPNTKKVYV QDKLKDYEDQ VFEMINNGAF IYVCGDAKGM AKGVSTALVG 660
ILSRGKSITT DEATELIKML KTSGRYQEDV W 691 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0005741; C:mitochondrial outer membrane; IDA:SGD.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0009055; F:electron carrier activity; IDA:SGD.
 GO:0010181; F:FMN binding; IEA:InterPro.
 GO:0005506; F:iron ion binding; IEA:InterPro.
 GO:0003958; F:NADPH-hemoprotein reductase activity; IEA:EC.
 GO:0006696; P:ergosterol biosynthetic process; IMP:SGD. 
Interpro
 IPR003097; FAD-binding_1.
 IPR017927; Fd_Rdtase_FAD-bd.
 IPR001094; Flavdoxin.
 IPR008254; Flavodoxin/NO_synth.
 IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
 IPR023173; NADPH_Cyt_P450_Rdtase_dom3.
 IPR001433; OxRdtase_FAD/NAD-bd.
 IPR023208; P450R.
 IPR017938; Riboflavin_synthase-like_b-brl. 
Pfam
 PF00667; FAD_binding_1
 PF00258; Flavodoxin_1
 PF00175; NAD_binding_1 
SMART
  
PROSITE
 PS51384; FAD_FR
 PS50902; FLAVODOXIN_LIKE 
PRINTS
 PR00369; FLAVODOXIN.
 PR00371; FPNCR.