CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001757
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 NADPH--cytochrome P450 reductase 
Protein Synonyms/Alias
 CPR; P450R 
Gene Name
 Por 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
311ELDISDSKIRYESGDubiquitination[1]
584EELARFHKDGALTQLacetylation[2]
610VYVQHLLKRDREHLWacetylation[2]
Reference
 [1] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113]
 [2] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 
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. 
Sequence Annotation
 DOMAIN 80 224 Flavodoxin-like.
 DOMAIN 279 521 FAD-binding FR-type.
 NP_BIND 170 201 FMN (By similarity).
 NP_BIND 314 325 FAD (By similarity).
 NP_BIND 451 461 FAD (By similarity).
 NP_BIND 530 548 NADP (By similarity).
 NP_BIND 625 641 NADP (By similarity).
 MOD_RES 2 2 N-acetylglycine (By similarity).
 MOD_RES 575 575 Phosphotyrosine (By similarity).  
Keyword
 3D-structure; Acetylation; Complete proteome; Endoplasmic reticulum; FAD; Flavoprotein; FMN; Membrane; NADP; Oxidoreductase; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 678 AA 
Protein Sequence
MGDSHEDTSA TMPEAVAEEV SLFSTTDMVL FSLIVGVLTY WFIFRKKKEE IPEFSKIQTT 60
APPVKESSFV EKMKKTGRNI IVFYGSQTGT AEEFANRLSK DAHRYGMRGM SADPEEYDLA 120
DLSSLPEIDK SLVVFCMATY GEGDPTDNAQ DFYDWLQETD VDLTGVKFAV FGLGNKTYEH 180
FNAMGKYVDQ RLEQLGAQRI FELGLGDDDG NLEEDFITWR EQFWPAVCEF FGVEATGEES 240
SIRQYELVVH EDMDVAKVYT GEMGRLKSYE NQKPPFDAKN PFLAAVTANR KLNQGTERHL 300
MHLELDISDS KIRYESGDHV AVYPANDSAL VNQIGEILGA DLDVIMSLNN LDEESNKKHP 360
FPCPTTYRTA LTYYLDITNP PRTNVLYELA QYASEPSEQE HLHKMASSSG EGKELYLSWV 420
VEARRHILAI LQDYPSLRPP IDHLCELLPR LQARYYSIAS SSKVHPNSVH ICAVAVEYEA 480
KSGRVNKGVA TSWLRAKEPA GENGGRALVP MFVRKSQFRL PFKSTTPVIM VGPGTGIAPF 540
MGFIQERAWL REQGKEVGET LLYYGCRRSD EDYLYREELA RFHKDGALTQ LNVAFSREQA 600
HKVYVQHLLK RDREHLWKLI HEGGAHIYVC GDARNMAKDV QNTFYDIVAE FGPMEHTQAV 660
DYVKKLMTKG RYSLDVWS 678 
Gene Ontology
 GO:0005829; C:cytosol; IBA:RefGenome.
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0016020; C:membrane; IDA:RGD.
 GO:0005739; C:mitochondrion; IDA:RGD.
 GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; IDA:RGD.
 GO:0009055; F:electron carrier activity; IDA:RGD.
 GO:0019899; F:enzyme binding; IDA:RGD.
 GO:0050660; F:flavin adenine dinucleotide binding; IMP:RGD.
 GO:0010181; F:FMN binding; IMP:RGD.
 GO:0016787; F:hydrolase activity; IDA:RGD.
 GO:0005506; F:iron ion binding; IEA:InterPro.
 GO:0047726; F:iron-cytochrome-c reductase activity; IDA:RGD.
 GO:0050661; F:NADP binding; IDA:RGD.
 GO:0003958; F:NADPH-hemoprotein reductase activity; IDA:BHF-UCL.
 GO:0008941; F:nitric oxide dioxygenase activity; IDA:RGD.
 GO:0016709; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen; IBA:RefGenome.
 GO:0009437; P:carnitine metabolic process; IEP:RGD.
 GO:0090346; P:cellular organofluorine metabolic process; IEA:Compara.
 GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IEP:RGD.
 GO:0071375; P:cellular response to peptide hormone stimulus; IEP:RGD.
 GO:0070988; P:demethylation; IDA:RGD.
 GO:0019395; P:fatty acid oxidation; IDA:RGD.
 GO:0009812; P:flavonoid metabolic process; IEP:RGD.
 GO:0018393; P:internal peptidyl-lysine acetylation; IDA:RGD.
 GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
 GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:RGD.
 GO:0060192; P:negative regulation of lipase activity; IDA:RGD.
 GO:0043602; P:nitrate catabolic process; IDA:RGD.
 GO:0046210; P:nitric oxide catabolic process; IDA:RGD.
 GO:0045542; P:positive regulation of cholesterol biosynthetic process; IMP:RGD.
 GO:0032332; P:positive regulation of chondrocyte differentiation; IMP:RGD.
 GO:0032770; P:positive regulation of monooxygenase activity; IEA:Compara.
 GO:0045880; P:positive regulation of smoothened signaling pathway; IMP:RGD.
 GO:0090031; P:positive regulation of steroid hormone biosynthetic process; IDA:RGD.
 GO:0003420; P:regulation of growth plate cartilage chondrocyte proliferation; IMP:RGD.
 GO:0042493; P:response to drug; IEP:RGD.
 GO:0007584; P:response to nutrient; IEP:RGD. 
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.