Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Nicotinamide phosphoribosyltransferase  

UniProtKB / Swiss-Prot ID :  NAMPT_HUMAN

Gene Name (Synonyms) : 
NAMPT, PBEF, PBEF1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm (By similarity). 

Protein Function :  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). 

Protein Sequence MNPAAEAEFNILLATDSYKVTHYKQYPPNTSKVYSYFECREKKTENSKLRKVKYEETVFYGLQYILNKYL...
Predicted Secondary Structure CCCCCCCEEEEEEEECCEEEEEEEECCCCHHHHHHHHHHHCCCCCCCCHHHHHHHHHHHHHHHHHHHHHH...
Protein Variant
LocationDescription
176L -> S (in a colorectal cancer sample;somatic mutation).
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
34PhosphotyrosineTSKVYSYFE
HHHHHHHHH
11.03HPRD
Link
34PhosphotyrosineTSKVYSYFE
HHHHHHHHH
11.03PhosphoELM
Link
34PhosphotyrosineTSKVYSYFE
HHHHHHHHH
11.03Phosphositeplus
Link
34Phosphotyrosine.TSKVYSYFE
HHHHHHHHH
11.03UniProtKB
Link
87PhosphotyrosineAKDVYKEHF
HHHHHHHHH
22.31HPRD
Link
88Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KDVYKEHFQ
HHHHHHHHC
44.56Phosphositeplus
Link
99Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VFNEKGWNY
CCHHHHHHH
71.04Phosphositeplus
Link
107Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)YILEKYDGH
HHHHHCCCC
45.24Phosphositeplus
Link
117Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PIEIKAVPE
CEEEEEEEC
30.46Phosphositeplus
Link
174Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KILAKYLLE
HHHHHHHHH
32.74Phosphositeplus
Link
188PhosphotyrosineDGLEYKLHD
CCEEEEEEE
24.72HPRD
Link
188PhosphotyrosineDGLEYKLHD
CCEEEEEEE
24.72PhosphoELM
Link
188PhosphotyrosineDGLEYKLHD
CCEEEEEEE
24.72Phosphositeplus
Link
188Phosphotyrosine.DGLEYKLHD
CCEEEEEEE
24.72UniProtKB
Link
189Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GLEYKLHDF
CEEEEEEEC
29.94Phosphositeplus
Link
228Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LALIKKYYG
HHHHHHCCC
35.26Phosphositeplus
Link
335PhosphothreonineKFPVTENSK
CCCCCCCCC
29.68Phosphositeplus
Link
338PhosphoserineVTENSKGYK
CCCCCCCCE
22.64Phosphositeplus
Link
342Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SKGYKLLPP
CCCCEECCC
52.82Phosphositeplus
Link
369Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VEGMKQKMW
HHHHHHCCC
58.59Phosphositeplus
Link
371Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GMKQKMWSI
HHHHCCCCH
36.50Phosphositeplus
Link
389Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GLLQKLTRD
HHHHHHHHH
52.36Phosphositeplus
Link
398PhosphoserineLLNCSFKCS
HHCEEEEEE
27.02HPRD
Link
398PhosphoserineLLNCSFKCS
HHCEEEEEE
27.02Phosphositeplus
Link
398PhosphoserineLLNCSFKCS
HHCEEEEEE
27.02SysPTM
Link
398Phosphoserine.LLNCSFKCS
HHCEEEEEE
27.02UniProtKB
Link
447Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LEEGKGDLE
EECCCCCHH
53.16Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
NAMPT_HUMANdirect interaction
direct interaction
direct interaction
DIP:57237EDIP16783377
16783377
16783377
CD38_HUMANENSP00000222553STRING
NUD12_HUMANENSP00000222553STRING
5NT1A_HUMANENSP00000222553STRING
5NT3_HUMANENSP00000222553STRING
NT5C_HUMANENSP00000222553STRING
5NTD_HUMANENSP00000222553STRING
BST1_HUMANENSP00000222553STRING
NMNA2_HUMANENSP00000222553STRING
NMNA3_HUMANENSP00000222553STRING
NNMT_HUMANENSP00000222553STRING
INSR_HUMANENSP00000222553STRING
5NTC_HUMANENSP00000222553STRING
ENPP3_HUMANENSP00000222553STRING
ENPP1_HUMANENSP00000222553STRING
5NT1B_HUMANENSP00000222553STRING
PNPH_HUMANENSP00000222553STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-188, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-34, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-398, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures