CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014631
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cytochrome P450 3A11 
Protein Synonyms/Alias
 CYPIIIA11; Cytochrome P-450IIIAM1; Cytochrome P-450UT 
Gene Name
 Cyp3a11 
Gene Synonyms/Alias
 Cyp3a-11 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
29LYRYGTRKHELFKKQacetylation[1]
42KQGIPGPKPLPFLGTubiquitination[2]
59NYYKGLWKFDMECYKubiquitination[2]
66KFDMECYKKYGKTWGacetylation[3]
66KFDMECYKKYGKTWGubiquitination[2]
70ECYKKYGKTWGLFDGubiquitination[2]
91VTDPETIKNVLVKECubiquitination[2]
96TIKNVLVKECFSVFTubiquitination[2]
116GPVGIMSKAISISKDubiquitination[2]
122SKAISISKDDEWKRYubiquitination[2]
127ISKDDEWKRYRALLSacetylation[4]
127ISKDDEWKRYRALLSubiquitination[2]
141SPTFTSGKLKEMFPVacetylation[3]
141SPTFTSGKLKEMFPVubiquitination[2]
143TFTSGKLKEMFPVIEacetylation[3]
143TFTSGKLKEMFPVIEubiquitination[2]
158QYGDILVKYLRQKAKubiquitination[2]
250KDSIEFFKKFVDRMKacetylation[3]
250KDSIEFFKKFVDRMKubiquitination[2]
251DSIEFFKKFVDRMKEubiquitination[2]
266SRLDSKQKHRVDFLQubiquitination[2]
283MNSHNNSKDKVSHKAubiquitination[2]
331THPDIQKKLQDEIDEubiquitination[2]
379NRLERVCKKDVELNGubiquitination[2]
380RLERVCKKDVELNGVubiquitination[2]
391LNGVYIPKGSTVMIPubiquitination[2]
422FQPERFSKENKGSIDubiquitination[2]
425ERFSKENKGSIDPYVubiquitination[2]
454RFALMNMKLALTKIMubiquitination[2]
459NMKLALTKIMQNFSFubiquitination[2]
470NFSFQPCKETQIPLKubiquitination[2]
477KETQIPLKLSRQGLLubiquitination[2]
488QGLLQPEKPIVLKVVacetylation[3, 4]
488QGLLQPEKPIVLKVVubiquitination[2]
493PEKPIVLKVVPRDAVacetylation[3, 4]
493PEKPIVLKVVPRDAVubiquitination[2]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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
Functional Description
 Catalyzes erythromycin N-demethylation, nifedipine oxidation and testosterone 6 beta-hydroxylation. 
Sequence Annotation
 METAL 443 443 Iron (heme axial ligand) (By similarity).  
Keyword
 Complete proteome; Direct protein sequencing; Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome; Monooxygenase; Oxidoreductase; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 504 AA 
Protein Sequence
MDLVSALSLE TWVLLAISLV LLYRYGTRKH ELFKKQGIPG PKPLPFLGTV LNYYKGLWKF 60
DMECYKKYGK TWGLFDGQTP LLAVTDPETI KNVLVKECFS VFTNRRDFGP VGIMSKAISI 120
SKDDEWKRYR ALLSPTFTSG KLKEMFPVIE QYGDILVKYL RQKAKKGKPV TMKDVLGAYS 180
MDVITSTSFG VNVDSLNNPE DPFVEKAKKL LRFDFFDPLL FSVVLFPFLT PVYEMLNICM 240
FPKDSIEFFK KFVDRMKESR LDSKQKHRVD FLQLMMNSHN NSKDKVSHKA LSDMEITAQS 300
IIFIFAGYET TSSTLSFTLH SLATHPDIQK KLQDEIDEAL PNKAPPTYDT VMEMEYLDMV 360
LNETLRLYPI ANRLERVCKK DVELNGVYIP KGSTVMIPSY ALHHDPQHWS EPEEFQPERF 420
SKENKGSIDP YVYLPFGNGP RNCLGMRFAL MNMKLALTKI MQNFSFQPCK ETQIPLKLSR 480
QGLLQPEKPI VLKVVPRDAV ITGA 504 
Gene Ontology
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0070330; F:aromatase activity; IEA:EC.
 GO:0009055; F:electron carrier activity; IEA:InterPro.
 GO:0020037; F:heme binding; IEA:InterPro.
 GO:0005506; F:iron ion binding; IEA:InterPro.
 GO:0004497; F:monooxygenase activity; IDA:MGI. 
Interpro
 IPR001128; Cyt_P450.
 IPR017972; Cyt_P450_CS.
 IPR008072; Cyt_P450_E_CYP3A.
 IPR002402; Cyt_P450_E_grp-II. 
Pfam
 PF00067; p450 
SMART
  
PROSITE
 PS00086; CYTOCHROME_P450 
PRINTS
 PR00464; EP450II.
 PR01689; EP450IICYP3A.
 PR00385; P450.