CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020942
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Sterol 26-hydroxylase, mitochondrial 
Protein Synonyms/Alias
 5-beta-cholestane-3-alpha,7-alpha,12-alpha-triol 27-hydroxylase; Cytochrome P-450C27/25; Cytochrome P450 27; Sterol 27-hydroxylase; Vitamin D(3) 25-hydroxylase 
Gene Name
 Cyp27a1 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
31CPQGARAKATIPAALubiquitination[1]
125QVMRQEGKYPIRDHMacetylation[2, 3, 4]
142WKDHRDHKGLTYGIFacetylation[5]
232EKRIGCLKPSIPEDTacetylation[4, 5, 6]
285DNIFSFGKKLIDEKVacetylation[2, 3, 4, 5]
291GKKLIDEKVQELKAQacetylation[3, 5]
296DEKVQELKAQLQETGacetylation[4, 5, 6]
296DEKVQELKAQLQETGubiquitination[1]
365EIQEALHKEVTGVVPacetylation[5]
365EIQEALHKEVTGVVPubiquitination[1]
375TGVVPFGKVPQHKDFacetylation[3, 4, 5]
375TGVVPFGKVPQHKDFubiquitination[1]
380FGKVPQHKDFAHMPLacetylation[3, 4, 5]
389FAHMPLLKAVIKETLacetylation[3]
389FAHMPLLKAVIKETLubiquitination[1]
393PLLKAVIKETLRLYPacetylation[3, 4, 5]
393PLLKAVIKETLRLYPubiquitination[1]
412NSRIITEKETEINGFacetylation[3]
412NSRIITEKETEINGFubiquitination[1]
423INGFLFPKNTQFVLCacetylation[3, 4]
456PHRWLRKKEADNPGIacetylation[5]
499MLSRLVQKYEIALAPacetylation[2, 3, 5]
499MLSRLVQKYEIALAPubiquitination[1]
512APGMGEVKTVSRIVLacetylation[3, 4, 5]
523RIVLVPSKKVRLHFLacetylation[3, 4, 5]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
 [3] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123]
 [4] Quantification of mitochondrial acetylation dynamics highlights prominent sites of metabolic regulation.
 Still AJ, Floyd BJ, Hebert AS, Bingman CA, Carson JJ, Gunderson DR, Dolan BK, Grimsrud PA, Dittenhafer-Reed KE, Stapleton DS, Keller MP, Westphall MS, Denu JM, Attie AD, Coon JJ, Pagliarini DJ.
 J Biol Chem. 2013 Jul 17;. [PMID: 23864654]
 [5] Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
 Rardin MJ, Newman JC, Held JM, Cusack MP, Sorensen DJ, Li B, Schilling B, Mooney SD, Kahn CR, Verdin E, Gibson BW.
 Proc Natl Acad Sci U S A. 2013 Apr 16;110(16):6601-6. [PMID: 23576753]
 [6] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758] 
Functional Description
 Catalyzes the first step in the oxidation of the side chain of sterol intermediates; the 27-hydroxylation of 5-beta- cholestane-3-alpha,7-alpha,12-alpha-triol. Has also a vitamin D3- 25-hydroxylase activity (By similarity). 
Sequence Annotation
 REGION 386 400 Sterol-binding (Potential).
 METAL 479 479 Iron (heme axial ligand) (By similarity).
 MOD_RES 125 125 N6-acetyllysine.
 MOD_RES 285 285 N6-acetyllysine.
 MOD_RES 499 499 N6-acetyllysine.  
Keyword
 Acetylation; Complete proteome; Heme; Iron; Membrane; Metal-binding; Mitochondrion; Monooxygenase; NADP; Oxidoreductase; Reference proteome; Transit peptide. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 533 AA 
Protein Sequence
MAAWSRTRLR WTLLDPRVVG RGLCPQGARA KATIPAALQA QESTEGPGTG QDRPRLRSPA 60
ELPGTGTLQF LFQLFLQGYV LHLPDLQVLN KTKYGPMWTT SFGTYTNVNL ASAPLLEQVM 120
RQEGKYPIRD HMDQWKDHRD HKGLTYGIFI AQGEQWYHLR QALKQRLLKP DEAALYTDAL 180
NEVISDFITR LDQVRAESES GDQVPDMAHL LYHLALEAIT YILFEKRIGC LKPSIPEDTA 240
AFIRSVAIMF QNSVYITFLP KWTRPLLPFW KRYLNGWDNI FSFGKKLIDE KVQELKAQLQ 300
ETGPDGVRVS GYLHFLLTNE LLSTQETIGT FPELLLAGVD TTSNTLTWAL YHLSKSPEIQ 360
EALHKEVTGV VPFGKVPQHK DFAHMPLLKA VIKETLRLYP VVPTNSRIIT EKETEINGFL 420
FPKNTQFVLC HYVVSRDPSV FPEPNSFQPH RWLRKKEADN PGILHPFGSV PFGYGVRSCL 480
GRRIAELEMQ LMLSRLVQKY EIALAPGMGE VKTVSRIVLV PSKKVRLHFL QRQ 533 
Gene Ontology
 GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
 GO:0047749; F:cholestanetriol 26-monooxygenase activity; IEA:EC.
 GO:0031073; F:cholesterol 26-hydroxylase activity; IEA:Compara.
 GO:0009055; F:electron carrier activity; IEA:InterPro.
 GO:0020037; F:heme binding; IEA:InterPro.
 GO:0005506; F:iron ion binding; IEA:InterPro.
 GO:0030343; F:vitamin D3 25-hydroxylase activity; IEA:Compara.
 GO:0036378; P:calcitriol biosynthetic process from calciol; IEA:GOC.
 GO:0008203; P:cholesterol metabolic process; IEA:Compara. 
Interpro
 IPR001128; Cyt_P450.
 IPR017972; Cyt_P450_CS.
 IPR002401; Cyt_P450_E_grp-I. 
Pfam
 PF00067; p450 
SMART
  
PROSITE
 PS00086; CYTOCHROME_P450 
PRINTS
 PR00463; EP450I.
 PR00385; P450.