CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007679
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Nicotinamide phosphoribosyltransferase 
Protein Synonyms/Alias
 NAmPRTase; Nampt; Pre-B-cell colony-enhancing factor 1; Pre-B cell-enhancing factor; Visfatin 
Gene Name
 NAMPT 
Gene Synonyms/Alias
 PBEF; PBEF1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
88QEAKDVYKEHFQDDVubiquitination[1]
99QDDVFNEKGWNYILEubiquitination[1, 2, 3, 4, 5]
107GWNYILEKYDGHLPIubiquitination[1, 3, 4, 6]
117GHLPIEIKAVPEGFVubiquitination[1, 3, 6, 7]
174EQKKILAKYLLETSGubiquitination[1, 4]
189NLDGLEYKLHDFGYRubiquitination[1, 3]
228VAGLALIKKYYGTKDubiquitination[1, 2, 5]
229AGLALIKKYYGTKDPubiquitination[3]
339FPVTENSKGYKLLPPubiquitination[3]
342TENSKGYKLLPPYLRubiquitination[2, 5]
369QEIVEGMKQKMWSIEubiquitination[1, 4]
371IVEGMKQKMWSIENIubiquitination[2, 5]
389SGGGLLQKLTRDLLNubiquitination[1]
423DPVADPNKRSKKGRLubiquitination[3]
447FVTLEEGKGDLEEYGubiquitination[1]
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] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [7] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
Functional Description
 Catalyzes the condensation of nicotinamide with 5- phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an intermediate in the biosynthesis of NAD. It is the rate limiting component in the mammalian NAD biosynthesis pathway (By similarity). 
Sequence Annotation
 REGION 311 313 Nicotinamide ribonucleotide binding.
 REGION 353 354 Nicotinamide ribonucleotide binding.
 BINDING 196 196 Diphosphate.
 BINDING 219 219 Nicotinamide ribonucleotide.
 BINDING 247 247 Diphosphate.
 BINDING 311 311 Diphosphate.
 BINDING 384 384 Nicotinamide ribonucleotide; via amide
 BINDING 392 392 Nicotinamide ribonucleotide.  
Keyword
 3D-structure; Complete proteome; Cytoplasm; Glycosyltransferase; Polymorphism; Pyridine nucleotide biosynthesis; Reference proteome; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 491 AA 
Protein Sequence
MNPAAEAEFN ILLATDSYKV THYKQYPPNT SKVYSYFECR EKKTENSKLR KVKYEETVFY 60
GLQYILNKYL KGKVVTKEKI QEAKDVYKEH FQDDVFNEKG WNYILEKYDG HLPIEIKAVP 120
EGFVIPRGNV LFTVENTDPE CYWLTNWIET ILVQSWYPIT VATNSREQKK ILAKYLLETS 180
GNLDGLEYKL HDFGYRGVSS QETAGIGASA HLVNFKGTDT VAGLALIKKY YGTKDPVPGY 240
SVPAAEHSTI TAWGKDHEKD AFEHIVTQFS SVPVSVVSDS YDIYNACEKI WGEDLRHLIV 300
SRSTQAPLII RPDSGNPLDT VLKVLEILGK KFPVTENSKG YKLLPPYLRV IQGDGVDINT 360
LQEIVEGMKQ KMWSIENIAF GSGGGLLQKL TRDLLNCSFK CSYVVTNGLG INVFKDPVAD 420
PNKRSKKGRL SLHRTPAGNF VTLEEGKGDL EEYGQDLLHT VFKNGKVTKS YSFDEIRKNA 480
QLNIELEAAH H 491 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005125; F:cytokine activity; TAS:ProtInc.
 GO:0047280; F:nicotinamide phosphoribosyltransferase activity; IEA:EC.
 GO:0004516; F:nicotinate phosphoribosyltransferase activity; IEA:InterPro.
 GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:InterPro.
 GO:0007267; P:cell-cell signaling; TAS:ProtInc.
 GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-UniPathway.
 GO:0019674; P:NAD metabolic process; TAS:Reactome.
 GO:0006769; P:nicotinamide metabolic process; TAS:Reactome.
 GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
 GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; IDA:BHF-UCL.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
 GO:0007165; P:signal transduction; TAS:ProtInc.
 GO:0006767; P:water-soluble vitamin metabolic process; TAS:Reactome. 
Interpro
 IPR015977; Nic_PRibTrfase-like.
 IPR016471; Nicotinamide_PRibTrfase.
 IPR002638; Quinolinate_PRibosylTrfase_C. 
Pfam
 PF04095; NAPRTase 
SMART
  
PROSITE
  
PRINTS